PHARMACEUTICAL AND ANTI-gpNMB ANTIBODY FOR REMOVING DISEASE-ASSOCIATED CELLS

Abstract

Provided is a new means capable of effectively removing disease-associated cells that induce a disease in various diseases or enhances the progression of the disease.　A pharmaceutical composition for removing disease-associated cells comprises an anti-gpNMB antibody or a fragment thereof or a derivative of foregoing that specifically binds to at least one site of a region from V78 to PKD domain of human gpNMB.

Description

Drugs and anti-gpNMB antibodies for removing disease-related cells The present invention relates to a new drug for removing disease-related cells, and a novel anti-gpNMB antibody to be used therein. <Immunoglobulin (antibody)> Human immunoglobulins (antibodies) are divided into five classes, IgG, IgM, IgA, IgD, and IgE, based on the number of Y-shaped units and the type of heavy chain. The heavy chains of IgG, IgM, IgA, IgD, and IgE are designated gamma, mu, alpha, delta, and epsilon, respectively. There are four subclasses of IgG: IgG1, IgG2, IgG3, and IgG4. The light chains of antibodies can be classified as either kappa (κ) or lambda (λ) types, depending on slight differences in polypeptide structure, but the heavy chains determine the subclass of the antibody. <phagocytic cells> Phagocytes include macrophages, microglia, dendritic cells, monocytes, neutrophils, etc., and tissue-resident phagocytes include Kupffer cells, Langerhans cells, osteoclasts, etc. Other macrophages include cancer-infiltrating macrophages, aging macrophages, fat-accumulating macrophages, sphingomyelin-accumulating macrophages, foam cells, alveolar macrophages, peritoneal macrophages, splenic macrophages, thymic macrophages, etc. Microglia include cancer-infiltrating microglia, aging microglia, fat-accumulating microglia, sphingomyelin-accumulating microglia, etc. Dendritic cells include subtypes such as standard type 1 dendritic cells (cDC1), standard type 2 dendritic cells (cDC2), monocyte-derived dendritic cells (MoDC), and plasmacytoid dendritic cells (pDC). <Macrophages> There are various types of macrophages, and broadly classified according to their origin, they can be divided into resident macrophages that reside in tissues and infiltrating macrophages that migrate and differentiate from monocytes from the blood in response to changes in the tissue environment. Resident macrophages in the liver are called Kupffer cells, resident macrophages in the brain are called microglia, resident macrophages in bone tissue are called osteoclasts, resident macrophages in the skin are called Langerhans cells, and resident macrophages in the lungs are called alveolar macrophages. In terms of properties, macrophages were largely divided into M1 macrophages, which induce inflammation and tissue repair, and anti-inflammatory M2 macrophages. However, in recent years, various subtypes of macrophages have been revealed by scRNAseq analysis, and the existence of disease-specific macrophages in various diseases has been reported. As mentioned above, macrophages differentiate into various types depending on the environment. It has been revealed that each subtype works to heal damage, or conversely, induces disease or accelerates its progression. <Aging cells> Senescent cells are cells in which the cessation of sustained cell proliferation has been induced by DNA damage, activation of cancer genes, stress, etc. In recent years, it has been revealed that senescent cells acquire a proinflammatory phenotype called SASP (Senescence-associated secretory phenotype), and it has been suggested that senescent cells are involved in many diseases (Non-Patent Document 1). While cellular senescence is thought to be a mechanism for preventing damaged cells from undergoing malignant transformation and becoming cancerous, many findings have been reported that cellular senescence is involved in various age-related pathologies (tissue degeneration, chronic inflammation, cancer progression, etc.). Thus, the biological role of cellular senescence is highly complex, with both beneficial and detrimental effects reported and varying depending on the physiological context. Meanwhile, several clinical trials are underway to treat intractable diseases with senolytic drugs. <Intractable cancer> Since the development of molecular targeted drugs, a certain degree of therapeutic effect has been achieved for cancers that were previously difficult to treat. Furthermore, the advent of immune checkpoint inhibitors has led to a greater understanding of cancer immunotherapy, and the therapeutic effect of molecular targeted drugs has been further improved (Non-Patent Document 2). However, since there are still many cancer patients suffering from intractable cancers (melanoma, TNBC, glioblastoma, multiple myeloma, etc.) for which sufficient efficacy has not yet been demonstrated, it is necessary to create further groundbreaking drugs with high therapeutic effects. In particular, the difficulty of creating drugs for glioblastoma, which requires delivery into the brain and has a diverse range of antigenic changes, remains high. In recent years, bispecific antibodies of anti-T cell antibodies and anti-cancer antigen antibodies intended for T cell engagement effect, aiming at enhancing the cancer cell killing effect of T cells (Non-Patent Document 3), and CAR-T cell therapy that directly delivers T cells to cancer cells (Non-Patent Document 4) have been developed, and higher therapeutic effects have been obtained. However, there are many patients who are resistant to treatment because the activity of T cells is not fully exerted, and there is a high unmet need. For this reason, NK cell engagement antibodies (Non-Patent Document 5), CAR-NK that delivers NK cells (Non-Patent Document 6), macrophage engagement antibodies (Non-Patent Document 7), and CAR macrophage (chimeric antigen receptor macrophage) that delivers macrophages have also been devised (Non-Patent Document 8, Non-Patent Document 9). In addition, the combined use of oncolytic viruses and T cell engagement has also been considered (Non-Patent Document 10). One of the reasons that cancer treatment is difficult is the formation of a cancer microenvironment. In the cancer microenvironment, cytokines produced by the cancer cells themselves and macrophages and microglia that infiltrate into the cancer tissue secrete humoral factors or directly interact with each other to form an immunosuppressive environment. Furthermore, it has been reported that senescent cells create an immunosuppressive environment and a chronic inflammatory environment, supporting the invasion and proliferation of cancer (Non-Patent Document 11). The cancer microenvironment helps cancer cells escape from host immune attack and supports their proliferation and stem cell formation. It has been reported that the cancer immunosuppressive environment is involved in refractory tumors and tumors with poor prognosis, which are resistant to treatments such as immune checkpoint inhibitors. Therefore, it is important to destroy the cancer microenvironment in cancer treatment (Non-Patent Document 12). Several attempts to remove cancer-infiltrating macrophages have been reported so far. For example, non-specific macrophage removal using a CSF1R inhibitor (Non-Patent Document 13) and cancer-infiltrating macrophage removal using an anti-TREM2 antibody (Non-Patent Document 14) have been reported. Furthermore, focusing on senescent macrophages, it has been reported that removing cancer-infiltrating senescent macrophages with a senescent cell removal drug suppresses cancer growth in lung cancer-bearing model mice and improves survival rate and survival time (Non-Patent Document 15). <Intractable cancer and gpNMB> It has been reported that when gpNMB levels in the blood of cancer patients who showed poor therapeutic effects with immune checkpoint inhibitors were examined, elevated gpNMB levels were found, and the combined effect of immune checkpoint inhibitors and anti-gpNMB antibodies has been demonstrated in model mice transplanted with melanoma (Non-Patent Document 16). It has also been shown that microglia and macrophages that infiltrate into glioblastomas show a profile different from M1 and M2, highly express gpNMB and Spp1, and that high expression of gpNMB and Spp1 in glioblastoma patients is correlated with poor prognosis (Non-Patent Document 17). The above reports suggest that gpNMB is involved in the immunosuppressive environment that forms the cancer microenvironment. <Fibrosis> Fibrosis is a disease in which organs important to vital functions, such as the lungs, liver, kidneys, heart, skin, and blood vessels, suffer transient or chronic damage, leading to excessive or abnormal accumulation of collagen and other fibers during the repair process, causing the organs to lose elasticity, harden, and become unable to perform their normal functions. No fundamental treatment for this disease has yet been developed. Idiopathic pulmonary fibrosis (IPF), a type of pulmonary fibrosis, is an intractable disease with no therapeutic drug. Clinical trials are being conducted to investigate the therapeutic effect of removing senescent cells using D+Q (Dasatinib and Quercetin), which contains an anticancer drug (Non-Patent Document 18). However, due to factors such as the dosage being restricted to avoid side effects, the efficacy has not been sufficient. Recently, the results of a phase 3 clinical trial of an anti-CTGF antibody (Non-Patent Document 19) have been reported, but no therapeutic effect was observed. Chronic kidney disease (CKD) is a condition in which abnormalities in the structure or function of the kidney continue for more than three months. There is no effective treatment, and as the disease progresses, it leads to end-stage renal failure, requiring dialysis or kidney transplantation. Clinical trials have been conducted with senolytic drugs for diabetic nephropathy, but no therapeutic effect has been demonstrated (Non-Patent Document 20). Nonalcoholic steatohepatitis (NASH), which progresses through the induction of hepatic fibrosis, is an intractable disease with no therapeutic drug, and it has been reported that fibrosis is induced by fat-accumulating macrophages (Non-Patent Document 21).On the other hand, it has also been reported that the removal of senescent cells improves the pathology of fatty liver (Non-Patent Document 22). Vasculitis is an autoimmune vascular inflammation of unknown etiology that causes destruction of the vascular wall and induces fibrosis. In Takayasu's vasculitis, giant cell arteritis (GCA), and other conditions, it has been reported that monocytes and macrophages, which stimulate fibroblasts to induce fibrosis, are involved in the pathogenesis (Non-Patent Document 23). Duchenne muscular dystrophy (DMD) is a progressive muscle atrophy, and it has been reported that fibrosis is induced in skeletal muscles and that a certain type of macrophage is involved (Non-Patent Document 24). It has also been reported that the pathology and muscle strength of a DMD rat model were improved by a senolytic drug (Non-Patent Document 25). <Fibrosis and gpNMB> There are several reports that gpNMB is involved in fibrosis, but there are both reports that it inhibits and promotes fibrosis. In silicosis, a lung fibrosis disease, scRNAseq analysis using a mouse model showed that gpNMB induces epithelial-mesenchymal transition in alveolar epithelial cells and enhances fibrosis (Non-Patent Document 26). It has been reported that gpNMB is expressed in scar-associated macrophages (SAMs), a subset of macrophages that are thought to induce fibrosis in liver and lung fibrosis (Non-Patent Document 27). On the other hand, it has been reported that overexpression of gpNMB improved fat accumulation and fibrosis in the liver in patients with nonalcoholic fatty liver disease (NAFLD) induced by a high-fat, high-sucrose (HFHS) diet (Non-Patent Document 28). There is also a report that macrophage-derived gpNMB enhances the repair of skin damage (Non-Patent Document 29). Fibrosis of the vascular wall is observed in Takayasu arteritis, a type of vascular fibrosis, and it has been reported that macrophages produce TGFβ and gpNMB to activate fibroblasts (Non-Patent Document 30). A database analysis of genes expressed in the skeletal muscle tissue of DMD patients has reported DMD-specific genes, and gpNMB is one of them (Non-Patent Document 31). <Metabolic diseases> Metabolic diseases include diabetes, high blood pressure, dyslipidemia (high cholesterol, high triglycerides, etc.), arteriosclerosis, fatty liver, hyperuricemia (gout), metabolic syndrome, and obesity, and many of these diseases are thought to be caused by chronic inflammation. Hyperglycemia in diabetes induces various diseases (Non-Patent Document 32). These include diabetic retinopathy, diabetic nephropathy, and diabetic neuropathy. Diabetic retinopathy (DR) is a microvascular complication characterized by abnormal angiogenesis and is the most common cause of irreversible blindness. Diabetic nephropathy develops when a hyperglycemic state caused by diabetes continues and damages the small blood vessels that run through the kidneys. If the condition worsens, it may progress to renal failure and require hemodialysis. Diabetic neuropathy is caused by prolonged hyperglycemia, which not only damages the blood vessels around the nerves, but also changes the properties of the nerves themselves, causing various disorders in the function of the nerves. Dyslipidemia includes abnormalities in the blood levels of LDL cholesterol (so-called bad cholesterol), HDL cholesterol (so-called good cholesterol), and triglycerides (neutral fats), all of which have been reported to be associated with the promotion of arteriosclerosis. In atherosclerosis, macrophages in the vascular endothelium phagocytose oxidized LDL and change into fat-accumulating macrophages called foam cells (Non-Patent Document 33), forming lipid cores that become the centers of arteriosclerotic lesions (plaques), narrowing the lumen of blood vessels. Abnormal accumulation of fat in the liver results in fatty liver. Nonalcoholic fatty liver disease (NAFLD) is a general term for fatty liver that is not caused by alcohol or viruses, and develops as a phenotype in the liver of lifestyle-related diseases such as obesity, diabetes, and metabolic syndrome. Even people who do not drink much alcohol can develop liver disease like those with alcoholic liver disease. Furthermore, 20 to 30% of these cases progress to nonalcoholic steatohepatitis (NASH), which is accompanied by inflammation and fibrosis and has the risk of progressing to cirrhosis or liver cancer. Research is being conducted on macrophage subsets involved in these progression processes (Non-Patent Document 34). <Metabolic diseases and gpNMB> There is a paper reporting that blood gpNMB is a biomarker that correlates with disease in diabetes and diabetic complications (Non-Patent Document 35). It is important to improve insulin resistance in diabetes, and it has been reported that in high-fat diet-fed diabetic model mice, soluble gpNMB produced in the liver enhances lipid synthesis in white adipocytes, and administration of anti-gpNMB polyclonal antibodies improved obesity and insulin resistance (Non-Patent Document 36). Furthermore, in human retinal microvascular endothelial cells (HRMEC), high glucose treatment increased gpNMB and integrin β1, suggesting that gpNMB functions as an angiogenic factor via integrin β1 / VEGFA. Knockdown of gpNMB using shRNA-expressing lentivirus inhibited cell viability, migration, and tube formation in HRMEC, suggesting that gpNMB is involved in the pathological progression of diabetic retinopathy (Non-Patent Document 37). It has been reported that macrophages involved in arteriosclerosis in ApoE-KO mice loaded with a high-fat diet are gpNMB positive (Non-Patent Document 38). It has also been reported that gpNMB is expressed in lipid-laden macrophages, known as foam cells, which are found in atherosclerosis (Non-Patent Document 39). <Circulatory diseases> Cardiovascular disease is a condition in which the heart and blood vessels, the organs that circulate blood throughout the body, stop functioning normally. It is classified into high blood pressure, heart disease (ischemic heart disease such as acute myocardial infarction and heart failure), cerebrovascular disease (cerebral infarction, cerebral hemorrhage, subarachnoid hemorrhage), aneurysm, etc. In cardiac disease, the infiltration of inflammatory cells such as monocytes and lymphocytes increases after myocardial infarction, inducing chronic inflammation, myocardial remodeling, and leading to cardiac failure. It has been reported that controlling the infiltration of inflammatory cells, the increased expression of inflammatory cytokines, and cardiac macrophages is important for suppressing progression (Non-Patent Document 40). Research has also been reported that analyzes common macrophage subsets related to cardiac disease (Non-Patent Document 41). <Cardiovascular disease and gpNMB> The involvement of macrophages in myocardial remodeling after myocardial infarction has been suggested, and expression of gpNMB in macrophages has been reported (Non-Patent Document 42). <Lysosomal stress-related diseases> Lysosomes become dysfunctional when subjected to various stresses, and toxic proteins accumulate in the body, inducing various diseases. Among these, lysosomal diseases are genetic diseases in which mucopolysaccharides and lipids accumulate in lysosomes due to a genetic deficiency or reduced activity of degradative enzymes in lysosomes, causing the lysosomes and cells to malfunction and produce symptoms. Examples of lysosomal diseases include Gaucher disease, Pompe disease, and Niemann-Pick disease types A, B, and C. <Lysosomal stress-related diseases and gpNMB> gpNMB is an important protein in the breakdown of proteins and lipids in lysosomes, and its expression increases when substances that need to be broken down accumulate and lysosomal stress occurs. Therefore, it is an indicator of cells that have experienced excessive lysosomal stress. Furthermore, high expression is observed in dysfunctional senescent cells. It has been reported that lipid-accumulating gpNMB-high expressing cells are observed in lysosomal diseases such as Gaucher disease and Niemann-Pick disease. In Gaucher disease, lipid-accumulating macrophages called Gaucher cells are observed, and in Niemann-Pick disease types A and B (acid sphingomyelinase deficiency (ASMD)), sphingomyelin-accumulating macrophages accumulate in the spleen and liver (Non-Patent Document 43). <Neuropathic pain-related disorders> Neuropathic pain is pain caused by direct damage to the brain or nerves (such as after stroke, spinal cord injury, surgery, or nerve compression due to cancer infiltration), and is difficult to treat as antipyretics and analgesics are ineffective, so there is a high possibility of suffering from the disease chronically, and a fundamental treatment is desired. The pain of fibromyalgia is classified as neuropathic pain, and it is thought that the pain is caused by inflammation of the nerves in the brain due to some cause. <Neuropathic pain-related disorders and gpNMB> It has been reported that pain was alleviated in a neuropathic pain model rat by injecting siRNA that suppresses the expression of gpNMB into the subarachnoid space (Non-Patent Document 97). <gpNMB> Glycoprotein nonmetastatic melanoma protein B (gpNMB) (also known as osteoactivin, DC-HIL, non-patent literature 44) is a single-pass transmembrane glycoprotein with 12 glycosylation sites in humans. It is usually expressed in intracellular organelles (endoplasmic reticulum, lysosomes, Golgi apparatus, melanosomes, etc.) (non-patent literature 45). However, it has been reported that it is also expressed on the cell membrane when overexpressed (non-patent literature 46). It has also been reported that gpNMB is expressed in cancer cells (non-patent literature 47), and it has been reported that the kringle-like domain (KLD) is important for cell proliferation and that the intracellular ITIM motif induces signals (non-patent literature 48). Furthermore, gpNMB has a region (hereinafter referred to as PMEL-CAF-like domain) that is homologous to the CAF (Core Amyloid Fragment) region of PMEL (Premelanosome Protein) family protein (Non-Patent Document 49) and a PKD (Polycystic Kidney Disease homology) domain. The PKD domain is a domain that forms a β-sandwich structure by folding a β-sheet consisting of three strands and a β-sheet consisting of four strands. It was named the PKD domain because it is a characteristic structure of polycystin-1, the causative gene of polycystic kidney disease (Non-Patent Document 50). As molecules with which gpNMB interacts, syndecan-4 (SD4, SDC4), CD44, integrin, Na+ / K+-ATPase, EGFR, etc. have been reported (Non-Patent Document 98). It has been reported that SD4 interacts with the PKD domain of gpNMB, and gpNMB controls the activity of T cells via SD4 on T cells. CD44 is expressed in mesenchymal stem cells, osteoclasts, astrocytes (star cells), adipocytes, etc., and it has been reported that gpNMB interacts with CD44 to control cell proliferation, adhesion, migration, and activity. In addition, gpNMB has an RGD sequence on the N-terminus side and interacts with integrin, which is an adhesion molecule, to control the migration and adhesion of various cells, and soluble gpNMB also modifies various physiological functions and pathological conditions by binding to cells via the RGD sequence. It has also been reported that gpNMB interacts with EGFR at the intracellular domain to control cell proliferation. It has also been reported that gpNMB interacts with the α subunit of Na+ / K+-ATPase and exerts a cytoprotective effect. gpNMB is important for the function of phagosomes and lysosomes (Non-Patent Document 51), and it has been reported that lysosomal function is reduced in gpNMB-deficient mice (Non-Patent Document 52). It has also been reported that mice lacking gpNMB exhibit iris abnormalities and glaucoma (Non-Patent Document 53), and that humans lacking gpNMB develop cutaneous amyloidosis (Non-Patent Document 54). Recent GWAS (genome-wide association studies) analyses have reported that gpNMB is a risk gene for Parkinson's disease (Non-Patent Document 55), and its involvement in the transmission of α-synuclein, a causative agent of Parkinson's disease, has also been suggested (Non-Patent Document 56). On the other hand, it has been reported that the deficiency of gpNMB does not affect synuclein-related pathology (Non-Patent Document 57). It is known that gpNMB is cleaved by membrane proteases such as ADAM10 and released as soluble gpNMB (Non-Patent Document 58). Soluble gpNMB has been reported to be involved in various physiological and pharmacological actions, such as cell protection (Non-Patent Document 59), neuroprotection (Non-Patent Document 60), inflammation (Non-Patent Document 45, Non-Patent Document 61, Non-Patent Document 62), and cell proliferation (Non-Patent Document 63). It has also been reported that gpNMB plays a protective role against metabolic disorders induced by obesity (Non-Patent Document 64). It has also been reported that transgenic mice overexpressing soluble gpNMB (extracellular domain gpNMB) showed improved neurological function (Non-Patent Document 65), and that the cognitive function of Alzheimer's disease model mice (APP / PS1) was improved when autophagy was enhanced by expressing gpNMB using a lentivirus vector (Non-Patent Document 66). On the other hand, it has been reported that administration of mouse gpNMB-specific vaccine peptides having a partial amino acid sequence of mouse gpNMB reduces aged vascular endothelial cells and fibroblasts, improves insulin resistance and arteriosclerosis in high-fat diet model mice, and extends the survival time of accelerated aging mice. It has also been reported that antibody-dependent cellular cytotoxicity (ADCC) activity is important in this regard, and a partial peptide sequence of gpNMB effective for removing senescent cells has been disclosed (Patent Document 1, Non-Patent Document 67). It has also been reported that administration of polyclonal antibodies against mouse gpNMB in high-fat diet model mice inhibits soluble gpNMB produced in the liver, thereby improving obesity and insulin resistance (Non-Patent Document 68). Soluble gpNMB has also been studied extensively as a biomarker, and it has been reported that the concentration of gpNMB in blood correlates with the progression of diabetes-related diseases (Non-Patent Document 35). Regarding the soluble gpNMB concentration in cerebrospinal fluid, there is a report on its correlation with Parkinson's disease (Non-Patent Document 69). It has also been reported to be related to ALS (Non-Patent Document 70). It has also been reported as a biomarker for cerebral adrenoleukodystrophy (Non-Patent Document 71). On the other hand, regarding its relationship with Alzheimer's disease, there is a report that its concentration is elevated in patients with Alzheimer's disease (Non-Patent Document 72), while there is also a report that there is no relationship (Non-Patent Document 73). <Anti-gpNMB antibody> As an anti-gpNMB antibody, Glembatumumab (Patent Document 2), an anti-human gpNMB specific human antibody, is known. Glembatumumab Vedotin (Non-Patent Document 74), a conjugate of Glembatumumab and an anticancer drug, progressed to phase 2 trials as a candidate cancer treatment drug, but development was discontinued. In addition, attempts have been made to use this antibody for diagnostic imaging (Non-Patent Document 75). Another anti-gpNMB antibody that binds to gpNMB expressed on the surface of cancer cells and treats cancer with an immunotoxin has also been disclosed (Patent Document 3). Furthermore, there is a report on the acquisition of another anti-human gpNMB specific antibody, and its application to the diagnosis and treatment of human-derived cancer cells is described (Non-Patent Document 76). In addition, an anti-rat gpNMB specific antibody specific to activated rat microglia has also been reported (Non-Patent Document 77). It has also been reported that anti-mouse DC-HIL specific antibodies deliver signals into cells (Non-Patent Document 78). <gpNMB expressing cells> Since gpNMB is highly expressed in several cancer tissues (breast cancer (Non-Patent Document 79), lung cancer (Non-Patent Document 80), hepatocellular carcinoma (Non-Patent Document 81), glioblastoma multiforme (Non-Patent Document 82), mesothelioma (Non-Patent Document 83), etc.), clinical development of ADCs (antibody-drug conjugates) that target gpNMB and deliver anticancer drugs via anti-gpNMB antibodies has progressed to phase II clinical trials (Non-Patent Document 74) in several refractory cancer types. In addition, it has been reported that gpNMB is highly expressed in cancers with poor prognosis (Non-Patent Document 84), in cancer stem cells (Non-Patent Document 85), and in infiltrating macrophages and microglia, myeloid-derived suppressor cells (MDSCs), dendritic cells (DCs), and other cells that form the cancer microenvironment (Non-Patent Document 86). Furthermore, it has been reported that the activity of T cells is suppressed by interaction between syndecan-4 (SD4, SDC4) on T cells and gpNMB-expressing cells (infiltrating macrophages and microglia that form the cancer microenvironment, myeloid-derived suppressor cells (MDSCs), dendritic cells (DCs), etc.) (Non-Patent Document 87). gpNMB has also been reported as a marker for senescent cells, and it has been reported that administration of a partial peptide of gpNMB to a senescence-accelerated mouse model removed gpNMB-expressing senescent vascular endothelial cells and gpNMB-expressing senescent fibroblasts, improving arteriosclerosis and diabetes (Non-Patent Document 71). Furthermore, gpNMB expression has been observed in white adipose tissue macrophages (adipose tissue macrophages with crown-like structures) in obese patients (Non-Patent Document 88). It has been reported that gpNMB is expressed in a subset of macrophages (scar-associated macrophages: SAMs), which are thought to induce fibrosis in liver and lung fibrosis (Non-Patent Document 27). It has been reported that macrophages involved in arteriosclerosis in ApoE-KO mice loaded with a high-fat diet are gpNMB positive (Non-Patent Document 38). It has also been reported that gpNMB is expressed in lipid-laden macrophages, known as foam cells, found in atherosclerosis (Non-Patent Document 39). It has also been reported that similar lipid-laden gpNMB-high expressing cells are observed in lysosomal diseases such as Gaucher disease and Niemann-Pick disease. In Gaucher disease, macrophages that have accumulated lipids, known as Gaucher cells, are observed, and in Niemann-Pick disease types A and B (acid sphingomyelinase deficiency (ASMD)), sphingomyelin-accumulating macrophages accumulate in the spleen and liver (Non-Patent Document 43). 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[0014] :5778-5787Gabriel et al., Diabetes, 2014, 63:3310-3323Chrystal et al., Molecules, 2021, 26:3529Alexander et al., Pigment Cell Melanoma Res. 2013, 26[4]:470-486Strohl et al., Current Opinion in Biotechnology 2009, 20, pp685-691.Lee et al., Nat Commun. 2019 Nov 6;10(1), 5031.Kouhi et al., Int. J. Mol. Sci. 2019, 20, 3108C. Spiess et al., Molecular Immunology 2015, Vol.67, pp95-106.Chocarro et al., Biomedicines 2022, 10:3035.Hendrickx et al., Front Immunol. 2017, 8:1810Hou et al., J Mol Neurosci, 2015, 55:533-540Tsou et al., The FASEB Journal., (2020), 34:8810-8823. Conventionally, attempts have been made to develop means for removing various cells (properly referred to as "disease-related cells") that induce or accelerate the progression of various diseases. However, reports of means for removing such disease-related cells are extremely limited so far. In particular, the development of a means for specifically removing highly malignant disease-related cells that are the root cause of disease induction has not been achieved so far. The present invention has been made in view of the above problems. That is, one of the objects of the present invention is to provide a novel means capable of effectively removing various disease-related cells. The present inventors conducted extensive research to develop a means capable of specifically removing highly malignant disease-related cells, and as a result focused on gpNMB (glycoprotein nonmetastatic melanoma protein B) as an antigen common to disease-related cells involved in various diseases. Based on this, through extensive research using various experimental means and methods under various restrictive conditions, the inventors succeeded in obtaining a novel anti-gpNMB antibody that binds to a new epitope on gpNMB that is different from that of conventionally known antibodies, thereby completing the present invention. That is, the present invention relates to the following. [Item 1] A pharmaceutical composition for removing disease-related cells, comprising: A pharmaceutical composition comprising an anti-gpNMB antibody or a fragment thereof or a derivative thereof, which specifically binds to at least one region spanning from V78 to the PKD domain of human gpNMB (glycoprotein nonmetastatic melanoma protein B) having the amino acid sequence of SEQ ID NO: 209. [Item 2] The pharmaceutical composition according to Item 1, wherein the anti-gpNMB antibody specifically binds to a region including amino acid residues D287 and / or H301 of human gpNMB having the amino acid sequence of SEQ ID NO:209. [Item 3] The pharmaceutical composition according to Item 1 or 2, wherein the anti-gpNMB antibody specifically binds to a region including the amino acid residues R214 and / or R215 of human gpNMB having the amino acid sequence of SEQ ID NO: 209. [Item 4] The pharmaceutical composition according to Item 2 or 3, wherein the anti-gpNMB antibody specifically binds to one or more of the following regions of human gpNMB having the amino acid sequence of SEQ ID NO: 209: a region including amino acid residues K257 and / or D258, a region including amino acid residues H268 and / or D269, a region including amino acid residue K282, a region including amino acid residue K316, a region including amino acid residue K186, and a region including amino acid residues H216 and / or R218. [Item 5] The pharmaceutical composition described in Item 1, wherein the anti-gpNMB antibody specifically binds to at least one site in the region spanning V78 to S92 of human gpNMB having the amino acid sequence of SEQ ID NO:209. [Item 6] The pharmaceutical composition according to any one of Items 1 to 5, wherein the anti-gpNMB antibody specifically binds to at least one site in the region spanning from V78 to the PKD domain of mouse gpNMB having the amino acid sequence of SEQ ID NO: 211. [Item 7] The pharmaceutical composition according to any one of Items 1 to 6, wherein the anti-gpNMB antibody is a monoclonal antibody, a fragment thereof, or a derivative thereof. [Item 8] The anti-gpNMB antibody comprises at least a heavy chain variable region, and the heavy chain variable region comprises: (1) As CDR-H1, an amino acid sequence of SEQ ID NO: 1, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence of SEQ ID NO: 1 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 1; As CDR-H2, an amino acid sequence of SEQ ID NO: 3, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence of SEQ ID NO: 3 have been substituted, deleted or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 3, and As CDR-H3, an amino acid sequence of SEQ ID NO:5, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence of SEQ ID NO:5 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 75.0% or more, 83.3% or more, or 91.6% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO:5, or (2) As CDR-H1, an amino acid sequence of SEQ ID NO: 17, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence of SEQ ID NO: 17 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 17; As CDR-H2, an amino acid sequence of SEQ ID NO: 19, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence of SEQ ID NO: 19 have been substituted, deleted or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 19, and As CDR-H3, an amino acid sequence of SEQ ID NO:21, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence of SEQ ID NO:21 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 66.6% or more, 73.3% or more, 80.0% or more, 86.6% or more, or 93.3% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO:21, or (3) As CDR-H1, an amino acid sequence set forth in SEQ ID NO: 33, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO: 33 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 33; As CDR-H2, an amino acid sequence of SEQ ID NO: 35, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence of SEQ ID NO: 35 have been substituted, deleted or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 35, and As CDR-H3, an amino acid sequence of SEQ ID NO: 37, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence of SEQ ID NO: 37 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 66.6% or more, 73.3% or more, 80.0% or more, 86.6% or more, or 93.3% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 37, or (4) As CDR-H1, an amino acid sequence set forth in SEQ ID NO: 49, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO: 49 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 49; As CDR-H2, an amino acid sequence of SEQ ID NO:51, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence of SEQ ID NO:51 have been substituted, deleted or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO:51, and As CDR-H3, an amino acid sequence of SEQ ID NO:53, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence of SEQ ID NO:53 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 68.7% or more, 75.0% or more, 81.2% or more, 87.5% or more, or 93.7% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO:53, or (5) As CDR-H1, an amino acid sequence set forth in SEQ ID NO: 65, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO: 65 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 65; As CDR-H2, an amino acid sequence of SEQ ID NO:67, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence of SEQ ID NO:67 have been substituted, deleted or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO:67, and As CDR-H3, an amino acid sequence of SEQ ID NO:69, or an amino acid sequence in which one, two, three, four, or five amino acid residues in the amino acid sequence of SEQ ID NO:69 have been substituted, deleted, or inserted, or an amino acid sequence having 64.2% or more, 71.4% or more, 78.5% or more, 85.7% or more, or 92.8% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO:69, or (6) As CDR-H1, an amino acid sequence of SEQ ID NO: 81, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence of SEQ ID NO: 81 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 81; As CDR-H2, an amino acid sequence of SEQ ID NO: 83, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence of SEQ ID NO: 83 have been substituted, deleted, or inserted, or an amino acid sequence having 71.4% or more or 85.7% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 83, and As CDR-H3, an amino acid sequence of SEQ ID NO: 85, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence of SEQ ID NO: 85 have been substituted, deleted, or inserted, or an amino acid sequence having 63.6% or more, 72.7% or more, 81.8% or more, or 90.9% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 85, or (7) As CDR-H1, an amino acid sequence set forth in SEQ ID NO: 97, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO: 97 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 97; As CDR-H2, an amino acid sequence of SEQ ID NO: 99, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence of SEQ ID NO: 99 have been substituted, deleted or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 99, and As CDR-H3, an amino acid sequence of SEQ ID NO: 101, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence of SEQ ID NO: 101 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more or 80.0% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 101, or (8) As CDR-H1, an amino acid sequence set forth in SEQ ID NO: 113, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 113 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 113; As CDR-H2, an amino acid sequence of SEQ ID NO: 115, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence of SEQ ID NO: 115 have been substituted, deleted, or inserted, or an amino acid sequence having 71.4% or more or 85.7% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 115, and As CDR-H3, an amino acid sequence of SEQ ID NO: 117, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence of SEQ ID NO: 117 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 66.6% or more, 73.3% or more, 80.0% or more, 86.6% or more, or 93.3% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 117, or (9) As CDR-H1, an amino acid sequence set forth in SEQ ID NO: 129, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 129 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 129; As CDR-H2, an amino acid sequence of SEQ ID NO: 131, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence of SEQ ID NO: 131 have been substituted, deleted, or inserted, or an amino acid sequence having 71.4% or more or 85.7% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 131, and As CDR-H3, an amino acid sequence of SEQ ID NO: 133, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence of SEQ ID NO: 133 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 66.6% or more, 73.3% or more, 80.0% or more, 86.6% or more, or 93.3% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 133, or (10) As CDR-H1, an amino acid sequence set forth in SEQ ID NO: 145, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO: 145 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 145; As CDR-H2, an amino acid sequence of SEQ ID NO: 147, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence of SEQ ID NO: 147 have been substituted, deleted or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 147, and As CDR-H3, an amino acid sequence of SEQ ID NO: 149, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence of SEQ ID NO: 149 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 66.6% or more, 73.3% or more, 80.0% or more, 86.6% or more, or 93.3% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 149, or (11) As CDR-H1, an amino acid sequence set forth in SEQ ID NO: 161, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 161 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 161; As CDR-H2, an amino acid sequence of SEQ ID NO: 163, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence of SEQ ID NO: 163 have been substituted, deleted, or inserted, or an amino acid sequence having 71.4% or more or 85.7% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 163, and As CDR-H3, an amino acid sequence of SEQ ID NO: 165, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence of SEQ ID NO: 165 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 66.6% or more, 73.3% or more, 80.0% or more, 86.6% or more, or 93.3% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 165, or (12) As CDR-H1, an amino acid sequence set forth in SEQ ID NO:255, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO:255 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:255; As CDR-H2, an amino acid sequence of SEQ ID NO:257, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence of SEQ ID NO:257 have been substituted, deleted, or inserted, or an amino acid sequence having 71.4% or more or 85.7% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO:257, and As CDR-H3, an amino acid sequence of SEQ ID NO:259, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence of SEQ ID NO:259 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO:259, or (13) As CDR-H1, an amino acid sequence set forth in SEQ ID NO:283, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO:283 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:283; As CDR-H2, an amino acid sequence of SEQ ID NO:285, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence of SEQ ID NO:285 have been substituted, deleted or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO:285; As CDR-H3, an amino acid sequence of SEQ ID NO:287, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence of SEQ ID NO:287 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 66.6% or more, 73.3% or more, 80.0% or more, 86.6% or more, or 93.3% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO:287, or (14) As CDR-H1, an amino acid sequence set forth in SEQ ID NO: 311, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 311 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 311; as CDR-H2, an amino acid sequence of SEQ ID NO:313, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence of SEQ ID NO:313 have been substituted, deleted, or inserted, or an amino acid sequence having 71.4% or more or 85.7% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO:313; As CDR-H3, an amino acid sequence of SEQ ID NO: 315, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence of SEQ ID NO: 315 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 66.6% or more, 73.3% or more, 80.0% or more, 86.6% or more, or 93.3% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 315, or (15) As the CDR grafting region-H1, an amino acid sequence of SEQ ID NO: 271, or an amino acid sequence in which one, two, three, or four amino acid residues other than tyrosine at position 27, asparagine at position 32, and tryptophan at position 33 of the amino acid sequence of SEQ ID NO: 271 have been substituted, deleted, or inserted; as CDR grafting region-H2, an amino acid sequence set forth in SEQ ID NO:273, or an amino acid sequence in which, in the amino acid sequence set forth in SEQ ID NO:273, any one, two, three, four, five, or six amino acid residues other than aspartic acid at position 55, phenylalanine at position 57, threonine at position 58, asparagine at position 59, tyrosine at position 60, and asparagine at position 61 have been substituted, deleted, or inserted; As the CDR grafting region-H3, an amino acid sequence of SEQ ID NO: 275, or an amino acid sequence in which one, two, three, four, five, or six amino acid residues other than arginine at position 98, glycine at position 100, and glycine at position 109 in the amino acid sequence of SEQ ID NO: 275 have been substituted, deleted, or inserted; or (16) As the CDR grafting region-H1, an amino acid sequence set forth in SEQ ID NO: 299, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 299 have been substituted, deleted, or inserted; as CDR grafting region-H2, an amino acid sequence as set forth in SEQ ID NO:301, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues other than aspartic acid at position 52, tryptophan at position 54, aspartic acid at position 58, and proline at position 63 of the amino acid sequence as set forth in SEQ ID NO:301 have been substituted, deleted, or inserted; As the CDR grafting region-H3, an amino acid sequence set forth in SEQ ID NO: 303, or an amino acid sequence in which, in the amino acid sequence set forth in SEQ ID NO: 303, any one, two, three, four, five, or six amino acid residues other than arginine at position 99, threonine at position 100, tyrosine at position 102, tyrosine at position 105, tyrosine at position 107, and methionine at position 110 have been substituted, deleted, or inserted; or (17) As CDR-H1, an amino acid sequence set forth in SEQ ID NO: 177, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 177 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 177; As CDR-H2, an amino acid sequence of SEQ ID NO: 179, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence of SEQ ID NO: 179 have been substituted, deleted or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 179, and As CDR-H3, an amino acid sequence of SEQ ID NO: 181, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence of SEQ ID NO: 181 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 181, or (18) As CDR-H1, an amino acid sequence set forth in SEQ ID NO: 330, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 330 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 330; As CDR-H2, an amino acid sequence of SEQ ID NO: 331, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence of SEQ ID NO: 331 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 331, and As CDR-H3, an amino acid sequence of SEQ ID NO: 332, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence of SEQ ID NO: 332 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 332, or (19) As CDR-H1, an amino acid sequence set forth in SEQ ID NO: 337, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 337 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 337; As CDR-H2, an amino acid sequence of SEQ ID NO: 338, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence of SEQ ID NO: 338 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 338, and As CDR-H3, an amino acid sequence of SEQ ID NO: 339, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence of SEQ ID NO: 339 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 339, or (20) As CDR-H1, an amino acid sequence set forth in SEQ ID NO: 344, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 344 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 344; As CDR-H2, an amino acid sequence of SEQ ID NO: 345, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence of SEQ ID NO: 345 have been substituted, deleted or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 345, and As CDR-H3, an amino acid sequence set forth in SEQ ID NO: 346, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO: 346 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 346, or (21) As the CDR grafting region-H1, an amino acid sequence set forth in SEQ ID NO: 327, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 327 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 327; As the CDR grafting region-H2, an amino acid sequence set forth in SEQ ID NO: 328, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence set forth in SEQ ID NO: 328 have been substituted, deleted, or inserted, or an amino acid sequence having 64.7% or more, 70.5% or more, 76.4% or more, 82.3% or more, 88.2% or more, or 94.1% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 328; As the CDR grafting region-H3, an amino acid sequence set forth in SEQ ID NO: 329, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 329 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 329, or (22) As the CDR grafting region-H1, an amino acid sequence set forth in SEQ ID NO: 334, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 334 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 334; As the CDR grafting region-H2, an amino acid sequence set forth in SEQ ID NO: 335, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence set forth in SEQ ID NO: 335 have been substituted, deleted, or inserted, or an amino acid sequence having 64.7% or more, 70.5% or more, 76.4% or more, 82.3% or more, 88.2% or more, or 94.1% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 335; As the CDR grafting region-H3, an amino acid sequence set forth in SEQ ID NO: 336, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 336 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 336, or (23) As the CDR grafting region-H1, an amino acid sequence set forth in SEQ ID NO: 341, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 341 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 341; As the CDR grafting region-H2, an amino acid sequence set forth in SEQ ID NO: 342, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence set forth in SEQ ID NO: 342 have been substituted, deleted, or inserted, or an amino acid sequence having 64.7% or more, 70.5% or more, 76.4% or more, 82.3% or more, 88.2% or more, or 94.1% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 342; As the CDR grafting region-H3, an amino acid sequence set forth in SEQ ID NO: 343, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 343 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 343. The pharmaceutical composition according to any one of items 1 to 7, comprising: [Item 9] The anti-gpNMB antibody comprises at least a heavy chain variable region, and the heavy chain variable region comprises: (1) an amino acid sequence set forth in SEQ ID NO: 13, or an amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 13, or (2) an amino acid sequence set forth in SEQ ID NO:29, or an amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO:29, or (3) an amino acid sequence set forth in SEQ ID NO: 45, or an amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 45, or (4) an amino acid sequence set forth in SEQ ID NO: 61, or an amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 61, or (5) an amino acid sequence set forth in SEQ ID NO: 77, or an amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 77; or (6) An amino acid sequence set forth in SEQ ID NO: 93, or an amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 93, or (7) An amino acid sequence set forth in SEQ ID NO: 109, or an amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 109, or (8) An amino acid sequence set forth in SEQ ID NO: 125, or an amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 125, or (9) An amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 141, or (10) An amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 157, or an amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 157, or (11) An amino acid sequence set forth in SEQ ID NO: 173, or an amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 173, or (12) An amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 267, or (13) An amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 295, or an amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 295, or (14) An amino acid sequence set forth in SEQ ID NO: 323, or an amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 323, or (17) An amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 189, or (18) An amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 333, or (19) An amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 340, or (20) An amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 347. The pharmaceutical composition according to any one of items 1 to 7, comprising: [Item 10] The pharmaceutical composition according to Item 8 or 9, wherein the heavy chain variable region comprises a framework sequence of any class of human immunoglobulin. [Item 11] The pharmaceutical composition according to any one of Items 8 to 10, wherein the anti-gpNMB antibody further comprises a heavy chain constant region, the heavy chain constant region having an amino acid sequence of a heavy chain constant region of any class of human immunoglobulin. [Item 12] The anti-gpNMB antibody comprises at least a light chain variable region, and the light chain variable region comprises: (1) as CDR-L1, an amino acid sequence as set forth in SEQ ID NO: 7, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 7 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 7; CDR-L2: an amino acid sequence of SEQ ID NO: 9, or an amino acid sequence in which any one amino acid residue in the amino acid sequence of SEQ ID NO: 9 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 9; and As CDR-L3, an amino acid sequence of SEQ ID NO: 11, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence of SEQ ID NO: 11 have been substituted, deleted or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 11, or (2) as CDR-L1, an amino acid sequence set forth in SEQ ID NO:23, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO:23 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more or 80.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:23; CDR-L2: an amino acid sequence of SEQ ID NO:25, or an amino acid sequence in which any one amino acid residue in the amino acid sequence of SEQ ID NO:25 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO:25; and As CDR-L3, an amino acid sequence of SEQ ID NO:27, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence of SEQ ID NO:27 have been substituted, deleted or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO:27, or (3) as CDR-L1, an amino acid sequence set forth in SEQ ID NO: 39, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 39 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more or 80.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 39; CDR-L2: an amino acid sequence of SEQ ID NO: 41, or an amino acid sequence in which any one amino acid residue in the amino acid sequence of SEQ ID NO: 41 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 41; and As CDR-L3, an amino acid sequence of SEQ ID NO: 43, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence of SEQ ID NO: 43 have been substituted, deleted or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 43, or (4) As CDR-L1, an amino acid sequence set forth in SEQ ID NO:55, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO:55 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:55; As CDR-L2, an amino acid sequence of SEQ ID NO:57, or an amino acid sequence in which any one amino acid residue in the amino acid sequence of SEQ ID NO:57 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO:57, and As CDR-L3, an amino acid sequence of SEQ ID NO:59, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence of SEQ ID NO:59 have been substituted, deleted or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO:59, or (5) As CDR-L1, an amino acid sequence set forth in SEQ ID NO: 71, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 71 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more or 80.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 71; CDR-L2, an amino acid sequence of SEQ ID NO: 73, or an amino acid sequence in which any one amino acid residue in the amino acid sequence of SEQ ID NO: 73 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 73; and As CDR-L3, an amino acid sequence of SEQ ID NO: 75, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence of SEQ ID NO: 75 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 75, or (6) As CDR-L1, an amino acid sequence set forth in SEQ ID NO: 87, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 87 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 87; CDR-L2: an amino acid sequence of SEQ ID NO: 89, or an amino acid sequence in which any one amino acid residue in the amino acid sequence of SEQ ID NO: 89 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 89; and As CDR-L3, an amino acid sequence of SEQ ID NO: 91, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence of SEQ ID NO: 91 have been substituted, deleted or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 91, or (7) As CDR-L1, an amino acid sequence set forth in SEQ ID NO: 103, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 103 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 103; As CDR-L2, an amino acid sequence of SEQ ID NO: 105, or an amino acid sequence in which any one amino acid residue in the amino acid sequence of SEQ ID NO: 105 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 105, and As CDR-L3, an amino acid sequence of SEQ ID NO: 107, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence of SEQ ID NO: 107 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 107, or (8) As CDR-L1, an amino acid sequence set forth in SEQ ID NO: 119, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 119 have been substituted, deleted, or inserted, or an amino acid sequence having 63.6% or more, 72.7% or more, 81.8% or more, or 90.9% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 119; As CDR-L2, an amino acid sequence of SEQ ID NO: 121, or an amino acid sequence in which any one amino acid residue in the amino acid sequence of SEQ ID NO: 121 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 121, and As CDR-L3, an amino acid sequence of SEQ ID NO: 123, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence of SEQ ID NO: 123 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 123, or (9) As CDR-L1, an amino acid sequence set forth in SEQ ID NO: 135, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 135 have been substituted, deleted, or inserted, or an amino acid sequence having 63.6% or more, 72.7% or more, 81.8% or more, or 90.9% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 135; As CDR-L2, an amino acid sequence of SEQ ID NO: 137, or an amino acid sequence in which any one amino acid residue in the amino acid sequence of SEQ ID NO: 137 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 137, and As CDR-L3, an amino acid sequence of SEQ ID NO: 139, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence of SEQ ID NO: 139 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 139, or (10) As CDR-L1, an amino acid sequence set forth in SEQ ID NO: 151, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 151 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 151; As CDR-L2, an amino acid sequence of SEQ ID NO: 153, or an amino acid sequence in which any one amino acid residue in the amino acid sequence of SEQ ID NO: 153 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 153, and As CDR-L3, an amino acid sequence of SEQ ID NO: 155, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence of SEQ ID NO: 155 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 155, or (11) As CDR-L1, an amino acid sequence set forth in SEQ ID NO: 167, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 167 have been substituted, deleted, or inserted, or an amino acid sequence having 63.6% or more, 72.7% or more, 81.8% or more, or 90.9% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 167; As CDR-L2, an amino acid sequence of SEQ ID NO: 169, or an amino acid sequence in which any one amino acid residue in the amino acid sequence of SEQ ID NO: 169 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 169, and As CDR-L3, an amino acid sequence of SEQ ID NO: 171, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence of SEQ ID NO: 171 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 171, or (12) As CDR-L1, an amino acid sequence set forth in SEQ ID NO:261, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO:261 have been substituted, deleted, or inserted, or an amino acid sequence having 63.6% or more, 72.7% or more, 81.8% or more, or 90.9% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:261; As CDR-L2, an amino acid sequence of SEQ ID NO:263, or an amino acid sequence in which any one amino acid residue in the amino acid sequence of SEQ ID NO:263 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO:263, and As CDR-L3, an amino acid sequence set forth in SEQ ID NO:265, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO:265 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:265, or (13) As CDR-L1, an amino acid sequence set forth in SEQ ID NO:289, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO:289 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more or 80.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:289; As CDR-L2, an amino acid sequence of SEQ ID NO:291, or an amino acid sequence in which any one amino acid residue in the amino acid sequence of SEQ ID NO:291 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO:291, and As CDR-L3, an amino acid sequence set forth in SEQ ID NO:293, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO:293 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:293, or (14) As CDR-L1, an amino acid sequence set forth in SEQ ID NO: 317, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 317 have been substituted, deleted, or inserted, or an amino acid sequence having 63.6% or more, 72.7% or more, 81.8% or more, or 90.9% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 317; As CDR-L2, an amino acid sequence of SEQ ID NO: 319, or an amino acid sequence in which any one amino acid residue in the amino acid sequence of SEQ ID NO: 319 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 319, and As CDR-L3, an amino acid sequence of SEQ ID NO: 321, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence of SEQ ID NO: 321 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 321, or (15) As the CDR grafting region-L1, the amino acid sequence of SEQ ID NO: 277, or the amino acid sequence of SEQ ID NO: 277 in which any one, two, three, or four amino acid residues other than isoleucine at position 29, tyrosine at position 31, and histidine at position 33 have been substituted, deleted, or inserted; As the CDR grafting region-L2, an amino acid sequence of SEQ ID NO:279 or an amino acid sequence in which one or two amino acid residues other than the 50th threonine in the amino acid sequence of SEQ ID NO:279 have been substituted, deleted or inserted; As the CDR grafting region-L3, an amino acid sequence set forth in SEQ ID NO:281, or an amino acid sequence in which one, two, or three amino acid residues other than histidine at position 88, glutamine at position 89, tryptophan at position 90, serine at position 92, tyrosine at position 93, proline at position 94, and cysteine ​​at position 95 of the amino acid sequence set forth in SEQ ID NO:281 have been substituted, deleted, or inserted; or (16) As the CDR grafting region-L1, an amino acid sequence of SEQ ID NO: 305, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues other than leucine at position 31, tyrosine at position 37, and glutamic acid at position 39 in the amino acid sequence of SEQ ID NO: 305 have been substituted, deleted, or inserted; As a CDR grafting region-L2, an amino acid sequence of SEQ ID NO: 307 or an amino acid sequence of SEQ ID NO: 307 in which one or two amino acid residues other than the lysine at position 55 have been substituted, deleted or inserted; As the CDR grafting region-L3, an amino acid sequence of SEQ ID NO: 309, or an amino acid sequence in which one, two, or three amino acid residues other than phenylalanine at position 94 in the amino acid sequence of SEQ ID NO: 309 have been substituted, deleted, or inserted; or (17) As CDR-L1, an amino acid sequence set forth in SEQ ID NO: 183, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 183 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 183; as CDR-L2, an amino acid sequence of SEQ ID NO: 185, or an amino acid sequence in which any one amino acid residue in the amino acid sequence of SEQ ID NO: 185 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 185; As CDR-L3, an amino acid sequence of SEQ ID NO: 187, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence of SEQ ID NO: 187 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 187, or (18) As CDR-L1, an amino acid sequence set forth in SEQ ID NO: 351, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 351 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 351; as CDR-L2, an amino acid sequence set forth in SEQ ID NO: 352, or an amino acid sequence in which any one amino acid residue in the amino acid sequence set forth in SEQ ID NO: 352 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 352; As CDR-L3, an amino acid sequence set forth in SEQ ID NO: 353, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO: 353 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 353, or (19) As CDR-L1, an amino acid sequence set forth in SEQ ID NO: 358, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 358 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 358; As CDR-L2, an amino acid sequence set forth in SEQ ID NO:359, or an amino acid sequence in which any one amino acid residue in the amino acid sequence set forth in SEQ ID NO:359 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:359; As CDR-L3, an amino acid sequence set forth in SEQ ID NO: 360, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO: 360 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 360, or (20) As CDR-L1, an amino acid sequence set forth in SEQ ID NO: 365, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 365 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 365; As CDR-L2, an amino acid sequence set forth in SEQ ID NO: 366, or an amino acid sequence in which any one amino acid residue in the amino acid sequence set forth in SEQ ID NO: 366 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 366; As CDR-L3, an amino acid sequence set forth in SEQ ID NO: 367, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO: 367 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 367, or (21) As the CDR grafting region-L1, an amino acid sequence set forth in SEQ ID NO: 348, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 348 have been substituted, deleted, or inserted, or an amino acid sequence having 63.6% or more, 72.7% or more, 81.8% or more, or 90.9% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 348; As the CDR grafting region-L2, an amino acid sequence set forth in SEQ ID NO: 349, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 349 have been substituted, deleted, or inserted, or an amino acid sequence having 71.4% or more or 85.7% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 349; As the CDR grafting region-L3, an amino acid sequence set forth in SEQ ID NO: 350, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence set forth in SEQ ID NO: 350 have been substituted, deleted or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 350, or (22) As the CDR grafting region-L1, an amino acid sequence set forth in SEQ ID NO: 355, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 355 have been substituted, deleted, or inserted, or an amino acid sequence having 63.6% or more, 72.7% or more, 81.8% or more, or 90.9% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 355; As the CDR grafting region-L2, an amino acid sequence set forth in SEQ ID NO: 356, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 356 have been substituted, deleted, or inserted, or an amino acid sequence having 71.4% or more or 85.7% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 356; As the CDR grafting region-L3, an amino acid sequence set forth in SEQ ID NO: 357, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO: 357 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 357, or (23) As the CDR grafting region-L1, an amino acid sequence set forth in SEQ ID NO: 362, or an amino acid sequence in which any one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 362 have been substituted, deleted, or inserted, or an amino acid sequence having 63.6% or more, 72.7% or more, 81.8% or more, or 90.9% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 362; As the CDR grafting region-L2, an amino acid sequence set forth in SEQ ID NO: 363, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 363 have been substituted, deleted, or inserted, or an amino acid sequence having 71.4% or more or 85.7% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 363; As the CDR grafting region-L3, an amino acid sequence set forth in SEQ ID NO:364, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO:364 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:364. Item 12. The pharmaceutical composition according to any one of items 1 to 11, comprising the formula: [Item 13] The anti-gpNMB antibody comprises at least a light chain variable region, and the light chain variable region comprises: (1) an amino acid sequence set forth in SEQ ID NO: 15, or an amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 15, or (2) an amino acid sequence set forth in SEQ ID NO: 31, or an amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 31, or (3) an amino acid sequence set forth in SEQ ID NO: 47, or an amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 47, or (4) an amino acid sequence set forth in SEQ ID NO: 63, or an amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 63, or (5) an amino acid sequence set forth in SEQ ID NO: 79, or an amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 79, or (6) An amino acid sequence set forth in SEQ ID NO: 95, or an amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 95, or (7) An amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 111, or an amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 111, or (8) An amino acid sequence set forth in SEQ ID NO: 127, or an amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 127, or (9) An amino acid sequence set forth in SEQ ID NO: 143, or an amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 143, or (10) An amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 159, or (11) An amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 175, or an amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 175, or (12) An amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 269, or (13) An amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 297, or (14) An amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 325, or an amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 325, or (17) An amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 191, or (18) An amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 354, or (19) An amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 361, or (20) An amino acid sequence set forth in SEQ ID NO: 368, or an amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 368. Item 12. The pharmaceutical composition according to any one of items 1 to 11, comprising the formula: [Item 14] The pharmaceutical composition according to Item 12 or 13, wherein the light chain variable region comprises a framework sequence of any class of human immunoglobulin. [Item 15] The pharmaceutical composition according to any one of Items 12 to 14, wherein the anti-gpNMB antibody further comprises a light chain constant region, the light chain constant region having an amino acid sequence of a light chain constant region of any class of human immunoglobulin. [Item 16] The pharmaceutical composition according to any one of items 1 to 15, wherein the anti-gpNMB antibody is a Fab, scFv, diabody, nanobody, VHH, bispecific antibody, or multispecific antibody, or a derivative thereof. [Item 17] A pharmaceutical composition for removing disease-related cells, comprising: A pharmaceutical composition comprising an anti-gpNMB antibody or a fragment thereof or a derivative thereof that competitively binds with the anti-gpNMB antibody or a fragment thereof or a derivative thereof according to any one of Items 1 to 16 for binding to at least one site in the region spanning from V78 to the PKD domain of human gpNMB (glycoprotein nonmetastatic melanoma protein B) having the amino acid sequence of SEQ ID NO: 209. [Item 18] A pharmaceutical composition for removing disease-related cells, comprising: A nucleic acid molecule consisting of a polynucleotide sequence encoding the anti-gpNMB antibody or a fragment thereof or a derivative thereof according to any one of items 1 to 17, and / or a cloning or expression vector comprising at least one of said nucleic acid molecules; and / or A recombinant cell into which the vector has been introduced 13. A pharmaceutical composition comprising: [Item 19] The pharmaceutical composition according to any one of Items 1 to 18, wherein the disease-related cells are selected from senescent cells, cancer-associated cells, and phagocytes. [Item 20] The pharmaceutical composition according to Item 19, wherein the cancer-related cells are selected from cancer cells, cancer stem cells, cancer progenitor cells, and cancer infiltrating cells. [Item 21] The pharmaceutical composition according to any one of Items 1 to 20, wherein the disease is selected from obesity, diabetes, arteriosclerosis, fibrosis, cancer, metabolic disease, circulatory system disease, lysosomal stress-related disease (e.g., lysosomal storage disease, etc.), autoimmune disease (e.g., multiple sclerosis, etc.), neuropathic pain, fibromyalgia, and glioblastoma. [Item 22] The pharmaceutical composition according to any one of Items 1 to 21, for treating or preventing a disease by removing disease-related cells. [Item 23] An anti-gpNMB antibody, a fragment thereof, or a derivative thereof, which specifically binds to at least one site in the region spanning V78 to S92 of human gpNMB (glycoprotein nonmetastatic melanoma protein B) having the amino acid sequence of SEQ ID NO: 209. [Item 24] The anti-gpNMB antibody or a fragment thereof or a derivative thereof according to Item 23, which also specifically binds to a region including the amino acid residue K186 of human gpNMB having the amino acid sequence of SEQ ID NO:209. [Item 25] The anti-gpNMB antibody or a fragment thereof or a derivative thereof described in Item 23 or 24, wherein the anti-gpNMB antibody specifically binds to at least one site in the region spanning V78 to S92 of mouse gpNMB having the amino acid sequence of SEQ ID NO: 211. [Item 26] The anti-gpNMB antibody or a fragment thereof or a derivative thereof according to any one of Items 23 to 25, which is a monoclonal antibody or a fragment thereof or a derivative thereof. [Item 27] ​​At least a heavy chain variable region, wherein the heavy chain variable region comprises: (17) As CDR-H1, an amino acid sequence set forth in SEQ ID NO: 177, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 177 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 177; As CDR-H2, an amino acid sequence of SEQ ID NO: 179, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence of SEQ ID NO: 179 have been substituted, deleted or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 179, and As CDR-H3, an amino acid sequence of SEQ ID NO: 181, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence of SEQ ID NO: 181 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 181, or (18) As CDR-H1, an amino acid sequence set forth in SEQ ID NO: 330, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 330 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 330; As CDR-H2, an amino acid sequence of SEQ ID NO: 331, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence of SEQ ID NO: 331 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 331, and As CDR-H3, an amino acid sequence of SEQ ID NO: 332, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence of SEQ ID NO: 332 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 332, or (19) As CDR-H1, an amino acid sequence set forth in SEQ ID NO: 337, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 337 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 337; As CDR-H2, an amino acid sequence of SEQ ID NO: 338, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence of SEQ ID NO: 338 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 338, and As CDR-H3, an amino acid sequence of SEQ ID NO: 339, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence of SEQ ID NO: 339 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 339, or (20) As CDR-H1, an amino acid sequence set forth in SEQ ID NO: 344, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 344 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 344; As CDR-H2, an amino acid sequence of SEQ ID NO: 345, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence of SEQ ID NO: 345 have been substituted, deleted or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 345, and As CDR-H3, an amino acid sequence set forth in SEQ ID NO: 346, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO: 346 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 346, or (21) As the CDR grafting region-H1, an amino acid sequence set forth in SEQ ID NO: 327, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 327 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 327; As the CDR grafting region-H2, an amino acid sequence set forth in SEQ ID NO: 328, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence set forth in SEQ ID NO: 328 have been substituted, deleted, or inserted, or an amino acid sequence having 64.7% or more, 70.5% or more, 76.4% or more, 82.3% or more, 88.2% or more, or 94.1% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 328; As the CDR grafting region-H3, an amino acid sequence set forth in SEQ ID NO: 329, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 329 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 329, or (22) As the CDR grafting region-H1, an amino acid sequence set forth in SEQ ID NO: 334, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 334 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 334; As the CDR grafting region-H2, an amino acid sequence set forth in SEQ ID NO: 335, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence set forth in SEQ ID NO: 335 have been substituted, deleted, or inserted, or an amino acid sequence having 64.7% or more, 70.5% or more, 76.4% or more, 82.3% or more, 88.2% or more, or 94.1% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 335; As the CDR grafting region-H3, an amino acid sequence set forth in SEQ ID NO: 336, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 336 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 336, or (23) As the CDR grafting region-H1, an amino acid sequence set forth in SEQ ID NO: 341, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 341 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 341; As the CDR grafting region-H2, an amino acid sequence set forth in SEQ ID NO: 342, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence set forth in SEQ ID NO: 342 have been substituted, deleted, or inserted, or an amino acid sequence having 64.7% or more, 70.5% or more, 76.4% or more, 82.3% or more, 88.2% or more, or 94.1% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 342; As the CDR grafting region-H3, an amino acid sequence set forth in SEQ ID NO: 343, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 343 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 343. Item 27. The anti-gpNMB antibody, or a fragment thereof, or a derivative thereof, according to Item 26, having the following structure: [Item 28] At least a heavy chain variable region, wherein the heavy chain variable region comprises: (17) An amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 189, or (18) An amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 333, or (19) An amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 340, or (20) An amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 347. Item 28. The anti-gpNMB antibody or a fragment thereof or a derivative thereof according to Item 26 or 27, [Item 29] The anti-gpNMB antibody or a fragment thereof or a derivative thereof according to any one of Items 25 to 28, wherein the heavy chain variable region comprises a framework sequence of any class of human immunoglobulin as a framework sequence. [Item 30] An anti-gpNMB antibody or a fragment thereof or a derivative thereof described in any one of Items 25 to 29, further comprising a heavy chain constant region, the heavy chain constant region having an amino acid sequence of a heavy chain constant region of any class of human immunoglobulin. [Item 31] At least a light chain variable region, wherein the light chain variable region comprises: (17) As CDR-L1, an amino acid sequence set forth in SEQ ID NO: 183, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 183 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 183; as CDR-L2, an amino acid sequence of SEQ ID NO: 185, or an amino acid sequence in which any one amino acid residue in the amino acid sequence of SEQ ID NO: 185 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 185; As CDR-L3, an amino acid sequence of SEQ ID NO: 187, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence of SEQ ID NO: 187 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 187, or (18) As CDR-L1, an amino acid sequence set forth in SEQ ID NO: 351, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 351 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 351; as CDR-L2, an amino acid sequence set forth in SEQ ID NO: 352, or an amino acid sequence in which any one amino acid residue in the amino acid sequence set forth in SEQ ID NO: 352 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 352; As CDR-L3, an amino acid sequence set forth in SEQ ID NO: 353, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO: 353 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 353, or (19) As CDR-L1, an amino acid sequence set forth in SEQ ID NO: 358, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 358 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 358; As CDR-L2, an amino acid sequence set forth in SEQ ID NO:359, or an amino acid sequence in which any one amino acid residue in the amino acid sequence set forth in SEQ ID NO:359 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:359; As CDR-L3, an amino acid sequence set forth in SEQ ID NO: 360, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO: 360 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 360, or (20) As CDR-L1, an amino acid sequence set forth in SEQ ID NO: 365, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 365 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 365; As CDR-L2, an amino acid sequence set forth in SEQ ID NO: 366, or an amino acid sequence in which any one amino acid residue in the amino acid sequence set forth in SEQ ID NO: 366 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 366; As CDR-L3, an amino acid sequence set forth in SEQ ID NO: 367, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO: 367 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 367, or (21) As the CDR grafting region-L1, an amino acid sequence set forth in SEQ ID NO: 348, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 348 have been substituted, deleted, or inserted, or an amino acid sequence having 63.6% or more, 72.7% or more, 81.8% or more, or 90.9% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 348; As the CDR grafting region-L2, an amino acid sequence set forth in SEQ ID NO: 349, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 349 have been substituted, deleted, or inserted, or an amino acid sequence having 71.4% or more or 85.7% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 349; As the CDR grafting region-L3, an amino acid sequence set forth in SEQ ID NO: 350, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence set forth in SEQ ID NO: 350 have been substituted, deleted or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 350, or (22) As the CDR grafting region-L1, an amino acid sequence set forth in SEQ ID NO: 355, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 355 have been substituted, deleted, or inserted, or an amino acid sequence having 63.6% or more, 72.7% or more, 81.8% or more, or 90.9% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 355; As the CDR grafting region-L2, an amino acid sequence set forth in SEQ ID NO: 356, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 356 have been substituted, deleted, or inserted, or an amino acid sequence having 71.4% or more or 85.7% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 356; As the CDR grafting region-L3, an amino acid sequence set forth in SEQ ID NO: 357, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO: 357 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 357, or (23) As the CDR grafting region-L1, an amino acid sequence set forth in SEQ ID NO: 362, or an amino acid sequence in which any one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 362 have been substituted, deleted, or inserted, or an amino acid sequence having 63.6% or more, 72.7% or more, 81.8% or more, or 90.9% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 362; As the CDR grafting region-L2, an amino acid sequence set forth in SEQ ID NO: 363, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 363 have been substituted, deleted, or inserted, or an amino acid sequence having 71.4% or more or 85.7% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 363; As the CDR grafting region-L3, an amino acid sequence set forth in SEQ ID NO:364, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO:364 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:364. Item 31. The anti-gpNMB antibody or a fragment thereof or a derivative thereof according to any one of Items 25 to 30, having the formula: [Item 32] At least a light chain variable region, wherein the light chain variable region comprises: (17) An amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 191, or (18) An amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 354, or (19) An amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 361, or (20) An amino acid sequence set forth in SEQ ID NO: 368, or an amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 368. Item 32. The anti-gpNMB antibody or a fragment thereof or a derivative thereof according to any one of Items 25 to 31, having the formula: [Item 33] The anti-gpNMB antibody or a fragment thereof or a derivative thereof described in Item 31 or 32, wherein the light chain variable region comprises a framework sequence of any class of human immunoglobulin as a framework sequence. [Item 34] An anti-gpNMB antibody or a fragment thereof or a derivative thereof described in any one of Items 25 to 33, further comprising a light chain constant region, the light chain constant region having an amino acid sequence of a light chain constant region of any class of human immunoglobulin. [Item 35] The anti-gpNMB antibody or a fragment thereof or a derivative thereof according to any one of Items 25 to 34, which is a Fab, scFv, diabody, nanobody, VHH, bispecific antibody, or multispecific antibody, or a derivative thereof. According to the present invention, a new means is provided that can effectively remove various gpNMB-positive disease-related cells by utilizing a novel anti-gpNMB antibody that binds to a specific epitope on gpNMB. FIG. 1 is a diagram showing an alignment of the amino acid sequences of human gpNMB (isotype a) and mouse gpNMB. In the diagram, the region from valine at amino acid residue 78 (V78) to the PKD domain is shown surrounded by a dashed line. As an example of the PKD domain, the region from amino acid residues 256 to 319 is shown surrounded by a dotted line. As an example of the PMEL-CAF-like domain, the region from amino acid residues 172 to 246 is shown surrounded by a solid line. FIG. 2 is a graph showing the results of evaluation of the ability of anti-gpNMB antibody clones to eliminate cells expressing human gpNMB. FIG. 3 is a graph showing the results of evaluation of the ability of anti-gpNMB antibody clones to eliminate cells expressing mouse gpNMB. FIG. 4 is a diagram showing the alignment of humanized mutant sequences hGPN06-1_VH1 to VH5 to mouse GPN06-1_VH. Figure 5 shows the alignment of humanized variants hGPN06-1_VL1-VL5 to mouse GPN06-1_VL. Figure 6 shows the alignment of humanized variants hGPN18-2_VH1-VH5 to mouse GPN18-2_VH. Figure 7 shows the alignment of humanized variants hGPN18-2_VL1-VL5 to mouse GPN18-2_VL. Figure 8 shows the alignment of humanized anti-gpNMB antibody variants hGPN18-5_VH1-VH3 to mouse GPN18-5_VH0. Figure 9 shows the alignment of humanized anti-gpNMB antibody variants hGPN18-5_VL1-VL3 to mouse GPN18-5_VL0. Fig. 10 is a graph showing the results of evaluation of the pain-improving effect of the anti-gpNMB antibody clone using a neuropathic pain model mouse. Fig. 11 is a diagram showing a schematic diagram of an administration schedule of the anti-gpNMB antibody clone to an obese model mouse. Fig. 12 is a graph showing the results of evaluation of the amount of gpNMB-positive SA-β-Gal-positive macrophages in the epididymal fat of the anti-gpNMB antibody clone using an obese model mouse. Fig. 13 is a graph showing the results of evaluation of the amount of TNF-α gene expression in the epididymal fat of the anti-gpNMB antibody clone using an obese model mouse. The present invention will be described below based on specific embodiments, but the present invention is not limited to these embodiments. All documents cited in this specification, including patent publications, patent application publications, and non-patent publications, are incorporated herein by reference in their entirety for all purposes. [overview] Conventionally, attempts have been made to develop means for removing various cells (disease-related cells) that induce or accelerate the progression of various diseases. Examples include senescent cell removal drugs that target senescent cells, anticancer drugs that target specific cancer cells (cancer targeted drugs), anticancer drugs that target the removal of cancer-infiltrating macrophages, and medicines that target nonspecific macrophages or microglia. However, reports on means for removing such disease-related cells have been extremely limited so far. In particular, no means has been developed to specifically remove highly malignant disease-related cells that are the root cause of disease induction. Examples of such highly malignant disease-related cells include senescent infiltrating cells or resident senescent cells that have a significant effect on surrounding cells and tissues to form or progress pathologies, or extremely nasty cancer cells or cancer stem cells. The present inventors have conducted extensive research to develop a means for efficiently removing disease-related cells, and as a result have focused on gpNMB (glycoprotein nonmetastatic melanoma protein B) as an antigen common to cells involved in various highly malignant diseases. Cells highly expressing gpNMB (gpNMB-positive cells) are observed in various diseases, and therefore may be significantly involved in the pathogenesis and progression of the disease. Specific examples of disease-related cells that may highly express gpNMB include senescent cells, cancer-related cells (e.g., cancer cells, cancer precursor cells, cancer-infiltrating cells (e.g., cancer-infiltrating immune cells, etc.), tissue-infiltrating phagocytes, chronically or abnormally activated (resident) phagocytes, and other phagocytes (e.g., macrophages, microglia, etc.). On the other hand, while gpNMB has been suggested to be involved in various diseases, it is unclear whether it acts to protect against various diseases or to aggravate them, and whether it is suitable as a therapeutic target. In other words, it was predicted that soluble gpNMB secreted from various cells plays a protective role in various pathological conditions. Therefore, it was hypothesized that a therapeutic effect against the disease would be obtained by removing only the disease-related cells that chronically overexpress gpNMB without adversely affecting the gpNMB-secreting cells that are (presumed to) playing such a protective role. To prove the hypothesis, we first needed to devise a method to remove gpNMB overexpressing cells. As a means to remove gpNMB overexpressing cells, we selected an antibody, which is the most specific means. In obtaining an anti-gpNMB antibody, we aimed to obtain an antibody with mouse-human cross-reactivity that could be used for clinical trials in humans as well as to verify the efficacy in model animals. There have been no known cases of obtaining anti-gpNMB antibodies cross-reactive with mice and humans. Glembatumumab (Patent Document 2), the only anti-gpNMB antibody that has progressed to clinical trials, is a human gpNMB-specific human antibody for delivering anticancer drugs to cancer cells. As mentioned above, an antibody drug conjugate (ADC) called Glembatumumab vedotin, which uses Glembatumumab, progressed to phase 2 trials as a candidate cancer treatment drug, but development was subsequently discontinued. In addition, when the elimination activity of T cells or NK cells is used as a means for eliminating such disease-related cells, inflammation may be induced. Therefore, we aimed to obtain an antibody that can induce the elimination activity of phagocytes such as macrophages, rather than the elimination activity of T cells or NK cells. The present inventors have succeeded in obtaining an anti-gpNMB antibody having a mouse-human cross-reactivity at a level that can exert an effect in vivo by making full use of various experimental means and methods under such various restrictive conditions. Analysis of the epitope of the anti-gpNMB antibody confirmed that it is a novel antibody that recognizes an epitope different from that of conventional vaccine peptides that have been reported to eliminate cells (Patent Document 1, Non-Patent Document 67). Furthermore, the present inventors selected several antibodies that recognize representative epitopes of the obtained anti-gpNMB antibodies and constructed a system to evaluate the elimination activity by phagocytes. Specifically, the elimination effect of gpNMB-expressing cells by a macrophage-derived cell line was evaluated, and antibodies with high elimination ability were selected. As a result, the elimination ability of gpNMB-expressing cells was confirmed for several antibodies that recognize epitope regions different from conventional vaccine epitopes, leading to the present invention. According to the anti-gpNMB antibody of the present invention, gpNMB-positive cells involved in the progression of various diseases can be effectively removed without inducing inflammation through the removal action of phagocytes, making it possible to provide effective treatment for various diseases that have been difficult to treat so far. In the following explanation, we will first explain the details of the anti-gpNMB antibody used in the present invention to remove disease-related cells (the anti-gpNMB antibody of the present invention) and its production method, and then explain the pharmaceutical composition (the pharmaceutical composition of the present invention) and treatment method (the treatment method of the present invention) that use such antibody to remove disease-related cells. Among the anti-gpNMB antibodies of the present invention described below, there are anti-gpNMB antibodies that have not been disclosed or suggested in prior art documents and are therefore patentable. These novel anti-gpNMB antibodies themselves are also intended to be included in the subject matter of the present invention. [Anti-gpNMB antibody] One aspect of the present invention is an anti-gpNMB antibody, and among them, an anti-gpNMB antibody that specifically binds to at least one site in the region spanning from V78 of gpNMB through the PMEL-CAF-like (PMEL Core Amyloid Fragment-like) domain to the PKD domain (hereinafter, may be abbreviated as "anti-gpNMB antibody of the present invention" or "antibody of the present invention") is preferred. At least one site in the region spanning from V78 of gpNMB to the PKD domain means, for example, at least one site in the region spanning from amino acid residues 78 to 319 of human gpNMB having the amino acid sequence of SEQ ID NO:209. ·antibody: In the present invention, an "antibody" is a glycoprotein comprising at least two heavy (H) chains and two light (L) chains interconnected by disulfide bonds. The heavy chain comprises a heavy chain variable region (abbreviated as VH) and a heavy chain constant region, which comprises three domains, CH1, CH2 and CH3. The light chain comprises a light chain variable region (abbreviated as VL) and a light chain constant region. The light chain constant region comprises one domain, CL. There are two types of light chain constant regions, called λ chains and κ chains. There are γ chains, μ chains, α chains, δ chains and ε chains in the heavy chain constant region, and there are antibody isotypes, IgG, IgM, IgA, IgD and IgE, depending on the difference in the heavy chain. The VH and VL regions are further subdivided into four more conserved regions (FR-1, FR-2, FR-3, FR-4) termed framework regions (FRs) and three regions that are variable (CDR-1, CDR-2, CDR-3) termed complementarity determining regions (CDRs). The VH contains three CDRs and four FRs arranged from amino-terminus to carboxy-terminus in the following order: FR-1, CDR-1 (CDR-H1), FR-2, CDR-2 (CDR-H2), FR-3, CDR-3 (CDR-H3), FR-4. The VL contains three CDRs and four FRs arranged from amino-terminus to carboxy-terminus in the following order: FR-1, CDR-1 (CDR-L1), FR-2, CDR-2 (CDR-L2), FR-3, CDR-3 (CDR-L3), FR-4. The variable regions of the heavy and light chains contain a binding domain that interacts with an antigen. The antibody of the present invention may be a fragment (e.g., an antigen-binding fragment) and / or a derivative of the antibody, so long as it has an activity of specifically binding to at least one site in the region spanning from V78 to the PKD domain of gpNMB. Examples of antibody fragments include F(ab') 2 , Fab, Fv, etc. Examples of antibody derivatives include antibodies in which amino acid mutations have been artificially introduced into the constant region portion, antibodies in which the configuration of the domain of the constant region has been modified, antibodies in a form having two or more Fcs per molecule, antibodies composed of only heavy chains or only light chains, glycosylated antibodies, bispecific antibodies, antibody conjugates bound to antibodies or antibody fragment compounds or proteins other than antibodies, antibody enzymes, nanobodies, tandem scFvs, bispecific tandem scFvs, diabodies, VHHs, etc. In the present invention, when the term "antibody" is used simply, it is intended to include antibody fragments and / or derivatives, unless otherwise specified. The antibody of the present invention may be a monoclonal antibody or a polyclonal antibody, but is preferably a monoclonal antibody. A monoclonal antibody classically refers to an antibody molecule obtained from a clone derived from a single antibody-producing cell, but refers to a single type of antibody molecule containing a combination of VH and VL consisting of a specific amino acid sequence. A monoclonal antibody can also be obtained by obtaining a nucleic acid molecule having a gene sequence that codes for the amino acids of the antibody protein, and it is also possible to produce an antibody by genetic engineering using such a nucleic acid molecule. In addition, it is a well-known technique to those skilled in the art in this field to perform modifications to improve the binding and specificity of an antibody using genetic information such as H chains, L chains, their variable regions, and CDR sequences, or to produce an antibody with a structure suitable for use as a therapeutic agent by modifying an antibody of an animal such as a mouse into a human antibody. It is also possible to obtain a human monoclonal antibody by using a transgenic animal into which a human antibody gene has been introduced as an animal to be sensitized to an antigen. In addition, as a method that does not require sensitization of animals, a person skilled in the art can appropriately carry out a technique of obtaining an antibody that specifically binds to a corresponding antigen or a phage clone consisting of a specific amino acid sequence using a phage library that expresses the antigen-binding region of a human antibody or a part thereof (human antibody phage display), and producing a human antibody from the information (see, for example, the review in Keio J. Med., (2011), 60:37-46, etc.). In addition, when designing an antibody to be administered to an animal other than a human, a person skilled in the art can appropriately design it using amino acid sequence information of the CDR or variable region, as in the case of humanization technology. The specificity of an antibody means that the antibody exhibits a high antigen-antibody reaction with a certain antigen. A person skilled in the art can appropriately select binding measurement in a solid-phase or liquid-phase system to measure the antigen-antibody reaction. Such methods include, but are not limited to, enzyme-linked immunosorbent assay (ELISA), enzyme immunoassay (EIA), surface plasmon resonance (SPR), fluorescence resonance energy transfer (FRET), luminescence resonance energy transfer (LRET), and the like. In addition, when measuring such antigen-antibody binding, it is also possible to label the antibody and / or antigen with an enzyme, a fluorescent substance, a luminescent substance, a radioisotope, or the like, and detect the antigen-antibody reaction using a measurement method suitable for the physical and / or chemical properties of the labeled substance. Specific binding to at least one site in the region spanning from V78 to the PKD domain of gpNMB: The antibody of the present invention specifically binds to at least one site in the region spanning from valine at position 78 (V78) to the PKD domain of human gpNMB. Such region includes the region spanning from valine at position 78 (V78) to serine at position 92 (S92), the PMEL-CAF-like domain, and the PKD domain, as well as the region intervening between these regions. In the present invention, "gpNMB" (glycoprotein nonmetastatic melanoma protein B) (also known as osteoactivin, DC-HIL) is the aforementioned single-pass transmembrane glycoprotein. For details, see the aforementioned documents (especially Non-Patent Document 20, etc.). The amino acid sequence of the full-length protein of human gpNMB (isotype a) is shown in SEQ ID NO: 209, and the nucleic acid sequence of the gene encoding said protein is shown in SEQ ID NO: 210. The amino acid sequence of the full-length protein of mouse gpNMB is shown in SEQ ID NO: 211, and the nucleic acid sequence of the gene encoding said protein is shown in SEQ ID NO: 212. The amino acid sequence of the full-length protein of rat gpNMB is shown in SEQ ID NO: 213, and the nucleic acid sequence of the gene encoding said protein is shown in SEQ ID NO: 214. An alignment of the amino acid sequences of human gpNMB (isotype a) and mouse gpNMB is shown in Figure 1. The region from V78 to S92 of gpNMB refers to a region including 7 amino acid residues around aspartic acid at position 85 (D85) of gpNMB. In Fig. 1, the regions from V78 to S92 of human gpNMB and mouse gpNMB are enclosed by dashed lines. The PKD (Polycystic Kidney Disease homology) domain of gpNMB is a domain in which a β-sandwich structure is formed by folding a β-sheet consisting of three strands and a β-sheet consisting of four strands. Since this is a characteristic structure of polycystin-1, a gene causing polycystic kidney disease, it was named the PKD domain (Non-Patent Document 26). According to one embodiment, in the case of human gpNMB shown in SEQ ID NO: 209 and mouse gpNMB shown in SEQ ID NO: 211, the region of amino acid residues 256 to 319 corresponds to the PKD domain. According to one embodiment, the PKD domain is preferably a region of amino acid residues 256 to 316, more preferably a region of amino acid residues 257 to 316, particularly preferably a region of amino acid residues 268 to 316, even more preferably a region of amino acid residues 270 to 316, even more preferably a region of amino acid residues 282 to 316, and especially preferably a region of amino acid residues 287 to 316. According to one embodiment, the PKD domain is preferably a region of amino acid residues 257 to 319, particularly preferably a region of amino acid residues 257 to 316, and further preferably a region of amino acid residues 257 to 301. According to one embodiment, the PKD domain is particularly preferably a region of amino acid residues 287 to 301. In Figure 1, the regions of amino acid residues 256 to 319 are shown enclosed by dotted lines as examples of the PKD domains of human gpNMB and mouse gpNMB. As described above, the PMEL-CAF-like (PMEL Core Amyloid Fragment-like) domain of gpNMB is a region that is homologous to the CAF region in PMEL, which is a protein of the same family, and is a region that induces the formation of amyloid-like aggregates in PMEL protein (Non-Patent Document 89). It is believed that the PMEL-CAF-like domain of gpNMB prevents the formation of aggregates due to the presence of many N-glycosylated binding sites in the adjacent PKD region (Non-Patent Document 90). According to one embodiment, in the case of human gpNMB shown in SEQ ID NO: 209 and mouse gpNMB shown in SEQ ID NO: 211, the region of amino acid residues 172 to 246 corresponds to the PMEL-CAF-like domain. Among them, the region of amino acid residues 178 to 228 is preferable as the PMEL-CAF-like domain, and the region of amino acid residues 186 to 218 is more preferable. In FIG. 1, the regions from amino acid residues 172 to 246 are enclosed by solid lines as examples of the PMEL-CAF-like domains of human gpNMB and mouse gpNMB. As described above, in the present invention, the "region spanning from V78 to the PKD domain of gpNMB" refers to a region including not only the region spanning from V78 to S92, the PMEL-CAF-like domain, and the PKD domain, but also a region interposed between the region spanning from V78 to S92 and the PMEL-CAF-like domain, and a region interposed between the PMEL-CAF-like domain and the PKD domain. According to one embodiment, in the case of human gpNMB shown in SEQ ID NO: 209 and mouse gpNMB shown in SEQ ID NO: 211, the regions from amino acid residues 78 to 319 correspond to the region spanning from V78 to the PKD domain. The antibody of the present invention may specifically bind to at least one site in the region spanning from V78 to the PKD domain of gpNMB of any vertebrate, but in consideration of human pharmaceutical applications, it is preferable that the antibody specifically binds to at least one site in the region spanning from V78 to the PKD domain of human gpNMB as shown in SEQ ID NO: 209. From the viewpoint of evaluating the effect on endogenous gpNMB in disease model mice and disease model rats, it is even more preferable that the antibody of the present invention specifically binds to at least one site in the region spanning from V78 to the PKD domain of mouse gpNMB as shown in SEQ ID NO: 211 in addition to at least one site in the region spanning from V78 to the PKD domain of human gpNMB. In the present invention, the term "specifically" binding of an antibody to gpNMB means that the gpNMB binding strength is 10 times or more, preferably 100 times or more, more preferably 1000 times or more, relative to the binding to proteins other than gpNMB (e.g., albumin). Furthermore, the "region spanning from V78 to the PKD domain" refers to the region spanning from V78 to S92, the PMEL-CAF-like domain, the PKD domain, the region between the region spanning from V78 to S92 and the PMEL-CAF-like domain, and the region between the PMEL-CAF-like domain and the PKD domain. In another aspect, the antibody of the present invention preferably binds to at least one site in the region spanning V78 to S92 of human gpNMB shown in SEQ ID NO:209, i.e., a region including 7 amino acid residues around D85, more preferably specifically binds to at least one site in the region including 4 amino acid residues around D85, even more preferably specifically binds to at least one site in the region including 2 amino acid residues around D85, and particularly preferably specifically binds to at least D85. As long as the antibody of the present invention specifically binds to at least one site in the region spanning from V78 to the PKD domain of human gpNMB, the epitope is not particularly limited. However, according to one embodiment, the antibody of the present invention preferably binds to at least one site from the PMEL-CAF-like domain to the PKD domain, and more preferably specifically binds to one or more of the following regions of human gpNMB shown in SEQ ID NO:209: a region comprising amino acid residues K257 and / or D258 of the PKD domain, a region comprising amino acid residues H268 and / or D269 of the PKD domain, a region comprising amino acid residue K282 of the PKD domain, a region comprising amino acid residues D287 and / or H301 of the PKD domain, a region comprising amino acid residue K316 of the PKD domain, a region comprising amino acid residue K186 of the PMEL-CAF-like domain, a region comprising amino acid residues R214 and / or R215 of the PMEL-CAF-like domain, and a region comprising amino acid residues H216 and / or R218 of the PMEL-CAF-like domain. In particular, it is preferable that the antibody of the present invention specifically binds to at least one or both of the regions containing amino acid residues D287 and / or H301, and the regions containing amino acid residues R214 and / or R215 of human gpNMB shown in SEQ ID NO:209, and it is more preferable that in addition to these regions, the antibody also specifically binds to one or more of the regions containing amino acid residues K257 and / or D258, the region containing amino acid residues H268 and / or D269, the region containing amino acid residue K282, the region containing amino acid residue K316, the region containing amino acid residue K186, and the region containing amino acid residues H216 and / or R218. The epitope of human gpNMB to which the antibody of the present invention binds may be a linear epitope consisting of a continuous region on the primary structure of human gpNMB (the amino acid sequence shown in SEQ ID NO: 209), or a conformational epitope consisting of two or more discrete partial regions on the primary structure in a conformational structure, so long as the epitope includes at least one part of the region spanning from V78 to the PKD domain. The region constituting the linear epitope and each partial region constituting the conformational epitope may be present in any one of the regions spanning from V78 to S92, the region between the region spanning from V78 to S92 and the PMEL-CAF-like domain, the PMEL-CAF-like domain, the PKD domain, and the region between the PMEL-CAF-like domain and the PKD domain, or may span two or more regions. Also, it may be present only in the region spanning from V78 to the PKD domain, or may span other regions. Furthermore, as long as at least one of the multiple partial regions constituting the three-dimensional epitope is partly or entirely present within the region spanning from V78 to the PKD domain, the other partial regions may be present outside the region spanning from V78 to the PKD domain. The binding strength of the antibody of the present invention to the region spanning from V78 to the PKD domain of gpNMB is not particularly limited, but may be determined as the 50% effective concentration (EC ) for the region spanning from V78 to the PKD domain of gpNMB measured in antigen ELISA using recombinant gpNMB and / or cell ELISA using gpNMB-expressing cells. 50 ) but usually 1 x 10 -7 M or less, or 1 x 10 -8 M or less, or 1 x 10 -9 In the present specification, the "50% effective concentration" (EC 50 ) refers to the antibody concentration at which the antibody shows 50% of the maximum binding affinity of the antibody binding to the antigen. EC by antigen ELISA using recombinant gpNMB and / or cell ELISA using gpNMB expressing cells 50 Specific measurement conditions include the conditions employed in the examples described below. The antibody of the present invention may bind to one or more sites in other regions of gpNMB in addition to the region spanning from V78 to the PKD domain. Amino acid sites to which the antibody of the present invention may bind other than the region spanning from V78 to the PKD domain of gpNMB include, but are not limited to, E385 of human gpNMB shown in SEQ ID NO:209. Amino acid and nucleic acid sequences of each antibody chain and region: The amino acid sequence of the antibody of the present invention is not particularly limited as long as it has specific binding activity to at least one site in the region spanning from V78 to the PKD domain of gpNMB described above. However, it is preferable that the antibody of the present invention has a specific amino acid sequence as each CDR sequence. Specifically, it is as follows. In this specification, the "identity" of an amino acid sequence means the proportion of amino acid residues that match, and the "similarity" means the proportion of amino acid residues that match or are similar. The homology and identity of amino acid sequences can be determined, for example, by the BLAST method (default conditions of PBLAST of NCBI). In addition, for example, when it is expressed as "homology of 80% or more", it is clear that the case of "identity of 80% or more" is included. Here, the term "similar amino acid residues" refers to amino acid residues having side chains with similar chemical properties (e.g., charge or hydrophobicity). Examples of similar amino acid residues include the following combinations: (1) Amino acid residues having an aliphatic side chain: glycine (Gly or G), alanine (Ala or A), valine (Val or V), leucine (Leu or L), and isoleucine (Ile or I) residues. (2) Amino acid residues having aliphatic hydroxyl side chains: serine (Ser or S) and threonine (Thr or T) residues. (3) Amino acid residues having amide-containing side chains: asparagine (Asn or N) and glutamine (Gln or Q) residues. (4) Amino acid residues having aromatic side chains: phenylalanine (Phe or F), tyrosine (Tyr or Y), and tryptophan (Trp or W) residues. (5) Amino acid residues having basic side chains: lysine (Lys or K), arginine (Arg or R), and histidine (His or H) residues. (6) Amino acid residues having acidic side chains: aspartic acid (Asp or D) and glutamic acid (Glu or E) residues. (7) Amino acid groups having sulfur-containing side chains: cysteine ​​(Cys or C) and methionine (Met or M) residues. Furthermore, the combination of (1) and a methionine (Met or M) residue, and the combination of (4) and a histidine (His or H) residue are also treated as similar amino acid residues. In addition, when a corresponding variant exists based on the germline sequence, it may be possible to make a substitution regardless of similarity. Variations based on the germline include substitutions, deletions, and additions. Substitutions may also be made with amino acids that are predicted to affect the direction of the side chain, such as proline (Pro or P) and glycine (Gly or G). One embodiment of the antibody of the present invention includes an antibody comprising a heavy chain variable region having the CDR-H1 to H3 sequences of (1) to (14) below. As used herein, the term "CDR grafting region" refers to a region of an antibody amino acid sequence having an amino acid sequence identical or overlapping with the amino acid sequence of a CDR defined herein, which contacts an antigen like a CDR and determines antigen specificity, and is important for binding to an antigen. (1) As CDR-H1, an amino acid sequence of SEQ ID NO: 1, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence of SEQ ID NO: 1 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 1; As CDR-H2, an amino acid sequence of SEQ ID NO: 3, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence of SEQ ID NO: 3 have been substituted, deleted or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 3, and As CDR-H3, the amino acid sequence set forth in SEQ ID NO:5, or an amino acid sequence in which any one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO:5 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 75.0% or more, 83.3% or more, or 91.6% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:5. (2) As CDR-H1, an amino acid sequence of SEQ ID NO: 17, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence of SEQ ID NO: 17 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 17; As CDR-H2, an amino acid sequence of SEQ ID NO: 19, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence of SEQ ID NO: 19 have been substituted, deleted or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 19, and As CDR-H3, an amino acid sequence set forth in SEQ ID NO:21, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence set forth in SEQ ID NO:21 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 66.6% or more, 73.3% or more, 80.0% or more, 86.6% or more, or 93.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:21. (3) As CDR-H1, an amino acid sequence set forth in SEQ ID NO: 33, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO: 33 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 33; As CDR-H2, an amino acid sequence of SEQ ID NO: 35, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence of SEQ ID NO: 35 have been substituted, deleted or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 35, and As CDR-H3, an amino acid sequence set forth in SEQ ID NO: 37, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence set forth in SEQ ID NO: 37 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 66.6% or more, 73.3% or more, 80.0% or more, 86.6% or more, or 93.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 37. (4) As CDR-H1, an amino acid sequence set forth in SEQ ID NO: 49, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO: 49 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 49; As CDR-H2, an amino acid sequence of SEQ ID NO:51, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence of SEQ ID NO:51 have been substituted, deleted or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO:51, and As CDR-H3, an amino acid sequence set forth in SEQ ID NO:53, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence set forth in SEQ ID NO:53 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 68.7% or more, 75.0% or more, 81.2% or more, 87.5% or more, or 93.7% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:53. (5) As CDR-H1, an amino acid sequence set forth in SEQ ID NO: 65, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO: 65 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 65; As CDR-H2, an amino acid sequence of SEQ ID NO:67, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence of SEQ ID NO:67 have been substituted, deleted or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO:67, and As CDR-H3, an amino acid sequence set forth in SEQ ID NO:69, or an amino acid sequence in which any one, two, three, four, or five amino acid residues in the amino acid sequence set forth in SEQ ID NO:69 have been substituted, deleted, or inserted, or an amino acid sequence having 64.2% or more, 71.4% or more, 78.5% or more, 85.7% or more, or 92.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:69. (6) As CDR-H1, an amino acid sequence of SEQ ID NO: 81, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence of SEQ ID NO: 81 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 81; As CDR-H2, an amino acid sequence of SEQ ID NO: 83, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence of SEQ ID NO: 83 have been substituted, deleted, or inserted, or an amino acid sequence having 71.4% or more or 85.7% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 83, and As CDR-H3, an amino acid sequence set forth in SEQ ID NO: 85, or an amino acid sequence in which any one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 85 have been substituted, deleted, or inserted, or an amino acid sequence having 63.6% or more, 72.7% or more, 81.8% or more, or 90.9% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 85. (7) As CDR-H1, an amino acid sequence set forth in SEQ ID NO: 97, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO: 97 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 97; As CDR-H2, an amino acid sequence of SEQ ID NO: 99, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence of SEQ ID NO: 99 have been substituted, deleted or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 99, and As CDR-H3, an amino acid sequence set forth in SEQ ID NO: 101, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 101 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more or 80.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 101. (8) As CDR-H1, an amino acid sequence set forth in SEQ ID NO: 113, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 113 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 113; As CDR-H2, an amino acid sequence of SEQ ID NO: 115, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence of SEQ ID NO: 115 have been substituted, deleted, or inserted, or an amino acid sequence having 71.4% or more or 85.7% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 115, and As CDR-H3, an amino acid sequence set forth in SEQ ID NO: 117, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence set forth in SEQ ID NO: 117 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 66.6% or more, 73.3% or more, 80.0% or more, 86.6% or more, or 93.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 117. (9) As CDR-H1, an amino acid sequence set forth in SEQ ID NO: 129, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 129 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 129; As CDR-H2, an amino acid sequence of SEQ ID NO: 131, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence of SEQ ID NO: 131 have been substituted, deleted, or inserted, or an amino acid sequence having 71.4% or more or 85.7% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 131, and As CDR-H3, an amino acid sequence set forth in SEQ ID NO: 133, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence set forth in SEQ ID NO: 133 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 66.6% or more, 73.3% or more, 80.0% or more, 86.6% or more, or 93.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 133. (10) As CDR-H1, an amino acid sequence set forth in SEQ ID NO: 145, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO: 145 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 145; As CDR-H2, an amino acid sequence of SEQ ID NO: 147, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence of SEQ ID NO: 147 have been substituted, deleted or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 147, and As CDR-H3, an amino acid sequence set forth in SEQ ID NO: 149, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence set forth in SEQ ID NO: 149 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 66.6% or more, 73.3% or more, 80.0% or more, 86.6% or more, or 93.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 149. (11) As CDR-H1, an amino acid sequence set forth in SEQ ID NO: 161, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 161 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 161; As CDR-H2, an amino acid sequence of SEQ ID NO: 163, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence of SEQ ID NO: 163 have been substituted, deleted, or inserted, or an amino acid sequence having 71.4% or more or 85.7% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 163, and As CDR-H3, an amino acid sequence set forth in SEQ ID NO: 165, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence set forth in SEQ ID NO: 165 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 66.6% or more, 73.3% or more, 80.0% or more, 86.6% or more, or 93.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 165. (12) As CDR-H1, an amino acid sequence set forth in SEQ ID NO:255, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO:255 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:255; As CDR-H2, an amino acid sequence of SEQ ID NO:257, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence of SEQ ID NO:257 have been substituted, deleted, or inserted, or an amino acid sequence having 71.4% or more or 85.7% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO:257, and As CDR-H3, an amino acid sequence set forth in SEQ ID NO:259, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO:259 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:259. (13) As CDR-H1, an amino acid sequence set forth in SEQ ID NO:283, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO:283 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:283; As CDR-H2, an amino acid sequence of SEQ ID NO:285, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence of SEQ ID NO:285 have been substituted, deleted or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO:285; As CDR-H3, an amino acid sequence set forth in SEQ ID NO:287, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence set forth in SEQ ID NO:287 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 66.6% or more, 73.3% or more, 80.0% or more, 86.6% or more, or 93.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:287. (14) As CDR-H1, an amino acid sequence set forth in SEQ ID NO: 311, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 311 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 311; as CDR-H2, an amino acid sequence of SEQ ID NO:313, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence of SEQ ID NO:313 have been substituted, deleted, or inserted, or an amino acid sequence having 71.4% or more or 85.7% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO:313; As CDR-H3, an amino acid sequence set forth in SEQ ID NO:315, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence set forth in SEQ ID NO:315 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 66.6% or more, 73.3% or more, 80.0% or more, 86.6% or more, or 93.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:315. As shown in Example 11 below, the present inventors investigated the importance of each amino acid residue in each CDR-grafting region sequence of the humanized anti-gpNMB antibody H1L1 (clone hGPN06-1_H1L1) in maintaining the binding ability by alanine scanning. As a result, it was identified that the following residues are important for maintaining the binding: tyrosine at position 27, asparagine at position 32, and tryptophan at position 33 in CDR grafting region-H1 (SEQ ID NO: 271); aspartic acid at position 55, phenylalanine at position 57, threonine at position 58, asparagine at position 59, tyrosine at position 60, and asparagine at position 61 in CDR grafting region-H2 (SEQ ID NO: 273); arginine at position 98, glycine at position 100, and glycine at position 109 in CDR grafting region-H3 (SEQ ID NO: 275) in the heavy chain variable region (SEQ ID NO: 295) of humanized anti-gpNMB antibody hGPN06-1_H1L1. On the other hand, it was identified that the amino acid residues in each CDR grafting region sequence other than those mentioned above have almost no effect on maintaining the binding. Based on these findings, one embodiment of the antibody of the present invention includes an antibody comprising a heavy chain variable region having the CDR grafting region-H1 to H3 sequence of the following (15) (note that the following amino acid positions are shown based on the amino acid sequence of the heavy chain variable region of humanized anti-gpNMB antibody hGPN06-1_H1L1 (sequence number 295)). (15) As the CDR grafting region-H1, an amino acid sequence of SEQ ID NO: 271, or an amino acid sequence in which one, two, three, or four amino acid residues other than tyrosine at position 27, asparagine at position 32, and tryptophan at position 33 of the amino acid sequence of SEQ ID NO: 271 have been substituted, deleted, or inserted; as CDR grafting region-H2, an amino acid sequence set forth in SEQ ID NO:273, or an amino acid sequence in which, in the amino acid sequence set forth in SEQ ID NO:273, any one, two, three, four, five, or six amino acid residues other than aspartic acid at position 55, phenylalanine at position 57, threonine at position 58, asparagine at position 59, tyrosine at position 60, and asparagine at position 61 have been substituted, deleted, or inserted; As the CDR grafting region-H3, the amino acid sequence of SEQ ID NO:275, or the amino acid sequence of SEQ ID NO:275 in which any one, two, three, four, five, or six amino acid residues other than arginine at position 98, glycine at position 100, and glycine at position 109 have been substituted, deleted, or inserted. Furthermore, as shown in Example 15 below, the present inventors investigated the importance of each amino acid residue in each CDR grafting region sequence of humanized anti-gpNMB antibody H2L3 (clone hGPN18-2_H2L3) in maintaining the binding by alanine scanning. As a result, it was identified that aspartic acid at position 52, tryptophan at position 54, aspartic acid at position 58, and proline at position 63 in CDR grafting region-H2 (SEQ ID NO: 301) of the heavy chain variable region of humanized anti-gpNMB antibody H2L3, and arginine at position 99, threonine at position 100, tyrosine at position 102, tyrosine at position 105, tyrosine at position 107, and methionine at position 110 in CDR grafting region-H3 (SEQ ID NO: 303) are important for maintaining the binding. On the other hand, it was identified that the amino acid residues in each CDR grafting region sequence other than those mentioned above have almost no effect on maintaining the binding. Based on these findings, one embodiment of the antibody of the present invention includes an antibody comprising a light chain variable region having the CDR grafting region-H1 to H3 sequence of the following (16) (note that the following amino acid positions are shown based on the amino acid sequence of the heavy chain variable region of the humanized anti-gpNMB antibody H2L3 (SEQ ID NO: 323)). (16) As the CDR grafting region-H1, an amino acid sequence set forth in SEQ ID NO: 299, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 299 have been substituted, deleted, or inserted; as CDR grafting region-H2, an amino acid sequence as set forth in SEQ ID NO:301, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues other than aspartic acid at position 52, tryptophan at position 54, aspartic acid at position 58, and proline at position 63 of the amino acid sequence as set forth in SEQ ID NO:301 have been substituted, deleted, or inserted; As the CDR grafting region-H3, the amino acid sequence of SEQ ID NO: 303, or an amino acid sequence in which, in the amino acid sequence of SEQ ID NO: 303, any one, two, three, four, five, or six amino acid residues other than arginine at position 99, threonine at position 100, tyrosine at position 102, tyrosine at position 105, tyrosine at position 107, and methionine at position 110 have been substituted, deleted, or inserted. One embodiment of the antibody of the present invention includes an antibody comprising a heavy chain variable region having the CDR-H1 to H3 sequences of the following (17) to (23). Note that antibodies comprising a heavy chain variable region having the CDR-H1 to H3 sequences of the following (17) to (23) have not been disclosed or suggested in the prior art and are therefore novel anti-gpNMB antibodies. (17) As CDR-H1, an amino acid sequence set forth in SEQ ID NO: 177, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 177 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 177; As CDR-H2, an amino acid sequence of SEQ ID NO: 179, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence of SEQ ID NO: 179 have been substituted, deleted or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 179, and As CDR-H3, an amino acid sequence set forth in SEQ ID NO: 181, or an amino acid sequence in which any one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO: 181 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 181. (18) As CDR-H1, an amino acid sequence set forth in SEQ ID NO: 330, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 330 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 330; As CDR-H2, an amino acid sequence of SEQ ID NO: 331, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence of SEQ ID NO: 331 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 331, and As CDR-H3, an amino acid sequence set forth in SEQ ID NO:332, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO:332 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:332. (19) As CDR-H1, an amino acid sequence set forth in SEQ ID NO: 337, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 337 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 337; As CDR-H2, an amino acid sequence of SEQ ID NO: 338, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence of SEQ ID NO: 338 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 338, and As CDR-H3, an amino acid sequence set forth in SEQ ID NO:339, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO:339 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:339. (20) As CDR-H1, an amino acid sequence set forth in SEQ ID NO: 344, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 344 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 344; As CDR-H2, an amino acid sequence of SEQ ID NO: 345, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence of SEQ ID NO: 345 have been substituted, deleted or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 345, and As CDR-H3, an amino acid sequence set forth in SEQ ID NO:346, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO:346 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:346. (21) As the CDR grafting region-H1, an amino acid sequence set forth in SEQ ID NO: 327, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 327 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 327; As the CDR grafting region-H2, an amino acid sequence set forth in SEQ ID NO: 328, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence set forth in SEQ ID NO: 328 have been substituted, deleted, or inserted, or an amino acid sequence having 64.7% or more, 70.5% or more, 76.4% or more, 82.3% or more, 88.2% or more, or 94.1% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 328; As the CDR grafting region-H3, an amino acid sequence set forth in SEQ ID NO:329, or an amino acid sequence in which any one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO:329 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:329. (22) As the CDR grafting region-H1, an amino acid sequence set forth in SEQ ID NO: 334, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 334 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 334; As the CDR grafting region-H2, an amino acid sequence set forth in SEQ ID NO: 335, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence set forth in SEQ ID NO: 335 have been substituted, deleted, or inserted, or an amino acid sequence having 64.7% or more, 70.5% or more, 76.4% or more, 82.3% or more, 88.2% or more, or 94.1% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 335; As the CDR grafting region-H3, an amino acid sequence set forth in SEQ ID NO:336, or an amino acid sequence in which any one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO:336 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:336. (23) As the CDR grafting region-H1, an amino acid sequence set forth in SEQ ID NO: 341, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 341 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 341; As the CDR grafting region-H2, an amino acid sequence set forth in SEQ ID NO: 342, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence set forth in SEQ ID NO: 342 have been substituted, deleted, or inserted, or an amino acid sequence having 64.7% or more, 70.5% or more, 76.4% or more, 82.3% or more, 88.2% or more, or 94.1% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 342; As the CDR grafting region-H3, an amino acid sequence set forth in SEQ ID NO:343, or an amino acid sequence in which any one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO:343 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:343. One embodiment of the antibody of the present invention includes an antibody comprising a light chain variable region having the CDR-L1 to L3 sequences of (1) to (14) below. (1) as CDR-L1, an amino acid sequence as set forth in SEQ ID NO: 7, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 7 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 7; CDR-L2: an amino acid sequence of SEQ ID NO: 9, or an amino acid sequence in which any one amino acid residue in the amino acid sequence of SEQ ID NO: 9 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 9; and As CDR-L3, an amino acid sequence set forth in SEQ ID NO:11, or an amino acid sequence in which any one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO:11 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:11. (2) as CDR-L1, an amino acid sequence set forth in SEQ ID NO:23, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO:23 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more or 80.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:23; As CDR-L2, an amino acid sequence of SEQ ID NO:25, or an amino acid sequence in which any one amino acid residue in the amino acid sequence of SEQ ID NO:25 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO:25, and As CDR-L3, an amino acid sequence set forth in SEQ ID NO:27, or an amino acid sequence in which any one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO:27 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:27. (3) as CDR-L1, an amino acid sequence set forth in SEQ ID NO: 39, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 39 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more or 80.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 39; CDR-L2: an amino acid sequence of SEQ ID NO: 41, or an amino acid sequence in which any one amino acid residue in the amino acid sequence of SEQ ID NO: 41 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 41; and As CDR-L3, an amino acid sequence set forth in SEQ ID NO:43, or an amino acid sequence in which any one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO:43 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:43. (4) As CDR-L1, an amino acid sequence set forth in SEQ ID NO:55, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO:55 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:55; As CDR-L2, an amino acid sequence of SEQ ID NO:57, or an amino acid sequence in which any one amino acid residue in the amino acid sequence of SEQ ID NO:57 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO:57, and As CDR-L3, an amino acid sequence set forth in SEQ ID NO:59, or an amino acid sequence in which any one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO:59 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:59. (5) As CDR-L1, an amino acid sequence set forth in SEQ ID NO: 71, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 71 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more or 80.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 71; CDR-L2, an amino acid sequence of SEQ ID NO: 73, or an amino acid sequence in which any one amino acid residue in the amino acid sequence of SEQ ID NO: 73 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 73; and As CDR-L3, an amino acid sequence set forth in SEQ ID NO: 75, or an amino acid sequence in which any one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 75 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 75. (6) As CDR-L1, an amino acid sequence set forth in SEQ ID NO: 87, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 87 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 87; CDR-L2: an amino acid sequence of SEQ ID NO: 89, or an amino acid sequence in which any one amino acid residue in the amino acid sequence of SEQ ID NO: 89 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 89; and As CDR-L3, an amino acid sequence set forth in SEQ ID NO:91, or an amino acid sequence in which any one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO:91 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:91. (7) As CDR-L1, an amino acid sequence set forth in SEQ ID NO: 103, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 103 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 103; As CDR-L2, an amino acid sequence of SEQ ID NO: 105, or an amino acid sequence in which any one amino acid residue in the amino acid sequence of SEQ ID NO: 105 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 105, and As CDR-L3, an amino acid sequence set forth in SEQ ID NO: 107, or an amino acid sequence in which any one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO: 107 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 107. (8) As CDR-L1, an amino acid sequence set forth in SEQ ID NO: 119, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 119 have been substituted, deleted, or inserted, or an amino acid sequence having 63.6% or more, 72.7% or more, 81.8% or more, or 90.9% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 119; As CDR-L2, an amino acid sequence of SEQ ID NO: 121, or an amino acid sequence in which any one amino acid residue in the amino acid sequence of SEQ ID NO: 121 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 121, and As CDR-L3, an amino acid sequence set forth in SEQ ID NO: 123, or an amino acid sequence in which any one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO: 123 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 123. (9) As CDR-L1, an amino acid sequence set forth in SEQ ID NO: 135, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 135 have been substituted, deleted, or inserted, or an amino acid sequence having 63.6% or more, 72.7% or more, 81.8% or more, or 90.9% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 135; As CDR-L2, an amino acid sequence of SEQ ID NO: 137, or an amino acid sequence in which any one amino acid residue in the amino acid sequence of SEQ ID NO: 137 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 137, and As CDR-L3, an amino acid sequence set forth in SEQ ID NO: 139, or an amino acid sequence in which any one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO: 139 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 139. (10) As CDR-L1, an amino acid sequence set forth in SEQ ID NO: 151, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 151 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 151; As CDR-L2, an amino acid sequence of SEQ ID NO: 153, or an amino acid sequence in which any one amino acid residue in the amino acid sequence of SEQ ID NO: 153 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 153, and As CDR-L3, an amino acid sequence set forth in SEQ ID NO: 155, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO: 155 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 155. (11) As CDR-L1, an amino acid sequence set forth in SEQ ID NO: 167, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 167 have been substituted, deleted, or inserted, or an amino acid sequence having 63.6% or more, 72.7% or more, 81.8% or more, or 90.9% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 167; As CDR-L2, an amino acid sequence of SEQ ID NO: 169, or an amino acid sequence in which any one amino acid residue in the amino acid sequence of SEQ ID NO: 169 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 169, and As CDR-L3, an amino acid sequence set forth in SEQ ID NO: 171, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO: 171 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 171. (12) As CDR-L1, an amino acid sequence set forth in SEQ ID NO:261, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO:261 have been substituted, deleted, or inserted, or an amino acid sequence having 63.6% or more, 72.7% or more, 81.8% or more, or 90.9% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:261; As CDR-L2, an amino acid sequence of SEQ ID NO:263, or an amino acid sequence in which any one amino acid residue in the amino acid sequence of SEQ ID NO:263 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO:263, and As CDR-L3, an amino acid sequence set forth in SEQ ID NO:265, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO:265 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:265. (13) As CDR-L1, an amino acid sequence set forth in SEQ ID NO:289, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO:289 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more or 80.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:289; As CDR-L2, an amino acid sequence of SEQ ID NO:291, or an amino acid sequence in which any one amino acid residue in the amino acid sequence of SEQ ID NO:291 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO:291, and As CDR-L3, an amino acid sequence set forth in SEQ ID NO:293, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO:293 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:293. (14) As CDR-L1, an amino acid sequence set forth in SEQ ID NO: 317, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 317 have been substituted, deleted, or inserted, or an amino acid sequence having 63.6% or more, 72.7% or more, 81.8% or more, or 90.9% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 317; As CDR-L2, an amino acid sequence of SEQ ID NO: 319, or an amino acid sequence in which any one amino acid residue in the amino acid sequence of SEQ ID NO: 319 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 319, and As CDR-L3, an amino acid sequence set forth in SEQ ID NO:321, or an amino acid sequence in which any one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO:321 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:321. As shown in Example 11 below, the present inventors investigated the importance of each amino acid residue in each CDR-grafting region sequence of the humanized anti-gpNMB antibody H1L1 (clone hGPN06-1_H1L1) in maintaining the binding ability by alanine scanning. As a result, it was identified that the following residues are important for maintaining the binding in the light chain variable region (SEQ ID NO: 297) of hGPN06-1_H1L1: isoleucine at position 29, tyrosine at position 31, and histidine at position 33 in CDR grafting region-L1 (SEQ ID NO: 277), threonine at position 50 in CDR grafting region-L2 (SEQ ID NO: 279), histidine at position 88, glutamine at position 89, tryptophan at position 90, serine at position 92, tyrosine at position 93, proline at position 94, and cysteine ​​at position 95 in CDR grafting region-L3 (SEQ ID NO: 281). On the other hand, it was identified that the amino acid residues in each CDR grafting region sequence other than those mentioned above have almost no effect on maintaining the binding. Based on these findings, one embodiment of the antibody of the present invention includes an antibody comprising a light chain variable region having the CDR grafting region-L1 to L3 sequence of the following (15) (note that the following amino acid positions are shown based on the amino acid sequence of the light chain variable region of humanized anti-gpNMB antibody H1L1 (sequence number 297)). (15) As the CDR grafting region-L1, the amino acid sequence of SEQ ID NO: 277, or the amino acid sequence of SEQ ID NO: 277 in which any one, two, three, or four amino acid residues other than isoleucine at position 29, tyrosine at position 31, and histidine at position 33 have been substituted, deleted, or inserted; As the CDR grafting region-L2, an amino acid sequence of SEQ ID NO:279 or an amino acid sequence in which one or two amino acid residues other than the 50th threonine in the amino acid sequence of SEQ ID NO:279 have been substituted, deleted or inserted; As the CDR grafting region-L3, the amino acid sequence of SEQ ID NO:281, or the amino acid sequence of SEQ ID NO:281 in which one, two, or three amino acid residues have been substituted, deleted, or inserted at any one, two, or three positions other than the histidine at position 88, the glutamine at position 89, the tryptophan at position 90, the serine at position 92, the tyrosine at position 93, the proline at position 94, and the cysteine ​​at position 95. Furthermore, as shown in Example 15 below, the present inventors investigated the importance of each amino acid residue in each CDR grafting region sequence of humanized anti-gpNMB antibody H2L3 (clone hGPN18-2_H2L3) in maintaining the binding by alanine scanning. As a result, it was identified that leucine at position 31 and tyrosine at position 37 in CDR grafting region-L1 (SEQ ID NO: 305), lysine at position 55 in CDR grafting region-L2 (SEQ ID NO: 307), and phenylalanine at position 94 in CDR grafting region-L3 (SEQ ID NO: 309) of the light chain variable region (SEQ ID NO: 325) of humanized anti-gpNMB antibody H2L3 are important for maintaining the binding. On the other hand, it was identified that amino acid residues in each CDR grafting region sequence other than those mentioned above have almost no effect on maintaining the binding. Based on these findings, one embodiment of the antibody of the present invention includes an antibody comprising a light chain variable region having the CDR grafting region-L1 to L3 sequence of the following (16) (note that the following amino acid positions are shown based on the amino acid sequence of the light chain variable region of humanized anti-gpNMB antibody H2L3 (sequence number 325)). (16) As the CDR grafting region-L1, an amino acid sequence of SEQ ID NO: 305, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues other than leucine at position 31, tyrosine at position 37, and glutamic acid at position 39 in the amino acid sequence of SEQ ID NO: 305 have been substituted, deleted, or inserted; As a CDR grafting region-L2, an amino acid sequence of SEQ ID NO: 307 or an amino acid sequence in which one or two amino acid residues other than the lysine at position 55 in the amino acid sequence of SEQ ID NO: 307 have been substituted, deleted or inserted; As the CDR grafting region-L3, the amino acid sequence of SEQ ID NO: 309 or the amino acid sequence of SEQ ID NO: 309 in which one, two, or three amino acid residues other than phenylalanine at position 94 have been substituted, deleted, or inserted. One embodiment of the antibody of the present invention includes an antibody comprising a light chain variable region having the CDR-H1 to H3 sequences shown in (17) to (23) below. Note that an antibody comprising a heavy chain variable region having the CDR-L1 to L3 sequences shown in (17) to (23) below has not been disclosed or suggested in the prior art and corresponds to a novel anti-gpNMB antibody. (17) As CDR-L1, an amino acid sequence set forth in SEQ ID NO: 183, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 183 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 183; as CDR-L2, an amino acid sequence of SEQ ID NO: 185, or an amino acid sequence in which any one amino acid residue in the amino acid sequence of SEQ ID NO: 185 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 185; As CDR-L3, an amino acid sequence set forth in SEQ ID NO:187, or an amino acid sequence in which any one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO:187 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:187. (18) As CDR-L1, an amino acid sequence set forth in SEQ ID NO: 351, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 351 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 351; as CDR-L2, an amino acid sequence set forth in SEQ ID NO: 352, or an amino acid sequence in which any one amino acid residue in the amino acid sequence set forth in SEQ ID NO: 352 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 352; As CDR-L3, an amino acid sequence set forth in SEQ ID NO:353, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO:353 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:353. (19) As CDR-L1, an amino acid sequence set forth in SEQ ID NO: 358, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 358 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 358; As CDR-L2, an amino acid sequence set forth in SEQ ID NO:359, or an amino acid sequence in which any one amino acid residue in the amino acid sequence set forth in SEQ ID NO:359 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:359; As CDR-L3, an amino acid sequence set forth in SEQ ID NO:360, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO:360 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:360. (20) As CDR-L1, an amino acid sequence set forth in SEQ ID NO: 365, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 365 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 365; As CDR-L2, an amino acid sequence set forth in SEQ ID NO: 366, or an amino acid sequence in which any one amino acid residue in the amino acid sequence set forth in SEQ ID NO: 366 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 366; As CDR-L3, an amino acid sequence set forth in SEQ ID NO:367, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO:367 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:367. (21) As the CDR grafting region-L1, an amino acid sequence set forth in SEQ ID NO: 348, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 348 have been substituted, deleted, or inserted, or an amino acid sequence having 63.6% or more, 72.7% or more, 81.8% or more, or 90.9% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 348; As the CDR grafting region-L2, an amino acid sequence set forth in SEQ ID NO: 349, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 349 have been substituted, deleted, or inserted, or an amino acid sequence having 71.4% or more or 85.7% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 349; As the CDR grafting region-L3, an amino acid sequence set forth in SEQ ID NO:350, or an amino acid sequence in which any one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO:350 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:350. (22) As the CDR grafting region-L1, an amino acid sequence set forth in SEQ ID NO: 355, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 355 have been substituted, deleted, or inserted, or an amino acid sequence having 63.6% or more, 72.7% or more, 81.8% or more, or 90.9% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 355; As the CDR grafting region-L2, an amino acid sequence set forth in SEQ ID NO: 356, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 356 have been substituted, deleted, or inserted, or an amino acid sequence having 71.4% or more or 85.7% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 356; As the CDR grafting region-L3, an amino acid sequence set forth in SEQ ID NO:357, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO:357 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:357. (23) As the CDR grafting region-L1, an amino acid sequence set forth in SEQ ID NO: 362, or an amino acid sequence in which any one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 362 have been substituted, deleted, or inserted, or an amino acid sequence having 63.6% or more, 72.7% or more, 81.8% or more, or 90.9% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 362; As the CDR grafting region-L2, an amino acid sequence set forth in SEQ ID NO: 363, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 363 have been substituted, deleted, or inserted, or an amino acid sequence having 71.4% or more or 85.7% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 363; As the CDR grafting region-L3, an amino acid sequence set forth in SEQ ID NO:364, or an amino acid sequence in which any one, two or three amino acid residues in the amino acid sequence set forth in SEQ ID NO:364 have been substituted, deleted or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:364. One embodiment of the antibody of the present invention is an antibody that combines a heavy chain variable region having any of the above-mentioned CDR-H1 to H3 sequences with a light chain variable region having any of the above-mentioned CDR-L1 to L3 sequences. One embodiment of the antibody of the present invention is an antibody having any one of the following amino acid sequences (a) to (c) as the sequence of the heavy chain variable region. Note that an antibody comprising a heavy chain variable region having the amino acid sequence of SEQ ID NO: 189 among the amino acid sequences of (a) below, or the corresponding amino acid sequence of (b) or (c) below, has not been disclosed or suggested in the prior art, and corresponds to a novel anti-gpNMB antibody. (a) any one of the amino acid sequences selected from SEQ ID NO:13, SEQ ID NO:29, SEQ ID NO:45, SEQ ID NO:61, SEQ ID NO:77, SEQ ID NO:93, SEQ ID NO:109, SEQ ID NO:125, SEQ ID NO:141, SEQ ID NO:157, SEQ ID NO:173, SEQ ID NO:189, and SEQ ID NO:267. (b) An amino acid sequence having at least 60% or more, or 65% or more, or 70% or more, or 75% or more, or 80% or more, or 85% or more, or 90% or more, or 95% or more, or 96% or more, or 97% or more, or 98% or more, or 99% or more homology (preferably identity) with the amino acid sequence of (a). (c) An amino acid sequence in which 1 to 12 (preferably 1 to 11, more preferably 1 to 10, 1 to 9, 1 to 8, 1 to 7, 1 to 6, 1 to 5, 1 to 4, 1 to 3, 1 to 2, or 1) amino acid residues are substituted, deleted, or added in the amino acid sequence of (a). One embodiment of the antibody of the present invention is an antibody (especially a humanized antibody) having any one of the following amino acid sequences (a) to (c) as the sequence of the heavy chain variable region. Note that antibodies (especially humanized antibodies) comprising a heavy chain variable region having the amino acid sequence of SEQ ID NO: 333, SEQ ID NO: 340, or SEQ ID NO: 347 among the amino acid sequences of (a) below, or the corresponding amino acid sequence of (b) or (c) below, have not been disclosed or suggested in the prior art, and are novel anti-gpNMB antibodies (especially humanized antibodies). (a) any one of the amino acid sequences selected from SEQ ID NO:295, SEQ ID NO:323, SEQ ID NO:333, SEQ ID NO:340, and SEQ ID NO:347. (b) An amino acid sequence having at least 60% or more, or 65% or more, or 70% or more, or 75% or more, or 80% or more, or 85% or more, or 90% or more, or 95% or more, or 96% or more, or 97% or more, or 98% or more, or 99% or more homology (preferably identity) with the amino acid sequence of (a). (c) An amino acid sequence in which 1 to 12 (preferably 1 to 11, more preferably 1 to 10, 1 to 9, 1 to 8, 1 to 7, 1 to 6, 1 to 5, 1 to 4, 1 to 3, 1 to 2, or 1) amino acid residues are substituted, deleted, or added in the amino acid sequence of (a). One embodiment of the antibody of the present invention is an antibody having any one of the following (a) to (c) as the sequence of the light chain variable region. Note that an antibody comprising a light chain variable region having the amino acid sequence of SEQ ID NO: 191 among the amino acid sequences of (a) below, or the corresponding amino acid sequence of (b) or (c) below, has not been disclosed or suggested in the prior art, and corresponds to a novel anti-gpNMB antibody. (a) any one of the amino acid sequences selected from SEQ ID NO:15, SEQ ID NO:31, SEQ ID NO:47, SEQ ID NO:63, SEQ ID NO:79, SEQ ID NO:95, SEQ ID NO:111, SEQ ID NO:127, SEQ ID NO:143, SEQ ID NO:159, SEQ ID NO:175, SEQ ID NO:191, and SEQ ID NO:269. (b) An amino acid sequence having at least 60% or more, or 65% or more, or 70% or more, or 75% or more, or 80% or more, or 85% or more, or 90% or more, or 95% or more, or 96% or more, or 97% or more, or 98% or more, or 99% or more homology (preferably identity) with the amino acid sequence of (a). (c) An amino acid sequence in which 1 to 10 (preferably 1 to 9, more preferably 1 to 8, 1 to 7, 1 to 6, 1 to 5, 1 to 4, 1 to 3, 1 to 2, or 1) amino acid residues have been substituted, deleted, or added in the amino acid sequence of (a). One embodiment of the antibody of the present invention is an antibody (especially a humanized antibody) having any one of the following amino acid sequences (a) to (c) as the sequence of the light chain variable region. Note that antibodies (especially humanized antibodies) comprising a light chain variable region having the amino acid sequences of SEQ ID NO: 354, SEQ ID NO: 361, and SEQ ID NO: 368 among the amino acid sequences of (a) below, or the corresponding amino acid sequences of (b) or (c) below, have not been disclosed or suggested in the prior art, and are novel anti-gpNMB antibodies (especially humanized antibodies). (a) any one of the amino acid sequences selected from SEQ ID NO:297, SEQ ID NO:325, SEQ ID NO:354, SEQ ID NO:361, and SEQ ID NO:368. (b) An amino acid sequence having at least 60% or more, or 65% or more, or 70% or more, or 75% or more, or 80% or more, or 85% or more, or 90% or more, or 95% or more, or 96% or more, or 97% or more, or 98% or more, or 99% or more homology (preferably identity) with the amino acid sequence of (a). (c) An amino acid sequence in which 1 to 12 (preferably 1 to 11, more preferably 1 to 10, 1 to 9, 1 to 8, 1 to 7, 1 to 6, 1 to 5, 1 to 4, 1 to 3, 1 to 2, or 1) amino acid residues are substituted, deleted, or added in the amino acid sequence of (a). One embodiment of the antibody of the present invention includes an antibody comprising a combination of any of the above-mentioned heavy chain variable regions and any of the above-mentioned light chain variable regions. Methods for identifying the sequences of CDR-H1, CDR-H2, CDR-H3, CDR-L1, CDR-L2, or CDR-L3 in an antibody include, for example, the Kabat method (NIH Publication, (1991), No. 91-3242) and the Chothia method (J. Mol. Biol., (1997), 273[4]:927-48). These methods are common technical knowledge to those skilled in the art, and an overview of them can be found, for example, on the Internet homepage of Dr. Andrew CR Martin's Group (http: / / www.bioinf.org.uk / abs / ). The CDRs in the present invention are described as Kabat CDRs. Each of the framework sequences of the heavy and light chain variable regions of the immunoglobulin antibody of the present invention is preferably a framework sequence of each class of vertebrate immunoglobulin, particularly preferably a framework sequence of each class of immunoglobulin of human or non-human animal including mouse or rat. By appropriately combining the amino acid sequences of the above-mentioned CDRs and / or variable regions of the heavy and light chains with the amino acid sequences of the framework regions and / or constant regions of the heavy and light chains of antibodies of humans or non-human animals including mice or rats, a person skilled in the art can design the anti-gpNMB-specific antibody of the present invention. In particular, by using the amino acid sequences of the framework regions and / or constant regions of the heavy and light chains of a human antibody, a humanized anti-gpNMB-specific antibody can be obtained. The amino acid sequences of the framework regions and / or constant regions of the heavy and light chains of the humanized antibody can be selected from, for example, human IgG, IgA, IgM, IgE, and IgD classes or variants thereof. There are four subclasses of IgG: IgG1, IgG2, IgG3, and IgG4. When the anti-gpNMB specific antibody of the present invention is a humanized antibody comprising the framework regions and / or constant regions of the heavy and light chains of the human IgG class, the amino acid sequences of the framework regions and / or constant regions of the heavy and light chains of such human IgG may be derived from any of the human IgG1 subclass, human IgG2 subclass, human IgG3 subclass, and human IgG4 subclass. The antibody of the present invention is preferably of IgG class or a variant thereof. The antibody of the present invention is more preferably of human IgG class or a variant thereof, human IgG4 subclass or a variant thereof, or human IgG1 subclass or a variant thereof. In one example, the stabilized IgG4 constant region contains a proline at position 241 of the hinge region according to the Kabat system. This position corresponds to position 228 of the hinge region according to the EU numbering system (Proc. Natl. Acad. Sci. USA, (1969), 63[1]:78-85), sequences of proteins of immunological interest (Washington DC United States Department of Health and Human Services, 2001 and NIH Publication, (1991), No. 91-3242). In human IgG4, this residue is generally serine, and substitution of serine with proline can induce stabilization. In one example, the constant region of IgG1 can incorporate the N297A mutation to minimize its ability to bind Fc receptors and / or fix complement. ・Competitive join: As an embodiment of the present invention, an antibody that competitively binds with the antibody of the present invention for binding to at least one site in the region spanning from V78 to the PKD domain of gpNMB is also included. Such competitively binding antibodies are also included within the scope of the present invention. In the present invention, "competitive binding" refers to a phenomenon in which, when multiple types of monoclonal antibodies coexist with an antigen, the binding of one antibody to the antigen is inhibited by the binding of the other antibody to the antigen. In general, when a fixed amount (concentration) of a monoclonal antibody is added with different amounts (concentrations) of another monoclonal antibody, the amount (concentration) of the monoclonal antibody added at which the binding amount of the former fixed amount of monoclonal antibody to the antigen decreases can be measured. The degree of inhibition is expressed as IC 50 A monoclonal antibody that competitively binds to the antibody of the present invention is, for example, an antibody that has an IC value of 10 nM when competitive antigen-antibody binding to at least one site in the region spanning from V78 to the PKD domain of gpNMB is detected. 50In the case of measuring competitive binding, the antibody to be used may be labeled with an enzyme, a fluorescent substance, a luminescent substance, a radioisotope, or the like, and the antibody may be detected using a measuring method suitable for the physical and / or chemical properties of the labeled substance, or a biosensor such as Surface Plasmon Resonance (SPR) or Bio-Layer Interferometry (BLI) may be used. ・Disease-related cell elimination activity: As described below, the anti-gpNMB antibody of the present invention has the activity of removing various disease-related cells that highly express gpNMB. Therefore, by using such an anti-gpNMB antibody of the present invention, as described below, various disease-related cells can be efficiently removed, and thus various diseases associated with such disease-related cells can be prevented or treated. In addition, preferred characteristics of the antibody of the present invention in the case of assuming the removal of such disease-related cells and the treatment or prevention of diseases via the same are exemplified, but the antibody of the present invention is not limited to those having these characteristics. In addition, in the examples of the present invention, it has been confirmed that some anti-gpNMB antibodies have an activity of inducing a signal via gpNMB by increasing the phosphorylation of ERK1 / 2 (extracellular signal-regulated kinase), S6 (ribosomal protein), and Akt (serine threonine kinase). That is, according to one aspect, an anti-gpNMB antibody having a signal induction activity via gpNMB is provided as the anti-gpNMB antibody of the present invention. Furthermore, according to one embodiment, the anti-gpNMB antibody of the present invention is an anti-gpNMB antibody that does not have gpNMB-mediated signal induction activity. The disease-associated cell elimination activity of the anti-gpNMB antibody of the present invention may be exerted in vivo, ex vivo, or both in vivo and ex vivo. In either case, the activity may be exerted in any subject, but is preferably exerted at least in vertebrates, more preferably in mammals, and particularly preferably in humans or non-human animals. Preferred embodiments of the antibody of the present invention, assuming the removal of such disease-associated cells and the treatment / prevention of diseases mediated thereby, are exemplified below; however, the antibody of the present invention is not limited to those having these characteristics. ・Effector function of antibodies According to one embodiment, the antibody of the present invention preferably has the ability to remove cells involved in pathology. In particular, an antibody having an Fc structure that confers phagocytic ability by phagocytes to remove cells involved in pathology is preferable. On the other hand, a subclass or mutant that does not confer or suppresses the function of inducing inflammation is preferable. However, it is assumed that the way in which the effector function is exerted varies depending on the pathology, the cells to be removed, and the tissue in which it is present, and is not necessarily limited to the above, and it is preferable to confer effector function and strength appropriate for each disease treatment (Non-Patent Document 91). Antibody half-life In one embodiment, the antibody of the present invention can have an increased serum half-life by using previously reported Fc variants, such as the YTE mutation, which can increase the serum half-life of the antibody and reduce the frequency of administration (Non-Patent Document 92). - Antibody passage through the blood-tissue barrier According to one embodiment, the antibody of the present invention can be fused to an anti-transferrin antibody or the like to enhance its migration into tissues isolated from the blood, such as the blood-tissue barrier (BBB) ​​(Non-Patent Document 93). Bispecific antibodies, multivalent antibodies The present inventors have created an anti-gpNMB antibody that has the specificity and binding affinity to produce a bispecific antibody or multivalent antibody with a high therapeutic effect and can eliminate gpNMB-positive cells. That is, in one aspect, the antibody of the present invention can be used to engage and attract T cells, NK cells, macrophages, and the like to various gpNMB-positive disease-related cells (dysfunctional macrophages, senescent cells, cancer cells, cancer-infiltrating cells, and the like), thereby eliminating the disease-related cells (Non-Patent Document 94). ・CAR cells The present inventors have created low molecular weight antibodies such as single chain variable region fragments (single chain Fv: scFv) of anti-gpNMB antibodies that have specificity and binding affinity for producing CAR (chimeric antigen receptor) cells with high therapeutic effects and can eliminate gpNMB-positive cells. That is, according to one embodiment, by producing CAR cells using the antibody of the present invention, T cells, NK cells, macrophages, etc. can be delivered to various gpNMB-positive disease-related cells (dysfunctional macrophages, senescent cells, cancer cells, cancer-infiltrating cells, etc.) to eliminate the disease-related cells (Non-Patent Document 95). In addition, a higher therapeutic effect of CAR cell therapy can be obtained by administering the anti-gpNMB antibody of the present invention in advance as a pretreatment for treatment. [Method of producing anti-gpNMB antibody] The antibody of the present invention can be obtained using techniques well known to those skilled in the art. The antibody of the present invention is a polyclonal antibody or a monoclonal antibody (Nature, (1983), 305(5934): 537-40). For example, a polyclonal antibody can be obtained by intramuscularly or subcutaneously administering to a mammal a human gpNMB protein having the amino acid sequence shown in SEQ ID NO: 209 or a gpNMB partial peptide having a partial amino acid sequence thereof (e.g., a peptide containing a PKD domain consisting of amino acid residues 256 to 319) as an antigen, or an antigen-expressing polynucleotide encoding the amino acid sequence of such a human gpNMB protein or gpNMB partial peptide, to express the antigen in the animal body, thereby sensitizing the animal, and recovering the antibody from the serum of the animal. When a peptide is used as an antigen, the antigen can be used in a form bound to a carrier protein such as BSA or KLH, or polylysine, etc. The non-humanized monoclonal antibody in the present invention can be obtained by sensitizing a mammal by administering human gpNMB protein or a gpNMB partial peptide, or an antigen-expressing polynucleotide encoding such human gpNMB protein or gpNMB partial peptide, and then cloning the hybridoma obtained by extracting immune cells from the mammal and fusing them with myeloma cells, etc., and recovering the hybridoma from the culture. Methods for obtaining such monoclonal antibodies (Nature, (1992), 356

[6365] : 152-4) and cell fusion techniques (Nature, (1975), 256

[5517] : 495-7) have already been reported and are common, and the efficiency of obtaining the monoclonal antibody can be further improved by administering an immunostimulant (Cancer Gene Ther., (2007), 14

[0011] : 904-17). Examples of monoclonal antibodies obtained by such methods include, but are not limited to, the following: Among the following antibodies, an anti-gpNMB monoclonal antibody (GPN18-5) having a heavy chain variable region having the amino acid sequence of SEQ ID NO: 189 and a light chain variable region having the amino acid sequence of SEQ ID NO: 191 has not been disclosed or suggested in the prior art and corresponds to a novel anti-gpNMB antibody (especially a humanized antibody). - An antibody (GPN05-1) having a heavy chain variable region having the amino acid sequence of SEQ ID NO: 13 and a light chain variable region having the amino acid sequence of SEQ ID NO: 15. - An antibody (GPN06-1) having a heavy chain variable region having the amino acid sequence of SEQ ID NO:29 and a light chain variable region having the amino acid sequence of SEQ ID NO:31. - An antibody (GPN07-1) having a heavy chain variable region having the amino acid sequence of SEQ ID NO: 45 and a light chain variable region having the amino acid sequence of SEQ ID NO: 47. - An antibody (GPN11-10) having a heavy chain variable region having the amino acid sequence of SEQ ID NO: 61 and a light chain variable region having the amino acid sequence of SEQ ID NO: 63. - An antibody (GPN15-2) having a heavy chain variable region having the amino acid sequence of SEQ ID NO: 77 and a light chain variable region having the amino acid sequence of SEQ ID NO: 79. - An antibody (GPN15-3) having a heavy chain variable region having the amino acid sequence of SEQ ID NO: 93 and a light chain variable region having the amino acid sequence of SEQ ID NO: 95. - An antibody (GPN18-4) having a heavy chain variable region having the amino acid sequence of SEQ ID NO: 109 and a light chain variable region having the amino acid sequence of SEQ ID NO: 111. - An antibody (GPN18-1) having a heavy chain variable region having the amino acid sequence of SEQ ID NO: 125 and a light chain variable region having the amino acid sequence of SEQ ID NO: 127. - An antibody (GPN18-2) having a heavy chain variable region having the amino acid sequence of SEQ ID NO: 141 and a light chain variable region having the amino acid sequence of SEQ ID NO: 143. - An antibody (GPN18-6) having a heavy chain variable region having the amino acid sequence of SEQ ID NO: 157 and a light chain variable region having the amino acid sequence of SEQ ID NO: 159. - An antibody (GPN18-7) having a heavy chain variable region having the amino acid sequence of SEQ ID NO: 173 and a light chain variable region having the amino acid sequence of SEQ ID NO: 175. - An antibody (GPN18-5) having a heavy chain variable region having the amino acid sequence of SEQ ID NO: 189 and a light chain variable region having the amino acid sequence of SEQ ID NO: 191. - An antibody (GPN09-1) having a heavy chain variable region having the amino acid sequence of SEQ ID NO: 267 and a light chain variable region having the amino acid sequence of SEQ ID NO: 269. In another method, a gene encoding the heavy and / or light chain of an antibody, more specifically a nucleic acid molecule encoding the heavy and / or light chain of an immunoglobulin, is prepared from a hybridoma producing the antibody to be obtained or a phage clone obtained by human antibody phage display. Here, such a nucleic acid molecule may be introduced into various vectors or plasmids to prepare a vector or plasmid containing the nucleic acid molecule. Next, a host cell is transformed with the nucleic acid molecule, vector, or plasmid. Examples of the host cell include eukaryotic cells such as mammalian cells, insect cells, yeast cells, or plant cells, or bacterial cells. Next, the transformed host cell is cultured under appropriate conditions for producing the anti-gpNMB-specific antibody of the present invention. Here, if necessary, the obtained anti-gpNMB-specific antibody of the present invention may be isolated from the host cell. All of the various techniques used in these procedures are well known to those skilled in the art. Here, a person skilled in the art can use known techniques to produce an antibody chimeric protein, a low molecular weight antibody, a scaffold antibody, etc. by genetically modifying a gene encoding an immunoglobulin heavy chain and / or light chain to introduce a desired trait or by using structural information on the variable region or CDR region of an immunoglobulin heavy chain and / or light chain. In addition, for the purpose of improving antibody performance or avoiding side effects, modifications can be made to the structure of the antibody constant region or modifications can be made in the sugar chain portion, as appropriate, using techniques well known to a person skilled in the art. [Humanized antibodies] In one embodiment, the anti-gpNMB antibody of the present invention is a humanized antibody. Hereinafter, the humanized anti-gpNMB antibody of the present invention may be appropriately referred to as the "anti-gpNMB humanized antibody of the present invention" or simply as the "humanized antibody of the present invention." Furthermore, the "anti-gpNMB antibody of the present invention" naturally includes the "anti-gpNMB humanized antibody of the present invention." Humanization of the non-humanized anti-gpNMB antibody of the present invention, that is, production of the humanized anti-gpNMB antibody of the present invention, can be carried out, for example, by the following procedure. That is, based on the amino acid sequence of the non-humanized (e.g., mouse) anti-gpNMB antibody obtained by the above-mentioned various techniques, the CDR region is identified with reference to IMGT (Lefranc, M.-P., Pommie, C., Ruiz, M., Giudicelli, V., Foulquier, E., Truong, L., Thouvenin-Contet, V. and Lefranc, G. "IMGT unique numbering for immunoglobulin and T cell receptor variable domains and Ig superfamily V-like domains". Dev. Comp. Immunol., 27, 55-77 (2003) PMID: 12477501 LIGM:268.) and Kabat numbering. The CDR loop structure is optimally maintained by a combined IMGT / Kabat method. Next, a human antibody frame is selected by the CDR grafting method so as to maintain the CDR loop structure, and an antibody variant is obtained. From the obtained antibody variants, one having the desired binding affinity (e.g., binding affinity to at least one site in the region extending from the PMEL-CAF-like domain to the PKD domain of gpNMB) can be selected to obtain a humanized antibody. Specifically, one human germline gene that is most similar to the amino acid sequences of the heavy and light chain variable regions of the non-humanized (e.g., mouse) anti-gpNMB antibody obtained by the above-mentioned various techniques is selected. Meanwhile, about 200 types of human IgG sequences that are highly homologous to the heavy and light chain variable regions are selected as candidates using a BLAST search. Then, for example, four types of framework sequences are selected from the viewpoints of framework homology, retention of key amino acids in the framework, loop structure, etc. CDR grafting is performed on them to obtain four types of humanized variants. In addition, CDR grafting is performed using a human germline sequence as a framework to obtain one type of humanized variant. The five types of humanized heavy and light chain variants obtained are combined to express and purify 25 types of humanized antibody variants, and their binding activity is evaluated. A humanized antibody can be obtained by selecting one that has a predetermined binding affinity (e.g., three times or one-third) in an activity comparison by SPR with a human chimeric antibody having mouse heavy and light chains of the parent antibody. As another example, an anti-gpNMB antibody that recognizes at least one portion of the region extending from the PMEL-CAF-like domain to the PKD domain recognized by the anti-gpNMB antibody disclosed in the present specification can be obtained directly from a human antibody-producing mouse or a human antibody phagemid library. Humanized anti-gpNMB monoclonal antibodies obtained by such a method include, but are not limited to, the following: Among the following antibodies, a humanized anti-gpNMB monoclonal antibody (hGPN18-5_H1-H3, L1-L3) having a heavy chain variable region having the amino acid sequence of SEQ ID NO: 333, SEQ ID NO: 340, or SEQ ID NO: 347 and a light chain variable region having the amino acid sequence of SEQ ID NO: 354, SEQ ID NO: 361, or SEQ ID NO: 368 has not been disclosed or suggested in the prior art and corresponds to a novel anti-gpNMB antibody (especially a humanized antibody). - An antibody (hGPN06-1_H1L1) having a heavy chain variable region having the amino acid sequence of SEQ ID NO:295 and a light chain variable region having the amino acid sequence of SEQ ID NO:297. - An antibody (hGPN18-2_H2L3) having a heavy chain variable region having the amino acid sequence of SEQ ID NO: 323 and a light chain variable region having the amino acid sequence of SEQ ID NO: 325. - An antibody (hGPN18-5_H1L1) having a heavy chain variable region having the amino acid sequence of SEQ ID NO: 333 and a light chain variable region having the amino acid sequence of SEQ ID NO: 354. - An antibody (hGPN18-5_H1L2) having a heavy chain variable region having the amino acid sequence of SEQ ID NO: 333 and a light chain variable region having the amino acid sequence of SEQ ID NO: 361. - An antibody (hGPN18-5_H1L3) having a heavy chain variable region having the amino acid sequence of SEQ ID NO: 333 and a light chain variable region having the amino acid sequence of SEQ ID NO: 368. - An antibody (hGPN18-5_H2L1) having a heavy chain variable region having the amino acid sequence of SEQ ID NO: 340 and a light chain variable region having the amino acid sequence of SEQ ID NO: 354. - An antibody (hGPN18-5_H2L2) having a heavy chain variable region having the amino acid sequence of SEQ ID NO: 340 and a light chain variable region having the amino acid sequence of SEQ ID NO: 361. - An antibody (hGPN18-5_H2L3) having a heavy chain variable region having the amino acid sequence of SEQ ID NO: 340 and a light chain variable region having the amino acid sequence of SEQ ID NO: 368. - An antibody (hGPN18-5_H3L1) having a heavy chain variable region having the amino acid sequence of SEQ ID NO: 347 and a light chain variable region having the amino acid sequence of SEQ ID NO: 354. - An antibody (hGPN18-5_H3L2) having a heavy chain variable region having the amino acid sequence of SEQ ID NO: 347 and a light chain variable region having the amino acid sequence of SEQ ID NO: 361. - An antibody (hGPN18-5_H3L3) having a heavy chain variable region having the amino acid sequence of SEQ ID NO: 347 and a light chain variable region having the amino acid sequence of SEQ ID NO: 368. Pharmaceutical Compositions One aspect of the present invention relates to a pharmaceutical composition for removing disease-related cells, which comprises the anti-gpNMB-specific antibody of the present invention as an active ingredient (hereinafter, collectively referred to as "pharmaceutical composition of the present invention" as appropriate). That is, by using the anti-gpNMB antibody of the present invention as an active ingredient, the pharmaceutical composition of the present invention can remove various disease-related cells. Therefore, the pharmaceutical composition of the present invention can be used for the treatment and prevention of various diseases. Disease-related cells that can be removed by the anti-gpNMB antibody of the present invention include, but are not limited to, senescent cells, cancer-related cells, phagocytes, and the like. As described above, senescent cells refer to cells in which the cessation of sustained cell proliferation has been induced by DNA damage, activation of cancer genes, stress, and the like. In recent years, it has been revealed that senescent cells acquire a proinflammatory phenotype called SASP (Senescence-associated secretory phenotype), and it has been suggested that senescent cells are involved in many diseases (Non-Patent Document 1). While cellular senescence is considered to be a mechanism for preventing damaged cells from undergoing malignant transformation and becoming cancerous, many findings have been reported that cellular senescence is involved in various age-related pathologies (tissue degeneration, chronic inflammation, cancer progression, etc.). In addition, examples of particularly highly malignant senescent cells include senescent infiltrating cells and resident senescent cells, which have a significant effect on surrounding cells and tissues to form or progress pathologies. Cancer-related cells include cancer cells, cancer stem cells, cancer precursor cells, cancer infiltrating cells, etc. Cancer infiltrating cells include cancer infiltrating macrophages, cancer infiltrating microglia, myeloid-derived suppressor cells (MDSCs), cancer infiltrating dendritic cells, etc. Examples of phagocytes include, but are not limited to, macrophages, microglia, dendritic cells, monocytes, Kupffer cells, Langerhans cells, osteoclasts, etc. Examples of macrophages include cancer-infiltrating macrophages, aging macrophages, fat-accumulating macrophages, sphingomyelin-accumulating macrophages, foam cells, alveolar macrophages, peritoneal macrophages, splenic macrophages, thymic macrophages, etc. Examples of microglia include cancer-infiltrating microglia, aging microglia, fat-accumulating microglia, sphingomyelin-accumulating microglia, etc. Dendritic cells include subtypes such as standard type 1 dendritic cells (cDC1), standard type 2 dendritic cells (cDC2), monocyte-derived dendritic cells (MoDC), and plasmacytoid dendritic cells (pDC). Diseases involving disease-involved cells that are removed by the pharmaceutical composition of the present invention include, but are not limited to, obesity / metabolic diseases (e.g., diabetes, fibrosis, etc.), circulatory system diseases (e.g., cardiomyopathy, arteriosclerosis, etc.), lysosomal stress-related diseases (e.g., lysosomal diseases, etc.), autoimmune diseases (e.g., multiple sclerosis, etc.), cancers (TNBC (Triple Negative Breast Cancer), melanoma, non-small cell lung cancer, glioblastoma, etc.), etc. The pharmaceutical composition of the present invention may be formulated in the form of a pharmaceutical composition containing, in addition to the anti-gpNMB specific antibody of the present invention as an active ingredient, a pharma- ceutical carrier and / or other additives. Formulation using a pharma- ceutical carrier and / or other additives can be carried out, for example, by the method described in University of the Sciences in Philadelphia, "Remington: The Science and Practice of Pharmacy, 20th EDITION", Lippincott Williams & Wilkins, (2000). One form of such a therapeutic or preventive agent is provided as a liquid preparation or a lyophilized preparation prepared by dissolving, suspending, or emulsifying in a sterile aqueous or oily liquid. Examples of such a solvent or dissolving solution include aqueous solutions such as distilled water for injection and physiological saline, and when an osmotic pressure regulator (e.g., D-glucose, D-sorbitol, D-mannitol, sodium chloride, etc.) is added, a suitable solubilizing agent such as alcohol (e.g., ethanol), polyalcohol (e.g., propylene glycol, polyethylene glycol), nonionic surfactant (e.g., polysorbate 80, polyoxyethylene hydrogenated castor oil 50), etc. may be used in combination. In addition, an oily liquid may be used as the solvent or dissolving solution, and examples of the oily liquid include sesame oil and soybean oil, and a solubilizing agent such as benzyl benzoate or benzyl alcohol may be used in combination. In such preparations, additives such as buffers (e.g., phosphate buffers, acetate buffers), soothing agents (e.g., benzalkonium chloride, procaine hydrochloride, etc.), stabilizers (e.g., human serum albumin, polyethylene glycol, etc.), preservatives (e.g., ascorbic acid, erythorbic acid, and salts thereof, etc.), colorants (e.g., copper chlorophyll, β-carotene, Red No. 2, Blue No. 1, etc.), preservatives (e.g., paraoxybenzoic acid esters, phenol, benzethonium chloride, benzalkonium chloride, etc.), thickeners (e.g., hydroxypropylcellulose, carboxymethylcellulose, and salts thereof, etc.), stabilizers (e.g., human serum albumin, mannitol, sorbitol, etc.), and odorants (e.g., menthol, citrus flavors, etc.) may be used as appropriate. In addition, other forms of therapeutic or preventive agents include solid preparations such as powders, tablets, granules, capsules, pills, suppositories, and troches. In the case of solid preparations administered in the form of oral preparations, additives such as excipients (e.g., crystalline cellulose, lactose, starch, etc.), lubricants (e.g., magnesium stearate, talc, etc.), binders (e.g., hydroxypropylcellulose, hydroxypropylmethylcellulose, macrogol, etc.), disintegrants (e.g., starch, carboxymethylcellulose calcium, etc.) are used. In addition, additives such as preservatives (e.g., benzyl alcohol, chlorobutanol, methyl parahydroxybenzoate, propyl parahydroxybenzoate, etc.), antioxidants, colorants, and sweeteners can be used as necessary. Further examples of the form include therapeutic or preventive agents for application to mucosa, and these preparations may contain additives such as adhesives, adhesion enhancers, thickeners, and viscosifiers (e.g., mucin, agar, gelatin, pectin, carrageenan, sodium alginate, locust bean gum, xanthan gum, tragacanth gum, gum arabic, chitosan, pullulan, waxy starch, sucralfate, cellulose, and derivatives thereof) for the main purpose of imparting adsorption and retention to the mucosa. However, the form, solvent, and additives of the therapeutic or preventive agent administered to the living body are not limited to these and can be appropriately selected by a person skilled in the art. The pharmaceutical composition of the present invention may contain other existing drugs (active ingredients) in addition to the anti-gpNMB specific antibody of the present invention, which is the active ingredient. Such other existing drugs (active ingredients) include, but are not limited to, various central nervous system disease therapeutic drugs, neurodegenerative disease therapeutic drugs, neurofunction recovery drugs, Alzheimer's disease therapeutic drugs, etc. Specific examples thereof include anti-Tau antibodies, anti-amyloid β antibodies, anti-CD33 antibodies, anti-semaphorin 4D antibodies, anti-TNFα antibodies, anti-sortilin antibodies, anti-galactose specific lectin (galectin) 3 antibodies, anti-TREM2 (Triggering receptor expressed on myeloid cells 2) antibodies, etc. These may be used alone or in combination of two or more types. The pharmaceutical composition of the present invention may be combined with other existing drugs to form a kit. The active ingredient to be combined with the anti-gpNMB specific antibody of the present invention may also be the drug (active ingredient) described above for the combination drug. The dose of the drug other than the anti-gpNMB specific antibody used in these combination drugs or kits may be the dose used in normal treatment, but may be increased or decreased depending on the situation. The pharmaceutical composition of the present invention can be administered parenterally for the purpose of improving symptoms. In the case of parenteral administration, for example, it can be a nasal preparation, and liquid preparations, suspensions, solid preparations, etc. can be selected. Another form of parenteral administration can be an injection, and the injection can be a subcutaneous injection, an intravenous injection, a drip injection, an intramuscular injection, an intraventricular injection, or an intraperitoneal injection. In addition, other preparations used for parenteral administration include suppositories, sublingual preparations, transdermal preparations, transnasal preparations, and other mucosal preparations. Furthermore, it can be locally administered intravascularly by being contained in or applied to a stent or intravascular embolization agent. In some cases, it can be administered in the form of DNA or RNA encoding the antibody, or even cells or resident bacteria that produce the antibody. The dosage of the pharmaceutical composition of the present invention varies depending on the age, sex, weight, symptoms, therapeutic effect, administration method, treatment time, or the type of active ingredient contained in the pharmaceutical composition, but usually, the main agent can be administered to an adult in a range of 0.1 mg to 1 g, preferably 0.5 mg to 300 mg, once every 1 to 4 weeks, or once every 1 to 6 months. However, since the dosage and frequency of administration vary depending on various conditions, there are cases where a dosage and frequency less than the above-mentioned dosage and frequency are sufficient, and there are also cases where a dosage and frequency exceeding the above-mentioned range are required. In addition, the therapeutic or prophylactic agent of the present invention can obtain an effect in a short administration period or can be administered for a long period by reducing side effects. The subjects to which the pharmaceutical composition of the present invention is administered are not limited, but typically include humans or non-human animals (e.g., dogs, cats, cows, horses, sheep, pigs, etc.). Among these, administration to humans is preferred. [Disease treatment and prevention] According to the pharmaceutical composition of the present invention, it is possible to treat or prevent various diseases by removing disease-related cells involved in various diseases through the action of the anti-gpNMB antibody of the present invention. Examples of the treatment and prevention of several specific diseases are described below, but the diseases that can be treated and prevented by the pharmaceutical composition of the present invention are not limited to these, and the pharmaceutical composition of the present invention can be applied to the treatment and prevention of the various diseases exemplified above. ・Treatment and prevention of obesity, diabetes, and arteriosclerosis: By using the anti-gpNMB antibody of the present invention, obesity, diabetes and arteriosclerosis can be treated. Specifically, by administering the antibody of the present invention to wild-type mice or ApoE-KO mice loaded with a high-fat diet, gpNMB-positive fat-accumulating macrophages can be reduced, and arteriosclerosis can be improved. Furthermore, insulin resistance can be improved, weight gain can be suppressed, and fat accumulation can be reduced. Similarly, fatty liver can be improved. ・Treatment and prevention of fibrosis: It is believed that gpNMB-positive macrophages present in fibrotic tissues induce collagen production enhancement or collagen production enhancement cells, and the anti-gpNMB antibody of the present invention having the activity of removing gpNMB-positive cells can be administered to fibrosis model mice to remove gpNMB-positive macrophages in tissues and improve fibrotic conditions in various organs. Specifically, fibrosis of organs can be suppressed by administering anti-gpNMB antibodies to fibrosis models such as bleomycin model, silica model, UUO renal fibrosis model, and liver fibrosis model. In addition, in DMD model animals, gpNMB-positive cells in skeletal muscle tissues can be removed by administering the antibody of the present invention, thereby suppressing muscle fibrosis and improving muscle quality. ・Cancer treatment and prevention: By administering the antibody of the present invention, it is possible to remove immunosuppressive macrophages, microglia, dendritic cells, myeloid-derived suppressor cells (MDSCs), etc. that have infiltrated into cancer cells, thereby suppressing the proliferation of cancer cells and improving their survival period and survival rate. Furthermore, by administering the antibody before or in combination with other conventional cancer treatments, it is possible to enhance the therapeutic effects of anticancer drugs, cancer targeted therapeutic drugs, immune checkpoint inhibitors, CAR cell therapy, and the like. For example, in a melanoma-implanted mouse model, administration of the antibody of the present invention can remove macrophages that have infiltrated into cancer cells, thereby suppressing the proliferation of cancer cells and improving the survival time and survival rate. Furthermore, by combining the antibody of the present invention with an anticancer drug or an immune checkpoint inhibitor, the survival time and survival rate can be further improved. Treatment of glioblastoma: In a syngenic mouse model in which a glioblastoma is transplanted into the brain, administration of the antibody of the present invention can remove immunosuppressive microglia, macrophages, etc. that have infiltrated into the glioblastoma, inhibit the proliferation of the glioblastoma, and improve the survival time and survival rate. Furthermore, by combining the antibody of the present invention with an anticancer drug such as temozolomide or an immune checkpoint inhibitor, the survival time and survival rate can be further improved. ・Treatment of age-related diseases: Accumulation of senescent cells induces various diseases and accelerates the progression of the pathology. By using the anti-gpNMB antibody of the present invention, it is possible to specifically remove senescent cells, which are the main cause of the disease, and it is possible to treat and suppress the progression of various diseases as a senescent cell removal drug with few side effects. For example, specifically, by administering the antibody to a high-fat diet-loaded model mouse in which aging is accelerated and senescent cells are accumulated, chronic inflammatory pathology is improved, and insulin resistance, fat accumulation, organ fibrosis, arteriosclerosis, etc. are suppressed. In addition, in the treatment of various diseases accompanied by chronic inflammation, the therapeutic effect of the original drug can be enhanced by pre-administration or concomitant use of the antibody. ・Treatment of lysosomal stress diseases: In lysosomal stress diseases, where cellular functions decline and pathology develops due to the accumulation of sugars, glycolipids, proteins, etc. in lysosomes caused by the deficiency or reduced activity of various lysosomal enzymes, a certain degree of therapeutic effect is expected by removing dysfunctional senescent cells. Specifically, by using model mice with reduced or deficient lysosomal enzyme activity and administering this antibody, senescent cells are removed, inflammation is reduced, and the condition is expected to improve. [others] As described above, the anti-gpNMB specific antibody of the present invention has the activity of removing various disease-related cells when administered to a subject such as a human. Based on such activity, the anti-gpNMB specific antibody of the present invention can be used for treating or preventing various diseases. Therefore, in addition to the above-mentioned pharmaceutical composition of the present invention, the subject of the present invention can include, for example, the following several aspects. That is, one aspect of the present invention relates to a method for removing various disease-related cells in a subject, which comprises administering an effective amount of an anti-gpNMB specific antibody of the present invention to a subject in need thereof. Another aspect of the present invention relates to a method for treating or preventing various diseases in a subject by removing various disease-related cells in the subject, which comprises administering an effective amount of an anti-gpNMB specific antibody of the present invention to a subject in need thereof. Details of such a method using the antibody of the present invention are as described above. One aspect of the present invention relates to an anti-gpNMB specific antibody of the present invention for use in removing various disease-related cells in a subject. Another aspect of the present invention relates to an anti-gpNMB specific antibody of the present invention for use in treating or preventing various diseases by removing various disease-related cells in a subject. Details of the antibody of the present invention used for such specific purposes are as described above. One aspect of the present invention relates to the use of an anti-gpNMB specific antibody of the present invention in the manufacture of a medicament for the purpose of removing various disease-related cells in a subject. Another aspect of the present invention relates to the use of an anti-gpNMB specific antibody of the present invention in the manufacture of a medicament for the purpose of treating or preventing various diseases in a subject by removing various disease-related cells. Details of the antibodies used in the manufacture of such medicaments for specific uses are as described above. In addition, the anti-gpNMB specific antibody of the present invention can be used for various applications. For example, the anti-gpNMB specific antibody of the present invention can be used as an Immuno-PET probe for image diagnosis of where and how many gpNMB-positive disease-related cells are present in the body. Furthermore, the anti-gpNMB specific antibody of the present invention can be used alone or in combination of two or more types to measure a specific gpNMB fragment, and can be used to select a patient group suitable for antibody treatment, to evaluate the effectiveness of treatment, and the like. The present invention will be described in more detail below with reference to examples. However, these examples are merely illustrative and are not intended to limit the present invention in any way. [Standard procedure] Antigen ELISA (Enzyme-Linked Immunosorbent Assay): Recombinant soluble human or mouse gpNMB was diluted with PBS to adjust to 2 μg / mL, added to a 96-well plate (Nunc, MaxiSorp) at 50 μL / well, and allowed to stand overnight at 4° C. This 96-well plate was blocked with 3% BSA / PBS and used as a recombinant soluble gpNMB-immobilized 96-well plate for ELISA. Anti-gpNMB antibody-containing hybridoma culture supernatant or 3% BSA / PBS solution was added to the above recombinant soluble gpNMB-immobilized 96-well plate at 30 μL / well and reacted at room temperature for 1 hour. After washing with a washing solution (TBS-T: Tris Buffered Saline, 0.025% Tween (registered trademark) 20), an antibody that reacts with all isotypes of mouse IgG, anti-mouse IgG antibody-ALP conjugate (SBA, 1050-04), was diluted 1000-fold with 3% BSA / PBS and added at 30 μL / well and reacted at room temperature for 1 hour. A substrate (PNPP (p-nitrophenyl phosphate), 1 mg / mL) solution was added at 100 μL / well and reacted at room temperature for 1 hour, and the absorbance at 405 to 550 nm was calculated. The obtained absorbance value was evaluated as binding activity. ・Cell-based ELISA: gpNMB expressing cells were seeded on a polylysine-coated 96-well plate, allowed to adhere, and then the culture supernatant was removed, followed by fixation with a 10% formalin-containing solution at room temperature for 10 minutes, followed by blocking with a 3% BSA / PBS solution, and storage in a refrigerator. The blocking solution of the obtained cell fixation plate was removed, and the antibody-containing medium or solution was added at 30 μL / well and incubated at room temperature for about 1 hour to 1 hour and 30 minutes. Then, washing was performed 2 to 4 times with washing solution (TBS-T), a 10,000-fold diluted solution of anti-mouse IgG-HRP-labeled secondary antibody was added, and incubation was performed at room temperature for 1 hour. Then, washing was performed 2 to 4 times with washing solution (TBS-T), and a substrate TMB solution was added at 50 μL / well and incubated at room temperature for 30 minutes. Then, 1N sulfuric acid was added at 50 μL / well to stop the reaction, and the absorbance at 450 to 650 nm was calculated. The obtained absorbance value was evaluated as binding activity. Antibody-dependent cellular phagocytosis (ADCP) assay: AZAMI-GREEN fusion mouse gpNMB expressing cells or AZAMI-GREEN fusion human gpNMB expressing cells were seeded in a 96-well plate (IWAKI, EZ-VIEW), suspended in anti-gpNMB antibody-containing medium, and incubated at 37°C, 5% CO in a total of 80 μL / well.２ The mixture was incubated at 37° C. for 2 hours. Then, 20 μL of phagocytes was added and incubated at 37° C. for 2 hours. ２ The cells were incubated at 4° C. for 0 to 12 days. The fluorescence intensity of AZAMI-GREEN was measured under a fluorescence microscope, and the decrease in fluorescence was evaluated as the cell elimination effect. [Example 1] Preparation and screening of mouse or rat monoclonal antibodies (antigen ELISA and cell ELISA): Mouse or rat monoclonal antibodies may be produced by the hybridoma method described in Koehler et al., Nature, (1975), 256:495-497, etc. Anti-gpNMB antibodies were produced by inducing immunity in mice or rats using a nucleic acid, protein, or peptide containing the full length or a part of the amino acid sequence (SEQ ID NO: 209) or nucleic acid sequence (SEQ ID NO: 210) of human gpNMB (isotype a), or the amino acid sequence (SEQ ID NO: 211) or nucleic acid sequence (SEQ ID NO: 212) of mouse gpNMB, and collecting lymphocyte cells from mice or rats with elevated antibody titers. All animal experiments were performed in accordance with the regulations of the facility. Hybridomas were produced by fusing lymphocyte cells collected from mice or rats with mouse myeloma cell lines (P3U1 (P3X63Ag8U.1) or SP2 / 0 (SP2 / 0-Ag14)) using standard hybridoma techniques. Hybridomas were selected using so-called HAT medium containing hypoxanthine, aminopterin, and thymidine. An alignment of the amino acid sequences of human gpNMB (isotype a) (SEQ ID NO: 209) and mouse gpNMB (SEQ ID NO: 211) is shown in FIG. 1. In the figure, the region from valine (V78) at amino acid residue position 78 to the PKD domain is shown surrounded by a dashed line. As an example of the PKD domain, the region from amino acid residue positions 256 to 319 is shown surrounded by a dotted line. As an example of the PMEL-CAF-like domain, the region from amino acid residue positions 172 to 246 is shown surrounded by a solid line. Using the culture medium of the obtained hybridoma, binding evaluation was performed by antigen ELISA using immobilized recombinant human soluble gpNMB (SEQ ID NO: 221) or mouse soluble gpNMB (SEQ ID NO: 223), and cell ELISA using cells expressing a protein containing human gpNMB (SEQ ID NO: 209), and positive hybridoma-containing wells were selected. The hybridomas contained in these wells were single-cloned by limiting dilution. The single-cloned positive hybridomas were cultured, and monoclonal antibodies were purified from the culture medium using a protein A column (Ab-Capcher, Protenova), to obtain multiple anti-gpNMB antibodies. Example 2: Determination of antibody sequence: In order to determine the gene sequences of the light and heavy chains of each of the anti-gpNMB antibody clones obtained in Example 1, SMARTer （登録商標） The RACE method was performed. Gene fragments of the heavy and light chains of the antibody, including the initiation and termination codons, were extracted from RNA derived from the hybridoma producing the antibody using SMARTer. （登録商標） The DNA was isolated by the RACE method and its base sequence was determined. （登録商標） First strand cDNA was synthesized using the RACE 5' / 3' Kit (634859, Clontech), and the cDNA was then amplified by PCR. Using the cDNA as a template, PCR was performed using a primer for the universal sequence included in the kit and primers specific to the heavy and light chains of the antibody. The resulting PCR product was used as a 5'RACE PCR product for TA cloning. Regarding the sequencing of the rat monoclonal antibody gene, PCR was carried out on the variable regions of the heavy and light chains of the rat antibody, and the resulting PCR fragment was bound to the mouse constant region to produce a mouse chimeric antibody, which was then sequenced. In TA cloning, the 5'RACE PCR product was electrophoresed and a cDNA fragment containing the desired molecular weight was purified using QIAEX II Gel Extraction Kit (20021, Qiagen). The purified cDNA was reacted with TaKaRa-Taq (R001A, Takara) at 72°C for 5 minutes to add adenine to the 3' end. The cDNA fragment was cloned into pMD20-T vector (hereinafter, MD20 vector) using Mighty TA-cloning Kit (6028, Takara) according to the attached protocol. The MD20 vector into which the desired cDNA was cloned was transformed into E. coli TOP10 and cultured on an agar medium containing 100 μg / mL ampicillin. The insertion of the desired cDNA fragment into the MD20 vector was confirmed by colony PCR. The nucleotide sequence of the cloned cDNA fragment was identified. Similarly, the nucleotide sequence of the 3' RACE PCR product was identified, and the full-length sequence of each antibody gene was determined. Of the anti-gpNMB antibody clones obtained in Example 1, for GPN05-1, GPN06-1, GPN07-1, GPN09-1, GPN11-10, GPN15-2, GPN15-3, GPN18-1, GPN18-2, GPN18-4, GPN18-5, GPN18-6, GPN18-7, and 1-5E, the amino acid sequences and base sequence sequence numbers of the heavy chain and light chain variable regions (VH and VL, respectively) and the complementarity determining regions contained therein (CDR-H1 to H3 and CDR-L1 to L3, respectively) determined by the above-mentioned procedures are shown in Tables 1-1 to 1-5. [Example 3] Analysis of binding sites of anti-gpNMB antibodies (antigen ELISA): In order to analyze the binding site of each of the anti-gpNMB antibodies obtained in Example 1 on human gpNMB protein, the following experiment was carried out. First, based on the amino acid sequence of the human gpNMB extracellular domain (SEQ ID NO: 215; in this amino acid sequence, the amino acid residues at positions 1 to 21 constitute a signal peptide, and the amino acid residues at positions 22 and onward constitute an isolated peptide of the human gpNMB extracellular domain), an N-terminal deletion mutant (hgpNMB_d07_76-498) and a C-terminal deletion mutant (hgpNMB_ hgpNMB_d03_1-251, hgpNMB_d04_1-321, hgpNMB_d05_1-375, hgpNMB_d06_1-418, hgpNMB_d13_1-412, hgpNMB_d14_1-406, hgpNMB_d15_1-400, hgpNMB_d16_1-394, hgpNMB_d17_1-388, hgpNMB_d18_1-382, and hgpNMB_d19_1-234) were prepared. The purified gpNMB protein was prepared by inserting the gpNMB gene into a transient animal cell expression vector and expressing the protein in a medium using an Expi293 Expression System (A14635, Thermo Fisher Scientific).Then, the protein was affinity purified with Ni-NTA agarose (143-09763, FUJIFILM Wako) using a histidine tag added to the C-terminus to obtain a purified protein. Next, 17 nmol / L of purified recombinant human soluble gpNMB (SEQ ID NO: 221), the N-terminal deletion mutants (hgpNMB_d07_76-498) and the C-terminal deletion mutants (hgpNMB_d03_1-251, hgpNMB_d04_1-321, hgpNMB_d05_1-375, hgpNMB_d06_1-41) of the extracellular domain of human gpNMB shown in Table 2 were added to a 96-well plate for ELISA. 8, hgpNMB_d13_1-412, hgpNMB_d14_1-406, hgpNMB_d15_1-400, hgpNMB_d16_1-394, hgpNMB_d17_1-388, hgpNMB_d18_1-382, and hgpNMB_d19_1-234), and purified recombinant mouse soluble gpNMB (SEQ ID NO: 223) were added at 100 μL / well and left at room temperature for 90 minutes. After that, blocking was performed with 3% BSA / PBS to prepare an antigen ELISA plate. The blocking solution of the antigen ELISA plate was removed, and anti-gpNMB antibody dilution solution (3% BSA / PBS solution) was added at 50 μL / well and reacted at room temperature for 1 hour. After washing with a washing solution, an antibody that specifically reacts with mouse IgG, anti-mouse IgG antibody-ALP conjugate (SBA, 1050-04), was added at 50 μL / well and reacted at room temperature for 1 hour. A substrate (PNPP) was added at 100 μL / well and reacted at room temperature for 1 hour, and the absorbance at 405 to 550 nm was calculated. The obtained absorbance value was evaluated as binding activity. [Example 4] Determination of epitopes of anti-gpNMB antibodies (antigen ELISA): In order to determine the epitopes of each of the anti-gpNMB antibodies obtained in Example 1 on gpNMB, the following experiment was carried out. First, the C-terminal deletion mutant (hgpNMB_d19_1-234) and point mutants (hgpNMB_d22_K245A, hgpNMB_d23_D252A, hgpNMB_d24_E253A, hgpNMB_d25_D264A, hgpNMB_d26_H272A, hgpNMB_d28_H297A, hgpNMB_d30_H376A) of the extracellular domain of human gpNMB shown in Table 3 below were used. , hgpNMB_d31_D247A_R248A, hgpNMB_d34_D287A, hgpNMB_d35_H301A, hgpNMB_d36_R331A_K334A, hgpNMB_d37_K344A_D347A, hgpNMB_d38_D356A, hgpNMB_d39_E360A, hgpNMB_d40_E367A, and hgpNMB_d41_R373A) were prepared. The purified gpNMB protein was prepared by preparing a transient animal cell expression vector into which the gpNMB gene was inserted, and expressing the protein in the medium using an Expi293 Expression System (A14635, Thermo Fisher Scientific). The protein was then affinity-purified using a histidine tag added to the C-terminus with Ni-NTA agarose (143-09763, FUJIFILM Wako) to obtain a purified protein. The outline of the C-terminal deletion mutants and point mutants of the human gpNMB extracellular domain is shown in Table 3. Using these alanine point mutants of the human gpNMB extracellular domain, antigen ELISA analysis was performed in the same manner as in Example 4 to evaluate the binding ability of each anti-gpNMB antibody. Specifically, each of the C-terminal deletion mutants and alanine point mutants of the human gpNMB extracellular domain shown in Table 2 above was added to a 96-well ELISA plate at a concentration of 17 nmol / L at 100 μL / well and allowed to stand at room temperature for 90 minutes. Thereafter, blocking was performed with 3% BSA / PBS to prepare an antigen ELISA plate. The blocking solution of the antigen ELISA plate was removed, and anti-gpNMB antibody dilution solution (3% BSA / PBS solution) was added at 50 μL / well and reacted at room temperature for 1 hour. After washing with a washing solution, an antibody that specifically reacts with mouse IgG, anti-mouse IgG antibody-ALP conjugate (SBA, 1050-04), was added at 50 μL / well and reacted at room temperature for 1 hour. A substrate (PNPP) was added at 100 μL / well and reacted at room temperature for 1 hour, and the absorbance at 405 to 550 nm was calculated. The obtained absorbance value was evaluated as binding activity. In the absorbance at 2 nM concentration, a mutant whose absorbance was reduced by 50% or more compared to the mutant that showed the maximum absorbance was described as +, and a mutant that showed an absorbance of 50% or more was described as -. The results are shown in Table 4 below. Furthermore, binding to alanine point mutants of the N-terminal human gpNMB extracellular domain was analyzed by antigen ELISA in the same manner using anti-gpNMB antibodies bound to a C-terminal deletion mutant (hgpNMB_d19_1-234) of the human gpNMB extracellular domain. First, the C-terminal deletion mutant (hgpNMB_d19_1-234) and point mutants (hgpNMB_d19_1-234, hgpNMB_d43_1-234_R77A, hgpNMB_d44_1-234_D85A, hgpNMB_d45_1-234_R104A, hgpNMB_d47_1-234_E117A,K118A, hgpNMB_d48_1-234_R121A,E123A, hgpNMB_d49_1-234_D129A, hgpNMB_d50_1-234_E140A,D150A,D160A,D170A,D180A,D190A,D200A,D210A,D220A,D310A,D320A,D430A,D440A,D85A,D450A,D104A,D170A,D220A,D320A,D430A,D440A,D85A,D450A,D104A,D170A,D220A,D320A,D430A,D440A,D85A,D450A,D104A,D170A,D180A,D220A,D320A,D43 ... 141A, hgpNMB_d51_1-234_D143A, E145A, hgpNMB_d52_1-234_H152A, H153A , hgpNMB_d53_1-234_D158A, K160A, hgpNMB_d54_1-234_H164A, H165A, hgpN The following recombinant proteins were prepared: hgpNMB_d55_1-234_R169A, hgpNMB_d58_1-234_R189A, hgpNMB_d59_1-234_R193A, hgpNMB_d61_1-234_R214A, R215A, and hgpNMB_d64_1-234_D109A. The purified gpNMB protein was expressed in the medium using an Expi293 Expression System (A14635, Thermo Fisher Scientific) after preparing a transient animal cell expression vector into which the gpNMB gene was inserted. The purified protein was then affinity purified using Ni-NTA agarose (143-09763, FUJIFILM Wako) using the histidine tag added to the C-terminus. The C-terminal deletion mutants and point mutants of the human gpNMB extracellular domain are summarized in Table 5 below. Using these human gpNMB extracellular domain alanine point mutants, antigen ELISA analysis was performed in the same manner as in Example 4 to evaluate the binding ability of each anti-gpNMB antibody. Specifically, the C-terminal deletion mutants and each gpNMB alanine point mutant shown in Table 5 above were added to a 96-well ELISA plate at a concentration of 17 nmol / L at 100 μL / well and allowed to stand at room temperature for 90 minutes. Thereafter, blocking was performed with 3% BSA / PBS to prepare an antigen ELISA plate. The blocking solution of the antigen ELISA plate was removed, and anti-gpNMB antibody dilution solution (3% BSA / PBS solution) was added at 50 μL / well and reacted at room temperature for 1 hour. After washing with a washing solution, an antibody that specifically reacts with mouse IgG, anti-mouse IgG antibody-ALP conjugate (SBA, 1050-04), was added at 50 μL / well and reacted at room temperature for 1 hour. A substrate (PNPP) was added at 100 μL / well and reacted at room temperature for 1 hour, and the absorbance at 405 to 550 nm was calculated. The obtained absorbance value was evaluated as binding activity. The results are shown in Table 6 below (Note that, as described above, in the amino acid sequence shown in SEQ ID NO:215, amino acid residues at positions 1 to 21 constitute a signal peptide, and amino acid residues at positions 22 and onwards constitute an isolated peptide of the extracellular domain of human gpNMB. Accordingly, each mutant protein shown in Table 6 below also starts from the amino acid residue at position 22.). The binding activity to the above C-terminal deletion mutant (hgpNMB_d19_22-234) was taken as 100%, and + was indicated when the binding activity was 50% or less. - was indicated when the binding activity of 50% or more was maintained. Taking into consideration the stability of the purified gpNMB mutants and the mutation sites that affected the binding ability, the epitope of each anti-gpNMB antibody was determined. As a result, it was revealed that the antibody clones GPN18-1, GPN18-2, GPN18-6, and GPN18-7 interact with amino acids (R214 and / or R215) present in the PMEL-CAF-like region. On the other hand, it was revealed that the antibody clone GPN18-5 further recognizes the N-terminal portion. The antibody clone 1-5E is an anti-gpNMB antibody obtained by immunization with a vaccine peptide disclosed in a paper report (Non-Patent Document 36), and the recognized epitope is "RRGDGRWKD", which is the amino acid residues 63-71 at the N-terminus. Example 5: Production of recombinant anti-gpNMB antibody: A plasmid was prepared by inserting a gene sequence obtained by adding a gene sequence encoding a signal sequence to the 5' end of each of the gene sequences encoding the H chain and the L chain of the anti-gpNMB antibody obtained in Example 2 into an animal cell expression vector pcDNA3.4, and the antibody was secreted into the medium by transient expression using an ExpiCHO Expression System (A29133, Thermo Fisher Scientific). The culture supernatant was then collected and purified using a protein A column (Ab-Capcher, Protenova) and a gel filtration column (Superdex 200 Increase, Cytiva). [Example 6] Analysis of anti-gpNMB antibody interactions by surface plasmon resonance method 1: In order to compare the binding characteristics (binding rate and dissociation rate) of each anti-gpNMB antibody clone obtained in Example 1 to gpNMB, measurements were performed by surface plasmon resonance (SPR) method. Specifically, the measurements were performed under the conditions described below. The measurement system used was the BIACORE T200 system. Anti-His monoclonal antibodies were immobilized at approximately 5000 RU on all flow cells of the sensor chip CM5 (BR-1005-30, Cytiva) using Amine Coupling Kit (BR-1000-50, GE) and His Capture Kit (28-9950-56, Cytiva), and used. HBS-EP+ (BR-1006-69, Cytiva) was used as the running buffer. As the ligand, recombinant human gpNMB-FLAG-His (SEQ ID NO: 221) or recombinant mouse gpNMB-FLAG-His (SEQ ID NO: 223) was captured in the measurement system and used. As the analyte, an anti-gpNMB antibody clone was used at a concentration of 100 nmol / L. As the analyte negative control, Shiga toxin 2 antibody (11E10) or control mouse IgG1 (leinco: Pro#M1411) was used. The temperature of the measurement system was set to 25°C. As a ligand, recombinant human gpNMB-FLAG-His was reacted with the anti-His monoclonal antibody of the flow cell (2) with a target of 100 RU or less. Recombinant mouse gpNMB-FLAG-His was reacted with the anti-His monoclonal antibody of the flow cell (4) with a target of 100 RU or less. The flow rate was set to 20 μL / min, and 10 nmol / L purified mouse IgG2a, κ, Isotype Ctrl, Clone: ​​MG2a-53 (401502, BioLegend, hereinafter Ctrl IgG2a) was reacted for 1 minute, and HBS-EP+ was allowed to flow for 10 minutes or more. The analyte was diluted with HBS-EP+ (100 nmol / L) and reacted with all flow cells for 600 seconds each to obtain a binding curve, and then reacted with HBS-EP+ for 600 seconds to obtain a dissociation curve. After the reaction, regeneration buffer 1 (0.2% SDS), regeneration buffer 2 (100 mmol / L Tris-HCl (pH 8.5), 1 mol / L NaCl, 15 mmol / L MgCl ２ ) and regeneration buffer 3 (10 mmol / L glycine-HCl (pH 1.5)) were reacted for 1 minute each, and gpNMB-FLAG-His from the measurement system was removed and washed. Using Biacore T200 Evaluation software (ver2.0), analysis was performed using a 1:1 Binding Model, and the binding rate value (Ass: 1 / Ms), binding stability value (Diss: 1 / s), and equilibrium dissociation value (Diss / Ass: M) were quantified as ordinal numbers. The results are shown in Table 7. [Example 7 (1)] Evaluation of the ability to remove human gpNMB-expressing cells (cell removal-inducing activity) by addition of anti-gpNMB antibody: The ability of each of the anti-gpNMB antibody clones (GPN15-2, GPN15-3, GPN18-2, and GPN18-5) obtained in Example 1 to remove human gpNMB-expressing cells was evaluated. Specifically, AZAMI-GREEN-fused human gpNMB-expressing cells were cultured in a 96-well plate (IWAKI, EZ-VIEW) at 7 × 10 ５ Cells were seeded per well, suspended in anti-gpNMB antibody-containing medium, and incubated at 37°C, 5% CO in a total of 80 μL per well. ２ The phagocytes were then incubated for 2 hours at 8 × 10 ３ Add 20 μL of cells / well and incubate at 37° C., 5% CO ２ The cells were cultured at 4°C for 6 to 7 days. The antibody concentration was evaluated at a final concentration of 100 nM. The fluorescence intensity (au = arbitrary unit) of AZAMI-GREEN was measured under a fluorescent microscope, and the decrease in fluorescence was evaluated as the cell elimination-inducing activity. Comparison was made with a non-Azami-Green fused human gpNMB expressing cell group (Non) and a control mouse IgG added group (NC IgG). The obtained results are shown in the graph of Figure 2. As a result, the antibodies GPN15-2 and GPN15-3 recognizing the PKD region, the antibody GPN18-2 recognizing the PMEL-CAF-like region, and the antibody GPN18-5 recognizing the region spanning from V78 to S92 were confirmed to have the activity of inducing elimination of human gpNMB-expressing cells. [Example 7 (2)] Evaluation of mouse gpNMB-expressing cell elimination ability (cell elimination-inducing activity) by addition of anti-gpNMB antibody: The mouse gpNMB-expressing cell removal ability of the two anti-gpNMB antibody clones (GPN18-5 and 1-5E) that recognize the N-terminal region obtained in Example 1 was evaluated. Specifically, AZAMI-GREEN fusion mouse gpNMB-expressing cells were cultured in a 96-well plate (IWAKI, EZ-VIEW) at 7 × 10 ５ Cells were seeded per well, suspended in anti-gpNMB antibody-containing medium, and incubated at 37°C, 5% CO in a total of 80 μL per well. ２ The phagocytes were then incubated for 2 hours at 8 × 10 ３ Add 20 μL of cells / well and incubate at 37° C., 5% CO ２The cells were cultured at 4°C for 6 to 7 days. The antibody concentration was evaluated at a final concentration of 100 nM. The fluorescence intensity (au = arbitrary unit) of AZAMI-GREEN was measured under a fluorescent microscope, and the decrease in fluorescence was evaluated as the cell elimination-inducing activity. Comparison was made with the control mouse IgG-added group (NC IgG). The obtained results are shown in the graph of Figure 3. As a result, of the two anti-gpNMB antibodies that recognize the N-terminal region, antibody GPN18-5, which recognizes the region spanning from V78 to S92, showed stronger activity of inducing elimination of mouse gpNMB-expressing cells than antibody 1-5E, which is a vaccine peptide antibody. [Example 8] Humanization design of mouse anti-gpNMB antibody: GPN06-1: Based on the amino acid sequence of anti-gpNMB antibody GPN06-1, the CDR regions were identified with reference to IMGT (Lefranc, M.-P., Pommie, C., Ruiz, M., Giudicelli, V., Foulquier, E., Truong, L., Thouvenin-Contet, V. and Lefranc, G. "IMGT unique numbering for immunoglobulin and T cell receptor variable domains and Ig superfamily V-like domains". Dev. Comp. Immunol., 27, 55-77 (2003) PMID: 12477501 LIGM:268.) and Kabat numbering. The CDR loop structure was optimized by a combined IMGT / Kabat method. <Heavy chain humanized design> The human germline gene most similar to the amino acid sequence of the mouse heavy chain variable region (GPN06-1_VH) (SEQ ID NO: 29) was IGHV1-46*01. Meanwhile, 200 types of human IgG sequences highly homologous to GPN06-1_VH were selected as candidates using a BLAST search. Then, four types of framework sequences were finally selected from the viewpoints of framework homology, retention of key amino acids in the framework, loop structure, and the like. CDR grafting was performed on these to obtain humanized mutant sequences hGPN06-1_VH1, hGPN06-1_VH2, hGPN06-1_VH3, and hGPN06-1_VH4. In addition, the sequence of IGHV1-46*01 was used as a framework to perform CDR grafting, and the humanized mutant sequence hGPN06-1_VH5 was obtained. The alignment of these humanized mutant sequences hGPN06-1_VH1 to VH5 to mouse GPN06-1_VH is shown in Figure 4. The underlined parts are the identified CDR regions. Table 8 also shows the identity and homology of these humanized mutant sequences hGPN06-1_VH1 to VH5 to mouse sequence GPN06-1_VH. The humanized mutant sequences hGPN06-1_VH1 to VH5 are arranged in order of high identity and homology to mouse GPN06-1_VH, VH3=VH5>VH2>VH1>VH4. <Light chain humanized design> The human germline gene most similar to the amino acid sequence of the mouse light chain variable region (GPN06-1_VL) (SEQ ID NO: 31) was IGKV1-9*01. Meanwhile, 200 types of human IgK sequences highly homologous to GPN06-1_VL were selected as candidates using a BLAST search. Then, four types of framework sequences were finally selected from the viewpoints of framework homology, retention of key amino acids in the framework, loop structure, and the like. CDR grafting was performed on these to obtain humanized mutant sequences hGPN06-1_VL1, hGPN06-1_VL2, hGPN06-1_VL3, and hGPN06-1_VL4 sequences. In addition, a humanized mutant sequence hGPN06-1_VL5 was obtained by CDR grafting using the sequence of IGKV1-9*01 as a framework. The alignment of these humanized mutant sequences hGPN06-1_VL1 to VL5 to mouse GPN06-1_VL is shown in Figure 5. The underlined parts are the identified CDR regions. Table 9 also shows the identity and homology of these humanized mutant sequences hGPN06-1_VL1 to VL5 to mouse sequence GPN06-1_VL. The humanized mutant sequences hGPN06-1_VL1 to VL5 are arranged in order of identity and homology to mouse GPN06-1_VL, as follows: VL5>VL4>VL1>VL3>VL2. [Example 9] Selection of humanized antibodies Anti-gpNMB antibodies designed in Example 8: 25 types of humanized antibodies were prepared by combining five types of humanized heavy chain sequences and five types of humanized light chain sequences of GPN06-1. The binding properties of these humanized antibodies were evaluated by antigen ELISA, and humanized antibodies with binding activity close to that of human chimeric antibodies were selected. Specifically, a plasmid was prepared by inserting a gene sequence in which a gene sequence encoding a signal sequence was added to the 5' end of each of the gene sequences encoding the H chain and the L chain of the humanized anti-gpNMB antibody designed in Example 8 into an animal cell expression vector pcDNA3.4, and the antibody was secreted into the medium by transient expression using an ExpiCHO Expression System (A29133, Thermo Fisher Scientific). The culture supernatant was then collected and purified using a Protein A column (Ab-Capcher, Protenova) and a gel filtration column (Superdex 200 Increase, Cytiva). A serially diluted solution of the purified humanized antibody was added to a plate on which recombinant human soluble gpNMB (SEQ ID NO: 221) was immobilized, and antigen ELISA was performed. The results are shown in Table 10. As a result, hGPN06-1_H1L1, hGPN06-1_H1L2, hGPN06-1_H2L1, hGPN06-1_H2L2, hGPN06-1_H3L1, hGPN06-1_H3L2, hGPN06-1_H4L1, hGPN06-1_H5L2, hGPN06-1_H5L4, and hGPN06-1_H5L5 had binding affinity at a level equivalent to that of the human chimeric antibody (hGPN06-1_H0L0) (EC ５０ The values ​​were within 3-fold of those of the chimeric antibody hGPN06-1_H0L0. [Example 10] Analysis of interaction of humanized anti-gpNMB antibody by surface plasmon resonance method 2: Among the humanized GPN06 antibody variants obtained in Example 9, hGPN06-1_H1L1, hGPN06-1_H1L2, hGPN06-1_H1L4, hGPN06-1_H2L1, hGPN06-1_H2L2, hGPN06-1_H3L1, hGPN06-1_H3L2, hGPN06-1_H4L1, and hGPN06-1_H5L2 were measured by surface plasmon resonance (SPR) for comparison of their binding characteristics (binding rate and dissociation rate) to human soluble gpNMB (SEQ ID NO: 221). Specifically, the same measurement and analysis conditions as those in Example 6 were used except for the conditions described below. As the analyte, human chimeric antibody hGPN06-1_H0L0 and humanized GPN06 antibody variants, hGPN06-1_H1L1, hGPN06-1_H1L2, hGPN06-1_H1L4, hGPN06-1_H2L1, hGPN06-1_H2L2, hGPN06-1_H3L1, hGPN06-1_H3L2, hGPN06-1_H4L1, and hGPN06-1_H5L2 were used. Each concentration of analyte was reacted for 600 seconds to obtain a binding curve, and then HBS-EP+ was reacted for 1200 seconds to obtain a dissociation curve. After the reaction, regeneration buffer 1 (0.2% SDS), regeneration buffer 2 (100 mmol / L Tris-HCl (pH 8.5), 1 mol / L NaCl, 15 mmol / L MgCl 2 ) and regeneration buffer 3 (10 mmol / L glycine-HCl (pH 1.5)) were reacted for 1 minute each, and gpNMB-FLAG-His from the measurement system was removed and washed. Using BIACORE T200 Evaluation software (ver2.0), analysis was performed using a 1:1 Binding Model to calculate the dissociation rate constant (ka, 1 / Ms), binding rate constant (kd, 1 / s), and dissociation constant (KD, M). The results are shown in Table 11. [Example 11] Identification of amino acids in CDR regions important for binding by alanine substitution of humanized antibodies Sixty-five CDR-substituted antibodies of the humanized anti-gpNMB antibody hGPN06-1_H1L1 prepared in Example 9 were prepared by substituting amino acids in the CDR region of the humanized anti-gpNMB antibody hGPN06-1_H1L1 with alanine. The binding of these alanine-substituted antibodies to recombinant human soluble gpNMB (SEQ ID NO: 221) was evaluated by antigen ELISA to determine the amino acids in the CDR grafting region that are important for binding. The alanine-substituted antibodies of the humanized anti-gpNMB antibody hGPN06-1_H1L1 prepared and the measurement results of the binding activity are shown in Tables 12 and 13 below. From the results obtained, the amino acids whose binding activity was reduced by alanine substitution in each CDR region were as follows: isoleucine at position 29, tyrosine at position 31, and histidine at position 33 in CDR grafting region-L1 (SEQ ID NO: 277) of the light chain variable region of humanized anti-gpNMB antibody hGPN06-1_H1L1; threonine at position 50 in CDR grafting region-L2 (SEQ ID NO: 279); histidine at position 88, glutamine at position 89, tryptophan at position 90, serine at position 92, tyrosine at position 93, proline at position 94, and cysteine ​​at position 95 in CDR grafting region-L3 (SEQ ID NO: 281); and In addition, the following residues were identified as being extremely important for maintaining binding: tyrosine at position 27, asparagine at position 32, and tryptophan at position 33 in CDR grafting region-H1 (SEQ ID NO: 271); aspartic acid at position 55, phenylalanine at position 57, threonine at position 58, asparagine at position 59, tyrosine at position 60, and asparagine at position 61 in CDR grafting region-H2 (SEQ ID NO: 273); and arginine at position 98, glycine at position 100, and glycine at position 109 in CDR grafting region-H3 (SEQ ID NO: 275). [Example 12] Humanization design of mouse anti-gpNMB antibody: GPN18-2: Anti-gpNMB antibody: Based on the amino acid sequence of GPN18-2, the CDR regions were identified with reference to IMGT (Lefranc, M.-P., Pommie, C., Ruiz, M., Giudicelli, V., Foulquier, E., Truong, L., Thouvenin-Contet, V. and Lefranc, G. "IMGT unique numbering for immunoglobulin and T cell receptor variable domains and Ig superfamily V-like domains". Dev. Comp. Immunol., 27, 55-77 (2003) PMID: 12477501 LIGM:268) and Kabat numbering. The CDR loop structure was optimized by a combined IMGT / Kabat method. <Heavy chain humanized design> The human germline gene most similar to the amino acid sequence of the mouse heavy chain variable region (GPN18-2_VH) ​​(SEQ ID NO: 141) was IGHV2-05*09. Meanwhile, 200 types of human IgG sequences highly homologous to GPN18-2_VH were selected as candidates using a BLAST search. Then, four types of framework sequences were finally selected from the viewpoints of framework homology, retention of key amino acids in the framework, loop structure, and the like. CDR grafting was performed on these to obtain humanized mutant sequences hGPN18-2_VH1, hGPN18-2_VH2, hGPN18-2_VH3, and hGPN18-2_VH4. In addition, the sequence of IGHV2-05*09 was used as a framework to perform CDR grafting, and the humanized mutant sequence hGPN18-2_VH5 was obtained. The alignment of these humanized mutant sequences VH1 to VH5 to mouse GPN18-2_VH is shown in Figure 6. The underlined parts are the identified CDR grafting regions. Table 14 below shows the identity and homology of these humanized mutant sequences hGPN18-2_VH1 to VH5 to mouse sequence GPN18-2_VH. The humanized mutant sequences hGPN18-2_VH1 to VH5 are arranged in order of identity and homology to mouse GPN18-2_VH, as follows: VH5>VH3>VH1>VH2>VH4. <Light chain humanized design> The human germline gene most similar to the amino acid sequence of the mouse light chain variable region (GPN18-2_VL) (SEQ ID NO: 143) was IGKV2-30*01. Meanwhile, 200 types of human IgK sequences highly homologous to GPN18-2_VL were selected as candidates using a BLAST search. Then, four types of framework sequences were finally selected from the viewpoints of framework homology, retention of key amino acids in the framework, loop structure, and the like. CDR grafting was performed on these to obtain humanized mutant sequences hGPN18-2_VL1, hGPN18-2_VL2, hGPN18-2_VL3, and hGPN18-2_VL4 sequences. In addition, a humanized mutant sequence hGPN18-2_VL5 was obtained by CDR grafting using the sequence of IGKV2-30*01 as a framework. The alignment of these humanized mutant sequences hGPN18-2_VL1 to VL5 to mouse GPN18-2_VL is shown in FIG. 7. The underlined parts are the identified CDR grafting regions. The identity and homology of these humanized mutant sequences hGPN18-2_VL1 to VL5 to mouse sequence GPN18-2_VL is also shown in Table 15 below. The humanized mutant sequences hGPN18-2_VL1 to VL5 are arranged in order of identity and homology to mouse GPN18-2_VL in the order VL5>VL1>VL2>VL3>VL4. [Example 13] Selection of humanized antibodies Anti-gpNMB antibodies designed in Example 12: 25 types of humanized antibodies were prepared by combining five types of humanized heavy chain sequences and five types of humanized light chain sequences of GPN18-2. The binding activity of these humanized antibodies was evaluated by antigen ELISA, and a humanized antibody with binding activity close to that of the human chimeric antibody hGPN18-2_H0L0 was selected. Specifically, a plasmid was prepared by inserting a gene sequence in which a gene sequence encoding a signal sequence was added to the 5' end of each of the gene sequences encoding the H chain and the L chain of the humanized anti-gpNMB antibody designed in Example 12 into an animal cell expression vector pcDNA3.4, and the antibody was secreted into the medium by transient expression using an ExpiCHO Expression System (A29133, Thermo Fisher Scientific). The culture supernatant was then collected and purified using a Protein A column (Ab-Capcher, Protenova) and a gel filtration column (Superdex 200 Increase, Cytiva). A serially diluted solution of the purified humanized antibody was added to a plate on which recombinant human soluble gpNMB (SEQ ID NO: 221) was immobilized, and antigen ELISA was performed. The results are shown in Table 16 below. As a result, hGPN18-2_H1L3, hGPN18-2_H1L4, hGPN18-2_H2L3, hGPN18-2_H2L4, hGPN18-2_H2L5, hGPN18-2_H3L3, hGPN18-2_H3L4, hGPN18-2_H5L3, and hGPN18-2_H5L4 had binding affinity at a level equivalent to that of the human chimeric antibody (hGPN18-2_H0L0) (EC ５０ The values ​​were within 3-fold of those of the human chimeric antibody hGPN18-2_H0L0. [Example 14] Analysis of interactions of humanized anti-gpNMB antibodies by surface plasmon resonance method: The binding characteristics (binding rate and dissociation rate) of the 25 types of humanized GPN18-2 antibodies obtained in Example 13 to human gpNMB were measured by surface plasmon resonance (SPR) for comparison. Specifically, the measurement and analysis conditions were the same as those in Example 6, except for the conditions described below. The temperature of the measurement system was set to 36°C. The humanized GPN18-2 antibody prepared in Example 20 was used as the analyte. The analyte was diluted with HBS-EP+ (100 nmol / L) and reacted with all flow cells for 300 seconds to obtain a binding curve, and then reacted with HBS-EP+ for 300 seconds to obtain a dissociation curve. After the reaction was completed, regeneration buffer 1 (0.2% SDS), regeneration buffer 2 (100 mmol / L Tris-HCl (pH 8.5), 1 mol / L NaCl, 15 mmol / L MgCl 2 ) and regeneration buffer 3 (10 mmol / L glycine-HCl (pH 1.5)) were reacted for 1 minute each, and gpNMB-FLAG-His from the measurement system was removed and washed. Using BIACORE T200 Evaluation software (ver2.0), the binding rate value (Ass: 1 / Ms), binding stability value (Diss: 1 / s) and equilibrium dissociation value (Diss / Ass: M) were quantified as ordinal numbers by analyzing with a 1:1 Binding Model. The results are shown in Table 17. [Example 15] Identification of amino acids in CDR regions important for binding by alanine substitution of humanized antibodies Seventy-four types of CDR-substituted humanized anti-gpNMB antibody hGPN18-2_H2L3 antibodies were prepared by substituting amino acids in the CDR region of the humanized anti-gpNMB antibody hGPN18-2_H2L3 prepared in Example 13 with alanine. The binding of these alanine-substituted antibodies to recombinant human soluble gpNMB (SEQ ID NO: 221) was evaluated by antigen ELISA to determine the amino acids in the CDR grafting region that are important for binding. The alanine-substituted humanized anti-gpNMB antibody hGPN18-2_H2L3 antibodies prepared and the measurement results of binding activity are shown in Tables 18 and 19 below. From the results obtained, the amino acids whose binding activity was reduced by alanine substitution in each CDR regi...

Claims

1. A pharmaceutical composition for removing disease-related cells, comprising an anti-gpNMB antibody or a fragment or derivative thereof that specifically binds to at least one site in the region spanning from V78 to the PKD domain of human gpNMB (glycoprotein nonmetastatic melanoma protein B) having the amino acid sequence of SEQ ID NO:

209.

2. The pharmaceutical composition of claim 1, wherein the anti-gpNMB antibody specifically binds to a region including amino acid residues D287 and / or H301 of human gpNMB having the amino acid sequence of SEQ ID NO:

209.

3. The pharmaceutical composition according to claim 1 or 2, wherein the anti-gpNMB antibody specifically binds to a region including amino acid residues R214 and / or R215 of human gpNMB having the amino acid sequence of SEQ ID NO:

209.

4. The pharmaceutical composition described in claim 2 or 3, wherein the anti-gpNMB antibody specifically binds to one or more of the following regions of human gpNMB having the amino acid sequence of SEQ ID NO: 209: a region including amino acid residues K257 and / or D258, a region including amino acid residues H268 and / or D269, a region including amino acid residue K282, a region including amino acid residue K316, a region including amino acid residue K186, and a region including amino acid residues H216 and / or R218.

5. The pharmaceutical composition of claim 1, wherein the anti-gpNMB antibody specifically binds to at least one site in the region spanning V78 to S92 of human gpNMB having the amino acid sequence of SEQ ID NO:

209.

6. The pharmaceutical composition of any one of claims 1 to 5, wherein the anti-gpNMB antibody also specifically binds to at least one site in the region spanning from V78 to the PKD domain of mouse gpNMB having the amino acid sequence of SEQ ID NO:

211.

7. The pharmaceutical composition according to any one of claims 1 to 6, wherein the anti-gpNMB antibody is a monoclonal antibody or a fragment thereof or a derivative thereof.

8. The anti-gpNMB antibody comprises at least a heavy chain variable region, the heavy chain variable region comprising: (1) as CDR-H1, an amino acid sequence as set forth in SEQ ID NO: 1, or an amino acid sequence in which any one, two or three amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 1 have been substituted, deleted or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 1; as CDR-H2, an amino acid sequence as set forth in SEQ ID NO: 3, or an amino acid sequence in which any one, two or three amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 3 have been substituted, deleted or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 3; and (1) as CDR-H3, an amino acid sequence as set forth in SEQ ID NO:5, or an amino acid sequence in which any one, two, three, or four amino acid residues in the amino acid sequence as set forth in SEQ ID NO:5 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 75.0% or more, 83.3% or more, or 91.6% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO:5; or (2) as CDR-H1, an amino acid sequence as set forth in SEQ ID NO:17, or an amino acid sequence in which any one, two, or three amino acid residues in the amino acid sequence as set forth in SEQ ID NO:17 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO:17; As CDR-H2, an amino acid sequence of SEQ ID NO: 19, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence of SEQ ID NO: 19 have been substituted, deleted or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 19, and(3) as CDR-H1, an amino acid sequence set forth in SEQ ID NO: 33, or an amino acid sequence set forth in SEQ ID NO: 33, in which one, two, three, four, five, or six amino acid residues are substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 66.6% or more, 73.3% or more, 80.0% or more, 86.6% or more, or 93.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 33; As CDR-H2, an amino acid sequence set forth in SEQ ID NO: 35, or an amino acid sequence in which any one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO: 35 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 35; and As CDR-H3, an amino acid sequence set forth in SEQ ID NO: 37, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence set forth in SEQ ID NO: 37 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 66.6% or more, 73.3% or more, 80.0% or more, 86.6% or more, or 93.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 37; (4) As CDR-H1, an amino acid sequence set forth in SEQ ID NO: 49, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO: 49 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 49;As CDR-H2, an amino acid sequence as set forth in SEQ ID NO:51, or an amino acid sequence in which any one, two, or three amino acid residues in the amino acid sequence as set forth in SEQ ID NO:51 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO:51; and As CDR-H3, an amino acid sequence as set forth in SEQ ID NO:53, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence as set forth in SEQ ID NO:53 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 68.7% or more, 75.0% or more, 81.2% or more, 87.5% or more, or 93.7% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO:53; (5) As CDR-H1, an amino acid sequence as set forth in SEQ ID NO: 65, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 65 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 65; As CDR-H2, an amino acid sequence as set forth in SEQ ID NO: 67, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 67 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 67; and As CDR-H3, an amino acid sequence of SEQ ID NO:69, or an amino acid sequence in which one, two, three, four, or five amino acid residues in the amino acid sequence of SEQ ID NO:69 have been substituted, deleted, or inserted, or an amino acid sequence having 64.2% or more, 71.4% or more, 78.5% or more, 85.7% or more, or 92.8% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO:69, or(6) As CDR-H1, an amino acid sequence as set forth in SEQ ID NO: 81, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 81 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 81; As CDR-H2, an amino acid sequence as set forth in SEQ ID NO: 83, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 83 have been substituted, deleted, or inserted, or an amino acid sequence having 71.4% or more or 85.7% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 83; (7) as CDR-H1, an amino acid sequence set forth in SEQ ID NO: 97, or an amino acid sequence set forth in SEQ ID NO: 97, in which one, two, or three amino acid residues are substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 97; As CDR-H2, an amino acid sequence of SEQ ID NO: 99, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence of SEQ ID NO: 99 have been substituted, deleted or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 99, and(8) as CDR-H1, an amino acid sequence set forth in SEQ ID NO: 113, or an amino acid sequence set forth in SEQ ID NO: 113, in which one, two, three, or four amino acid residues are substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 113; As CDR-H2, an amino acid sequence as set forth in SEQ ID NO: 115, or an amino acid sequence in which any one or two amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 115 have been substituted, deleted, or inserted, or an amino acid sequence having 71.4% or more or 85.7% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 115; and As CDR-H3, an amino acid sequence as set forth in SEQ ID NO: 117, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 117 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 66.6% or more, 73.3% or more, 80.0% or more, 86.6% or more, or 93.3% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 117; (9) As CDR-H1, an amino acid sequence set forth in SEQ ID NO: 129, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 129 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 129;As CDR-H2, an amino acid sequence set forth in SEQ ID NO: 131, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 131 have been substituted, deleted, or inserted, or an amino acid sequence having 71.4% or more or 85.7% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 131; and As CDR-H3, an amino acid sequence set forth in SEQ ID NO: 133, or an amino acid sequence in which one, two, three, four, five, or six amino acid residues in the amino acid sequence set forth in SEQ ID NO: 133 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 66.6% or more, 73.3% or more, 80.0% or more, 86.6% or more, or 93.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 133; (10) As CDR-H1, an amino acid sequence as set forth in SEQ ID NO: 145, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 145 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 145; As CDR-H2, an amino acid sequence as set forth in SEQ ID NO: 147, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 147 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 147; and As CDR-H3, an amino acid sequence of SEQ ID NO: 149, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence of SEQ ID NO: 149 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 66.6% or more, 73.3% or more, 80.0% or more, 86.6% or more, or 93.3% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 149, or(11) As CDR-H1, an amino acid sequence as set forth in SEQ ID NO: 161, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 161 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 161; As CDR-H2, an amino acid sequence as set forth in SEQ ID NO: 163, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 163 have been substituted, deleted, or inserted, or an amino acid sequence having 71.4% or more or 85.7% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 163; (11) As CDR-H3, an amino acid sequence as set forth in SEQ ID NO: 165, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 165 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 66.6% or more, 73.3% or more, 80.0% or more, 86.6% or more, or 93.3% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 165; or (12) As CDR-H1, an amino acid sequence as set forth in SEQ ID NO: 255, or an amino acid sequence in which any one, two, or three amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 255 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 255; As CDR-H2, an amino acid sequence of SEQ ID NO:257, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence of SEQ ID NO:257 have been substituted, deleted, or inserted, or an amino acid sequence having 71.4% or more or 85.7% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO:257, and(13) as CDR-H1, an amino acid sequence set forth in SEQ ID NO:283, or an amino acid sequence set forth in SEQ ID NO:283, in which one, two, or three amino acid residues are substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:283; As CDR-H2, an amino acid sequence as set forth in SEQ ID NO:285, or an amino acid sequence in which any one, two, or three amino acid residues in the amino acid sequence as set forth in SEQ ID NO:285 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO:285; As CDR-H3, an amino acid sequence as set forth in SEQ ID NO:287, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence as set forth in SEQ ID NO:287 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 66.6% or more, 73.3% or more, 80.0% or more, 86.6% or more, or 93.3% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO:287; (14) As CDR-H1, an amino acid sequence set forth in SEQ ID NO: 311, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 311 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 311;As CDR-H2, an amino acid sequence set forth in SEQ ID NO:313, or an amino acid sequence in which any one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO:313 have been substituted, deleted, or inserted, or an amino acid sequence having 71.4% or more or 85.7% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:313; As CDR-H3, an amino acid sequence set forth in SEQ ID NO:315, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence set forth in SEQ ID NO:315 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 66.6% or more, 73.3% or more, 80.0% or more, 86.6% or more, or 93.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:315; (15) As the CDR grafting region-H1, an amino acid sequence as set forth in SEQ ID NO:271, or an amino acid sequence in which any one, two, three, or four amino acid residues other than tyrosine at position 27, asparagine at position 32, and tryptophan at position 33 of the amino acid sequence as set forth in SEQ ID NO:271 have been substituted, deleted, or inserted; As the CDR grafting region-H2, an amino acid sequence as set forth in SEQ ID NO:273, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues other than aspartic acid at position 55, phenylalanine at position 57, threonine at position 58, asparagine at position 59, tyrosine at position 60, and asparagine at position 61 of the amino acid sequence as set forth in SEQ ID NO:273 have been substituted, deleted, or inserted; As the CDR grafting region-H3, an amino acid sequence of SEQ ID NO: 275, or an amino acid sequence in which one, two, three, four, five, or six amino acid residues other than arginine at position 98, glycine at position 100, and glycine at position 109 in the amino acid sequence of SEQ ID NO: 275 have been substituted, deleted, or inserted; or(16) As the CDR grafting region-H1, an amino acid sequence as set forth in SEQ ID NO:299, or an amino acid sequence in which any one, two, three, or four amino acid residues in the amino acid sequence as set forth in SEQ ID NO:299 have been substituted, deleted, or inserted; As the CDR grafting region-H2, an amino acid sequence as set forth in SEQ ID NO:301, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence as set forth in SEQ ID NO:301 have been substituted, deleted, or inserted, except for aspartic acid at position 52, tryptophan at position 54, aspartic acid at position 58, and proline at position 63; (17) As CDR-H1, an amino acid sequence set forth in SEQ ID NO: 177, or an amino acid sequence set forth in SEQ ID NO: 177, or an amino acid sequence set forth in SEQ ID NO: 177, in which any one, two, three, or four amino acid residues are substituted, deleted, or inserted, other than arginine at position 99, threonine at position 100, tyrosine at position 102, tyrosine at position 105, tyrosine at position 107, and methionine at position 110; or (18) an amino acid sequence set forth in SEQ ID NO: 177, or an amino acid sequence set forth in SEQ ID NO: 177, in which any one, two, three, or four amino acid residues are substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 177; As CDR-H2, an amino acid sequence of SEQ ID NO: 179, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence of SEQ ID NO: 179 have been substituted, deleted or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 179, and(18) as CDR-H1, an amino acid sequence set forth in SEQ ID NO: 330, or an amino acid sequence set forth in SEQ ID NO: 330 in which one, two, three, or four amino acid residues are substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 330; As CDR-H2, an amino acid sequence as set forth in SEQ ID NO: 331, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 331 have been substituted, deleted or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 331; and As CDR-H3, an amino acid sequence as set forth in SEQ ID NO: 332, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 332 have been substituted, deleted or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 332; (19) As CDR-H1, an amino acid sequence set forth in SEQ ID NO: 337, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 337 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 337;As CDR-H2, an amino acid sequence as set forth in SEQ ID NO: 338, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 338 have been substituted, deleted or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 338; and As CDR-H3, an amino acid sequence as set forth in SEQ ID NO: 339, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 339 have been substituted, deleted or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 339; (20) As CDR-H1, an amino acid sequence as set forth in SEQ ID NO: 344, or an amino acid sequence in which any one, two, three, or four amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 344 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 344; As CDR-H2, an amino acid sequence as set forth in SEQ ID NO: 345, or an amino acid sequence in which any one, two, or three amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 345 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 345; As CDR-H3, an amino acid sequence set forth in SEQ ID NO: 346, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO: 346 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 346, or(21) As the CDR grafting region-H1, an amino acid sequence as set forth in SEQ ID NO: 327, or an amino acid sequence in which any one, two, three, or four amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 327 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 327; As the CDR grafting region-H2, an amino acid sequence as set forth in SEQ ID NO: 328, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 328 have been substituted, deleted, or inserted, or an amino acid sequence having 64.7% or more, 70.5% or more, 76.4% or more, 82.3% or more, 88.2% or more, or 94.1% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 328; (21) As the CDR grafting region-H3, an amino acid sequence as set forth in SEQ ID NO: 329, or an amino acid sequence in which any one or two amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 329 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 329; or (22) As the CDR grafting region-H1, an amino acid sequence as set forth in SEQ ID NO: 334, or an amino acid sequence in which any one, two, three, or four amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 334 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 334;As the CDR grafting region-H2, an amino acid sequence as set forth in SEQ ID NO: 335, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 335 have been substituted, deleted, or inserted, or an amino acid sequence having 64.7% or more, 70.5% or more, 76.4% or more, 82.3% or more, 88.2% or more, or 94.1% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 335; As the CDR grafting region-H3, an amino acid sequence as set forth in SEQ ID NO: 336, or an amino acid sequence in which any one or two amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 336 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 336; (23) As the CDR grafting region-H1, an amino acid sequence as set forth in SEQ ID NO: 341, or an amino acid sequence in which any one, two, three, or four amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 341 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 341; As the CDR grafting region-H2, an amino acid sequence as set forth in SEQ ID NO: 342, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 342 have been substituted, deleted, or inserted, or an amino acid sequence having 64.7% or more, 70.5% or more, 76.4% or more, 82.3% or more, 88.2% or more, or 94.1% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 342; As the CDR grafting region-H3, an amino acid sequence set forth in SEQ ID NO: 343, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 343 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 343.The pharmaceutical composition according to any one of claims 1 to 7, comprising:

9. The anti-gpNMB antibody comprises at least a heavy chain variable region, the heavy chain variable region being: (1) an amino acid sequence set forth in SEQ ID NO: 13, or an amino acid sequence having 60% or more homology with the amino acid sequence set forth in SEQ ID NO: 13; (2) an amino acid sequence set forth in SEQ ID NO: 29, or an amino acid sequence having 60% or more homology with the amino acid sequence set forth in SEQ ID NO: 29; (3) an amino acid sequence set forth in SEQ ID NO: 45, or an amino acid sequence having 60% or more homology with the amino acid sequence set forth in SEQ ID NO: 45; (4) an amino acid sequence set forth in SEQ ID NO: 61, or an amino acid sequence having 60% or more homology with the amino acid sequence set forth in SEQ ID NO: 61; (5) an amino acid sequence set forth in SEQ ID NO: 77, or an amino acid sequence having 60% or more homology with the amino acid sequence set forth in SEQ ID NO: 77; or (6) an amino acid sequence set forth in SEQ ID NO: 93, or an amino acid sequence having 60% or more homology with the amino acid sequence set forth in SEQ ID NO: 93; (7) an amino acid sequence set forth in SEQ ID NO: 109, or an amino acid sequence having 60% or more homology with the amino acid sequence set forth in SEQ ID NO: 109; or (8) an amino acid sequence set forth in SEQ ID NO: 125, or an amino acid sequence having 60% or more homology with the amino acid sequence set forth in SEQ ID NO: 125; or (9) an amino acid sequence set forth in SEQ ID NO: 141, or an amino acid sequence having 60% or more homology with the amino acid sequence set forth in SEQ ID NO: 141; or (10) an amino acid sequence set forth in SEQ ID NO: 157, or an amino acid sequence having 60% or more homology with the amino acid sequence set forth in SEQ ID NO: 157; or (11) an amino acid sequence set forth in SEQ ID NO: 173, or an amino acid sequence having 60% or more homology with the amino acid sequence set forth in SEQ ID NO: 173; or (12) an amino acid sequence set forth in SEQ ID NO: 267, or an amino acid sequence having 60% or more homology with the amino acid sequence set forth in SEQ ID NO: 267; or (13) an amino acid sequence set forth in SEQ ID NO:295, or an amino acid sequence having 60% or more homology with the amino acid sequence set forth in SEQ ID NO:295; or (14) an amino acid sequence set forth in SEQ ID NO:323, or an amino acid sequence having 60% or more homology with the amino acid sequence set forth in SEQ ID NO:323; or(17) an amino acid sequence set forth in SEQ ID NO: 189, or an amino acid sequence having 60% or more homology with the amino acid sequence set forth in SEQ ID NO: 189; or (18) an amino acid sequence set forth in SEQ ID NO: 333, or an amino acid sequence having 60% or more homology with the amino acid sequence set forth in SEQ ID NO: 333; or (19) an amino acid sequence set forth in SEQ ID NO: 340, or an amino acid sequence having 60% or more homology with the amino acid sequence set forth in SEQ ID NO: 340; or (20) an amino acid sequence set forth in SEQ ID NO: 347, or an amino acid sequence having 60% or more homology with the amino acid sequence set forth in SEQ ID NO:

347. The pharmaceutical composition according to any one of claims 1 to 7, 10. The pharmaceutical composition according to claim 8 or 9, wherein the heavy chain variable region comprises as framework sequences framework sequences of any class of human immunoglobulins.

11. The pharmaceutical composition according to any one of claims 8 to 10, wherein the anti-gpNMB antibody further comprises a heavy chain constant region, the heavy chain constant region having an amino acid sequence of a heavy chain constant region of any class of human immunoglobulin.

12. The anti-gpNMB antibody comprises at least a light chain variable region, the light chain variable region comprising: (1) as CDR-L1, an amino acid sequence as set forth in SEQ ID NO: 7, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 7 have been substituted, deleted or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 7; as CDR-L2, an amino acid sequence as set forth in SEQ ID NO: 9, or an amino acid sequence in which one amino acid residue in the amino acid sequence as set forth in SEQ ID NO: 9 has been substituted, deleted or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 9; and (1) as CDR-L3, an amino acid sequence set forth in SEQ ID NO: 11, or an amino acid sequence in which any one, two or three amino acid residues in the amino acid sequence set forth in SEQ ID NO: 11 have been substituted, deleted or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 11; or (2) as CDR-L1, an amino acid sequence set forth in SEQ ID NO: 23, or an amino acid sequence in which any one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 23 have been substituted, deleted or inserted, or an amino acid sequence having 60.0% or more or 80.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 23; as CDR-L2, an amino acid sequence as set forth in SEQ ID NO:25, or an amino acid sequence in which any one amino acid residue in the amino acid sequence as set forth in SEQ ID NO:25 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO:25; and as CDR-L3, an amino acid sequence as set forth in SEQ ID NO:27, or an amino acid sequence in which any one, two, or three amino acid residues in the amino acid sequence as set forth in SEQ ID NO:27 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO:27;(3) as CDR-L1, an amino acid sequence as set forth in SEQ ID NO: 39, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 39 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more or 80.0% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 39; as CDR-L2, an amino acid sequence as set forth in SEQ ID NO: 41, or an amino acid sequence in which one amino acid residue in the amino acid sequence as set forth in SEQ ID NO: 41 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 41; and (3) an amino acid sequence as CDR-L3, which is an amino acid sequence as set forth in SEQ ID NO: 43, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 43 have been substituted, deleted or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 43; or (4) an amino acid sequence as CDR-L1, which is an amino acid sequence as set forth in SEQ ID NO: 55, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 55 have been substituted, deleted or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 55; as CDR-L2, an amino acid sequence as set forth in SEQ ID NO:57, or an amino acid sequence in which any one amino acid residue in the amino acid sequence as set forth in SEQ ID NO:57 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO:57; and as CDR-L3, an amino acid sequence as set forth in SEQ ID NO:59, or an amino acid sequence in which any one, two, or three amino acid residues in the amino acid sequence as set forth in SEQ ID NO:59 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO:59;(5) As CDR-L1, an amino acid sequence as set forth in SEQ ID NO: 71, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 71 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more or 80.0% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 71; As CDR-L2, an amino acid sequence as set forth in SEQ ID NO: 73, or an amino acid sequence in which one amino acid residue in the amino acid sequence as set forth in SEQ ID NO: 73 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 73; and (5) as CDR-L3, an amino acid sequence as set forth in SEQ ID NO: 75, or an amino acid sequence in which any one, two, three or four amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 75 have been substituted, deleted or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more or 90.0% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 75; or (6) as CDR-L1, an amino acid sequence as set forth in SEQ ID NO: 87, or an amino acid sequence in which any one or two amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 87 have been substituted, deleted or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 87; as CDR-L2, an amino acid sequence as set forth in SEQ ID NO:89, or an amino acid sequence in which any one amino acid residue in the amino acid sequence as set forth in SEQ ID NO:89 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO:89; and as CDR-L3, an amino acid sequence as set forth in SEQ ID NO:91, or an amino acid sequence in which any one, two, or three amino acid residues in the amino acid sequence as set forth in SEQ ID NO:91 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO:91;(7) As CDR-L1, an amino acid sequence as set forth in SEQ ID NO: 103, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 103 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 103; As CDR-L2, an amino acid sequence as set forth in SEQ ID NO: 105, or an amino acid sequence in which one amino acid residue in the amino acid sequence as set forth in SEQ ID NO: 105 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 105; and (8) as CDR-L1, an amino acid sequence set forth in SEQ ID NO: 119, or an amino acid sequence set forth in SEQ ID NO: 119, in which one, two, three, or four amino acid residues are substituted, deleted, or inserted, or an amino acid sequence having 63.6% or more, 72.7% or more, 81.8% or more, or 90.9% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 119; As CDR-L2, an amino acid sequence of SEQ ID NO: 121, or an amino acid sequence in which any one amino acid residue in the amino acid sequence of SEQ ID NO: 121 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 121, and(9) as CDR-L1, an amino acid sequence set forth in SEQ ID NO: 135, or an amino acid sequence set forth in SEQ ID NO: 135, in which one, two, three, or four amino acid residues are substituted, deleted, or inserted, or an amino acid sequence having 63.6% or more, 72.7% or more, 81.8% or more, or 90.9% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 135; As CDR-L2, an amino acid sequence set forth in SEQ ID NO: 137, or an amino acid sequence in which any one amino acid residue in the amino acid sequence set forth in SEQ ID NO: 137 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 137; and As CDR-L3, an amino acid sequence set forth in SEQ ID NO: 139, or an amino acid sequence in which any one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO: 139 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 139; (10) As CDR-L1, an amino acid sequence set forth in SEQ ID NO: 151, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 151 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 151;As CDR-L2, an amino acid sequence set forth in SEQ ID NO: 153, or an amino acid sequence in which any one amino acid residue in the amino acid sequence set forth in SEQ ID NO: 153 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 153; and As CDR-L3, an amino acid sequence set forth in SEQ ID NO: 155, or an amino acid sequence in which any one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO: 155 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 155; (11) As CDR-L1, an amino acid sequence as set forth in SEQ ID NO: 167, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 167 have been substituted, deleted, or inserted, or an amino acid sequence having 63.6% or more, 72.7% or more, 81.8% or more, or 90.9% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 167; As CDR-L2, an amino acid sequence as set forth in SEQ ID NO: 169, or an amino acid sequence in which one amino acid residue in the amino acid sequence as set forth in SEQ ID NO: 169 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 169; As CDR-L3, an amino acid sequence of SEQ ID NO: 171, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence of SEQ ID NO: 171 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 171, or(12) As CDR-L1, an amino acid sequence as set forth in SEQ ID NO:261, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence as set forth in SEQ ID NO:261 have been substituted, deleted, or inserted, or an amino acid sequence having 63.6% or more, 72.7% or more, 81.8% or more, or 90.9% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO:261; As CDR-L2, an amino acid sequence as set forth in SEQ ID NO:263, or an amino acid sequence in which one amino acid residue in the amino acid sequence as set forth in SEQ ID NO:263 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO:263; (13) as CDR-L1, an amino acid sequence set forth in SEQ ID NO:289, or an amino acid sequence set forth in SEQ ID NO:289, in which one or two amino acid residues are substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more or 80.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:289; As CDR-L2, an amino acid sequence of SEQ ID NO:291, or an amino acid sequence in which any one amino acid residue in the amino acid sequence of SEQ ID NO:291 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO:291, and(13) as CDR-L3, an amino acid sequence as set forth in SEQ ID NO:293, or an amino acid sequence in which any one, two, or three amino acid residues in the amino acid sequence as set forth in SEQ ID NO:293 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO:293; or (14) as CDR-L1, an amino acid sequence as set forth in SEQ ID NO:317, or an amino acid sequence in which any one, two, three, or four amino acid residues in the amino acid sequence as set forth in SEQ ID NO:317 have been substituted, deleted, or inserted, or an amino acid sequence having 63.6% or more, 72.7% or more, 81.8% or more, or 90.9% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO:317; As CDR-L2, an amino acid sequence set forth in SEQ ID NO:319, or an amino acid sequence in which any one amino acid residue in the amino acid sequence set forth in SEQ ID NO:319 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:319; and As CDR-L3, an amino acid sequence set forth in SEQ ID NO:321, or an amino acid sequence in which any one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO:321 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:321; (15) As the CDR grafting region-L1, the amino acid sequence of SEQ ID NO:277, or the amino acid sequence of SEQ ID NO:277 in which any one, two, three, or four amino acid residues other than the isoleucine at position 29, the tyrosine at position 31, and the histidine at position 33 have been substituted, deleted, or inserted; As the CDR grafting region-L2, the amino acid sequence of SEQ ID NO:279, or the amino acid sequence of SEQ ID NO:279 in which any one or two amino acid residues other than the threonine at position 50 have been substituted, deleted, or inserted;(15) as the CDR grafting region-L3, an amino acid sequence as set forth in SEQ ID NO:281, or an amino acid sequence as set forth in SEQ ID NO:281 in which any one, two, or three amino acid residues other than histidine at position 88, glutamine at position 89, tryptophan at position 90, serine at position 92, tyrosine at position 93, proline at position 94, and cysteine ​​at position 95 have been substituted, deleted, or inserted; or (16) as the CDR grafting region-L1, an amino acid sequence as set forth in SEQ ID NO:305, or an amino acid sequence as set forth in SEQ ID NO:305 in which any one, two, three, four, five, or six amino acid residues other than leucine at position 31, tyrosine at position 37, and glutamic acid at position 39 have been substituted, deleted, or inserted; (16) as CDR-L1, an amino acid sequence set forth in SEQ ID NO: 183, or an amino acid sequence set forth in SEQ ID NO: 183, or an amino acid sequence set forth in SEQ ID NO: 183, in which one or two amino acid residues other than lysine at position 55 have been substituted, deleted or inserted; as CDR-grafting region-L2, an amino acid sequence set forth in SEQ ID NO: 307, or an amino acid sequence set forth in SEQ ID NO: 307 in which one or two amino acid residues other than phenylalanine at position 94 have been substituted, deleted or inserted; (17) as CDR-L1, an amino acid sequence set forth in SEQ ID NO: 183, or an amino acid sequence set forth in SEQ ID NO: 183 in which one or two amino acid residues have been substituted, deleted or inserted; or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 183; as CDR-L2, an amino acid sequence of SEQ ID NO: 185, or an amino acid sequence in which any one amino acid residue in the amino acid sequence of SEQ ID NO: 185 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 185;As CDR-L3, an amino acid sequence as set forth in SEQ ID NO:187, or an amino acid sequence in which any one, two or three amino acid residues in the amino acid sequence as set forth in SEQ ID NO:187 have been substituted, deleted or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO:187; or (18) As CDR-L1, an amino acid sequence as set forth in SEQ ID NO:351, or an amino acid sequence in which any one or two amino acid residues in the amino acid sequence as set forth in SEQ ID NO:351 have been substituted, deleted or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO:351; as CDR-L2, an amino acid sequence as set forth in SEQ ID NO:352, or an amino acid sequence in which any one amino acid residue in the amino acid sequence as set forth in SEQ ID NO:352 has been substituted, deleted or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO:352; as CDR-L3, an amino acid sequence as set forth in SEQ ID NO:353, or an amino acid sequence in which any one, two or three amino acid residues in the amino acid sequence as set forth in SEQ ID NO:353 have been substituted, deleted or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO:353; (19) As CDR-L1, an amino acid sequence as set forth in SEQ ID NO:358, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence as set forth in SEQ ID NO:358 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO:358; As CDR-L2, an amino acid sequence as set forth in SEQ ID NO:359, or an amino acid sequence in which one amino acid residue in the amino acid sequence as set forth in SEQ ID NO:359 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO:359;(20) as CDR-L1, an amino acid sequence set forth in SEQ ID NO: 365, or an amino acid sequence set forth in SEQ ID NO: 365, in which one or two amino acid residues are substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 365; as CDR-L2, an amino acid sequence as set forth in SEQ ID NO:366, or an amino acid sequence in which any one amino acid residue in the amino acid sequence as set forth in SEQ ID NO:366 has been substituted, deleted or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO:366; as CDR-L3, an amino acid sequence as set forth in SEQ ID NO:367, or an amino acid sequence in which any one, two or three amino acid residues in the amino acid sequence as set forth in SEQ ID NO:367 has been substituted, deleted or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO:367; (21) As the CDR grafting region-L1, an amino acid sequence set forth in SEQ ID NO: 348, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 348 have been substituted, deleted, or inserted, or an amino acid sequence having 63.6% or more, 72.7% or more, 81.8% or more, or 90.9% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 348;As the CDR grafting region-L2, an amino acid sequence as set forth in SEQ ID NO:349, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence as set forth in SEQ ID NO:349 have been substituted, deleted or inserted, or an amino acid sequence having 71.4% or more or 85.7% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO:349; As the CDR grafting region-L3, an amino acid sequence as set forth in SEQ ID NO:350, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence as set forth in SEQ ID NO:350 have been substituted, deleted or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO:350; (22) As the CDR grafting region-L1, an amino acid sequence as set forth in SEQ ID NO: 355, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 355 have been substituted, deleted, or inserted, or an amino acid sequence having 63.6% or more, 72.7% or more, 81.8% or more, or 90.9% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 355; As the CDR grafting region-L2, an amino acid sequence as set forth in SEQ ID NO: 356, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 356 have been substituted, deleted, or inserted, or an amino acid sequence having 71.4% or more or 85.7% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 356; As the CDR grafting region-L3, an amino acid sequence set forth in SEQ ID NO: 357, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence set forth in SEQ ID NO: 357 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 357, or(23) As the CDR grafting region-L1, an amino acid sequence as set forth in SEQ ID NO: 362, or an amino acid sequence in which any one, two, three, or four amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 362 have been substituted, deleted, or inserted, or an amino acid sequence having 63.6% or more, 72.7% or more, 81.8% or more, or 90.9% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 362; As the CDR grafting region-L2, an amino acid sequence as set forth in SEQ ID NO: 363, or an amino acid sequence in which any one or two amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 363 have been substituted, deleted, or inserted, or an amino acid sequence having 71.4% or more or 85.7% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 363; The pharmaceutical composition according to any one of claims 1 to 11, comprising, as a CDR grafting region-L3, an amino acid sequence set forth in SEQ ID NO:364, or an amino acid sequence in which any one, two or three amino acid residues in the amino acid sequence set forth in SEQ ID NO:364 have been substituted, deleted or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO:

364.

13. The anti-gpNMB antibody comprises at least a light chain variable region, the light chain variable region being: (1) an amino acid sequence set forth in SEQ ID NO: 15, or an amino acid sequence having 60% or more homology with the amino acid sequence set forth in SEQ ID NO: 15; or (2) an amino acid sequence set forth in SEQ ID NO: 31, or an amino acid sequence having 60% or more homology with the amino acid sequence set forth in SEQ ID NO: 31; or (3) an amino acid sequence set forth in SEQ ID NO: 47, or an amino acid sequence having 60% or more homology with the amino acid sequence set forth in SEQ ID NO: 47; or (4) an amino acid sequence set forth in SEQ ID NO: 63, or an amino acid sequence having 60% or more homology with the amino acid sequence set forth in SEQ ID NO: 63; or (5) an amino acid sequence set forth in SEQ ID NO: 79, or an amino acid sequence having 60% or more homology with the amino acid sequence set forth in SEQ ID NO: 79; or (6) an amino acid sequence set forth in SEQ ID NO: 95, or an amino acid sequence having 60% or more homology with the amino acid sequence set forth in SEQ ID NO: 95; or (7) an amino acid sequence set forth in SEQ ID NO: 111, or an amino acid sequence having 60% or more homology with the amino acid sequence set forth in SEQ ID NO: 111; or (8) an amino acid sequence set forth in SEQ ID NO: 127, or an amino acid sequence having 60% or more homology with the amino acid sequence set forth in SEQ ID NO: 127; or (9) an amino acid sequence set forth in SEQ ID NO: 143, or an amino acid sequence having 60% or more homology with the amino acid sequence set forth in SEQ ID NO: 143; or (10) an amino acid sequence set forth in SEQ ID NO: 159, or an amino acid sequence having 60% or more homology with the amino acid sequence set forth in SEQ ID NO: 159; or (11) an amino acid sequence set forth in SEQ ID NO: 175, or an amino acid sequence having 60% or more homology with the amino acid sequence set forth in SEQ ID NO: 175; or (12) an amino acid sequence set forth in SEQ ID NO: 269, or an amino acid sequence having 60% or more homology with the amino acid sequence set forth in SEQ ID NO: 269; or (13) An amino acid sequence having 60% or more homology to the amino acid sequence set forth in SEQ ID NO: 297, or(14) an amino acid sequence set forth in SEQ ID NO: 325, or an amino acid sequence having 60% or more homology with the amino acid sequence set forth in SEQ ID NO: 325; or (17) an amino acid sequence set forth in SEQ ID NO: 191, or an amino acid sequence having 60% or more homology with the amino acid sequence set forth in SEQ ID NO: 191; or (18) an amino acid sequence set forth in SEQ ID NO: 354, or an amino acid sequence having 60% or more homology with the amino acid sequence set forth in SEQ ID NO: 354; or (19) an amino acid sequence set forth in SEQ ID NO: 361, or an amino acid sequence having 60% or more homology with the amino acid sequence set forth in SEQ ID NO: 361; or (20) an amino acid sequence set forth in SEQ ID NO: 368, or an amino acid sequence having 60% or more homology with the amino acid sequence set forth in SEQ ID NO:

368. The pharmaceutical composition according to any one of claims 1 to 11.

14. The pharmaceutical composition according to claim 12 or 13, wherein the light chain variable region comprises as framework sequences the framework sequences of any class of human immunoglobulins.

15. The pharmaceutical composition of any one of claims 12 to 14, wherein the anti-gpNMB antibody further comprises a light chain constant region, the light chain constant region having an amino acid sequence of a light chain constant region of any class of human immunoglobulin.

16. The pharmaceutical composition according to any one of claims 1 to 15, wherein the anti-gpNMB antibody is a Fab, scFv, diabody, nanobody, VHH, bispecific antibody, or multispecific antibody, or a derivative thereof.

17. A pharmaceutical composition for removing disease-related cells, comprising an anti-gpNMB antibody or a fragment thereof or a derivative thereof that competitively binds with the anti-gpNMB antibody or a fragment thereof or a derivative thereof described in any one of claims 1 to 16 for binding to at least one site in the region spanning from V78 to the PKD domain of human gpNMB (glycoprotein nonmetastatic melanoma protein B) having the amino acid sequence of SEQ ID NO:

209.

18. A pharmaceutical composition for removing disease-related cells, comprising: a nucleic acid molecule consisting of a polynucleotide sequence encoding an anti-gpNMB antibody or a fragment thereof or a derivative thereof described in any one of claims 1 to 17; and / or a cloning vector or expression vector containing at least one of the nucleic acid molecules; and / or a recombinant cell into which the vector has been introduced.

19. The pharmaceutical composition according to any one of claims 1 to 18, wherein the disease-related cells are selected from senescent cells, cancer-associated cells, and phagocytes.

20. The pharmaceutical composition according to claim 19, wherein the cancer-associated cells are selected from cancer cells, cancer stem cells, cancer progenitor cells, and cancer infiltrating cells.

21. The pharmaceutical composition according to any one of claims 1 to 20, wherein the disease is selected from obesity, diabetes, arteriosclerosis, fibrosis, cancer, metabolic diseases, cardiovascular diseases, lysosomal stress-related diseases (e.g., lysosomal diseases, etc.), autoimmune diseases (e.g., multiple sclerosis, etc.), neuropathic pain, fibromyalgia, and glioblastoma.

22. A pharmaceutical composition according to any one of claims 1 to 21 for treating or preventing a disease by removing disease-related cells.

23. An anti-gpNMB antibody, a fragment thereof, or a derivative thereof, which specifically binds to at least one site in the region spanning V78 to S92 of human gpNMB (glycoprotein nonmetastatic melanoma protein B) having the amino acid sequence of SEQ ID NO:

209.

24. The anti-gpNMB antibody or a fragment thereof or a derivative thereof according to claim 23, which also specifically binds to a region including the amino acid residue K186 of human gpNMB having the amino acid sequence of SEQ ID NO:

209.

25. The anti-gpNMB antibody or a fragment thereof or a derivative thereof described in claim 23 or 24, wherein the anti-gpNMB antibody also specifically binds to at least one portion of the region spanning V78 to S92 of mouse gpNMB having the amino acid sequence of SEQ ID NO:

211.

26. An anti-gpNMB antibody or a fragment thereof or a derivative thereof according to any one of claims 23 to 25, which is a monoclonal antibody or a fragment thereof or a derivative thereof.

27. A peptide comprising at least a heavy chain variable region, the heavy chain variable region comprising: (17) as CDR-H1, an amino acid sequence as set forth in SEQ ID NO: 177, or an amino acid sequence in which any one, two, three, or four amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 177 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 177; as CDR-H2, an amino acid sequence as set forth in SEQ ID NO: 179, or an amino acid sequence in which any one, two, or three amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 179 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 179; and (18) as CDR-H1, an amino acid sequence set forth in SEQ ID NO: 330, or an amino acid sequence set forth in SEQ ID NO: 330 in which one, two, three, or four amino acid residues are substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 330; As CDR-H2, an amino acid sequence of SEQ ID NO: 331, or an amino acid sequence in which one, two, or three amino acid residues in the amino acid sequence of SEQ ID NO: 331 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 331, andAs CDR-H3, an amino acid sequence as set forth in SEQ ID NO: 332, or an amino acid sequence in which any one, two, or three amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 332 have been substituted, deleted, or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 332, or (19) As CDR-H1, an amino acid sequence as set forth in SEQ ID NO: 337, or an amino acid sequence in which any one, two, three, or four amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 337 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 337, As CDR-H2, an amino acid sequence as set forth in SEQ ID NO: 338, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 338 have been substituted, deleted or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 338; and As CDR-H3, an amino acid sequence as set forth in SEQ ID NO: 339, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 339 have been substituted, deleted or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 339; (20) As CDR-H1, an amino acid sequence set forth in SEQ ID NO: 344, or an amino acid sequence in which one, two, three, or four amino acid residues in the amino acid sequence set forth in SEQ ID NO: 344 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 344;As CDR-H2, an amino acid sequence as set forth in SEQ ID NO: 345, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 345 have been substituted, deleted or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 345; and As CDR-H3, an amino acid sequence as set forth in SEQ ID NO: 346, or an amino acid sequence in which one, two or three amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 346 have been substituted, deleted or inserted, or an amino acid sequence having 62.5% or more, 75.0% or more, or 87.5% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 346; (21) As the CDR grafting region-H1, an amino acid sequence as set forth in SEQ ID NO: 327, or an amino acid sequence in which any one, two, three, or four amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 327 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 327; As the CDR grafting region-H2, an amino acid sequence as set forth in SEQ ID NO: 328, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 328 have been substituted, deleted, or inserted, or an amino acid sequence having 64.7% or more, 70.5% or more, 76.4% or more, 82.3% or more, 88.2% or more, or 94.1% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 328; As the CDR grafting region-H3, an amino acid sequence set forth in SEQ ID NO: 329, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 329 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 329, or(22) As the CDR grafting region-H1, an amino acid sequence as set forth in SEQ ID NO: 334, or an amino acid sequence in which any one, two, three, or four amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 334 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 334; As the CDR grafting region-H2, an amino acid sequence as set forth in SEQ ID NO: 335, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 335 have been substituted, deleted, or inserted, or an amino acid sequence having 64.7% or more, 70.5% or more, 76.4% or more, 82.3% or more, 88.2% or more, or 94.1% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 335; (21) As the CDR grafting region-H3, an amino acid sequence as set forth in SEQ ID NO: 336, or an amino acid sequence in which any one or two amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 336 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 336; or (22) As the CDR grafting region-H1, an amino acid sequence as set forth in SEQ ID NO: 341, or an amino acid sequence in which any one, two, three, or four amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 341 have been substituted, deleted, or inserted, or an amino acid sequence having 60.0% or more, 70.0% or more, 80.0% or more, or 90.0% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 341;27. The anti-gpNMB antibody or a fragment thereof or a derivative thereof according to claim 26, comprising, as a CDR grafting region-H2, an amino acid sequence as set forth in SEQ ID NO: 342, or an amino acid sequence in which any one, two, three, four, five, or six amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 342 have been substituted, deleted, or inserted, or an amino acid sequence having 64.7% or more, 70.5% or more, 76.4% or more, 82.3% or more, 88.2% or more, or 94.1% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 342; and as a CDR grafting region-H3, an amino acid sequence as set forth in SEQ ID NO: 343, or an amino acid sequence in which any one or two amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 343 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO:

343.

28. The anti-gpNMB antibody or a fragment thereof or a derivative thereof according to claim 26 or 27, comprising at least a heavy chain variable region, the heavy chain variable region having: (17) an amino acid sequence set forth in SEQ ID NO: 189 or an amino acid sequence having 60% or more identity with the amino acid sequence set forth in SEQ ID NO: 189; or (18) an amino acid sequence set forth in SEQ ID NO: 333 or an amino acid sequence having 60% or more identity with the amino acid sequence set forth in SEQ ID NO: 333; or (19) an amino acid sequence set forth in SEQ ID NO: 340 or an amino acid sequence having 60% or more identity with the amino acid sequence set forth in SEQ ID NO: 340; or (20) an amino acid sequence set forth in SEQ ID NO: 347 or an amino acid sequence having 60% or more identity with the amino acid sequence set forth in SEQ ID NO:

347.

29. An anti-gpNMB antibody or a fragment thereof or a derivative thereof according to any one of claims 25 to 28, wherein the heavy chain variable region comprises as a framework sequence a framework sequence of any class of human immunoglobulin.

30. An anti-gpNMB antibody or a fragment thereof or a derivative thereof described in any one of claims 25 to 29, further comprising a heavy chain constant region, said heavy chain constant region having an amino acid sequence of a heavy chain constant region of any class of human immunoglobulin.

31. A nucleic acid sequence comprising at least a light chain variable region, the light chain variable region comprising: (17) an amino acid sequence as CDR-L1, the amino acid sequence of SEQ ID NO: 183, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence of SEQ ID NO: 183 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 183; and an amino acid sequence as CDR-L2, the amino acid sequence of SEQ ID NO: 185, or an amino acid sequence in which one amino acid residue in the amino acid sequence of SEQ ID NO: 185 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence of SEQ ID NO: 185; As CDR-L3, an amino acid sequence as set forth in SEQ ID NO:187, or an amino acid sequence in which any one, two or three amino acid residues in the amino acid sequence as set forth in SEQ ID NO:187 have been substituted, deleted or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO:187; or (18) As CDR-L1, an amino acid sequence as set forth in SEQ ID NO:351, or an amino acid sequence in which any one or two amino acid residues in the amino acid sequence as set forth in SEQ ID NO:351 have been substituted, deleted or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO:351; as CDR-L2, an amino acid sequence as set forth in SEQ ID NO:352, or an amino acid sequence in which any one amino acid residue in the amino acid sequence as set forth in SEQ ID NO:352 has been substituted, deleted or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO:352; as CDR-L3, an amino acid sequence as set forth in SEQ ID NO:353, or an amino acid sequence in which any one, two or three amino acid residues in the amino acid sequence as set forth in SEQ ID NO:353 have been substituted, deleted or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO:353;(19) As CDR-L1, an amino acid sequence as set forth in SEQ ID NO:358, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence as set forth in SEQ ID NO:358 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more or 83.3% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO:358; As CDR-L2, an amino acid sequence as set forth in SEQ ID NO:359, or an amino acid sequence in which one amino acid residue in the amino acid sequence as set forth in SEQ ID NO:359 has been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO:359; (20) as CDR-L1, an amino acid sequence set forth in SEQ ID NO: 365, or an amino acid sequence set forth in SEQ ID NO: 365, in which one or two amino acid residues are substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 365; as CDR-L2, an amino acid sequence as set forth in SEQ ID NO:366, or an amino acid sequence in which any one amino acid residue in the amino acid sequence as set forth in SEQ ID NO:366 has been substituted, deleted or inserted, or an amino acid sequence having 66.6% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO:366; as CDR-L3, an amino acid sequence as set forth in SEQ ID NO:367, or an amino acid sequence in which any one, two or three amino acid residues in the amino acid sequence as set forth in SEQ ID NO:367 has been substituted, deleted or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO:367;(21) As the CDR grafting region-L1, an amino acid sequence as set forth in SEQ ID NO: 348, or an amino acid sequence in which any one, two, three, or four amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 348 have been substituted, deleted, or inserted, or an amino acid sequence having 63.6% or more, 72.7% or more, 81.8% or more, or 90.9% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 348; As the CDR grafting region-L2, an amino acid sequence as set forth in SEQ ID NO: 349, or an amino acid sequence in which any one or two amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 349 have been substituted, deleted, or inserted, or an amino acid sequence having 71.4% or more or 85.7% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 349; As the CDR grafting region-L3, an amino acid sequence as set forth in SEQ ID NO: 350, or an amino acid sequence in which any one, two, or three amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 350 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 350; or (22) As the CDR grafting region-L1, an amino acid sequence as set forth in SEQ ID NO: 355, or an amino acid sequence in which any one, two, three, or four amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 355 have been substituted, deleted, or inserted, or an amino acid sequence having 63.6% or more, 72.7% or more, 81.8% or more, or 90.9% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 355; As the CDR grafting region-L2, an amino acid sequence set forth in SEQ ID NO: 356, or an amino acid sequence in which one or two amino acid residues in the amino acid sequence set forth in SEQ ID NO: 356 have been substituted, deleted, or inserted, or an amino acid sequence having 71.4% or more or 85.7% or more homology (preferably identity) with the amino acid sequence set forth in SEQ ID NO: 356;As the CDR grafting region-L3, an amino acid sequence as set forth in SEQ ID NO: 357, or an amino acid sequence in which any one, two, or three amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 357 have been substituted, deleted, or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 357; or (23) As the CDR grafting region-L1, an amino acid sequence as set forth in SEQ ID NO: 362, or an amino acid sequence in which any one, two, three, or four amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 362 have been substituted, deleted, or inserted, or an amino acid sequence having 63.6% or more, 72.7% or more, 81.8% or more, or 90.9% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 362; The anti-gpNMB antibody or a fragment thereof or a derivative thereof according to any one of claims 25 to 30, having, as a CDR grafting region-L2, an amino acid sequence as set forth in SEQ ID NO: 363, or an amino acid sequence in which any one or two amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 363 have been substituted, deleted or inserted, or an amino acid sequence having 71.4% or more or 85.7% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO: 363; and as a CDR grafting region-L3, an amino acid sequence as set forth in SEQ ID NO: 364, or an amino acid sequence in which any one, two or three amino acid residues in the amino acid sequence as set forth in SEQ ID NO: 364 have been substituted, deleted or inserted, or an amino acid sequence having 66.6% or more, 77.7% or more, or 88.8% or more homology (preferably identity) with the amino acid sequence as set forth in SEQ ID NO:

364.

32. The anti-gpNMB antibody or a fragment thereof or a derivative thereof according to any one of claims 25 to 31, comprising at least a light chain variable region, the light chain variable region having: (17) an amino acid sequence set forth in SEQ ID NO: 191 or an amino acid sequence having 60% or more identity with the amino acid sequence set forth in SEQ ID NO: 191; or (18) an amino acid sequence set forth in SEQ ID NO: 354 or an amino acid sequence having 60% or more identity with the amino acid sequence set forth in SEQ ID NO: 354; or (19) an amino acid sequence set forth in SEQ ID NO: 361 or an amino acid sequence having 60% or more identity with the amino acid sequence set forth in SEQ ID NO: 361; or (20) an amino acid sequence set forth in SEQ ID NO: 368 or an amino acid sequence having 60% or more identity with the amino acid sequence set forth in SEQ ID NO:

368.

33. An anti-gpNMB antibody or a fragment thereof or a derivative thereof according to claim 31 or 32, wherein the light chain variable region comprises as a framework sequence a framework sequence of any class of human immunoglobulin.

34. An anti-gpNMB antibody or a fragment thereof or a derivative thereof according to any one of claims 25 to 33, further comprising a light chain constant region, said light chain constant region having an amino acid sequence of a light chain constant region of any class of human immunoglobulin.

35. An anti-gpNMB antibody or a fragment thereof or a derivative thereof described in any one of claims 25 to 34, which is a Fab, scFv, diabody, nanobody, VHH, bispecific antibody, or multispecific antibody, or a derivative thereof.

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