Means and methods for protein glycosylation profiling

Abstract

The present invention provides magnetic carriers, anti-glycoprotein antibodies, antigen-binding portions thereof, one or more lectins, compositions, kits, methods, and uses based thereon, including their use in methods for glycoprofiling of glycoproteins using lectins, for example, in the diagnosis of cancer. The magnetic carriers, anti-glycoprotein antibodies, antigen-binding portions thereof, one or more lectins, compositions, kits, methods, and uses based thereon can be applied to any glycoprotein. [Selected Figure] Figure 1

Description

[Technical field]

[0001] This application contains a sequence listing in computer readable format, which is incorporated herein by reference.

[0002] The present invention relates to magnetic carriers, anti-glycoprotein antibodies, antigen-binding portions thereof, one or more lectins, compositions, kits, methods and uses thereof, including their use in methods of glycoprofiling of glycoproteins using lectins, for example in the diagnosis of cancer (e.g. Table 1). The magnetic carriers, anti-glycoprotein antibodies, antigen-binding portions thereof, one or more lectins, compositions, kits, methods and uses based thereon are applicable to any glycoprotein (e.g. Table 1). However, due to their superior sensitivity and / or specificity, the magnetic carriers, anti-glycoprotein antibodies, antigen-binding portions thereof, one or more lectins, compositions, kits, methods and uses based thereon of the present invention are particularly suitable for isoform-specific detection and analysis of glycoproteins (e.g. in the diagnosis of cancer). [Background technology]

[0003] Prostate-specific antigen (PSA) assays have revolutionized prostate cancer (PCa) screening because elevated serum PSA levels precede clinical diagnosis of PCa disease by 5-10 years or even more. However, PSA is also elevated in many benign conditions, leading to a large number of false PSA-positive tests. Furthermore, PSA does not distinguish between significant and insignificant tumors. Thus, in a large subset of patients diagnosed with PCa, the disease progresses slowly and is clinically harmless. These patients are at risk of side effects from unnecessary procedures. Thus, the major problem with PSA-based PCa screening is the unnecessary, expensive, and intrusive testing for patients (e.g., imaging, prostate biopsy, etc.). For these reasons, the United States Preventive Services Task Force (USPSTF) proposed in 2012 to discontinue the use of PSA for PCa screening. The same organization published guidance in 2017 for the use of PSA for individualized PCa screening in men aged 55–69 years.

[0004] Among PCa patients diagnosed after a moderately positive (4-10 ng / ml) PSA screening test, nearly 75% of tumors are organ-confined and potentially curable, whereas in patients with PSA levels above 10 ng / mL, the proportion of organ-confined and curable PCa drops below 50%. Thus, detecting curable PCa with high specificity (avoiding unnecessary follow-up examination procedures) is a diagnostic challenge. Moreover, overdiagnosis / overtreatment may cause complications including urinary incontinence, sexual dysfunction, and bowel problems in patients with harmless PCa. Therefore, improved screening tests would also allow for classification of tumors according to their clinical significance. Summary of the Invention [Problem to be solved by the invention]

[0005] PCa screening is usually recommended for men over 55 years of age by measuring PSA in serum. Existing methods used in clinical laboratories worldwide are not sensitive or specific enough, so it is often very difficult to accurately identify healthy from PCa patients at an early, potentially curable stage. Thus, clinicians / urologists are in need of novel diagnostically useful PCa biomarkers. [Means for solving the problem]

[0006] The present invention relates to a method for determining the glycoprofile of a protein, the method comprising the steps of: (a) contacting a sample containing the protein with an antibody against the protein to form an antibody-protein complex; (b) isolating the antibody-protein complex obtained in step (a); and (c) contacting the antibody-protein complex with one or more lectins to determine the glycoprofile of the protein.

[0007] In the method for determining the glycoprofile of a protein, it is preferred that the antibody in step (a) is not immobilized, preferably not immobilized on a solid surface, and / or that the protein is not released from the antibody during the method.

[0008] The present invention further relates to a method for diagnosing that a subject may be at risk for or suffer from cancer, the method comprising: (a) contacting a sample obtained from the subject, the sample containing a cancer biomarker protein, with an antibody against the cancer biomarker protein to form an antibody-cancer biomarker protein complex; (b) isolating the antibody-protein complex obtained in step (a); and (c) contacting the antibody-cancer biomarker protein complex with one or more lectins to determine the glycoprofile of the cancer biomarker protein; Deviation of the glycoprofile from a healthy glycoprofile of the cancer biomarker protein indicates that the subject may be at risk of or suffer from cancer.

[0009] In the method of diagnosing that a subject may be at risk for or suffer from cancer, it is preferred that the antibody in step (a) is not immobilized, preferably not immobilized on a solid surface, and / or that the protein is not released from the antibody during the performance of the method.

[0010] The present invention also relates to a method of diagnosing that a subject may be at risk for or suffer from an autoimmune disease, the method comprising: (a) contacting a sample obtained from the subject, the sample including an autoimmune disease biomarker protein, with an antibody against the autoimmune disease biomarker protein to form an antibody-autoimmune disease biomarker protein complex; (b) isolating the antibody-protein complex obtained in step (a); and (c) contacting the antibody-autoimmune disease biomarker protein complex with one or more lectins to determine the glycoprofile of the autoimmune disease biomarker protein; Deviation of the glycoprofile from a healthy glycoprofile of the autoimmune disease biomarker protein indicates that the subject may be at risk for or suffer from an autoimmune disease.

[0011] In the method of diagnosing that a subject may be at risk for or suffer from an autoimmune disease, it is preferred that the antibody in step (a) is not immobilized, preferably not immobilized on a solid surface, and / or that the protein is not released from the antibody during the performance of the method.

[0012] The present invention further relates to a method for diagnosing that a subject may be at risk for or suffer from an inflammatory disease, the method comprising: (a) contacting a sample obtained from the subject that contains an inflammatory disease biomarker protein with an antibody to the inflammatory disease biomarker protein to form an antibody-inflammatory disease biomarker protein complex; (b) isolating the antibody-protein complex obtained in step (a); and (c) contacting the antibody-inflammatory disease biomarker protein complex with one or more lectins to determine the glycoprofile of the inflammatory disease biomarker protein; Deviation of the glycoprofile from a healthy glycoprofile of the inflammatory disease biomarker protein indicates that the subject may be at risk for or suffer from an inflammatory disease.

[0013] In the method of diagnosing that a subject may be at risk for or suffer from an inflammatory disease, it is preferred that the antibody in step (a) is not immobilised, preferably not immobilised on a solid surface, and / or that the protein is not released from the antibody when the method is being performed.

[0014] Furthermore, the present invention provides a kit for carrying out a method for determining the glycoprofile of a protein as described herein, the kit comprising an antibody specific for said protein as described herein and a lectin as described herein.

[0015] The present invention also provides kits for performing a method of diagnosing that a subject may be at risk for or suffer from cancer, the kits comprising an antibody specific for a cancer biomarker protein as described herein and one or more lectins as described herein.

[0016] Furthermore, the present invention provides a kit for performing a method of diagnosing that a subject may be at risk for or suffer from an autoimmune disease, the kit comprising an antibody specific for an autoimmune disease biomarker protein that is IgG and one or more lectins as described herein.

[0017] Furthermore, the present invention provides a kit for performing a method of diagnosing that a subject may be at risk for or suffer from an inflammatory disease, the kit comprising an antibody specific for an inflammatory disease biomarker protein, which is IgG, IgA, or CRP, and one or more lectins as described herein.

[0018] Furthermore, the present invention relates to a magnetic carrier comprising i) an immobilized anti-glycoprotein antibody or an antigen-binding portion thereof, and ii) an immobilized polypeptide having peroxidase activity and having a molecular weight of less than 2 kDa. Furthermore, the present invention relates to an anti-glycoprotein antibody or an antigen-binding portion thereof immobilized on a magnetic carrier, the magnetic carrier further comprising a polypeptide having peroxidase activity immobilized on the magnetic carrier, the polypeptide having a molecular weight of less than 2 kDa.

[0019] The present application fulfills this need by providing magnetic carriers, anti-glycoprotein antibodies, antigen-binding portions thereof, one or more lectins, compositions, and kits, as described herein below, as claimed, and as illustrated in the accompanying examples and drawings.

[0020] Additionally, other suitable lectins within the contemplation of the present invention, including their post-translationally processed and mature forms, include: Neu5Ac(α2-6)Gal / GalNAc(α2-6Neu5Ac)-specific agglutinin (SNA-I) from Sambucus nigra, UniProtKB accession number: Q945S3. Galβ1-3GalNAc-binding Agaricus bisporus agglutinin (ABA), UniProtKB accession number: Q00022. Neu5Acα2-3Galβ1-4GlcNAc-binding Allomyrina dichotoma agglutinin (AlloA), which currently has no UniProtKB accession number, can be purified, for example, as described by Umetsu et al. (1984), i.e., by a purification method involving affinity chromatography on acid-treated cross-lined beaded agarose (Sepharose) and diethylaminoethanol-spherical cellulose beads (DEAE-Cellulofine). Galβ1-3GalNAc-binding Amaranthus caudatus agglutinin (ACA), UniProtKB accession number: Q6YNX3 or Q71QF2. Galβ1-3GalNAc-binding Arachis hypogaea agglutinin (AHA) = peanut agglutinin (PNA), UniProtKB accession number: P02872. Galβ1-3GalNAc-binding Artocarpus integrifolia agglutinin (AIA) = jacalin, UniProtKB accession number: P18670. Fucose-binding Aspergillus oryzae lectin (AOL), UniProtKB accession number: Q2UNX8. Mannose / glucose-binding Musa paradisiaca lectin (BanLec), UniProtKB accession number: Q8L5H4 (also mentioned, e.g., by Singh et al. (2005) and described in the RCSB Protein Data Bank (https: / / www.rcsb.org) under PDB accession code 1X1V (Released Date: 2005-11-08; Version 1.2: 2011-07-13)). (GlcNAcβ1-4) 2-4 , Galβ1-4GlcNAc-binding Datura stramonium agglutinin (jacalin) (DSA), UniProtKB accession number: A0A089ZWN7. GalNAcα1-3GalNAc-binding Dolichos biflorus agglutinin (DBA), UniProtKB accession number: P05045 or P19588. Galβ4GlcNAc-binding Erythrina cristagalli lectin (ECL), UniProtKB accession number: P83410. Galactose-binding galectin 3, UniProtKB accession number: P17931. Galactose- and lactose-binding galectin 4, UniProtKB accession number: P56470. α-GalNAc, α-Gal-binding Griffonia (Bandeiraea) simplicifolia lectin I (GSL I), UniProtKB accession number: P24146. α-GlcNAc, β-GlcNAc, and GlcNAcα1-4Galβ1-4GlcNAc binding Griffonia (Bandeiraea) simplicifolia lectin II (GSL II), UniProtKB accession number: Q41263. α-Mannose-binding Hippeastrum hybrid (Amaryllis) lectin (HHL), UniProtKB accession number: Q39990. α-GalNAc and GalNAcβ1-4Gal-binding Helix pomatia agglutinin (HPA), UniProtKB accession number: Q2F1K8. (GlcNAcβ1-4) 1-4 Binding Lycopersicon esculentum (tomato) lectin (LEL), UniProtKB accession number G9M5T0 or B3XYC5. Lens culinaris agglutinin (LCA) specific for N-linked oligosaccharides containing D-mannose or Fucα1-6GlcNAc-N-Asn, UniProtKB accession number: P02870. Fucα1-2Galβ1-4(Fucα1-3)GlcNAc-specific Lotus tetragonolobus lectin (LTA), UniProtKB accession number: P19664. Galβ1-4GlcNAc-specific Maackia amurensis agglutinin I (MAA I), UniProtKB accession number: P0DKL3. Galβ1-3(Fucα1-4)GlcNAc and Galβ1-4(Fucα1-3)GlcNAc binding macrophage galactose-binding lectin 1 (MGBL 1), UniProtKB accession number: P49300. GalNAc and galactose-binding macrophage galactose-binding lectin 2 (MGBL 2), UniProtKB accession number: A9XX86. α-Mannose-binding Narcissus pseudonarcissus lectin (NPA), UniProtKB accession number: Q40423. GalNAcα1-3(Fucα1-2)Gal-binding Phaseolus lunatus agglutinin (lima bean, LBA), UniProtKB accession number: P16300. N-linked biantennary binding Phaseolus vulgaris agglutinin E (PHA E), UniProtKB accession number: P05088. N-linked 3 / 4 antennary binding Phaseolus vulgaris agglutinin L (PHA L), UniProtKB accession number: P05087. Fucα1-6-specific Pholiota squarrosa lectin (PhoSL) purified as described by Kobayashi et al. (2012) (also described, for example, in SEQ ID NO: 58 herein), currently does not have a UniProtKB accession number. GlcNAc-conjugated Phytolacca Americana agglutinin (PWM), UniProtKB accession number: Q9AVB0. α-Mannose, α-glucose, or Fucα1-6GlcNAc binding Pisum sativum lectin (PSL), UniProtKB accession number: P02867. GalNAc or galactose-binding Psophocarpus tetragonolobus lectin I (PTA I), UniProtKB accession number: O24313. GalNAc or galactose-binding Psophocarpus tetragonolobus lectin II (PTA II), UniProtKB accession number: Q9SM56. Galactose-binding Ricinus communis agglutinin I (RCA I), UniProtKB accession number: P06750. Galactose- and GalNAc-binding Ricinus communis agglutinin II (RCA II), UniProtKB accession number: B9SPG3. Sialic acid-binding immunoglobulin-like lectin 1 (Siglec-1); Preferential binding of Neu5Acα2-3Galβ1-4Glc / GlcNAc over Neu5Acα2-6Galβ1-4Glc / GlcNAc by Siglec-1; UniProtKB accession number: Q9BZZ2. Sialic acid-binding immunoglobulin-like lectin 4 (Siglec-4); Preferential binding of Neu5Acα2-3Galβ1-4Glc / GlcNAc over Neu5Acα2-6Galβ1-4Glc / GlcNAc by Siglec-4; UniProtKB accession number: P20916. Sialic acid-binding immunoglobulin-like lectin 8 (Siglec-8); preferential binding of Neu5Acα2-3Galβ1-4Glc / GlcNAc over Neu5Acα2-6Galβ1-4Glc / GlcNAc by Siglec-8; UniProtKB accession number: Q9NYZ4. Sialic acid-binding immunoglobulin-like lectin 11 (Siglec-11), Preferential binding of Neu5Acα2-8Neu5Ac (polysialic acid) by Siglec-11, UniProtKB accession number: Q96RL6. GalNAcα1-3GalNAc-conjugated soybean agglutinin (SBA), UniProtKB accession number: P05046. βGalNAc-conjugated Sophora japonica agglutinin (SJA), UniProtKB accession number: P93535. Neu5Ac(α2-6)Gal / GalNAc-binding Sambucus sieboldiana agglutinin (SSA) purified as described by Kaku et al. (1996) (also described, for example, in SEQ ID NO:59 herein), currently does not have a UniProtKB accession number. GalNAc-binding Salvia sclarea lectin purified as described by Wu AM (2005), currently no UniProtKB accession number. (GlcNAcβ1-4) 2-5 and Neu5Ac-binding Triticum vulgaris agglutinin (TVA) = WGA-wheat germ agglutinin, UniProtKB accession numbers: P02876, P10968, or P10969. Fucα1-2Gal_binding Ulex europaeus agglutinin (UEA), UniProtKB accession number: P22972. GalNAc-serine-binding Vicia villosa lectin (VVL), UniProtKB accession number: P56625.

[0021] The lectins of the present invention can be isolated and optionally purified using conventional methods known in the art. For example, when isolated from their natural source, the lectins can be purified to homogeneity on a suitable immobilized carbohydrate matrix and eluted with a suitable hapten. See Goldstein and Poretz (1986) (The lectins. Properties, functions and applications in biology and medicine (Liener et al. eds.), pp. 33-247. Academic Press, Orlando, Fla.), Rudiger (1993) (Glycosciences: Status and perspectives (Gabius and Gabius eds.), pp. 415-438. Chapman and Hall, Weinheim, Germany). Alternatively, the lectins can be produced recombinantly according to recognized methods. See Streicher and Sharon (2003) Methods Enzymol. 363:47-77. As yet another alternative, the lectins can be produced using standard peptide synthesis techniques known in the art or using chemical cleavage methods based on the amino acid sequences of known lectins or lectins disclosed herein (e.g., U.S. Pat. No. 9,169,327). Another alternative can be an artificial lectin prepared by chemical modification of any of the above-identified lectins (see YW Lu, CW Chien, PC Lin, LD Huang, CY Chen, SW Wu, CL Han, KH Khoo, CC Lin, YJ Chen, BAD-Lectins: Boronic Acid-Decorated Lectins with Enhanced Binding Affinity for the Selective Enrichment of Glycoproteins, Analytical Chemistry, 85 (2013) 8268-8276.). [Brief description of the drawings]

[0022] [Figure 1] Figure 1 shows PSA with glycan composition from (A) healthy men and (B) PCa patients (showing a large variety of possible glycan structures). Assay protocols for detecting (C) PSA levels, (D) PSA glycan profiling in ELLA format, and (E) PSA glycan profiling in MELLA (i.e. magnetic ELLA) format are shown. Abbreviations: PSA-prostate specific antigen, Ab1-anti-PSA antibody 1 labeled with horseradish peroxidase (HRP), Ab2-anti-PSA antibody 2, L-lectin, HRP-horseradish peroxidase. [Diagram 2] Figure 2 shows the ROC of PSA glycan profiling in magnetic ELLA format vs. PSA in ELISA format using two different lectins, AAL (left) and ConA (right), in BPH vs. PCa samples. [Diagram 3] FIG. 3 shows the ROC of PSA glycoprofiling in magnetic ELLA format vs. PSA in ELISA format with two different lectins, MAA-II (left) and SNA-I (right), in BPH vs. PCa samples. [Figure 4] FIG. 4 shows the ROC of PSA glycan profiling in magnetic ELLA format vs. PSA in ELISA format with WFA lectin (left) and four different lectins, AAL (negative predictor), ConA (negative predictor), MAA-II (positive predictor), and SNA-I (negative predictor), in BPH vs. PCa samples. [Diagram 5] FIG. 5 shows the ROC of PSA glycoprofiling in magnetic ELLA format vs. PSA using two biomarkers: BPH samples vs. PCa samples. [Figure 6] Figure 6 shows the ROC of PSA glycoprofiling in magnetic ELLA format vs. PSA using the three biomarkers: BPH samples vs. PCa samples. [Figure 7]Figure 7 shows the ROC of PSA glycoprofiling in magnetic ELLA format vs. PSA (AAL and Con A) using single biomarkers. PCa- samples vs. PCa+ samples. [Figure 8] Figure 8 shows the ROC of PSA glycoprofiling in magnetic ELLA format vs. PSA using single biomarkers (MAA II and SNA-I). PCa- samples vs. PCa+ samples. PCa- refers to prostate cancer without metastasis and PCa+ refers to prostate cancer with metastasis. [Figure 9] Figure 9 shows box plots showing the discrimination ability of two different biomarkers (PSA and MAA) in different types of samples including BPH, PCa+, PCa-, and PCa (PCa+ and PCa- combined). PCa- refers to prostate cancer without metastasis, and PCa+ refers to prostate cancer with metastasis. [Figure 10] Figure 10 depicts box plots showing the ability of the PSA biomarker to discriminate samples in different types of samples including BPH, PCa+, PCa-, and PCa (PCa+ and PCa- combined), where PCa- refers to prostate cancer without metastasis and PCa+ refers to prostate cancer with metastasis. [Figure 11] FIG. 11 shows the ROC curve for the analysis of human serum samples to discriminate BPH (benign prostatic hyperplasia) patients from PCa (prostate cancer) patients using magnetic particles (MPs) without immobilized antibodies. [Figure 12] FIG. 12 shows the ROC curve for the analysis of human serum samples to discriminate BPH patients from PCa patients using magnetic particles containing immobilized antibodies to release PSA from MPs for subsequent lectin-based glycoprofiling. [Figure 13] FIG. 13 shows the ROC curve for the analysis of human serum samples to discriminate BPH patients from PCa patients using antibodies immobilized on ELISA plates followed by lectin-based glycan profiling. DETAILED DESCRIPTION OF THE PREFERRED EMBODIMENTS

[0023] definition Abbreviations for carbohydrates used herein include "Neu5Ac" for N-acetylneuraminic acid, "Fuc" for fucose, "GalNAc" for N-acetylgalactosamine, "GlcNAc" for N-acetylglucosamine, and "Gal" for galactose (e.g., Varki A, Cummings RD, Esko JD, Freeze HH, Stanley P, Bertozzi CR, Hart GW, E. ME., Essentials of Glycobiology, 2nd edition, Cold Spring Harbor Laboratory Press, Cold Spring Harbor (NY), 2009).

[0024] Additionally, as used herein, the following terms are defined below. "Core fucose" means that fucose is attached by an α-glycosidic bond from its C1 atom to the C6 atom of N-acetylglucosamine. "Antennary fucose" means that fucose is bound to the C3 atom of N-acetylglucosamine by an α-glycosidic bond of its C1 atom, or that fucose is bound to the C2 atom of an adjacent fucose by an α-glycosidic bond of its C1 atom. "Fucα1-6GlcNAc-N-Asn-containing N-linked oligosaccharide" refers to an oligosaccharide having fucose bound via an α-glycosidic bond to the C6 atom of N-acetylglucosamine, which is bound to asparagine via an N-glycosidic bond. "Fucα1-6 / 3GlcNAc" means that fucose is attached by an α-glycosidic bond from its C1 atom to the C6 (C3) atom of N-acetylglucosamine. "α-L-Fuc" means α-L-fucose. "Fucα1-2Galβ1-4(Fucα1-3)GlcNAc" means that a fucose is bound to the C2 atom of a galactose which is bound to the C4 atom of N-acetylglucosamine via a β-glycosidic bond at its C1 atom, and at the same time, a second fucose is bound to the C3 atom of N-acetylglucosamine via an α-glycosidic bond at its C1 atom. "Fucα1-2Gal" means that fucose is attached by an α-glycosidic bond from its C1 atom to the C2 atom of galactose. "Fucα1-6GlcNAc" means that fucose is attached by an α-glycosidic bond from its C1 atom to the C6 atom of N-acetylglucosamine. "Manβ1-4GlcNAcβ1-4GlcNAc" means that mannose is bound to the C4 atom of N-acetylglucosamine via a β-glycosidic bond at the C1 atom, which is bound to the C4 atom of N-acetylglucosamine via a β-glycosidic bond at the C1 atom. "Branched N-linked hexasaccharide" means a non-linear glycan composed of six carbohydrate units linked to an asparagine by N-glycosidic bonds. "Manα1-3Man" means that mannose is linked by a β-glycosidic bond of its C1 atom to the C3 atom of mannose. "α-D-Man" means α-D-mannose. "(GlcNAcβ1-4) 2-4 " means that N-acetylglucosamine is repeatedly linked to the C4 atom of N-acetylglucosamine by a β-glycosidic bond of its C1 atom. "Galβ1-4GlcNAc" means that galactose is attached by a β-glycosidic bond from its C1 atom to the C4 atom of N-acetylglucosamine. "GlcNAcα1-4Galβ1-4GlcNAc" means that N-acetylglucosamine is bound by an α-glycosidic bond at its C1 atom to the C4 atom of galactose, which is bound to the C4 atom of N-acetylglucosamine via a β-glycosidic bond at its C1 atom. "N-acetylglucosamine" means the amide between glucosamine and acetic acid. "(GlcNAcβ1-4) 2-5 " means that N-acetylglucosamine is repeatedly linked to the C4 atom of N-acetylglucosamine by a β-glycosidic bond of its C1 atom. "Neu5Ac" (or sialic acid) means N-acetylneuraminic acid. "Galβ1-3GalNAc-serine / threonine" means that galactose is bound to the C3 atom of N-acetylglucosamine, which is bound to serine / threonine, via a β-glycosidic bond at its C1 atom. "Galα1-3GalNAc" means that galactose is attached by an α-glycosidic bond from its C1 atom to the C3 atom of N-acetylgalactosamine. "Galβ1-6Gal" means that galactose is linked by a β-glycosidic bond from its C1 atom to the C6 atom of galactose. "Galβ1-4GlcNAc" means that galactose is attached by a β-glycosidic bond from its C1 atom to the C3 atom of N-acetylglucosamine. "Galβ1-3GalNAc" means that galactose is attached by a β-glycosidic bond from its C1 atom to the C3 atom of N-acetylgalactosamine. "GalNAcα1-3GalNAc" means that N-acetylgalactosamine is linked by an α-glycosidic bond from its C1 atom to the C3 atom of N-acetylgalactosamine. "GalNAcα1-3Gal" means that N-acetylgalactosamine is attached via an α-glycosidic bond from its C1 atom to the C3 atom of galactose. "GalNAcα / β1-3 / 4Gal" means that N-acetylgalactosamine is linked via an α- or β-glycosidic bond of its C1 atom to the C3 or C4 atom of galactose. "α-GalNAc" refers to the amide between α-galactosamine and acetic acid. "GalNAcβ1-4Gal" means that N-acetylgalactosamine is attached via a β-glycosidic bond from its C1 atom to the C4 atom of galactose. "GalNAcβ1-3(Fucα1-2)Gal" means that N-acetylglucosamine is linked to the C3 atom of galactose through an α-glycosidic bond of its C1 atom, and at the same time, fucose is linked to the C2 atom of galactose through an α-glycosidic bond of its C1 atom. "GalNAcα1-2Gal" means that N-acetylgalactosamine is attached via an α-glycosidic bond from its C1 atom to the C3 atom of galactose. "GalNAcα1-3GalNAc" means that N-acetylgalactosamine is linked by an α-glycosidic bond from its C1 atom to the C3 atom of N-acetylgalactosamine. "GalNAcβ1-3 / 4Gal" means that N-acetylgalactosamine is linked via a β-glycosidic bond from its C1 atom to the C3 or C4 atom of galactose. "GalNAc-Ser / Thr" (or Tn antigen) means that N-acetylgalactosamine is attached to serine / threonine by an O-glycosidic bond. "Galβ1-3GalNAc-Ser / Thr" (T antigen or Thomsen-Friedenreich antigen) refers to a galactose bond via a β-glycosidic bond to the C3 atom of N-acetylgalactosamine, which is bound to serine / threonine via an O-glycosidic bond. "GalNAcβ1-4GlcNAc" (or LacdiNAc) means that N-acetylgalactosamine is linked by a β-glycosidic bond from its C1 atom to the C4 atom of N-acetylglucosamine. "α2-3Neu5Ac" (or α2-3-linked sialic acid) means that N-acetylneuraminic acid is linked by an α-glycosidic bond from its C2 atom to the C3 atom of an adjacent saccharide. "α2-6Neu5Ac" (or α2-6-linked sialic acid) means that N-acetylneuraminic acid is linked by an α-glycosidic bond from its C2 atom to the C6 atom of an adjacent saccharide. "α2-8Neu5Ac" (or α2-8-linked sialic acid) means that N-acetylneuraminic acid is linked by an α-glycosidic bond from its C2 atom to the C8 atom of an adjacent N-acetylneuraminic acid. "Neu5Acα4 / 9-O-Ac-Neu5Ac" means that N-acetylneuraminic acid is linked by an α-glycosidic bond of its C4 atom to the C9 atom of the adjacent O-acetyl-N-acetylneuraminic acid. "Neu5Acα2-3Galβ1-4Glc / GlcNAc" means that N-acetylneuraminic acid is bound via an α-glycosidic bond at the C2 atom to the C3 atom of galactose, which is bound via a β-glycosidic bond at the C1 atom to the C4 atom of glucose or N-acetylglucosamine. "Neu5Acα2-6Gal / GalNAc" means that N-acetylneuraminic acid is linked by an α-glycosidic bond from its C2 atom to the C6 atom of galactose or N-acetylgalactosamine. "N-linked biantennary" means a non-linear glycan having two antennae (carbohydrate chains) attached to an asparagine by N-glycosidic bonds. "N-linked 3 / 4 antennary" means a non-linear glycan having 3 / 4 antennae (carbohydrate chains) attached to asparagine by N-glycosidic bonds. "Bisecting β1-6GlcNAc" means that the N-acetylglucosamine is linked by a β-glycosidic bond from its C1 atom to the C6 atom of an adjacent saccharide. "Galα1-3(Fucα1-2)Galβ1-3 / 4GlcNAc" means that galactose is bound to the C3 atom of galactose via an α-glycosidic bond at the C1 atom, which is bound to the C3 or C4 of N-acetylglucosamine via a β-glycosidic bond at the C1 atom, and at the same time, fucose is bound to the C2 atom of N-acetylglucosamine via an α-glycosidic bond at the C1 atom. "Galβ1-3(Fucα1-4)GlcNAc" means that galactose is linked to the C3 atom of N-acetylglucosamine by a β-glycosidic bond at its C1 atom, and at the same time, fucose is linked to the C4 atom of N-acetylglucosamine by an α-glycosidic bond at its C1 atom. "NeuAcα2-3Galβ1-3(Fucα1-4)GlcNAc" means that N-acetylneuraminic acid is bound to the C3 atom of galactose via a β-glycosidic bond at its C1 atom, which is bound to the C3 atom of N-acetylglucosamine via a β-glycosidic bond at its C1 atom, and at the same time, fucose is bound to the C4 atom of N-acetylglucosamine via an α-glycosidic bond at its C1 atom. "Fucα1-2Galβ1-3(Fucα1-4)GlcNAc" means that a fucose is bound to the C2 atom of a galactose which is bound to the C3 atom of N-acetylglucosamine via a β-glycosidic bond at its C1 atom, and at the same time, a second fucose is bound to the C4 atom of N-acetylglucosamine via an α-glycosidic bond at its C1 atom. "Galβ1-4(Fucα1-3)GlcNAc" means that galactose is linked to the C4 atom of N-acetylglucosamine by a β-glycosidic bond at its C1 atom, and at the same time, fucose is linked to the C3 atom of N-acetylglucosamine by an α-glycosidic bond at its C1 atom. "NeuAcα2-3Galβ1-4(Fucα1-3)GlcNAc" means that N-acetylneuraminic acid is bound to the C3 atom of galactose via an α-glycosidic bond at its C2 atom, which is bound to the C4 atom of N-acetylglucosamine via a β-glycosidic bond at its C1 atom, and at the same time, fucose is bound to the C3 atom of N-acetylglucosamine via an α-glycosidic bond at its C1 atom. "Fucα1-2Galβ1-4(Fucα1-3)GlcNAc" means that a fucose is bound by an α-glycosidic bond to the C2 atom of a galactose which is bound to the C4 atom of N-acetylglucosamine via a β-glycosidic bond to its C1 atom, and at the same time, a second fucose is bound to the C3 atom of N-acetylglucosamine via an α-glycosidic bond to its C1 atom. "High mannose" means a glycan that contains more than three mannose units. "Cialil Lewis a " (Sialyl Le a) The antigen is Neu5Acα2-3 / 6Galβ1-3(Fucα1-4)GlcNAc, which means that N-acetylneuraminic acid is bound by an α-glycosidic bond at the C2 atom to the C3 or C6 atom of galactose which is bound to the C3 atom of N-acetylglucosamine via a β-glycosidic bond at its C1 atom, and at the same time, fucose is bound to the C4 atom of N-acetylglucosamine via an α-glycosidic bond at its C1 atom. "Cialil Lewis x " (Sialyl Le x ) The antigen is Neu5Acα2-3 / 6Galβ1-4(Fucα1-3)GlcNAc, which means that N-acetylneuraminic acid is bound by an α-glycosidic bond at the C2 atom to the C3 or C6 atom of galactose which is bound to the C4 atom of N-acetylglucosamine via a β-glycosidic bond at its C1 atom, and at the same time, fucose is bound to the C3 atom of N-acetylglucosamine via an α-glycosidic bond at its C1 atom. "Lewis x " " x ) antigen is "Galβ1-4(Fucα1-3)GlcNAc", which means that galactose is bound to the C4 atom of N-acetylglucosamine by a β-glycosidic bond at its C1 atom, and at the same time, fucose is bound to the C3 atom of N-acetylglucosamine by an α-glycosidic bond at its C1 atom. The "sialyl-Tn antigen" is "Neu5Acα2-3 / 6GalNAc-Ser / Thr," which means that N-acetylneuraminic acid is bound to the C3 or C6 atom of N-acetylgalactosamine via an O-glycosidic bond at the C2 atom via an α-glycosidic bond. "Sialyl T antigen" is "Neu5Acα2-3 / 6Galβ1-3GalNAc-Ser / Thr," which means that N-acetylneuraminic acid is bound to the C3 or C6 atom of galactose via an α-glycosidic bond at the C2 atom of galactose, which is bound to the C3 atom of N-acetylgalactosamine via an O-glycosidic bond at the C1 atom of galactose. "Lewis y " " y ) The antigen is "Fucα1-2Galβ1-4(Fucα1-3)GlcNAc," which means that a fucose is bound by an α-glycosidic bond to the C2 atom of galactose which is bound to the C4 atom of N-acetylglucosamine via a β-glycosidic bond to its C1 atom, and at the same time, a second fucose is bound to the C3 atom of N-acetylglucosamine via an α-glycosidic bond to its C1 atom. The "sulfated core 1 glycan" is a glycan based on the sulfated extended form of T antigen. The "core 2 glycan" is an glycan based on an extended form of Galβ1-3(GlcNAcβ1-6)GalNAc-Ser / Thr, which means an extended form of glycan having galactose bound to the C3 atom of N-acetylgalactosamine by a β-glycosidic bond of its C1 atom, and at the same time, N-acetylglucosamine bound to the C6 atom of N-acetylgalactosamine which is bound to serine / threonine by a β-glycosidic bond of its C1 atom. "Lewis a " " a ) antigen is Galβ1-3(Fucα1-4)GlcNAc, which means that galactose is attached to the C3 atom of N-acetylglucosamine by a β-glycosidic bond of its C1 atom, and at the same time, fucose is attached to the C4 atom of N-acetylglucosamine by an α-glycosidic bond of its C1 atom. "(GlcNAcβ1-4) n " means that N-acetylglucosamine is repeatedly linked to the C4 atom of N-acetylglucosamine by a β-glycosidic bond of its C1 atom. "β-D-GlcNAc" refers to the amide between β-D-glucosamine and acetic acid. "GalNAc" refers to the amide between galactosamine and acetic acid. "Gal-GlcNAc" means that galactose is attached to N-acetylglucosamine by a non-specific bond. "GlcNAc" refers to the amide between glucosamine and acetate. "Galα1-3Gal" means that galactose is linked by an α-glycosidic bond from its C1 atom to the C3 atom of galactose. "Galβ1-3GalNAc" means that galactose is attached by a β-glycosidic bond from its C1 atom to the C3 atom of N-acetylgalactosamine. "α-Gal" means α-galactose. "α-GalNAc" refers to the amide between α-D-galactosamine and acetic acid. "(GlcNAc) n " means that the N-acetylglucosamine is bound to the N-acetylglucosamine by a non-specific bond. "Branch (LacNAc) n " is a branched and repeating form of Galβ1,4-GlcNAc, which means a branched and repeating form of galactose attached by a β-glycosidic bond of its C1 atom to the C4 atom of N-acetylglucosamine.

[0025] The term "glycoprotein" (or "glycosylated protein") as used herein means a protein containing one or more of various types of N-, O-, S-, or C-covalently linked carbohydrates, ranging from, for example, monosaccharides to branched polysaccharides (including modifications thereof such as the addition of sulfo or phospho groups). An N-linked glycan is a carbohydrate attached to the -NH2 group of asparagine. An O-linked glycan is a carbohydrate attached to the -OH group of serine, threonine, or a hydroxylated amino acid. An S-linked glycan is a carbohydrate attached to the -SH group of cysteine. A C-linked glycan is a carbohydrate attached to tryptophan by a C-C bond.

[0026] The term "carbohydrate" refers to a substance with the stoichiometric chemical formula C n (H2O) n (e.g., aldoses, ketoses, etc.). The general term "carbohydrate" includes monosaccharides, oligosaccharides, and polysaccharides, as well as substances derived from monosaccharides by reduction of a carbonyl group (alditols), by oxidation of one or more terminal groups to a carboxylic acid, or by replacement of one or more hydroxyl groups by a hydrogen atom, an amino group, a thiol group, or a similar group. The general term "carbohydrate" also includes derivatives of these compounds.

[0027] The term "glycoprofile of a protein" refers to the carbohydrate structure of a protein, e.g., the composition and / or structure of covalently bound carbohydrates, e.g., the amount, presence, or absence of covalently bound carbohydrates.

[0028] The term "glycoprofiling" refers to determining the carbohydrate structure (e.g., the composition and / or structure of covalently bound carbohydrates, e.g., the amount, presence, or absence of covalently bound carbohydrates) of a glycoconjugate, such as a glycoprotein, a glycolipid, or a proteoglycan.

[0029] The term "DART" refers to dual-affinity re-targeting antibodies, which are bispecific antibody-derived molecules capable of simultaneously binding to two distinct cell surface molecules (e.g., Sung JAM et al., 2015).

[0030] The term "Adnectin" (or "monobody") refers to synthetic binding proteins capable of binding antigens; for example, they can be constructed using the fibronectin type III I domain (FN3) as a molecular scaffold. Monobodies are a simple and robust alternative to antibodies in generating target-binding proteins.

[0031] The term "single domain antibody" (or "nanobody") refers to an antibody fragment consisting of a single monomeric variable antibody domain.

[0032] The term "FN3 scaffold" refers to a fibronectin type III domain I (FN3) scaffold that can be used as a non-antibody scaffold in generating binding proteins (e.g., antigen-binding proteins) (e.g., Koide A. et al., 2012).

[0033] The term "affibody" refers to a group of engineered affinity proteins that are capable of binding to target proteins or peptides with high affinity that mimics monoclonal antibodies and are therefore a member of a family of antibody-mimetic molecules (e.g., Lofblom J et al., 2010).

[0034] The term "anticalin" refers to an artificial protein capable of binding to an antigen and either to a protein or to a small molecule. Anticalins are not structurally related to antibodies and are a class of antibody mimetic molecules. Preferably, an "anticalin" is a protein derived from lipocalin (also known as cytosolic fatty acid binding protein) that has been genetically modified to alter its binding properties. Anticalins have the advantages of the specificity of monoclonal antibodies for small lipid molecules (e.g., steroids, bilins, retinoids, and lipids), excellent tissue penetration, and thermal stability, but without the large size (e.g., they are 1 / 8 times smaller) and can be batch produced in E. coli, without the need for extraction from animals.

[0035] "Avimer" (e.g., an abbreviation of avidity multimer) refers to an artificial protein capable of specifically binding to an antigen through multiple binding sites. Avimers are structurally unrelated to antibodies and are classified as a class of antibody mimetic molecules.

[0036] The term "cyclic peptide" refers to a polypeptide chain that contains a circular arrangement of bonds. The term "bicyclic peptide" (e.g., amanitin in amatoxins, phalloidin in phallotoxins) generally refers to a cyclic peptide that contains a bridging group (e.g., a thioether or disulfide bond) between two polypeptide side chains. In amatoxins, this bridge is formed as a thioether between Trp and Cys residues. Other bicyclic peptides include echinomycin, triostin A, and serogentin C. There are also cyclic peptide hormones that are cyclized by a disulfide bond between two cysteines, such as somatostatin and oxytocin. For example, a "bicyclic peptide" screening and production method can use a phage library displaying peptides that contain three Cys residues. The phage is treated under mild conditions with tris-(bromomethyl)benzene, which reacts with all three cysteines, forming two peptide loops of six amino acids that are linked to the benzene ring (e.g., Mund T et al., 2014).

[0037] "DARPins" (short for "designed ankyrin repeat proteins") refer to engineered antibody mimetic molecular proteins that exhibit high specificity and high affinity target protein binding. They are derived from natural ankyrin proteins that are responsible for diverse functions such as cell signaling, cell regulation and structural integrity. DARPins consist of at least three repeat motif proteins, usually four or five repeat motif proteins. Their molecular mass is approximately 14 or 18 kDa (kilodaltons) for four or five repeat DARPins, respectively (e.g. Pluckthun A, 2015; Rasool M et al., 2017).

[0038] The term "Kunitz domain" refers to an active domain of a protein capable of inhibiting the function of a proteolytic enzyme (e.g., a protein domain characteristic of inhibitors of the S1 serine peptidase family). Preferred examples include aprotinin, trypstatin, rat mast cell trypsin inhibitor, and tissue factor pathway inhibitor (TFPI).

[0039] The term "obody" refers to a single domain protein module (e.g., a single domain scaffold) that can bind to a specific target molecule (e.g., protein, carbohydrate, nucleic acid, and small molecule ligand) (e.g., Steemson JD et al., 2014).

[0040] The term "aptamer" refers to an oligonucleotide or peptide molecule that binds to a specific target molecule.

[0041] The term "agglutinin" refers to any substance that causes cells to clump together (i.e., clump together), particularly certain antibodies that form in the blood in response to the presence of an invading agent, or lectins that have such an effect. More specifically, the term "agglutinin," as used herein, refers to carbohydrate-binding proteins (lectins, see 153).

[0042] The term "glycan" refers to a compound consisting of glycosidically linked monosaccharides, and can also refer to the carbohydrate portion of a glycoconjugate such as a glycoprotein, glycolipid, or proteoglycan, even if the carbohydrate is only a monosaccharide or oligosaccharide.

[0043] As used herein, the term "lectin" refers to a carbohydrate-binding protein. Lectins may have high specificity for carbohydrate moiety(s) (e.g., lectins react specifically with terminal glycosidic residues of other molecules, such as glycans of glycoproteins (e.g., branched sugar molecules of glycoproteins, such as target polypeptides in the sense of the present invention and biomarkers as described in Table 1 herein). Lectins are well known in the art. A person skilled in the art can easily determine which lectins can be used to bind carbohydrate moiety(s) of interest, such as carbohydrate moiety(s) of glycans attached to proteins. Preferred lectins to be applied in the context of the present invention are described herein. The term "lectin" also includes siglecs (sialic acid-binding immunoglobulin-like lectins). In particular, as used herein, the term "lectin" also refers to carbohydrate-binding antibodies. Thus, as used herein, the term "lectin" includes lectins, siglecs, and carbohydrate-binding antibodies.

[0044] As used herein, an "antibody" is a protein comprising one or more polypeptides (including one or more binding domains, preferably antigen binding domains) substantially or partially encoded by immunoglobulin genes or fragments of immunoglobulin genes. Preferably, an antibody to a protein whose glycoprofile has been determined as described herein is not directed to a glycochain attached to the protein. Stated differently, an antibody to a protein whose glycoprofile has been determined as described herein is preferably directed to the protein itself, i.e., to an epitope within the amino acid sequence of the protein. The epitope may be a linear epitope or a conformational epitope. The epitope may be a continuous epitope or a discontinuous epitope. The term "immunoglobulin" (Ig) is used interchangeably with "antibody" herein. Recognized immunoglobulin genes include the kappa, lambda, alpha, gamma, delta, epsilon, and mu constant region genes, as well as the myriad immunoglobulin variable region genes. In particular, as used herein, an "antibody" is typically a tetrameric glycosylated protein composed of two light (L) chains of about 25 kDa each and two heavy (H) chains of about 50 kDa each. Two types of light chains, called lambda and kappa, may be found in antibodies. Depending on the amino acid sequence of the constant domain of the heavy chain, immunoglobulins can be classified into five main classes, A, D, E, G, and M, some of which can be further divided into subclasses (isotypes), e.g., IgG1, IgG2, IgG3, IgG4, IgA1, and IgA2, with IgG being preferred in the context of the present invention. Antibodies of the present invention are also envisaged that have an IgE constant domain or a portion thereof that is bound to the Fc epsilon receptor I. IgM antibodies consist of five basic heterotetrameric units with an additional polypeptide called the J chain and contain ten antigen-binding sites, whereas IgA antibodies contain two to five basic four-chain units that polymerize and combine with the J chain to form multivalent aggregates. For IgG, the four-chain unit is typically about 150,000 daltons.Each light chain comprises an N-terminal variable (V) domain (VL) and a constant (C) domain (CL). Each heavy chain comprises an N-terminal V domain (VH), three or four C domains (CH), and a hinge region. The constant domains are not directly involved in binding the antibody to the antigen, but may exhibit various effector functions, such as involvement in antibody-dependent cellular cytotoxicity (ADCC). If the antibody confers ADCC, it is preferably of the IgG1 subtype, while the IgG4 subtype is not considered to have the ability to confers ADCC.

[0045] The term "antibody" also includes, but is not limited to, monoclonal antibodies, monospecific antibodies, multispecific or multi-specific antibodies such as bispecific antibodies, humanized antibodies, camelized antibodies, human antibodies, single-chain antibodies, chimeric antibodies, synthetic antibodies, recombinant antibodies, hybrid antibodies, mutated antibodies, grafted antibodies, and in vitro generated antibodies, with chimeric or humanized antibodies being preferred. The term "humanized antibody" is generally defined for antibodies in which the specificity-encoding CDRs of the HC and LC have been transferred onto a suitable human variable framework ("CDR grafted"). The term "antibody" also includes scFv, single-chain antibodies, diabodies or tetrabodies, domain antibodies (dAbs), and nanobodies. In the present invention, the term "antibody" is also intended to include dimeric, trimeric, or multimeric antibodies having multiple antigen-binding sites, or bifunctional, trifunctional, or multifunctional antibodies. The term also includes antigen-binding portions. The term "antibody" also includes an FN3 scaffold, an adnectin, an affibody, an anticalin, an avimer, a bicyclic peptide, a DARPin, a Kunitz domain, an obody, or an aptamer, such as a DNA, RNA or peptide aptamer.

[0046] Preferred antibodies of the present invention include, but are not limited to, anti-PSA antibody, anti-AFP antibody, anti-MUC16 antibody, anti-WFDC2 antibody, anti-MUC1 antibody, anti-ERBB2 antibody, anti-CEACAM5 antibody, anti-FUT3 antibody, or anti-TG antibody, etc. Further preferred antibodies related to the present invention are shown in Table 1 below.

[0047] Furthermore, the term "antibody" as used in the present invention also relates to derivatives (including fragments) of the antibodies described herein. A "derivative" of an antibody includes an amino acid sequence that has been altered by the introduction of substitutions, deletions, or additions of amino acid residues. Furthermore, derivatives include antibodies that have been modified by the covalent attachment of any type of molecule to the antibody or protein. Examples of such molecules include, but are not limited to, sugars, PEG, hydroxyl groups, ethoxy groups, carboxy groups, or amine groups. In effect, covalent modifications of antibodies result in, but are not limited to, glycosylation, pegylation, acetylation, phosphorylation, amidation.

[0048] The antibody of the present invention is preferably an "isolated" antibody. When used to describe the antibodies disclosed herein, "isolated" means an antibody that has been identified, separated, and / or recovered from components of its production environment. Preferably, an isolated antibody is free of association with all other components from its production environment. Contaminating components of its production environment, such as those resulting from recombinantly transfected cells, are typically substances that may interfere with diagnostic or therapeutic uses of the polypeptide and may include enzymes, hormones, and other proteinaceous or non-proteinaceous solutes. In a preferred embodiment, the antibody can be (1) purified sufficiently to obtain at least 15 residues of N-terminal or internal amino acid sequence using a spinning cup sequenator, or (2) purified to homogeneity by SDS-PAGE under non-reducing or reducing conditions using Coomassie blue, or preferably silver staining. Ordinarily, however, an isolated antibody can be prepared by at least one purification step.

[0049] As used herein, the term "antigen-binding portion" refers to a fragment of an immunoglobulin (or an intact antibody) and includes any polypeptide that contains an antigen-binding fragment or an antigen-binding domain. Preferably, it includes fragments such as Fab, F(ab'), F(ab')2, Fv, scFv, Fd, disulfide-linked Fv (sdFv), and other antibody fragments that retain antigen-binding function as described herein (e.g., single-chain antibody fragments (scAbs)). Typically, such fragments contain the antigen-binding domain and may have the same properties as the antibodies described herein.

[0050] Preferred antigen-binding portions of antibodies of the invention include, but are not limited to, antigen-binding portions of anti-PSA, anti-AFP, anti-MUC16, anti-WFDC2, anti-MUC1, anti-ERBB2, anti-CEACAM5, anti-FUT3, or anti-TG antibodies. Further preferred antibodies in the context of the invention are shown in Table 1 below.

[0051] As used herein, the term "specifically binds" refers to an antibody or a fragment or derivative thereof that specifically binds to a target glycoprotein or target polypeptide and does not specifically bind to other proteins or polypeptides. The antibodies or fragments or derivatives thereof according to the invention bind to their respective targets via the variable domains of the antibody.

[0052] Preferred anti-glycoprotein antibodies or antigen-binding portions thereof include: i) prostate specific antigen (PSA), preferably SEQ ID NO: 1, 2, 3, 4, 5, or 6; more preferably SEQ ID NO: 6; ii) alpha-fetoprotein (AFP), preferably SEQ ID NO: 11 or 12; more preferably SEQ ID NO: 12; iii) mucin-16 (MUC16), preferably SEQ ID NO: 13; vi) WAP4-disulfide core domain protein 2 (WFDC2), preferably SEQ ID NO: 14, 15, 16, 17, 18, or 19; more preferably SEQ ID NO: 19; v) mucin-1 (MUC1), preferably SEQ ID NO: 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, or 37; more preferably SEQ ID NO: 28, No. 37; vii) receptor tyrosine protein kinase erbB-2 (ERBB2), preferably SEQ ID NO: 38, 39, 40, 41, 42, 43, or 44; more preferably SEQ ID NO: 44; viii) carcinoembryonic antigen-related cell adhesion molecule 5 (CEACAM5), preferably SEQ ID NO: 45, 46, or 47; more preferably SEQ ID NO: 47; ix) galactoside 3(4)-L-fucosyltransferase (FUT3), preferably SEQ ID NO: 48; x) thyroglobulin (TG), preferably SEQ ID NO: 49, 50, or 51; more preferably SEQ ID NO: 51. Further preferred antibodies in the context of the present invention are shown in Table 1 below.

[0053] The term "epitope" also refers to a site on an antigen (in the context of the present invention, the antigen is a glycoprotein) to which an antibody molecule binds. Preferably, the epitope is a site on an antibody or an antigen-binding portion thereof, preferably a molecule to which the antibody is raised and / or to which the antibody binds (in the context of the present invention, the antigen is a glycoprotein). For example, an epitope can be recognized by an antibody or an antigen-binding portion thereof. An epitope may be a linear epitope or a conformational epitope. An epitope may be a continuous epitope or a discontinuous epitope. A "linear epitope" is an epitope whose primary amino acid sequence comprises the recognized epitope. A linear epitope typically comprises at least 3, more usually at least 5, e.g., about 8 to about 10 amino acids in a unique sequence.

[0054] Specific binding is believed to be influenced by specific motifs in the amino acid sequences of the binding domain and the antigen that bind to each other as a result of their primary, secondary or tertiary structure and as a result of secondary modifications of said structure. The specific interaction of the antigen interaction site with its specific antigen can also result in the simple binding of the site to the antigen. Furthermore, the specific interaction of the antigen interaction site with its specific antigen can alternatively result in the initiation of a signal, for example by inducing a change in the structure of the antigen, oligomerization of the antigen, etc. A preferred example of a binding domain according to the present invention is an antibody.

[0055] Typically, the binding affinity is 10 -6 Binding is considered specific when the binding affinity is greater than M. Preferably, the binding affinity is about 10 -11 ~about 10 -8 M(K D ), preferably about 10 -11 ~about 10 -9 Binding is considered to be specific when M. If necessary, non-specific binding can be reduced by altering the binding conditions without substantially affecting specific binding.

[0056] When the sugar chain is bound to a lectin, the binding affinity is preferably 10 -3 ~10 -6 (K D ) range. The corresponding K for binding glycans to lectins D Methods for measuring are known in the art and readily available to one of skill in the art.

[0057] Whether an antibody or antigen-binding portion thereof reacts specifically as described above can be readily tested, inter alia, by comparing the reaction of the antibody or antigen-binding portion thereof with its respective target glycoprotein with the reaction of the antibody or antigen-binding portion thereof with other non-target proteins.

[0058] The term "polypeptide" is used herein in the same way as the term "protein". Proteins (including fragments thereof, preferably biologically active fragments, and peptides, usually having less than 30 amino acids) comprise one or more amino acids (resulting in an amino acid chain) bound together via covalent peptide bonds. The term "polypeptide" as used herein refers to a group of molecules, e.g., consisting of more than 30 amino acids. Polypeptides can further form multimers, such as dimers, trimers, and higher oligomers, i.e., consisting of two or more polypeptide molecules. The polypeptide molecules forming such dimers, trimers, etc., can be identical or non-identical. The corresponding higher order structures of such multimers are consequently referred to as homo- or heterodimers, homo- or heterotrimers, etc. An example of a heteromultimer is an antibody molecule, which in its naturally occurring form consists of two identical polypeptide light chains and two identical polypeptide heavy chains. The terms "polypeptide" and "protein" also refer to naturally modified polypeptides / proteins, where the modifications are affected by post-translational modifications, e.g., glycosylation, acetylation, phosphorylation, etc. Such modifications are known in the art.

[0059] The term "amino acid" or "amino acid residue" typically refers to an amino acid having its art-recognized definition, such as an amino acid selected from the group consisting of alanine (Ala or A); arginine (Arg or R); asparagine (Asn or N); aspartic acid (Asp or D); cysteine ​​(Cys or C); glutamine (GIn or Q); glutamic acid (GIu or E); glycine (GIy or G); histidine (His or H); isoleucine (He or I); leucine (Leu or L); lysine (Lys or K); methionine (Met or M); phenylalanine (Phe or F); proline (Pro or P); serine (Ser or S); threonine (Thr or T); tryptophan (Trp or W); tyrosine (Tyr or Y); and valine (VaI or V), although modified, synthetic, or rare amino acids can be used if desired. In general, amino acids can be grouped as having nonpolar side chains (e.g., Ala, Cys, He, Leu, Met, Phe, Pro, VaI); negatively charged side chains (e.g., Asp, GIu); positively charged side chains (e.g., Arg, His, Lys); or polar uncharged side chains (e.g., Asn, Cys, GIn, GIy, His, Met, Phe, Ser, Thr, Trp, and Tyr).

[0060] "Polyclonal antibody" or "polyclonal antiserum" refers to an immune serum containing a mixture of antibodies specific for one (monovalent or specific antiserum) or more (polyvalent antiserum) antigens, which can be prepared from the blood of an animal immunized with an antigen(s).

[0061] Furthermore, the term "antibody" as used in the present invention also relates to derivatives or variants of the antibodies described herein that exhibit the same specificity as the antibodies described herein. Examples of "antibody variants" include humanized variants of non-human antibodies, "affinity matured" antibodies (see, e.g., Hawkins et al. J. Mol. Biol. 254, 889-896 (1992) and Lowman et al., Biochemistry 30, 10832- 10837 (1991)), and antibody mutants with altered effector functions (see, e.g., U.S. Patent No. 5,648,260).

[0062] As used herein, the terms "antigen-binding domain", "antigen-binding portion", "antigen-binding fragment" and "antibody-binding region" refer to a portion of an antibody molecule that contains amino acids responsible for the specific binding between the antibody and the antigen. The portion of the antigen that is specifically recognized and bound by the antibody is referred to as an "epitope" as described above in this specification. As described above, an antigen-binding domain typically includes an antibody light chain variable region (VL) and an antibody heavy chain variable region (VH), but may not include both. An Fd fragment, for example, has two VH regions and often retains some antigen-binding function of a normal antigen-binding domain. Examples of antigen-binding fragments of antibodies include (1) a Fab fragment, which is a monovalent fragment having the VL, VH, CL, and CH1 domains; (2) a F(ab')2 fragment, which is a bivalent fragment having two Fab fragments linked by a disulfide bridge at the hinge region; (3) an Fd fragment having two VH and CH1 domains; (4) an Fv fragment having two VH and VH domains in a single antigen arm; (5) a dAb fragment having a VH domain (Ward et al., (1989) Nature 341:544-546); (6) an isolated complementarity-determining region (CDR); and (7) a single-chain Fv (scFv). Although the two domains of the Fv fragment, VL and VH, are encoded by separate genes, they can be joined using recombinant techniques by a synthetic linker that allows the VL and VH regions to pair into a single protein chain forming a monovalent molecule (known as a single-chain Fv (scFv); see, e.g., Bird et al. (1988) Science 242:423-426; and Huston et al. (1988) Proc. Natl. Acad. Sci USA 85:5879-5883). These antibody fragments are obtained using conventional techniques known to those of skill in the art, and the fragments are evaluated for function in the same manner as intact antibodies.

[0063] The term "monoclonal antibody" as used herein refers to an antibody obtained from a population of substantially homogeneous antibodies, i.e., the individual antibodies constituting the population are identical except for possible minor amounts of naturally occurring mutations and / or post-translational modifications (e.g., isomerization, amidation). Monoclonal antibodies are highly specific, being directed against a single antigenic site. Moreover, in contrast to conventional (polyclonal) antibody preparations that typically contain different antibodies directed against different determinants (epitopes), each monoclonal antibody is directed against a single determinant on the antigen. In addition to their specificity, monoclonal antibodies are advantageous in that they are synthesized by a hybridoma culture uncontaminated by other immunoglobulins. The modifier "monoclonal" indicates the character of the antibody as being obtained from a population of substantially homogeneous antibodies and is not to be construed as requiring production of the antibody by any method. For example, the monoclonal antibodies to be used in the present invention may be made by the hybridoma method first described by Kohler et al. (Nature, 256: 495 (1975)), or may be made by recombinant DNA methods (see, e.g., U.S. Pat. No. 4,816,567). The "monoclonal antibodies" may also be isolated from phage antibody libraries using the techniques described, for example, in Clackson et al. (Nature, 352: 624-628 (1991)) and Marks et al. (J. Mol. Biol., 222: 581-597 (1991)).

[0064] Furthermore, the term "monoclonal antibody" as used in the present invention also relates to specific monoclonal antibodies such as those produced by DB Biotech (http: / / www.dbbiotech.com / about-us.html), which method involves an in vitro cloning technique that allows the production of pure immunoglobulin fractions corresponding to a single clone of B lymphocytes, with the resulting immunoglobulin recognizing only a single linear epitope on the antigen molecule.

[0065] Monoclonal antibodies herein include, inter alia, "chimeric" antibodies (immunoglobulins) in which portions of the heavy and / or light chains are identical or homologous to corresponding sequences of antibodies from a particular species or belonging to a particular antibody class or subclass, while the remainder of the chains are identical or homologous to corresponding sequences of antibodies from another species or belonging to another antibody class or subclass, and fragments of such antibodies, so long as the desired biological activity is exhibited (U.S. Pat. No. 4,816,567; Morrison et al., Proc. Natl. Acad. Sci. USA, 81: 6851-6855 (1984)). Chimeric antibodies of interest herein include "primitized" antibodies that contain variable domain antigen-binding sequences derived from a non-human primate (e.g., Old World Monkey, Ape, etc.) and human constant region sequences.

[0066] "Humanized" forms of non-human (e.g., murine) antibodies are chimeric immunoglobulins, immunoglobulin chains or fragments thereof (such as Fv, Fab, Fab', F(ab')2, or other antigen-binding sequences of antibodies) of mostly human sequence that contain minimal sequence derived from non-human immunoglobulin. For the most part, humanized antibodies are human immunoglobulins (recipient antibody) in which residues from a hypervariable region (also called CDR) of the recipient are replaced by residues from a hypervariable region of a non-human species (donor antibody) such as mouse, rat, or rabbit having the desired specificity, affinity, and capacity. In some instances, Fv framework region (FR) residues of the human immunoglobulin are replaced by corresponding non-human residues. Furthermore, as used herein, "humanized antibodies" can also include residues that are not found in the recipient antibody or in the donor antibody. These modifications are made to further refine and optimize antibody function. Humanized antibodies may also suitably comprise at least a portion of an immunoglobulin constant region (Fc), typically that of a human immunoglobulin. For further details, see Jones et al. (Nature, 321: 522-525 (1986)); Reichmann et al. (Nature, 332: 323-329 (1988)); and Presta (Curr. Op. Struct. Biol., 2: 593-596 (1992)).

[0067] The term "human antibody" includes antibodies having variable and constant regions substantially corresponding to human germline immunoglobulin sequences known in the art, including, for example, those described by Kabat et al. (See, Kabat, et al. (1991) loc. cit.). The human antibodies of the invention may include, for example, in the CDRs, particularly CDR3, amino acid residues not encoded by human germline immunoglobulin sequences (e.g., mutations introduced by random or site-specific mutagenesis in vitro or by somatic mutation in vivo). Human antibodies can have at least one, two, three, four, five, or more positions substituted with an amino acid residue not encoded by human germline immunoglobulin sequences.

[0068] As used herein, "in vitro generated antibody" refers to an antibody in which all or a portion of the variable region (e.g., at least one CDR) is generated by non-immune cell selection (e.g., in vitro phage display, protein chip, or any other method that allows testing the ability of candidate sequences to bind to an antigen). Thus, the term preferably excludes sequences generated by genomic rearrangement in immune cells.

[0069] A "bispecific" or "bifunctional antibody" is an artificial hybrid antibody having two different heavy / light chain pairs and two different binding sites. Bispecific antibodies can be produced in a variety of ways, including fusion of hybridomas or linking of Fab' fragments. See, e.g., Songsivilai & Lachmann, Clin. Exp. Immunol. 79:315-321 (1990); Kostelny et al., J. Immunol. 148, 1547-1553 (1992). In one embodiment, a bispecific antibody comprises a first binding domain polypeptide, such as a Fab' fragment, linked via an immunoglobulin constant region to a second binding domain polypeptide.

[0070] The antibodies described herein can be used to form bispecific molecules. The anti-PSA antibodies or antigen-binding portions thereof can be derivatized or conjugated to another functional molecule, such as another peptide or protein (e.g., another antibody or a ligand for a receptor), to create a bispecific molecule that binds to at least two different binding sites or target molecules. The antibodies described herein may in fact be derivatized or linked to more than one other functional molecule to create a multispecific molecule that binds to more than two different binding sites and / or target molecules. Such multispecific molecules are also intended to be encompassed by the term "bispecific molecule" as used herein. To create the bispecific molecules described herein, the antibodies described herein can be functionally conjugated (e.g., by chemical bond, genetic fusion, non-covalent association, or other means) to one or more other binding molecules, such as another antibody, antibody fragment, peptide, or binding mimetic molecule, such that a bispecific molecule results.

[0071] Immunoconjugates and antibody derivatives. The antibodies described herein can be used for diagnostic purposes, including sample testing and in vivo imaging, and for this purpose, the antibodies (or binding fragments thereof) can be conjugated to a suitable detectable agent to form an immunoconjugate. For diagnostic purposes, suitable agents are detectable labels, including radioisotopes for whole body imaging, radioisotopes, enzymes, fluorescent labels, and other suitable antibody tags for sample testing. The detectable label can be any of a variety of types currently used in the field of in vitro diagnostics, including particulate labels, including metal sols such as colloidal gold, isotopic labels, chromogenic labels, including fluorescent markers, biotin, luminescent markers, phosphorescent markers, and the like, enzyme labels that convert a given substrate into a detectable marker, and polynucleotide tags that are revealed following amplification, such as by polymerase chain reaction, and the like. Biotin-labeled antibodies may also be detectable by binding of avidin or streptavidin. Suitable enzyme labels include horseradish peroxidase, alkaline phosphatase, and the like. For example, the label can be the enzyme alkaline phosphatase, which is detected by measuring the presence or formation of chemiluminescence following conversion of 1,2 dioxetane substrates such as adamantyl methoxyphosphoryloxyphenyl dioxetane (AMPPD), disodium 3-(4-(methoxyspiro{1,2-dioxetane-3,2'-(5'-chloro)tricyclo{3.3.1.1 3,7}decan}-4-yl)phenyl phosphate (CSPD), and CDP and CDP-star, or other luminescent substrates known to those skilled in the art, such as chelates of suitable lanthanides, e.g., terbium(III) and europium(III). The means of detection will be determined by the label chosen. The appearance of the label or its reaction products can be obtained by eye, if the label is particulate and has accumulated at an appropriate level, or using instruments such as spectrophotometers, luminometers, fluorometers, and the like, according to standard measurement techniques.

[0072] Numerous methods known to those skilled in the art are available for obtaining antibodies or antigen-binding fragments thereof. For example, antibodies can be produced using recombinant DNA methods (U.S. Patent No. 4,816,567). Monoclonal antibodies may also be produced by generating hybridomas (see, e.g., Kohler and Milstein (1975) Nature, 256: 495-499) according to known methods. The hybridomas so formed are then screened using standard methods, such as enzyme-linked immunosorbent assay (ELISA) and surface plasmon resonance (BIACORE®) analysis, to identify one or more hybridomas that produce an antibody that specifically binds to the particular antigen. Any form of a particular antigen can be used as the immunogen, for example, recombinant antigens, naturally occurring forms, variants or fragments thereof, and antigenic peptides thereof.

[0073] One exemplary method of generating antibodies involves screening a protein expression library, such as a phage or ribosome display library. Phage display is described, for example, in U.S. Pat. No. 5,223,409 to Ladner et al., Smith ((1985) Science 228:1315-1317), Clackson et al. ((1991) Nature, 352: 624-628), Marks et al. ((1991) J. MoI. Biol., 222: 581-597), WO 92 / 18619, WO 91 / 17271, WO 92 / 20791, WO 92 / 15679, WO 93 / 01288, WO 92 / 01047, WO 92 / 09690, and WO 90 / 02809.

[0074] In addition to using display libraries, a specific antigen can be used to immunize a non-human animal, such as a rodent, such as a mouse, hamster, or rat. In one embodiment, the non-human animal contains at least a portion of a human immunoglobulin gene. For example, it is possible to engineer mouse strains deficient in mouse antibody production with large fragments of the human Ig locus. Using hybridoma technology, antigen-specific monoclonal antibodies derived from genes with the desired specificity can be produced and selected. See, for example, XENOMOUSE®, Green et al. (1994) Nature Genetics 7:13-21, U.S. Patent Application Publication No. 2003-0070185, WO 96 / 34096, and WO 96 / 33735.

[0075] In other embodiments, monoclonal antibodies may be obtained from non-human animals and then modified, e.g., humanized, deimmunized, chimerized, and produced using recombinant DNA techniques known in the art. Various techniques for producing chimeric antibodies have been described. See, for example, Morrison et al. (Proc. Natl. Acad. Sci. USA 81:6851, 1985), Takeda et al. (Nature 314:452, 1985), U.S. Patent No. 4,816,567 to Cabilly et al., U.S. Patent No. 4,816,397 to Boss et al., EP 171496, EP 173494, and GB 2177096 to Tanaguchi et al. Humanized antibodies may also be produced using, for example, transgenic mice that express human heavy and light chain genes but are incapable of expressing endogenous mouse immunoglobulin heavy and light chain genes. Winter describes an exemplary CDR grafting method that can be used to prepare the humanized antibodies described herein (U.S. Patent No. 5,225,539). All of the CDRs of a particular human antibody may be replaced with at least a portion of a non-human CDR, or only a portion of the CDRs may be replaced with a non-human CDR. It is only necessary to replace the number of CDRs necessary to allow the humanized antibody to bind to a given antigen.

[0076] Humanized antibodies or fragments thereof can be made by replacing sequences of Fv variable domains not directly involved in antigen binding with equivalent sequences from human Fv variable domains. Exemplary methods for making humanized antibodies or fragments thereof are provided by Morrison ((1985) Science 229:1202-1207), Oi et al. ((1986) BioTechniques 4:214), and U.S. Pat. Nos. 5,585,089, 5,693,761, 5,693,762, 5,859,205, and 6,407,213. These methods include isolating, manipulating, and expressing nucleic acid sequences that encode all or part of immunoglobulin Fv variable domains from at least one of the heavy or light chains. Such nucleic acids may be obtained from hybridomas producing antibodies against a predetermined target, as described above, or from other sources. The recombinant DNA encoding the humanized antibody molecule can also be cloned into an appropriate expression vector.

[0077] In certain embodiments, humanized antibodies are optimized by introducing conservative substitutions, consensus sequence substitutions, germline substitutions, and / or back mutations. Such modified immunoglobulin molecules can be made by any of several techniques known in the art (e.g., Teng et al., Proc. Natl. Acad. Sci. USA, 80: 7308-7312, 1983; Kozbor et al., Immunology Today, 4: 7279, 1983; Olsson et al., Meth. Enzymol., 92: 3-16, 1982), and can be made following the teachings of WO 92 / 06193 or EP 239400.

[0078] Antibodies or fragments thereof may also be modified by specific deletion or "deimmunization" of human T-cell epitopes by the methods disclosed in WO 98 / 52976 and WO 00 / 34317. Briefly, the heavy and light chain variable domains of the antibody can be analyzed for peptides that bind to MHC class II. These peptides represent potential T-cell epitopes (as defined in WO 98 / 52976 and WO 00 / 34317). For detection of potential T-cell epitopes, a computer modeling approach called "peptide threading" can be applied; furthermore, as described in WO 98 / 52976 and WO 00 / 34317, databases of human MHC class II binding peptides can be searched for motifs present in the VH and VL sequences. These motifs bind to any of the 18 major MHC class IIDR allotypes and therefore constitute potential T-cell epitopes. Detected potential T cell epitopes can be eliminated by substitution of a small number of amino acid residues in the variable domain, preferably by single amino acid substitution. Typically, conservative substitutions are made. In many cases, but not exclusively, common amino acids at positions in human germline antibody sequences can be used. Human germline sequences are published, for example, in Tomlinson et al. ((1992) J. MoI. Biol. 227:776-798), Cook, GP et al. ((1995) Immunol. Today Vol. 16 (5): 237-242), Chothia et al. ((1992) J. MoI. Biol. 227:799-817), and Tomlinson et al. ((1995) EMBO J. 14:4628-4638). The V BASE directory provides a comprehensive directory of human immunoglobulin variable region sequences (Tomlinson, L. A. et al., MRC Centre for Protein Engineering, Cambridge, UK). These sequences can be used as a source of human sequences, e.g., for the framework regions and CDRs.Consensus human framework regions can also be used, for example, as described in US Pat. No. 6,300,064.

[0079] Techniques for generating antibodies, including polyclonal, monoclonal, humanized, bispecific, and heteroconjugate antibodies, are known in the art, some of which are exemplified below.

[0080] Heteroconjugate antibodies Heteroconjugate antibodies are also within the scope of the present invention.

[0081] Heteroconjugate antibodies are composed of two covalently linked (e.g., conjugated) antibodies. For example, one of the antibodies in the heteroconjugate can be conjugated to avidin, the other to biotin. It is contemplated that the antibodies can be prepared in vitro using known methods in synthetic protein chemistry, including those involving cross-linking agents. For example, immunotoxins can be constructed using a disulfide exchange reaction or by forming a thioether bond. Examples of suitable reagents for this purpose include iminothiolate and methyl-4-mercaptobutyrimidate, as well as those disclosed, for example, in U.S. Pat. No. 4,676,980. Heteroconjugate antibodies can be made using any convenient cross-linking method. Suitable cross-linking agents are known in the art and are disclosed in U.S. Pat. No. 4,676,980, along with a number of cross-linking techniques.

[0082] For further antibody production techniques, see Antibodies: A Laboratory Manual, eds. Harlow et al., Cold Spring Harbor Laboratory, 1988. The present invention is not necessarily limited to any particular source, method of production, or other particular characteristics of the antibodies.

[0083] The antibody of the present invention is preferably an "isolated" antibody. When used to describe the antibodies disclosed herein, "isolated" means an antibody that has been identified, separated, and / or recovered from components of its production environment. Preferably, an isolated antibody is free of association with all other components from its production environment. Contaminating components of its production environment, such as those resulting from recombinantly transfected cells, are typically substances that may interfere with diagnostic or therapeutic uses of the polypeptide and may include enzymes, hormones, and other proteinaceous or non-proteinaceous solutes. In a preferred embodiment, the antibody can be (1) purified sufficiently to obtain at least 15 residues of N-terminal or internal amino acid sequence using a spinning cup sequenator, or (2) purified to homogeneity by SDS-PAGE under non-reducing or reducing conditions using Coomassie blue, or preferably silver staining. Ordinarily, however, an isolated antibody can be prepared by at least one purification step.

[0084] As used herein, the term "position" refers to the position of an amino acid within an amino acid sequence described herein. Also, as used herein, the term "corresponding" includes that the position is not solely determined by the number of preceding nucleotides / amino acids.

[0085] A given amino acid position in the present invention may be substituted by deletion or addition of amino acids elsewhere in the polypeptide.

[0086] Thus, under "corresponding positions" in the present invention, it is understood that amino acids may differ in the indicated number and still have similar adjacent amino acids. Also, said amino acids that may be replaced, deleted or added are included in the term "corresponding positions".

[0087] To determine whether an amino acid residue in a given amino acid sequence corresponds to a particular position in an amino acid sequence, one skilled in the art can use means and methods known in the art, such as alignment, either manually or by using a computer program such as BLAST 2.0, which stands for Basic Local Alignment Search Tool, or ClustalW, or any other suitable program suitable for generating sequence alignments.

[0088] As used herein, the term "% identity" refers to the percentage of identical amino acid residues at corresponding positions in two amino acid sequences when comparing them in optimal sequence alignment, as exemplified by the ClustalW or X technology available at www.clustal.org, or equivalent technology. That is, both sequences (reference and subject sequences) are aligned, identical amino acid residues between both sequences are identified, and the total number of identical amino acids is divided by the total number of amino acids (amino acid length). The result of this division is a percentage value, i.e., percent identity value / degree.

[0089] In another aspect, the invention provides an antibody, or antigen-binding portion thereof, of the invention for use as a diagnostic composition, i.e., the antibody, or antigen-binding portion thereof, can be used in a diagnostic assay for the antigen, e.g., to detect its expression in specific cells, tissues, or serum.

[0090] A variety of diagnostic assay techniques known in the art can be used, including competitive binding assays, direct or indirect sandwich assays, and immunoprecipitation assays, performed in either heterogeneous or homogeneous phases (Zola, Monoclonal Antibodies: A Manual of Techniques, CRC Press, Inc. (1987) pp. 147-158). The antibodies or antigen-binding portions thereof used in diagnostic assays can be labeled with a detectable moiety. For example, the antibodies or antigen-binding portions thereof may be modified with detectable markers, including ligand groups (e.g., biotin), fluorophores and chromogens, radioisotopes, electron-dense reagents, or enzymes. Enzymes are detected by their activity. For example, horseradish peroxidase is detected by its ability to convert tetramethylbenzidine (TMB) to a blue pigment that is quantifiable by a spectrophotometer. Other suitable binding partners include biotin and avidin, IgG and protein A, and other receptor-ligand pairs known in the art.

[0091] The detectable moiety should be capable of producing, either directly or indirectly, a detectable signal. For example, the detectable moiety can be, for example, 3 H, 14 C. 32 P, 35 S, or 125 The detectable moiety may be a radioisotope such as I, a fluorescent or chemiluminescent compound such as fluorescein isothiocyanate, rhodamine, or luciferin, or an enzyme such as alkaline phosphatase, β-galactosidase, or horseradish peroxidase. Any method known in the art for conjugating an antibody to a detectable moiety can be used.

[0092] When administered to a subject, the antibody or antigen-binding portion thereof of the invention is preferably in the form of a composition. The composition is preferably suitable for pharmaceutical use and administration to a subject.

[0093] Thus, the antibodies, or antigen-binding portions thereof, of the invention are contemplated for use in diagnostics.Thus, the invention contemplates pharmaceutical compositions (or medicaments) comprising the antibodies, or antigen-binding portions thereof, described herein.

[0094] In yet other embodiments, the invention provides methods of treating a subject with cancer comprising administering a therapeutically effective amount of an antibody, or antigen-binding portion thereof, of the invention.

[0095] As used herein, "cancer" refers to a broad group of diseases characterized by the uncontrolled growth of abnormal cells in the body. Unregulated cell division can lead to the formation of malignant tumors or cells that invade adjacent tissues and can metastasize to distant parts of the body via the lymphatic system or bloodstream.

[0096] Cancers whose growth may be inhibited using the antibodies of the present invention include cancers that typically respond to immunotherapy. Non-limiting examples of cancers that may be treated include squamous cell carcinoma, small cell lung cancer, non-small cell lung cancer, squamous non-small cell lung cancer (NSCLC), non-NSCLC, glioma, gastrointestinal cancer, renal cancer (e.g., clear cell carcinoma), ovarian cancer, liver cancer, colorectal cancer, endometrial cancer, renal cancer (e.g., renal cell carcinoma (RCC)), prostate cancer (e.g., hormone refractory prostate cancer), thyroid cancer, neuroblastoma, pancreatic cancer, glioblastoma (glioblastoma multiforme), cervical cancer, stomach cancer, bladder cancer, hepatoma, breast cancer, colon carcinoma, and head and neck cancer (or carcinoma), gastric cancer, and other cancers.cancer), germ cell tumors, childhood sarcomas, sinonasal natural killer, melanoma (e.g., metastatic melanoma such as cutaneous melanoma or intraocular melanoma), bone cancer, skin cancer, uterine cancer, anal cancer, testicular cancer, fallopian tube carcinoma, endometrial carcinoma, cervical carcinoma, vaginal carcinoma, vulvar carcinoma, esophageal cancer, small intestine cancer, endocrine system cancer, parathyroid cancer, adrenal cancer, soft tissue sarcoma, urethral cancer, penile cancer, childhood solid tumors, ureteral cancer, renal pelvis carcinoma, central nervous system (CNS) S) neoplasms, primary CNS lymphomas, tumor angiogenesis, spinal axis tumors, brain stem gliomas, pituitary adenomas, Kaposi's sarcoma, epidermoid carcinoma, squamous cell carcinoma, T-cell lymphomas, environmentally induced cancers including those induced by asbestos, virus-associated cancers (e.g., human papillomavirus (HPV)-associated tumors), and the two major blood cell lineages, i.e., myeloid cell lines (which produce granulocytes, erythrocytes, platelets, macrophages, and mast cells) or lymphocytes. Hematological malignancies derived from any of the lymphoid cell lines (producing B, T, NK and plasma cells), such as all types of leukemia, lymphoma and myeloma, including, for example, acute myeloid leukemia (ALL), acute myeloid leukemia (AML), chronic lymphocytic leukemia (CLL) and chronic myeloid leukemia (CML), anaplastic AML (MO), myeloblastic leukemia (M1), myeloblastic leukemia (M2, with cell maturation), promyelocytic leukemia (M3), myeloblastic leukemia (M4), myeloblastic leukemia (M5), myeloblastic leukemia (M6), myeloblastic leukemia (M7), myeloblastic leukemia (M8), myeloblastic leukemia (M9), myeloblastic leukemia (M10), myeloblastic leukemia (M11), myeloblastic leukemia (M12), myeloblastic leukemia (M13), myeloblastic leukemia (M14), myeloblastic leukemia (M15), myeloblastic leukemia (M16), myeloblastic leukemia (M17), myeloblastic leukemia (M18), myeloblastic leukemia (M19 ... acute, chronic, lymphoid and / or myeloid leukemias, such as myelomonocytic leukemia (M4 or M4 variant [M4V]), myelomonocytic leukemia (M4 or M4 variant [M4E], with eosinophilia), monocytic leukemia (M5), erythroleukemia (M6), megakaryoblastic leukemia (M7), isolated granulocytic sarcoma, and chloroma; Hodgkin's lymphoma (HL), non-Hodgkin's lymphoma (NHL), B-cell lymphoma, T-cell lymphoma, lymphoplasmacytoid lymphoma, monocytic B-cell lymphoma, mucosal intralymphoid tissue (MALT) lymphoma, anaplastic (e.g., Ki1+) Lymphomas such as large cell lymphoma, adult T-cell lymphoma / leukemia, mantle cell lymphoma, angioimmunoblastic T-cell lymphoma, hemocentric lymphoma, intestinal T-cell lymphoma, primary mediastinal B-cell lymphoma, precursor T-lymphoblastic lymphoma, T-lymphoblastic lymphoma; and lymphoma / leukemia (T-Lbly / T-ALL), peripheral T-cell lymphoma, lymphoblastic lymphoma, post-transplant lymphoproliferative disorder, true histiocytic lymphoma, primary central nervous system Lymphomas of the lymphoid lineage, primary effusion lymphoma, lymphoblastic lymphoma (LBL), lymphoid hematopoietic neoplasms, acute lymphoblastic leukemia, diffuse large B-cell lymphoma, Burkitt lymphoma, follicular lymphoma, diffuse histiocytic lymphoma (DHL), immunoblastic large cell lymphoma, precursor B-lymphoblastic lymphoma, cutaneous T-cell lymphoma (CTLC) (also called mycosis fungoides or Sézary syndrome), and Waldenstrom macroglobulinemia. Lymphoplasmacytic lymphoma with lymphadenopathy (LPL); myelomas such as IgG myeloma, light chain myeloma, nonsecretory myeloma, smoldering myeloma (also called low-grade myeloma), solitary myeloma, plasmacytoma, and multiple myeloma; chronic lymphocytic leukemia (CLL), hairy cell lymphoma; hematopoietic tumors of myeloid lineage, tumors of mesenchymal origin including fibrosarcoma and rhabdomyosarcoma; tumors of the central and peripheral nervous system including seminoma, teratocarcinoma, astrocytoma, Schwann's disease, and leukemia. tumors of mesenchymal origin including fibrosarcoma, rhabdomyosarcoma, and osteosarcoma; and other tumors including malignant melanoma, xeroderma pigmentosum, keratoacanthoma, seminoma, thyroid follicular carcinoma and teratocarcinoma, hematopoietic tumors of lymphoid lineage, including but not limited to T cell disorders such as T-prolymphocytic leukemia (T-PLL) including small cell and cerebrospinal cell types, T cell tumors and B cell tumors; large granular lymphocyte leukemia (LGL), preferably of the T cell type; a / d T-NHL hepatosplenic lymphoma; peripheral / post-thymic T cell lymphoma (pleomorphic and immunoblastic subtypes); hemangiocentric (nasal) T cell lymphoma; head and neck cancer, renal cancer, rectal cancer, thyroid cancer; acute myeloid lymphoma, and any combination of these cancers. The methods described herein can also be used for the treatment of metastatic cancers, refractory cancers (e.g., cancers refractory to previous immunotherapy with blocking CTLA-4 antibodies or PD-1 antibodies or PD-L1 antibodies), and recurrent cancers.

[0097] Additionally, preferred antibodies of the present invention are shown in Table 1 below.

[0098] In a preferred embodiment, the cancer is selected from the group consisting of leukemia, lymphoma, myeloma, breast cancer, colorectal cancer, glioblastoma, ovarian cancer, hematological cancer, epithelial cancer, pancreatic cancer, bladder cancer, uterine / cervical cancer, ovarian cancer, prostate cancer, testicular cancer, esophageal cancer, gastrointestinal cancer, colon cancer, renal cancer, head and neck cancer, lung cancer, gastric cancer, germ cell cancer, bone cancer, liver cancer, thyroid cancer, skin cancer, central nervous system neoplasms, sarcoma, and virus-associated cancer.

[0099] As used herein, "autoimmune disease" refers to a broad group of diseases characterized by disease associated with the production of antibodies against own tissue.Non-limiting examples of autoimmune disease include, but are not limited to, Hashimoto's disease, primary biliary cirrhosis, systemic lupus erythematosus, rheumatic fever, rheumatoid arthritis, autoimmune hemolytic anemia, idiopathic thrombocytopenic purpura, and post-viral encephalomyelitis, Addison's disease, autoimmune enteropathy, primary biliary cirrhosis, Goodpasture's syndrome, Hashimoto's thyroiditis, myasthenia gravis, myxedema, pemphigoid, rheumatoid arthritis, Sjogren's syndrome, sympathetic ophthalmia, both forms of lupus erythematosus, thyrotoxicosis, ulcerative colitis, multiple sclerosis, celiac disease, type 1 diabetes, Graves' disease, inflammatory bowel disease, and psoriasis.

[0100] As used herein, "inflammatory disease" refers to a broad group of diseases characterized by impaired and / or abnormal functioning of the body's inflammatory mechanisms. Non-limiting examples of inflammatory diseases include, but are not limited to, necrotizing enterocolitis, gastroenteritis, pelvic inflammatory disease (PID), empyema, pleuritis, pyelitis, pharyngitis, angina, arthritis, acne, urinary tract infection, acne vulgaris, asthma, celiac disease, chronic prostatitis, colitis, diverticulitis, glomerulonephritis, hidradenitis suppurativa, hypersensitivity, inflammatory bowel disease, interstitial cystitis, mast cell activation syndrome, mastocytosis, otitis, pelvic inflammatory disease, reperfusion injury, rheumatic fever, rheumatoid arthritis, rhinitis, sarcoidosis, transplant rejection, and vasculitis.

[0101] The term "subject" is intended to include living organisms. Examples of subjects include mammals, such as humans, dogs, cows, horses, pigs, sheep, goats, cats, mice, rabbits, rats, and transgenic non-human animals. In a preferred embodiment of the invention, the subject is a human.

[0102] As used herein, the terms "injury" and "disease" are used interchangeably to refer to a pathological condition in a subject. In particular, the term "cancer" is used interchangeably with "tumor."

[0103] Furthermore, the antibodies of the present invention can be used for diagnostic purposes to detect, diagnose, or monitor diseases or disorders, particularly cancer and cancer-related diseases. The antibodies or fragments or derivatives thereof of the present invention can be used to assay glycoprotein levels in biological samples using conventional immunohistological methods as described herein or known to those skilled in the art (see, for example, Jalkanen et al., 1985, J. Cell. Biol. 101: 976-985; Jalkanen et al., 1987, J. Cell. Biol. 105: 3087-3096). Other antibody-based methods useful for detecting protein gene expression include immunoassays such as enzyme-linked immunosorbent assays (ELISAs) and radioimmunoassays (RIAs).

[0104] Thus, the present invention further relates to a diagnostic composition comprising the antibody of the present invention.

[0105] As used herein, the term "diagnosis" relates to any use of the antibodies of the invention to diagnose the presence of a target polypeptide or glycoprotein in cancer or a related disease.

[0106] In further embodiments of the invention, articles of manufacture and kits are provided that include the antibodies or antigen-binding portions thereof, which can be used, for example, for therapeutic or non-therapeutic applications as described above. The articles of manufacture include a labeled container. Suitable containers include, for example, bottles, vials, and test tubes. The container may be formed from a variety of materials, such as glass or plastic. The container holds a composition that includes an active agent effective for therapeutic or non-therapeutic applications as described above. The active agent of the composition is the antibody or antigen-binding portion thereof. The label on the container indicates that the composition is to be used for a particular therapeutic or non-therapeutic application, and can also indicate instructions for either in vivo or in vitro use, as described above.

[0107] Kits of the present invention will typically include the containers described above, as well as one or more other containers containing materials desirable from a commercial and user standpoint, including buffers, diluents, filters, needles, syringes, and package inserts with instructions for use.

[0108] As used herein, the term "immobilized" refers to an antibody or antigen-binding portion thereof or a lectin that is bound, usually covalently, to an insoluble organic or inorganic matrix (e.g., a magnetic carrier). Furthermore, it is preferred that the antibody is not immobilized, preferably not immobilized on a solid surface, when applied in the method, use, or kit of the present invention.

[0109] As used herein, the term "magnetic carrier" refers to a particle or bead that comprises a magnetic material or substance (e.g., iron or ferritin). Preferably, the magnetic carrier is a magnetic particle or bead (e.g., ferritin conjugate). However, for the avoidance of doubt, the magnetic carrier, as referred to herein, is not a solid surface such as a plate, e.g., an ELISA plate, as used herein.

[0110] As used herein, the term "bead" refers to small spherical objects made, for example, from glass, plastic, metal, agarose, latex, metal nanoparticles or microparticles, metal oxide nanoparticles or microparticles, or magnetic materials.

[0111] As used herein, the term "microperoxidase" or "MP" refers to a heme containing peptide portion of cytochrome c (e.g., cytochrome c from Equus caballus, shown as SEQ ID NO: 10, NCBI Reference Sequence: NP_001157486.1) that retains peroxidase activity (e.g., EC 1.11.1.7 enzyme activity, e.g., microperoxidase-11). Preferably, the heme containing peptide moiety of cytochrome c is at least 60% or more (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) identical to a polypeptide sequence selected from the group consisting of SEQ ID NO:7 (MP-11 peptide), SEQ ID NO:8 (MP-9 peptide), and SEQ ID NO:9 (MP-8 peptide), and preferably the microperoxidase (MP) peptide is selected from the group consisting of SEQ ID NO:7 (MP-11 peptide), SEQ ID NO:8 (MP-9 peptide), and SEQ ID NO:9 (MP-8 peptide).

[0112] As used herein, some lectins can agglutinate cells. Lectins can be obtained from the seeds of legumes, but also from other plant and animal sources. Lectins can contain binding sites for specific monosaccharides and oligosaccharides (e.g., glycans of glycoproteins). Lectins can agglutinate cells by binding to specific sugar residues in membrane glycoproteins. Preferably, the lectin of the present invention is selected from the group consisting of Maackia amurensis lectin II (MAA II), concanavalin A (Con A), Aleuria aurantia lectin (AAL), Sambucus nigra (SNA-I) lectin, Wisteria floribunda lectin (WFL) as described herein.

[0113] Further preferred lectins of the present invention are shown in Table 1 below.

[0114] Particularly preferred lectins of the present invention are P0DKL3, P02866, P18891, O04366, A0A218PFP3, Q945S3, Q00022, Q6YNX3, Q71QF2, P02872, P18670, Q2UNX8, Q8L5H4, A0A089ZWN7, P05045, P19588, P83410, P17931, P56470, P24146, Q41263, Q39990, Q2F1K8, G9M5T0, B3XYC5, P02870, P1966 4, P0DKL3, P49300, A9XX86, Q40423, P16300, P05088, P05087, Q9AVB0, P02867, O24313, Q9SM56, P06750, B9SPG3, Q9BZZ2, P20916, Q9NYZ4, Q96RL6, P05046, P93535, P02876, P10968, P10969, P22972, or P56625, and the corresponding mature forms thereof.

[0115] Exemplary lectins of the present invention further include: Maackia amurensis lectin II (MAA II) is a hemagglutinin isolectin from Maackia seeds. Sialic acid binding lectins recognize oligosaccharides containing a terminal sialic acid linked via an α2-3 linkage to the penultimate galactose residue. They bind the trisaccharide sequence Neu5Acα2-3-Gal-β-1-4-GlcNAc. Preferably, MAA II has SEQ ID NO: 52 (or its mature form). Concanavalin A (Con A) is a D-mannose specific lectin originally extracted from the jack bean Canavalia ensiformis. Preferably, Con A has SEQ ID NO: 53 or SEQ ID NO: 54 (Con A, mature form). Aleuria aurantia lectin (AAL) is a fucose-specific lectin extracted from Aleuria aurantia (Orange peel mushroom). Preferably, AAL has SEQ ID NO: 55 (or its mature form). Isolation of AAL has been described, for example, by Debray et al. and Kochibe et al. Sambucus nigra (SNA-I) lectin is a Neu5Acα2-6)Gal / GalNAc specific agglutinin extracted from Sambucus nigra (European elder). Preferably, SNA-I has SEQ ID NO: 56 (or its mature form). Wisteria floribunda lectin (WFL) is an agglutinin extracted from Wisteria floribunda (Japanese wisteria). Preferably, WFL has SEQ ID NO: 57 (or its mature form).

[0116] Other preferred lectins of the present invention are also disclosed herein in the sections "Other lectins within the contemplation of the present invention (eg, their post-translationally processed and mature forms)" and "Sequence Listing".

[0117] Moreover, other suitable lectins within the contemplation of the present invention expressly include post-translationally processed and mature forms of lectins as disclosed herein.

[0118] The problems that the invention seeks to solve may be found, among others, in one or more of the following: i) to identify new tools (e.g. biomarkers and methods) for improved diagnosis of cancer (e.g. prostate cancer diagnosis, Table 1); ii) to increase the sensitivity of cancer detection (e.g. prostate cancer detection), e.g. to reduce the amount of sample (e.g. 0.04 ml or less) required for accurate diagnosis of cancer (e.g. prostate cancer diagnosis); iii) to reduce the analysis time of cancer diagnosis (e.g. prostate cancer diagnosis), e.g. by using magnetic particles for PSA enrichment and / or signal generation; iv) to increase the versatility of cancer diagnosis (e.g. prostate cancer diagnosis, Table 1), e.g. by identifying new tools (e.g. biomarkers and methods) for glycoprofiling of any protein (e.g. cancer biomarker); v) to reduce the number of false positives (e.g. false positives arising from elevated glycoprotein levels in benign conditions) in glycoprotein-based (e.g. PSA-based) diagnosis of cancer (e.g. prostate cancer). vi) distinguishing between important and non-important tumors, for example, by glycoprotein-based (e.g., PSA-based) diagnosis of cancer (e.g., prostate cancer); vii) distinguishing between low-proliferative tumors (e.g., clinically harmless) and high-proliferative tumors (e.g., clinically relevant), for example, by glycoprotein-based (e.g., PSA-based) diagnosis of cancer (e.g., prostate cancer); viii) reducing the risk of side effects of cancer treatment and / or unnecessary procedures (e.g., prostate cancer treatment, side effects such as urinary incontinence, sexual dysfunction, and bowel problems) in patients with harmless PCa; ix) reducing the cost of cancer diagnosis (e.g., prostate cancer diagnosis, for example, glycoprotein-based (e.g., PSA-based) prostate cancer diagnosis); x) increasing the convenience of cancer diagnosis (e.g., prostate cancer diagnosis, for example, glycoprotein-based (e.g., PSA-based) prostate cancer diagnosis) in subjects in need of diagnosis, for example, by reducing the number of intrusive tests required (e.g., imaging, prostate biopsy, etc.). xi) Detecting curable cancers (e.g., prostate cancer) with high and improved specificity (e.g., eliminating unnecessary follow-up testing procedures).xii) For example, glycoprotein-based (e.g. PSA-based) diagnosis of cancer to identify organ-confined and / or potentially curable cancers (e.g. prostate cancer). The problems are solved by the claims of the present invention. The magnetic carriers, anti-glycoprotein antibodies, antigen-binding portions thereof, one or more lectins, compositions, kits, methods and uses based thereon are applicable to any glycoprotein, any cancer biomarker with aberrant glycosylation.

[0119] Also within the contemplation of the present invention, preferred cancers, cancer biomarkers with aberrant glycosylation, lectins, antibodies, and corresponding glycosylation modifications are shown below in Table 1. The abbreviations of the lectins used in Table 1 are as follows: AAA-Anguilla anguilla agglutinin (UniProtKB accession number: Q7SIC1), AAL-Aleuria aurantia lectin, ABA-Agaricus bisporus agglutinin, ACA-Amaranthus caudatus agglutinin, AHA-Arachis hypogaea agglutinin = peanut agglutinin (PNA), AIA-Artocarpus integrifolia agglutinin = jacalin, AlloA-Allomyrina dichotoma agglutinin, AOL-Aspergillus oryzae lectin, BanLec-Musa paradisiaca lectin, BS-I-Bandeiraea simplicifolia lectin = Griffonia(Bandeiraea) simplicifolia lectin I, Con A-concanavalin A, DBA-Dolichos biflorus agglutinin, DSA-Datura stramonium agglutinin (Jacalin), ECL-Erythrina cristagalli lectin, GNA-Galanthus nivalis agglutinin, GSA I (GSL I) -Griffonia (Bandeiraea) simplicifolia lectin I, GSL II-Griffonia (Bandeiraea) simplicifolia lectin II, HHL-Hippeastrum hybrid (amaryllis) lectin, HPA-Helix pomatia agglutinin, LBA-Phaseolus lunatus (lima bean, LBA), LEL-Lycopersicon esculentum (tomato) lectin, LCA-Lens culinaris agglutinin, LTA-Lotus tetragonolobus lectin, MAA I-Maackia amurensis agglutinin I, MAA II-Maackia amurensis agglutinin II, MGBL 1-macrophage galactose-binding lectin 1, MGBL 2 (macrophage galactose-binding lectin 2, NPA-Narcissuspseudonarcissus lectin, PHA E-Phaseolus vulgaris agglutinin E, PHA L-Phaseolus vulgaris agglutinin L, PhoSL-Pholiota squarrosa lectin, PNA-peanut agglutinin, PSL-Pisum sativum lectin, PTA I-Psophocarpus tetragonolobus lectin I, PTA II-Psophocarpus tetragonolobus II, PWM-Phytolacca americana, RCA I-Ricinus communis agglutinin I, RCA II-Ricinus communis agglutinin II, SBA-soybean agglutinin (Glycine max agglutinin), SCA-Sambucus canadensis agglutinin = Sambucus nigra agglutinin (SNA), SJA-Sophora japonica agglutinin II, SNA-Sambucus nigra agglutinin, SSA-Sambucus sieboldiana agglutinin, SSL-Salvia sclarea lectin, STL-Solanum tuberosum lectin, TJA-I-Trichosanthes japonica agglutinin I, TJA-II-Trichosanthes japonica agglutinin (Yamashita et al.), TVA-Triticum vulgaris agglutinin = WGA-wheat germ agglutinin, UEA-Ulex europaeus agglutinin, VVA-Vicia villosa lectin, WFA-Wisteria floribunda lectin, WGA-wheat germ agglutinin = TVA-Triticum vulgaris agglutinin. The up arrow symbol "↑" means an increase in the concentration of the corresponding glycan or complex (e.g., dimer, trimer, etc.). The down arrow symbol "↓" means an increase in the concentration of the corresponding glycan or complex (e.g., dimer, trimer, etc.). Table 1 shows the cancers, corresponding cancer biomarkers, and aberrant glycosylation, lectins, and antibodies. [Table 1] TIFF0007672150000002.tif204165TIFF0007672150000003.tif213165TIFF0007672150000004.t if209165TIFF0007672150000005.tif205165TIFF0007672150000006.tif189165TIFF00076721500 00007.tif184165TIFF0007672150000008.tif189165TIFF0007672150000009.tif176165TIFF000 7672150000010.tif199165TIFF0007672150000011.tif196165TIFF0007672150000012.tif211165 TIFF0007672150000013.tif194165TIFF0007672150000014.tif201165TIFF0007672150000015.t if204165TIFF0007672150000016.tif205165TIFF0007672150000017.tif202165TIFF00076721500 00018.tif186165TIFF0007672150000019.tif181165TIFF0007672150000020.tif197165TIFF000 7672150000021.tif192165TIFF0007672150000022.tif196165TIFF0007672150000023.tif129165

[0120] Due to their excellent sensitivity and / or specificity, the magnetic carriers, anti-glycoprotein antibodies, antigen-binding portions thereof, one or more lectins, compositions, kits, methods and uses based thereon of the present invention are particularly suitable for isoform-specific detection and analysis of glycoproteins (e.g. in cancer diagnosis).

[0121] In some embodiments, the present invention relates to an anti-glycoprotein antibody (e.g., an anti-PSA antibody, an anti-AFP antibody, an anti-MUC16 antibody, an anti-WFDC2 antibody, an anti-MUC1 antibody, an anti-ERBB2 antibody, an anti-CEACAM5 antibody, an anti-FUT3 antibody, or an anti-TG antibody, preferably an anti-PSA antibody), or an antigen-binding portion thereof (e.g., a single-chain antibody fragment (scAb)), immobilized (e.g., conjugated) on a magnetic support (e.g., a magnetic particle or a magnetic bead), which further comprises a polypeptide having peroxidase activity (e.g., a polypeptide having EC 1.11.1.7 enzymatic activity, such as microperoxidase-11). Further preferred antibodies in the context of the present invention are shown in Table 1.

[0122] In some aspects, the present invention relates to an anti-glycoprotein antibody, or an antigen-binding portion thereof, wherein the polypeptide having peroxidase activity has a molecular weight of less than 2 kDa (e.g., about 1.5 kDa or about 1.6 kDa or about 1.9 kDa), preferably a molecular weight of between 1 kDa and 2 kDa.

[0123] In some aspects, the present invention relates to an anti-glycoprotein antibody, or an antigen-binding portion thereof, wherein said polypeptide having peroxidase activity is immobilized (eg, conjugated) onto said magnetic support.

[0124] In some aspects, the invention relates to an anti-glycoprotein antibody, or antigen-binding portion thereof, that is or is not specifically directed to: i) prostate specific antigen (PSA), preferably SEQ ID NO: 1, 2, 3, 4, 5, or 6; more preferably SEQ ID NO: 6; ii) alpha-fetoprotein (AFP), preferably SEQ ID NO: 11 or 12; more preferably SEQ ID NO: 12; iii) mucin-16 (MUC16), preferably SEQ ID NO: 13; iv) WAP4-disulfide core domain protein 2 (WFDC2), preferably SEQ ID NO: 14, 15, 16, 17, 18, or 19; more preferably SEQ ID NO: 19; v) mucin-1 (MUC1), preferably SEQ ID NO: 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, or 37; more preferably SEQ ID NO: 37; and more preferably SEQ ID NO: 44; vii) carcinoembryonic antigen-related cell adhesion molecule 5 (CEACAM5), preferably SEQ ID NO: 45, 46, or 47; more preferably SEQ ID NO: 47; viii) galactoside 3(4)-L-fucosyltransferase (FUT3), preferably SEQ ID NO: 48; ix) thyroglobulin (TG), preferably SEQ ID NO: 49, 50, or 51; more preferably SEQ ID NO: 51.

[0125] In some aspects, the invention relates to an anti-glycoprotein antibody, or antigen-binding portion thereof, wherein the target polypeptide is prostate specific antigen (PSA) having peptidase activity (eg, EC 3.4.21.77 enzymatic activity).

[0126] In some embodiments, the invention relates to an anti-glycoprotein antibody, or antigen-binding portion thereof, comprising: i) a polypeptide that is at least 60% or more identical (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) to the polypeptide sequence of SEQ ID NO:6, preferably the polypeptide has SEQ ID NO:6; ii) a polypeptide that is at least 60% or more identical (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) to the polypeptide sequence of SEQ ID NO:1; , at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) identical to the polypeptide sequence of SEQ ID NO:1, preferably the polypeptide has SEQ ID NO:2; iii) a polypeptide that is at least 60% or more (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) identical to the polypeptide sequence of SEQ ID NO:2; %, at least 97%, at least 98%, at least 99%, or 100%) identical to the polypeptide sequence of SEQ ID NO:2, preferably the polypeptide has SEQ ID NO:2; iv) a polypeptide that is at least 60% or more (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) identical to the polypeptide sequence of SEQ ID NO:3, preferably the polypeptide has SEQ ID NO:3. , v) a polypeptide that is at least 60% or more (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) identical to the polypeptide sequence of SEQ ID NO:4, preferably the polypeptide has SEQ ID NO:4; vi) a polypeptide that is at least 60% or more (e.g., at least 65%, at least 70%, at least 75%, at least 80%,The present invention relates to an anti-glycoprotein antibody or antigen-binding portion thereof that specifically binds to a target polypeptide (e.g., PSA) comprising a polypeptide selected from the group consisting of: a polypeptide that is at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the polypeptide of SEQ ID NO: 5, preferably wherein the polypeptide has SEQ ID NO: 5.

[0127] In some aspects, the present invention relates to an anti-glycoprotein antibody, or an antigen-binding portion thereof, wherein the target polypeptide is human, rabbit, rat, or mouse, preferably, the target polypeptide is human.

[0128] In some aspects, the invention relates to an antibody, or antigen-binding portion thereof, wherein said polypeptide having peroxidase activity comprises microperoxidase (MP) (eg, microperoxidase-11).

[0129] In some aspects, the invention relates to an antibody, or antigen-binding portion thereof, wherein the microperoxidase (MP) is a heme containing peptide portion of cytochrome c (e.g., cytochrome c from Equus caballus, shown as SEQ ID NO: 10, NCBI Reference Sequence: NP_001157486.1) that retains peroxidase activity (e.g., EC 1.11.1.7 enzymatic activity, e.g., microperoxidase-11).

[0130] In some aspects, the invention relates to an antibody, or antigen-binding portion thereof, wherein the heme containing cytochrome c peptide portion is at least 60% or more (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) identical to a polypeptide sequence selected from the group consisting of SEQ ID NO:7 (MP-11 peptide), SEQ ID NO:8 (MP-9 peptide), and SEQ ID NO:9 (MP-8 peptide), and preferably the microperoxidase (MP) peptide is selected from the group consisting of SEQ ID NO:7 (MP-11 peptide), SEQ ID NO:8 (MP-9 peptide), and SEQ ID NO:9 (MP-8 peptide).

[0131] In some aspects, the invention relates to an antibody or antigen-binding portion thereof, wherein said magnetic carrier is a magnetic particle or a magnetic bead.

[0132] In some aspects, the present invention relates to an anti-glycoprotein antibody or antigen-binding portion thereof, which is capable of binding to the target polypeptide (e.g., PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3 or TG) in a sample and generating a detectable signal (e.g., by optical means).

[0133] In some aspects, the invention relates to anti-glycoprotein antibodies or antigen-binding portions thereof, which are capable of both binding to and concentrating the target polypeptide (e.g., PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3 or TG) in a sample and generating a detection signal (e.g., by optical means).

[0134] In some aspects, the present invention relates to an anti-glycoprotein antibody, or antigen-binding portion thereof, capable of detecting a target polypeptide (e.g., PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3 or TG) in a sample (e.g., a serum sample) having a target polypeptide in an amount corresponding to 0.04 mL or less of an undiluted biological sample (e.g., an undiluted serum sample), preferably in the range of 0.01 to 0.04 mL, more preferably in the range of 0.02 to 0.04 mL, and most preferably in the range of 0.02 to 0.04 mL.

[0135] In some aspects, the invention relates to an anti-glycoprotein antibody, or an antigen-binding portion thereof, wherein said anti-glycoprotein antibody is a monoclonal antibody.

[0136] In some aspects, the present invention relates to an anti-glycoprotein antibody, or an antigen-binding portion thereof, wherein the anti-glycoprotein antibody is selected from the group consisting of a chimeric antibody, a humanized antibody, or a human antibody.

[0137] In some aspects, the present invention relates to a magnetic support (e.g., a magnetic particle or bead) comprising i) an immobilized (e.g., conjugated) anti-glycoprotein antibody (e.g., an anti-PSA antibody, an anti-AFP antibody, an anti-MUC16 antibody, an anti-WFDC2 antibody, an anti-MUC1 antibody, an anti-ERBB2 antibody, an anti-CEACAM5 antibody, an anti-FUT3 antibody, or an anti-TG antibody), or an antigen-binding portion thereof (e.g., a single-chain antibody fragment (scAb)); and ii) a polypeptide having peroxidase activity (e.g., an EC 1.11.1.7 enzymatic activity, such as microperoxidase-11).

[0138] In some aspects, the present invention relates to a magnetic carrier, wherein the polypeptide having peroxidase activity has a molecular weight of less than 2 kDa (eg, about 1.5 kDa or about 1.6 kDa or about 1.9 kDa), preferably a molecular weight of 1 kDa to 2 kDa.

[0139] In some embodiments, the present invention relates to a magnetic carrier, on which the polypeptide having peroxidase activity is immobilized (eg, conjugated).

[0140] In some aspects, the invention relates to an anti-glycoprotein antibody, or antigen-binding portion thereof, that is selected from the group consisting of: i) prostate specific antigen (PSA), preferably SEQ ID NO: 1, 2, 3, 4, 5, or 6; more preferably SEQ ID NO: 6; ii) alpha-fetoprotein (AFP), preferably SEQ ID NO: 11 or 12; more preferably SEQ ID NO: 12; iii) mucin-16 (MUC16), preferably SEQ ID NO: 13; iv) WAP4-disulfide core domain protein 2 (WFDC2), preferably SEQ ID NO: 14, 15, 16, 17, 18, or 19; more preferably SEQ ID NO: 19; v) mucin-1 (MUC1), preferably SEQ ID NO: 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, or 37; more preferably SEQ ID NO: 37; and more preferably SEQ ID NO: 44; vii) carcinoembryonic antigen-related cell adhesion molecule 5 (CEACAM5), preferably SEQ ID NO: 45, 46, or 47; more preferably SEQ ID NO: 47; viii) galactoside 3(4)-L-fucosyltransferase (FUT3), preferably SEQ ID NO: 48; ix) thyroglobulin (TG), preferably SEQ ID NO: 49, 50, or 51; more preferably SEQ ID NO: 51.

[0141] In some embodiments, the present invention relates to a magnetic carrier, wherein the target polypeptide is prostate specific antigen (PSA) having peptidase activity (eg, EC 3.4.21.77 enzymatic activity).

[0142] In some embodiments, the invention relates to an anti-glycoprotein antibody, or antigen-binding portion thereof, comprising: i) a polypeptide that is at least 60% or more identical (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) to the polypeptide sequence of SEQ ID NO:6, preferably the polypeptide has SEQ ID NO:6; ii) a polypeptide that is at least 60% or more identical (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) to the polypeptide sequence of SEQ ID NO:1; , at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) identical to the polypeptide sequence of SEQ ID NO:1, preferably the polypeptide has SEQ ID NO:2; iii) a polypeptide that is at least 60% or more (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) identical to the polypeptide sequence of SEQ ID NO:2; %, at least 97%, at least 98%, at least 99%, or 100%) identical to the polypeptide sequence of SEQ ID NO:2, preferably the polypeptide has SEQ ID NO:2; iv) a polypeptide that is at least 60% or more (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) identical to the polypeptide sequence of SEQ ID NO:3, preferably the polypeptide has SEQ ID NO:3. , v) a polypeptide that is at least 60% or more (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) identical to the polypeptide sequence of SEQ ID NO:4, preferably the polypeptide has SEQ ID NO:4; vi) a polypeptide that is at least 60% or more (e.g., at least 65%, at least 70%, at least 75%, at least 80%,a polypeptide having at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to said target polypeptide (e.g., PSA) (e.g., a target glycoprotein comprises said polypeptide, e.g., an anti-glycoprotein antibody is raised against said polypeptide, e.g., an antigen glycoprotein comprises said polypeptide), preferably comprising a polypeptide having SEQ ID NO:5;

[0143] In some embodiments, the present invention relates to a magnetic carrier, wherein the target polypeptide is human, rabbit, rat, or mouse, preferably the target glycoprotein is human.

[0144] In some embodiments, the present invention relates to a magnetic carrier, wherein said polypeptide having peroxidase activity comprises microperoxidase (MP) (eg, microperoxidase-11).

[0145] In some embodiments, the present invention relates to a magnetic carrier, wherein the microperoxidase (MP) is a heme containing peptide portion of cytochrome c (e.g., cytochrome c from Equus caballus, shown as SEQ ID NO: 10, NCBI Reference Sequence: NP_001157486.1) that retains peroxidase activity (e.g., EC 1.11.1.7 enzyme activity, e.g., microperoxidase-11).

[0146] In some embodiments, the present invention relates to a magnetic carrier, wherein the heme containing peptide portion of cytochrome c is at least 60% or more (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) identical to a polypeptide sequence selected from the group consisting of SEQ ID NO:7 (MP-11 peptide), SEQ ID NO:8 (MP-9 peptide), and SEQ ID NO:9 (MP-8 peptide), and preferably, the microperoxidase (MP) peptide is selected from the group consisting of SEQ ID NO:7 (MP-11 peptide), SEQ ID NO:8 (MP-9 peptide), and SEQ ID NO:9 (MP-8 peptide).

[0147] In some embodiments, the present invention relates to a magnetic carrier, wherein the magnetic carrier is a magnetic particle or a magnetic bead.

[0148] In some aspects, the present invention relates to a magnetic carrier, which is capable of binding to the target polypeptide (e.g., PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3 or TG) in a sample and generating a detection signal (e.g., by optical means).

[0149] In some aspects, the present invention relates to a magnetic carrier capable of both binding and concentrating the target polypeptide (e.g., PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3 or TG) in a sample and generating a detection signal (e.g., by optical means).

[0150] In some aspects, the present invention relates to a magnetic carrier capable of detecting a target polypeptide (e.g., PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3 or TG) in a sample (e.g., a serum sample) having a target polypeptide in an amount corresponding to 0.04 mL or less of an undiluted biological sample (e.g., an undiluted serum sample), preferably in the range of 0.01 to 0.04 mL, more preferably in the range of 0.02 to 0.04 mL, and most preferably in the range of 0.02 to 0.04 mL.

[0151] In some embodiments, the present invention relates to a magnetic carrier, wherein the anti-glycoprotein antibody is a monoclonal antibody.

[0152] In some aspects, the present invention relates to a magnetic carrier, wherein the anti-glycoprotein antibody is selected from the group consisting of a chimeric antibody, a humanized antibody, or a human antibody.

[0153] In some aspects, the present invention relates to a method of making an anti-glycoprotein antibody (e.g., an anti-PSA antibody, an anti-AFP antibody, an anti-MUC16 antibody, an anti-WFDC2 antibody, an anti-MUC1 antibody, an anti-ERBB2 antibody, an anti-CEACAM5 antibody, an anti-FUT3 antibody, or an anti-TG antibody) or an antigen-binding portion thereof, comprising conjugating a magnetic support (e.g., a magnetic particle or a magnetic bead) to: i) an anti-glycoprotein antibody (e.g., an anti-PSA antibody, an anti-AFP antibody, an anti-MUC16 antibody, an anti-WFDC2 antibody, an anti-MUC1 antibody, an anti-ERBB2 antibody, an anti-CEACAM5 antibody, an anti-FUT3 antibody, or an anti-TG antibody) or an antigen-binding portion thereof; and ii) a polypeptide having peroxidase activity.

[0154] In some aspects, the present invention relates to a method for producing a magnetic carrier, the method comprising conjugating the magnetic carrier (e.g., a magnetic particle or a magnetic bead) to: i) an anti-glycoprotein antibody (e.g., an anti-PSA antibody, an anti-AFP antibody, an anti-MUC16 antibody, an anti-WFDC2 antibody, an anti-MUC1 antibody, an anti-ERBB2 antibody, an anti-CEACAM5 antibody, an anti-FUT3 antibody, or an anti-TG antibody), or an antigen-binding portion thereof; and ii) a polypeptide having peroxidase activity.

[0155] In some embodiments, the present invention relates to a method comprising the steps of: a) providing i) a magnetic carrier, or an anti-glycoprotein antibody (e.g., an anti-PSA antibody, an anti-AFP antibody, an anti-MUC16 antibody, an anti-WFDC2 antibody, an anti-MUC1 antibody, an anti-ERBB2 antibody, an anti-CEACAM5 antibody, an anti-FUT3 antibody, or an anti-TG antibody), or an antigen-binding portion thereof; ii) one or more lectins, preferably the one or more lectins are selected from the group consisting of Maackia amurensis lectin II (MAA II), concanavalin A (Con A) lectin, Aleuria aurantia lectin (AAL), Sambucus nigra (SNA-I) lectin, Wisteria floribunda lectin (WFL), more preferably the one or more lectins comprise MAA II, and most preferably the one or more lectins are MAA II. and most preferably, the one or more lectins are two lectins comprising MAA II in combination with aa) AAL (preferably, the method has a sensitivity of about 100% and / or the method has a specificity of about 81.3%), or bb) Con A (preferably, the method has a sensitivity of about 100% and / or the method has a specificity of about 93.8%), or cc) SNA-I (preferably, the method has a sensitivity of about 100% and / or the method has a specificity of about 93.8%); b) a target polypeptide of the anti-glycoprotein antibody (e.g., a target polypeptide, such as PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3 or and determining the amount, presence or absence of oligosaccharide chains (e.g., glycans) covalently bound to a PSA target polypeptide, preferably wherein the target polypeptide is PSA, and more preferably wherein the determining comprises the use of a magnetic carrier, and / or an anti-glycoprotein antibody, and / or an antigen-binding portion thereof, and / or one or more lectins, and / or a composition based thereon, and / or a kit based thereon.

[0156] In some aspects, the present invention relates to a method for detecting a glycosylated polypeptide, in which both binding and detection (e.g., by optical means) of the target polypeptide (e.g., PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3 or TG) are performed, preferably the target polypeptide is PSA.

[0157] In some aspects, the present invention relates to a method for detecting a glycosylated polypeptide, in which the binding, enrichment and detection (e.g., by optical means) of the target polypeptide (e.g., PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3 or TG) are performed together, preferably the target polypeptide is PSA.

[0158] In some embodiments, the present invention relates to a method for detecting a glycosylated polypeptide, the method being for one or more of: i) selective capture and / or enrichment of a target polypeptide (e.g., PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3 or TG), preferably the target polypeptide is PSA; ii) selective capture and / or enrichment of a target polypeptide (e.g., PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3 or TG, preferably the target polypeptide is PSA), the method for selective capture and / or enrichment comprising the use of one or more lectins (e.g., immobilized lectins), preferably the one or more lectins are immobilized at a sample location (e.g., an enzyme-linked immunosorbent assay (ELISA), enzyme-linked lectin assay (ELLA), or magnetic enzyme-linked lectin assay (MELLA) microplate). iii) glycoprofiling of a target polypeptide (e.g., PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3 or TG, preferably the target polypeptide is PSA); iv) screening and / or analysis of oligosaccharides (e.g., glycosyl) chains covalently attached to a target polypeptide (e.g., PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3 or TG, preferably the target polypeptide is PSA); v) diagnosing cancer (e.g., prostate cancer); vi) positive and / or negative prediction of cancer (e.g., prostate cancer); vii) determining the clinical stage of cancer (e.g., prostate cancer); viii) distinguishing between prostate cancer and metastatic prostate cancer; ix) identifying prostate cancer that may metastasize (e.g., may metastasize to bone); x) distinguishing between benign prostatic hyperplasia (BPH) and prostate cancer. xi) Prevention and / or treatment of cancer (e.g., prostate cancer).xii) Distinguishing between important and non-important tumors, for example, by glycoprotein-based (e.g., target polypeptide-based, e.g., PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3 or TG-based, preferably the target polypeptide is PSA) diagnosis of cancer (e.g., prostate cancer). xiii) Distinguishing between low-proliferative (e.g., clinically harmless) and high-proliferative (e.g., clinically relevant) tumors, for example, by glycoprotein-based (e.g., target polypeptide-based, e.g., PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3 or TG-based, preferably the target polypeptide is PSA) diagnosis of cancer (e.g., prostate cancer). xiv) Identification of organ-confined and / or potentially curable cancers (e.g. prostate cancer), for example by glycoprotein-based (e.g. target polypeptide-based, e.g. PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3 or TG-based, preferably the target polypeptide is PSA) diagnosis of cancer. xv) Compound screening.

[0159] In some embodiments, the present invention relates to a method of screening a compound, the method comprising: a) i) providing a prostate cancer sample with a test compound; b) contacting the prostate cancer sample with the test compound; and c) determining the likelihood of the prostate cancer cells to metastasize based on the amount, presence, or absence of determined oligosaccharide chains (e.g., glycans) covalently attached to a target polypeptide (e.g., PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3 or TG, preferably the target polypeptide is PSA) in the prostate cancer sample before and after contacting the prostate cancer sample with the test compound.

[0160] In some aspects, the present invention relates to a method as described herein, wherein i) for positive prediction of prostate cancer, and / or ii) for distinguishing between benign prostatic hyperplasia (BPH) and prostate cancer, the one or more lectins comprise MAA II or WFL, preferably, the one or more lectins comprise MAA II.

[0161] In some embodiments, the present invention relates to the methods described herein, wherein the one or more lectins used is MAA II, and wherein the sensitivity and / or specificity of the method is about 87.5%.

[0162] In some embodiments, the present invention relates to a method described herein, wherein the one or more lectins used are two lectins comprising i) Con A (the method has a sensitivity of about 100% and / or the method has a specificity of about 93.8%), or ii) SNA-I (the method has a sensitivity of about 100% and / or the method has a specificity of about 93.8%), or iii) MAA II in combination with AAL (the method has a sensitivity of about 100% and / or the method has a specificity of about 81.3%).

[0163] In some embodiments, the present invention relates to the methods described herein, wherein the lectin used is WFL, and wherein the sensitivity of the method is about 50% and / or the specificity of the method is about 75%.

[0164] In some aspects, the present invention relates to a method as described herein, i) for negative prediction of prostate cancer, and / or ii) for distinguishing between benign prostatic hyperplasia (BPH) and prostate cancer, wherein the lectin is selected from the group consisting of Con A, AAL, and SNA-I.

[0165] In some embodiments, the present invention relates to the methods described herein, wherein the lectin used is Con A, and wherein the sensitivity of the method is about 50% and / or the specificity of the method is about 75%.

[0166] In some embodiments, the present invention relates to the methods described herein, wherein the lectin used is AAL, and wherein the sensitivity of the method is about 50% and / or the specificity of the method is about 75%.

[0167] In some embodiments, the present invention relates to a method as described herein, wherein the lectin used is SNA-I, and wherein the sensitivity of the method is about 57% and / or the specificity of the method is about 75%.

[0168] In some aspects, the invention relates to a method described herein, comprising determining a course of treatment based on the amount, presence, or absence of determined oligosaccharide chains (e.g., glycans) covalently attached to a target polypeptide (e.g., a target polypeptide, e.g., PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3 or TG, preferably the target polypeptide is PSA) of an anti-glycoprotein antibody.

[0169] In some aspects, the present invention relates to a method described herein, which distinguishes between prostate cancer and metastatic prostate cancer in a sample (e.g., in a serum sample), wherein the one or more lectins used are selected from the group consisting of AAL and Con A.

[0170] In some aspects, the present invention relates to methods as described herein, wherein the methods are performed on a sample.

[0171] In some aspects, the present invention relates to a method as described herein, wherein the suitable sample is selected from the group of urine, blood, serum, biopsy specimen, and post-operative tissue sample, preferably a serum sample.

[0172] In some aspects, the present invention relates to lectins for use in the methods of the invention, preferably for use in methods for i) predicting (e.g., positive or negative) prostate cancer, and / or ii) distinguishing between benign prostatic hyperplasia (BPH) and prostate cancer, and / or iii) distinguishing between prostate cancer and metastatic prostate cancer.

[0173] In some embodiments, the present invention relates to one or more lectins selected from the group consisting of Maackia amurensis lectin II (MAA II), concanavalin A (Con A) lectin, Aleuria aurantia lectin (AAL), Sambucus nigra (SNA-I) lectin, Wisteria floribunda lectin (WFL), preferably the one or more lectins comprise MAA II, more preferably the one or more lectins are two lectins comprising MAA II, and most preferably the one or more lectins are two lectins comprising MAA II in combination with AAL, Con A, or SNA-I.

[0174] In some aspects, the invention relates to one or more lectins, which are immobilized (e.g., at a sample location, e.g., a microplate, e.g., an Enzyme-Linked Immunosorbent Assay (ELISA), Enzyme-Linked Lectin Assay (ELLA), or Magnetic Enzyme-Linked Lectin Assay (MELLA) microplate).

[0175] In some embodiments, the present invention relates to a composition comprising one or more of the following: i) a glycoprotein antibody (e.g., an anti-PSA antibody, an anti-AFP antibody, an anti-MUC16 antibody, an anti-WFDC2 antibody, an anti-MUC1 antibody, an anti-ERBB2 antibody, an anti-CEACAM5 antibody, an anti-FUT3 antibody, or an anti-TG antibody, preferably an anti-PSA antibody), or an antigen-binding portion thereof; ii) a magnetic carrier. iii) one or more lectins, preferably the one or more lectins are selected from the group consisting of Maackia amurensis lectin II (MAA II), concanavalin A (Con A) lectin, Aleuria aurantia lectin (AAL), Sambucus nigra (SNA-I) lectin, Wisteria floribunda lectin (WFL), more preferably the one or more lectins comprise MAA II, most preferably the one or more lectins are two lectins comprising MAA II, and even more preferably the one or more lectins are two lectins comprising MAA II in combination with AAL, Con A, or SNA-I.

[0176] In some aspects, the present invention relates to a kit comprising a glycoprotein antibody (e.g., an anti-PSA antibody, an anti-AFP antibody, an anti-MUC16 antibody, an anti-WFDC2 antibody, an anti-MUC1 antibody, an anti-ERBB2 antibody, an anti-CEACAM5 antibody, an anti-FUT3 antibody, or an anti-TG antibody, preferably an anti-PSA antibody), an antigen-binding portion thereof, a magnetic carrier, one or more lectins, or a composition.

[0177] In some aspects, the present invention relates to a glycoprotein antibody (e.g., an anti-PSA antibody, an anti-AFP antibody, an anti-MUC16 antibody, an anti-WFDC2 antibody, an anti-MUC1 antibody, an anti-ERBB2 antibody, an anti-CEACAM5 antibody, an anti-FUT3 antibody, or an anti-TG antibody, preferably an anti-PSA antibody), an antigen-binding portion thereof, a magnetic carrier, one or more lectins, or a composition, for use as a medicament.

[0178] In some aspects, the invention relates to a glycoprotein antibody (e.g., an anti-PSA antibody, an anti-AFP antibody, an anti-MUC16 antibody, an anti-WFDC2 antibody, an anti-MUC1 antibody, an anti-ERBB2 antibody, an anti-CEACAM5 antibody, an anti-FUT3 antibody, or an anti-TG antibody, preferably an anti-PSA antibody), an antigen-binding portion thereof, a magnetic carrier, one or more lectins, or a composition, for use in one or more of the following methods (e.g., in vitro, in vivo, or ex vivo methods): i) selective capture and / or enrichment of a target polypeptide (e.g., PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3 or TG), preferably the target polypeptide is PSA. ii) selective capture and / or enrichment of a target polypeptide (e.g., PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3 or TG, preferably the target polypeptide is PSA), the method for selective capture and / or enrichment comprising the use of one or more lectins (e.g., immobilized lectins), preferably the one or more lectins are immobilized at a sample location (e.g., an enzyme-linked immunosorbent assay (ELISA), enzyme-linked lectin assay (ELLA), or magnetic enzyme-linked lectin assay (MELLA) microplate); iii) glycoprofiling of a target polypeptide (e.g., PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3 or TG, preferably the target polypeptide is PSA). iv) screening and / or analysis of oligosaccharide chains (e.g., glycans) covalently attached to a target polypeptide (e.g., PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3 or TG, preferably the target polypeptide is PSA); v) diagnosing cancer (e.g., prostate cancer); vi) positive and / or negative prediction of cancer (e.g., prostate cancer); vii) determining the clinical stage of cancer (e.g., prostate cancer); viii) distinguishing between prostate cancer and metastatic prostate cancer; ix) identifying prostate cancer that may metastasize (e.g., may metastasize to bone); xi) distinguishing between benign prostatic hyperplasia (BPH) and prostate cancer.xii) prevention and / or treatment of cancer (e.g. prostate cancer); xiii) differentiation between important and non-important tumors, for example by glycoprotein-based (e.g. target polypeptide-based, e.g. PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3 or TG-based, preferably the target polypeptide is PSA) diagnosis of cancer (e.g. prostate cancer); xiv) differentiation between low-proliferative tumors (e.g. clinically harmless) and high-proliferative tumors (e.g. clinically relevant), for example by glycoprotein-based (e.g. target polypeptide-based, e.g. PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3 or TG-based, preferably the target polypeptide is PSA) diagnosis of cancer (e.g. prostate cancer). xv) identification of organ-confined and / or potentially curable cancers (e.g. prostate cancer), for example by glycoprotein-based (e.g. target polypeptide-based, e.g. PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3 or TG-based, preferably the target polypeptide is PSA) diagnosis of cancer; xvi) screening of compounds; xvii) use in the methods of the invention.

[0179] In some aspects, the invention relates to a glycoprotein antibody (e.g., an anti-PSA antibody, an anti-AFP antibody, an anti-MUC16 antibody, an anti-WFDC2 antibody, an anti-MUC1 antibody, an anti-ERBB2 antibody, an anti-CEACAM5 antibody, an anti-FUT3 antibody, or an anti-TG antibody, preferably an anti-PSA antibody), an antigen-binding portion thereof, a magnetic carrier, one or more lectins, or a composition for one or more of the following: i) selective capture and / or enrichment of a target polypeptide (e.g., PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3 or TG), preferably the target polypeptide is PSA. ii) selective capture and / or enrichment of a target polypeptide (e.g., PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3 or TG, preferably the target polypeptide is PSA), the selective capture and / or enrichment comprising the use of one or more lectins (e.g., immobilized lectins), preferably the one or more lectins are immobilized at a sample location (e.g., an enzyme-linked immunosorbent assay (ELISA), enzyme-linked lectin assay (ELLA), or magnetic enzyme-linked lectin assay (MELLA) microplate); iii) glycoprofiling of a target polypeptide (e.g., PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3 or TG, preferably the target polypeptide is PSA). iv) screening and / or analysis of oligosaccharide chains (e.g., glycans) covalently bound to a target polypeptide (e.g., PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3 or TG, preferably the target polypeptide is PSA); v) diagnosis of cancer (e.g., prostate cancer); vi) positive and / or negative prediction of cancer (e.g., prostate cancer); vii) determination of the clinical stage of cancer (e.g., prostate cancer); viii) differentiation between prostate cancer and metastatic prostate cancer; ix) identification of prostate cancer that may metastasize (e.g., may metastasize to bone); x) differentiation between benign prostatic hyperplasia (BPH) and prostate cancer; xi) prevention and / or treatment of cancer (e.g., prostate cancer).xii) Distinguishing between important and non-important tumors, for example, by glycoprotein-based (e.g., target polypeptide-based, e.g., PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3 or TG-based, preferably the target polypeptide is PSA) diagnosis of cancer (e.g., prostate cancer). xiii) Distinguishing between low-proliferative (e.g., clinically harmless) and high-proliferative (e.g., clinically relevant) tumors, for example, by glycoprotein-based (e.g., target polypeptide-based, e.g., PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3 or TG-based, preferably the target polypeptide is PSA) diagnosis of cancer (e.g., prostate cancer). xiv) identification of organ-confined and / or potentially curable cancers (e.g. prostate cancer), for example by glycoprotein-based (e.g. target polypeptide-based, e.g. PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3 or TG-based, preferably the target polypeptide is PSA) diagnosis of cancer; xv) screening of compounds; xvi) use in the methods of the invention.

[0180] In some aspects, the present invention relates to the uses of the present invention, which are in vitro, ex vivo, or in vivo uses, or a combination thereof.

[0181] In some aspects, the present invention relates to a glycoprotein antibody, an antigen-binding portion thereof, a magnetic carrier, one or more lectins, a kit, a composition, a use, or a method of the present invention, wherein the lectin is a polypeptide sequence selected from the group consisting of SEQ ID NOs: 52, 53, 54, 55, 56, 57, 58, 59, UniProtKB Accession Nos. P0DKL3, P02866, P18891, O04366, A0A218PFP3, Q945S3, Q00022, Q6YNX3, Q71QF2, P02872, P18670, Q2UNX8, Q8L5H4, A0A089ZWN7, P05 045, P19588, P83410, P17931, P56470, P24146, Q41263, Q39990, Q2F1K8, G9 M5T0, B3XYC5, P02870, P19664, P0DKL3, P49300, A9XX86, Q40423, P16300, P 05088, P05087, Q9AVB0, P02867, O24313, Q9SM56, P06750, B9SPG3, Q9BZZ2, P20916, Q9NYZ4, Q96RL6, P05046, P93535, P02876, P10968, P10969, P22972 or P56625, the lectin is at least 60% or more (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) identical to a lectin described in Table 1 herein, and said lectin is capable of specifically reacting with glycosidic residues (e.g., terminal glycosidic residues) of other molecules (e.g., cell wall polysaccharides and / or glycoproteins (e.g., a target polypeptide in any one of the preceding paragraphs, or a biomarker selected from the group consisting of the biomarkers described in Table 1 herein).

[0182] In some aspects, the present invention relates to a glycoprotein antibody, an antigen-binding portion thereof, a magnetic carrier, one or more lectins, a kit, a composition, a use, or a method of the present invention, wherein the lectins are selected from the group consisting of SEQ ID NOs: 52, 53, 54, 55, 56, 57, 58, 59, UniProtKB Accession Nos. P0DKL3, P02866, P18891, O04366, A0A218PFP3, Q945S3, Q00022, Q6YNX3, Q71QF2, P02872, P18670, Q2UNX8, Q8L5H4, A0A089ZWN7, P05045, P19588, P83410, P17931, P56470, P24146, Q41263, Q39990, Q2F1K8, G9M5T0, B3XYC5, P02870, P19664, P0DKL3, P49300, A9XX86, Q40423, P16300, P05088, P05087, Q9AVB0, P02867, O24313, Q9SM56, P06750, B9SPG3, Q9BZZ2, P20916, Q9NYZ4, Q96RL6, P05046, P93535, P02876, P10968, P10969, P22972, or P56625 lectins, or the lectins listed in Table 1 herein.

[0183] In some aspects, the present invention relates to a glycoprotein antibody, an antigen-binding portion thereof, a magnetic carrier, one or more lectins, a kit, a composition, a use, or a method of the present invention, wherein the lectin is mature.

[0184] In some aspects, the present invention relates to a glycoprotein antibody, an antigen-binding portion thereof, a magnetic carrier, one or more lectins, a kit, a composition, a use, or a method of the present invention, wherein the antibody is selected from the group consisting of the antibodies described in Table 1 herein.

[0185] In some aspects, the present invention relates to a glycoprotein antibody, an antigen-binding portion thereof, a magnetic carrier, one or more lectins, a kit, a composition, a use, or a method of the present invention, wherein the biomarker is selected from the group consisting of the biomarkers listed in Table 1 herein.

[0186] In some aspects, the present invention relates to a glycoprotein antibody, an antigen-binding portion thereof, a magnetic carrier, one or more lectins, a kit, a composition, a use, or a method of the present invention, wherein the cancer is selected from the group consisting of the cancers listed in Table 1 herein.

[0187] In some aspects, the present invention relates to a glycoprotein antibody, an antigen-binding portion thereof, a magnetic carrier, one or more lectins, a kit, a composition, a use, or a method of the present invention, wherein the antibody, the biomarker, the cancer, and the lectin are selected from the group consisting of the corresponding antibodies, biomarkers, cancers, and lectins described in Table 1 herein.

[0188] In some aspects, the present invention relates to a glycoprotein antibody, antigen-binding portion thereof, magnetic carrier, one or more lectins, kit, composition, use, or method according to any one of the preceding paragraphs, wherein the corresponding glycomodification (e.g., a corresponding change (e.g., a detectable change)) in the glycosylation state, and / or the glycocomposition, and / or the glycoconjugate, and / or the glycoconjugation (e.g., dimerization, trimerization, etc.) is selected from the group consisting of the glycomodifications listed in Table 1 herein.

[0189] The references shown in Table 1 herein are as follows: [1] C. Ohyama, M. Hosono, K. Nitta, M. Oh-eda, K. Yoshikawa, T. Habuchi, Y. Arai, M. Fukuda, Carbohydrate structure and differential binding of prostate specific antigen to Maackia amurensis lectin between prostate cancer and benign prostate hypertrophy, Glycobiology, 14 (2004) 671-679. [2] K. Fukushima, T. Satoh, S. Baba, K. Yamashita, α1,2-Fucosylated and β-N-acetylgalactosaminylated prostate-specific antigen as an efficient marker of prostatic cancer, Glycobiology, 20 (2010) 452-460. [3] Ishikawa T, Yoneyama T, Tobisawa Y, Hatakeyama S, Kurosawa T, Nakamura K, Narita S, Mitsuzuka K, Duivenvoorden W, Pinthus JH, Hashimoto Y, Koie T, Habuchi T, Arai Y, Ohyama C, An Automated Micro-Total Immunoassay System for Measurement Cancer-Associated 2,3-Linked Sialyl N-Glycan-Carrying Prostate-Specific Antigen May Improve the Accuracy of Prostate Cancer Diagnosis, Int. J. Mol. Sci., 18 (2017) [4] D. Pihikova, P. Kasak, P. Kubanikova, R. Sokol, J. Tkac, Aberrant sialylation of a prostate-specific antigen: Electrochemical label-free glycoprofiling in prostate cancer serum samples, Anal. Chim. Acta, 934 (2016) 72-79. [5] C. Ohyama, T. Koie, T. Yoneyama, Y. Tobisawa, Quantification of prostate cancer-associated aberrant glycosylation of prostate-specific antigen, Glycoscience: Biology and Medicine, Springer2015, pp. 1373-1377. [6] E. Llop, M. Ferrer-Batalle, S. Barrabes, P.E. Guerrero, M. Ramirez, R. Saldova, P.M. Rudd, R.N. Aleixandre, J. Comet, R. de Llorens, R. Peracaula, Improvement of Prostate Cancer Diagnosis by Detecting PSA Glycosylation-Specific Changes, Theranostics, 6 (2016) 1190-1204. [7] M. Ferrer-Batalle, E. Llop, M. Ramirez, R.N. Aleixandre, M. Saez, J. Comet, R. de Llorens, R. Peracaula, Comparative Study of Blood-Based Biomarkers, alpha 2,3-Sialic Acid PSA and PHI, for High-Risk Prostate Cancer Detection, International Journal of Molecular Sciences, 18 (2017) 12. [8] T. Yoneyama, C. Ohyama, S. Hatakeyama, S. Narita, T. Habuchi, T. Koie, K. Mori, K.I. Hidari, M. Yamaguchi, T. Suzuki, Measurement of aberrant glycosylation of prostate specific antigen can improve specificity in early detection of prostate cancer, Biochem. Biophys. Res. Commun., 448 (2014) 390-396. [9] N. Idil, I. Percin, V. Karakoc, H. Yavuz, N. Aksoz, A. Denizli, Concanavalin A immobilized magnetic poly(glycidyl methacrylate) beads for prostate specific antigen binding, Colloid Surf. B-Biointerfaces, 134 (2015) 461-468.

[10] M.V. Dwek, A. Jenks, A.J. Leathem, A sensitive assay to measure biomarker glycosylation demonstrates increased fucosylation of prostate specific antigen (PSA) in patients with prostate cancer compared with benign prostatic hyperplasia, Clin. Chim. Acta, 411 (2010) 1935-1939.

[11] K. Hagiwara, Y. Tobisawa, T. Kaya, T. Kaneko, S. Hatakeyama, K. Mori, Y. Hashimoto, T. Koie, Y. Suda, C. Ohyama, T. Yoneyama, Wisteria floribunda Agglutinin and Its Reactive-Glycan-Carrying Prostate-Specific Antigen as a Novel Diagnostic and Prognostic Marker of Prostate Cancer, Int. J. Mol. Sci., 18 (2017) 16.

[12] T. Kaya, T. Kaneko, S. Kojima, Y. Nakamura, Y. Ide, K. Ishida, Y. Suda, K. Yamashita, High-sensitivity immunoassay with surface plasmon field-enhanced fluorescence spectroscopy using a plastic sensor chip: Application to quantitative analysis of total prostate-specific antigen and GalNAcβ1-4GlcNAc-linked prostate-specific antigen for prostate cancer diagnosis, Anal. Chem., 87 (2015) 1797-1803.

[13] Q.K. Li, L. Chen, M.-H. Ao, J.H. Chiu, Z. Zhang, H. Zhang, D.W. Chan, Serum fucosylated prostate-specific antigen (PSA) improves the differentiation of aggressive from non-aggressive prostate cancers, Theranostics, 5 (2015) 267.

[14] K. Fujita, T. Hayashi, K. Matsuzaki, W. Nakata, M. Masuda, A. Kawashima, T. Ujike, A. Nagahara, M. Tsuchiya, Y. Kobayashi, S. Nojima, M. Uemura, E. Morii, E. Miyoshi, N. Nonomura, Decreased fucosylated PSA as a urinary marker for high Gleason score prostate cancer, Oncotarget, 7 (2016) 56643-56649.

[15] S. Takahashi, T. Sugiyama, M. Shimomura, Y. Kamada, K. Fujita, N. Nonomura, E. Miyoshi, M. Nakano, Site-specific and linkage analyses of fucosylated N-glycans on haptoglobin in sera of patients with various types of cancer: possible implication for the differential diagnosis of cancer, Glycoconjugate J., 33 (2016) 471-482.

[16] S. Kazuno, T. Fujimura, T. Arai, T. Ueno, K. Nagao, M. Fujime, K. Murayama, Multi-sequential surface plasmon resonance analysis of haptoglobin-lectin complex in sera of patients with malignant and benign prostate diseases, Anal. Biochem., 419 (2011) 241-249.

[17] S.-J. Yoon, S.-Y. Park, P.-C. Pang, J. Gallagher, J.E. Gottesman, A. Dell, J.-H. Kim, S.-I. Hakomori, N-glycosylation status of β-haptoglobin in sera of patients with prostate cancer vs. benign prostate diseases, Int. J. Oncol., 36 (2010) 193-203.

[18] T. Fujimura, Y. Shinohara, B. Tissot, P.C. Pang, M. Kurogochi, S. Saito, Y. Arai, M. Sadilek, K. Murayama, A. Dell, Glycosylation status of haptoglobin in sera of patients with prostate cancer vs. benign prostate disease or normal subjects, Int. J. Cancer, 122 (2008) 39-49.

[19] K. Fujita, M. Shimomura, M. Uemura, W. Nakata, M. Sato, A. Nagahara, Y. Nakai, S. Takamatsu, E. Miyoshi, N. Nonomura, Serum fucosylated haptoglobin as a novel prognostic biomarker predicting high‐Gleason prostate cancer, The Prostate, 74 (2014) 1052-1058.

[20] S. Weiz, M. Wieczorek, C. Schwedler, M. Kaup, E.I. Braicu, J. Sehouli, R. Tauber, V. Blanchard, Acute‐phase glycoprotein N‐glycome of ovarian cancer patients analyzed by CE‐LIF, Electrophoresis, 37 (2016) 1461-1467.

[21] R. Saldova, L. Royle, C.M. Radcliffe, U.M. Abd Hamid, R. Evans, J.N. Arnold, R.E. Banks, R. Hutson, D.J. Harvey, R. Antrobus, Ovarian cancer is associated with changes in glycosylation in both acute-phase proteins and IgG, Glycobiology, 17 (2007) 1344-1356.

[22] G. Turner, M. Goodarzi, S. Thompson, Glycosylation of alpha-1-proteinase inhibitor and haptoglobin in ovarian cancer: evidence for two different mechanisms, Glycoconjugate J., 12 (1995) 211-218.

[23] K. Chen, A. Gentry-Maharaj, M. Burnell, C. Steentoft, L. Marcos-Silva, U. Mandel, I. Jacobs, A. Dawnay, U. Menon, O. Blixt, Microarray Glycoprofiling of CA125 improves differential diagnosis of ovarian cancer, J. Proteome Res., 12 (2013) 1408-1418.

[24] R. Saldova, W.B. Struwe, K. Wynne, G. Elia, M.J. Duffy, P.M. Rudd, Exploring the glycosylation of serum CA125, International journal of molecular sciences, 14 (2013) 15636-15654.

[25] H. Zhuang, J. Gao, Z. Hu, J. Liu, D. Liu, B. Lin, Co-expression of Lewis y antigen with human epididymis protein 4 in ovarian epithelial carcinoma, PLoS One, 8 (2013) e68994.

[26] J. Wu, X. Xie, S. Nie, R.J. Buckanovich, D.M. Lubman, Altered expression of sialylated glycoproteins in ovarian cancer sera using lectin-based ELISA assay and quantitative glycoproteomics analysis, J. Proteome Res., 12 (2013) 3342-3352.

[27] H. Ideo, Y. Hinoda, K. Sakai, I. Hoshi, S. Yamamoto, M. Oka, K. Maeda, N. Maeda, S. Hazama, J. Amano, Expression of mucin 1 possessing a 3′‐sulfated core1 in recurrent and metastatic breast cancer, Int. J. Cancer, 137 (2015) 1652-1660.

[28] S.A. Svarovsky, L. Joshi, Cancer glycan biomarkers and their detection-past, present and future, Anal. Methods, 6 (2014) 3918-3936.

[29] S.J. Storr, L. Royle, C.J. Chapman, U.M.A. Hamid, J.F. Robertson, A. Murray, R.A. Dwek, P.M. Rudd, The O-linked glycosylation of secretory / shed MUC1 from an advanced breast cancer patient's serum, Glycobiology, 18 (2008) 456-462.

[30] H.A. Badr, D.M. AlSadek, A.A. Darwish, A.I. ElSayed, B.O. Bekmanov, E.M. Khussainova, X. Zhang, W.C. Cho, L.B. Djansugurova, C.-Z. Li, Lectin approaches for glycoproteomics in FDA-approved cancer biomarkers, Expert review of proteomics, 11 (2014) 227-236.

[31] Y. Taeda, M. Nose, S. Hiraizumi, N. Ohuchi, Expression of L-PHA-binding proteins in breast cancer: Reconstitution and molecular characterization of beta 1-6 branched oligosaccharides in three-dimensional cell culture, Breast Cancer Res. Treat., 38 (1996) 313-324.

[32] S.Y. Park, S.J. Yoon, Y.T. Jeong, J.M. Kim, J.Y. Kim, B. Bernert, T. Ullman, S.H. Itzkowitz, J.H. Kim, S.i. Hakomori, N‐glycosylation status of β‐haptoglobin in sera of patients with colon cancer, chronic inflammatory diseases and normal subjects, Int. J. Cancer, 126 (2010) 142-155.

[33] Y. Takeda, S. Shinzaki, K. Okudo, K. Moriwaki, K. Murata, E. Miyoshi, Fucosylated haptoglobin is a novel type of cancer biomarker linked to the prognosis after an operation in colorectal cancer, Cancer, 118 (2012) 3036-3043.

[34] S.Y. Park, S.H. Lee, N. Kawasaki, S. Itoh, K. Kang, S. Hee Ryu, N. Hashii, J.M. Kim, J.Y. Kim, J. Hoe Kim, α1‐3 / 4 fucosylation at Asn 241 of β‐haptoglobin is a novel marker for colon cancer: A combinatorial approach for development of glycan biomarkers, Int. J. Cancer, 130 (2012) 2366-2376.

[35] S.-Y. Park, S.-J. Yoon, S.-I. Hakomori, J.-M. Kim, J.-Y. Kim, B. Bernert, T. Ullman, S.H. Itzkowitz, J.H. Kim, Dimeric Lea (Lea-on-Lea) status of β-haptoglobin in sera of colon cancer, chronic inflammatory disease and normal subjects, Int. J. Oncol., 36 (2010) 1291-1297.

[36] R.S. Bresalier, J.C. Byrd, D. Tessler, J. Lebel, J. Koomen, D. Hawke, E. Half, K.F. Liu, N. Mazurek, C. Great Lakes-New England, A circulating ligand for galectin-3 glycoprotein elevated in individual is a haptoglobin-related with colon cancer, Gastroenterology, 127 (2004) 741-748.

[37] E. Saeland, A.I. Belo, S. Mongera, I. van Die, G.A. Meijer, Y. van Kooyk, Differential glycosylation of MUC1 and CEACAM5 between normal mucosa and tumour tissue of colon cancer patients, Int. J. Cancer, 131 (2012) 117-128.

[38] Y. Qiu, T.H. Patwa, L. Xu, K. Shedden, D.E. Misek, M. Tuck, G. Jin, M.T. Ruffin, D.K. Turgeon, S. Synal, Plasma glycoprotein profiling for colorectal cancer biomarker identification by lectin glycoarray and lectin blot, J. Proteome Res., 7 (2008) 1693-1703.

[39] C. Li, D.M. Simeone, D.E. Brenner, M.A. Anderson, K.A. Shedden, M.T. Ruffin, D.M. Lubman, Pancreatic cancer serum detection using a lectin / glyco-antibody array method, J. Proteome Res., 8 (2008) 483-492.

[40] J. Zhao, T.H. Patwa, W. Qiu, K. Shedden, R. Hinderer, D.E. Misek, M.A. Anderson, D.M. Simeone, D.M. Lubman, Glycoprotein microarrays with multi-lectin detection: unique lectin binding patterns as a tool for classifying normal, chronic pancreatitis and pancreatic cancer sera, J. Proteome Res., 6 (2007) 1864-1874.

[41] E. Miyoshi, M. Nakano, Fucosylated haptoglobin is a novel marker for pancreatic cancer: detailed analyses of oligosaccharide structures, Proteomics, 8 (2008) 3257-3262.

[42] S. Nie, A. Lo, J. Wu, J. Zhu, Z. Tan, D.M. Simeone, M.A. Anderson, K.A. Shedden, M.T. Ruffin, D.M. Lubman, Glycoprotein biomarker panel for pancreatic cancer discovered by quantitative proteomics analysis, J. Proteome Res., 13 (2014) 1873-1884.

[43] K. Kusama, Y. Okamoto, K. Saito, T. Kasahara, T. Murata, Y. Ueno, Y. Kobayashi, Y. Kamada, E. Miyoshi, Reevaluation of Pholiota squarrosa lectin-reactive haptoglobin as a pancreatic cancer biomarker using an improved ELISA system, Glycoconjugate J., (2017) 1-8.

[44] N. Parker, C. Makin, C. Ching, D. Eccleston, O. Taylor, D. Milton, J.M. Rhodes, A new enzyme‐linked lectin / mucin antibody sandwich assay (CAM 17.1 / WGA) assessed in combination with CA 19‐9 and peanut lectin binding assay for the diagnosis of pancreatic cancer, Cancer, 70 (1992) 1062-1068.

[45] J.Y. Yiannakou, P. Newland, F. Calder, A.N. Kingsnorth, J.M. Rhodes, Prospective study of CAM 17 center dot 1 / WGA mucin assay for serological diagnosis of pancreatic cancer, Lancet, 349 (1997) 389-392.

[46] T. Yue, I.J. Goldstein, M.A. Hollingsworth, K. Kaul, R.E. Brand, B.B. Haab, The prevalence and nature of glycan alterations on specific proteins in pancreatic cancer patients revealed using antibody-lectin sandwich arrays, Mol. Cel. Proteom., 8 (2009) 1697-1707.

[47] S. Pan, T.A. Brentnall, R. Chen, Glycoproteins and glycoproteomics in pancreatic cancer, World journal of gastroenterology, 22 (2016) 9288.

[48] K. Shimizu, K. Nakamura, S. Kobatake, S. Satomura, M. Maruyama, F. Kameko, J. Tajiri, R. Kato, The clinical utility of Lens culinaris agglutinin-reactive thyroglobulin ratio in serum for distinguishing benign from malignant conditions of the thyroid, Clin. Chim. Acta, 379 (2007) 101-104.

[49] T. Kanai, M. Amakawa, R. Kato, K. Shimizu, K. Nakamura, K.-i. Ito, Y. Hama, M. Fujimori, J. Amano, Evaluation of a new method for the diagnosis of alterations of Lens culinaris agglutinin binding of thyroglobulin molecules in thyroid carcinoma, Clinical chemistry and laboratory medicine, 47 (2009) 1285-1290.

[50] K. YAMAMOTO, T. TSUJI, O. TARUTANI, T. OSAWA, Structural changes of carbohydrate chains of human thyroglobulin accompanying malignant transformations of thyroid glands, The FEBS Journal, 143 (1984) 133-144.

[51] A. Naitoh, Y. Aoyagi, H. Asakura, Highly enhanced fucosylation of serum glycoproteins in patients with hepatocellular carcinoma, Journal of gastroenterology and hepatology, 14 (1999) 436-445.

[52] Y.H. Ahn, P.M. Shin, N.R. Oh, G.W. Park, H. Kim, J.S. Yoo, A lectin-coupled, targeted proteomic mass spectrometry (MRM MS) platform for identification of multiple liver cancer biomarkers in human plasma, J. Proteomics, 75 (2012) 5507-5515.

[53] Y.H. Ahn, P.M. Shin, Y.S. Kim, N.R. Oh, E.S. Ji, K.H. Kim, Y.J. Lee, S.H. Kim, J.S. Yoo, Quantitative analysis of aberrant protein glycosylation in liver cancer plasma by AAL-enrichment and MRM mass spectrometry, Analyst, 138 (2013) 6454-6462.

[54] J.H. Lee, C.H. Cho, S.H. Kim, J.G. Kang, J.S. Yoo, C.L. Chang, J.-H. Ko, Y.-S. Kim, Semi-quantitative measurement of a specific glycoform using a DNA-tagged antibody and lectin affinity chromatography for glyco-biomarker development, Mol. Cel. Proteom., 14 (2015) 782-795.

[55] H. Toyoda, T. Kumada, T. Tada, Y. Kaneoka, A. Maeda, F. Kanke, S. Satomura, Clinical utility of highly sensitive Lens culinaris agglutinin‐reactive alpha‐fetoprotein in hepatocellular carcinoma patients with alpha‐fetoprotein< 20 ng / mL, Cancer Sci., 102 (2011) 1025-1031.

[56] X. Yi, S. Yu, Y. Bao, Alpha-fetoprotein-L3 in hepatocellular carcinoma: a meta-analysis, Clin. Chim. Acta, 425 (2013) 212-220.

[57] M.A. Comunale, M. Wang, J. Hafner, J. Krakover, L. Rodemich, B. Kopenhaver, R.E. Long, O. Junaidi, A.M.D. Bisceglie, T.M. Block, Identification and development of fucosylated glycoproteins as biomarkers of primary hepatocellular carcinoma, J. Proteome Res., 8 (2008) 595-602.

[58] Y. Liu, J. He, C. Li, R. Benitez, S. Fu, J. Marrero, D.M. Lubman, Identification and Confirmation of Biomarkers Using an Integrated Platform for Quantitative Analysis of Glycoproteins and Their Glycosylations, J. Proteome Res., 9 (2010) 798-805.

[59] L.F. Hoagland, M.J. Campa, E.B. Gottlin, J.E. Herndon, E.F. Patz, Haptoglobin and posttranslational glycan‐modified derivatives as serum biomarkers for the diagnosis of nonsmall cell lung cancer, Cancer, 110 (2007) 2260-2268.

[60] D. Wang, M. Hincapie, T. Rejtar, B.L. Karger, Ultrasensitive characterization of site-specific glycosylation of affinity-purified haptoglobin from lung cancer patient plasma using 10 μm id porous layer open tubular liquid chromatography- linear ion trap collision-induced dissociation / electron transfer dissociation mass spectrometry, Anal. Chem., 83 (2011) 2029-2037.

[61] H.Y. Tsai, K. Boonyapranai, S. Sriyam, C.J. Yu, S.W. Wu, K.H. Khoo, S. Phutrakul, S.T. Chen, Glycoproteomics analysis to identify a glycoform on haptoglobin associated with lung cancer, Proteomics, 11 (2011) 2162-2170.

[62] Arnold JN, Saldova R, Galligan MC, Murphy TB, Mimura-Kimura Y, Telford JE, Godwin AK, Rudd PM, Novel Glycan Biomarkers for the Detection of Lung Cancer, J. Proteome Res.

[63] Y. Hirao, H. Matsuzaki, J. Iwaki, A. Kuno, H. Kaji, T. Ohkura, A. Togayachi, M. Abe, M. Nomura, M. Noguchi, Glycoproteomics approach for identifying glycobiomarker candidate molecules for tissue type classification of non-small cell lung carcinoma (2014) 4705–4

[64] M. Ferens-Sieczkowska, EM Kratz, B. Kossowska, E. Passowicz-Muszynska, R. Jankowska, Comparison of Haptoglobin and Alpha(1)-Acid Glycoprotein Glycosylation in the Sera of Small Cell and Non-Small Cell Lung Cancer Patients, Postep. Hig. Med. Dosw., 67 (2013) 828–836.

[65] Y.Q. Liang, T.R. Ma, A. Thakur, H.J. Yu, L. Gao, P.Y. Shi, X.T. Li, H. Ren, L.Y. Jia, S. Zhang, Z. Li, M.W. Chen, Differentially expressed glycosylated patterns of alpha-1-antitrypsin as serum biomarkers for the diagnosis of lung cancer, Glycobiology, 25 (2015) 331-340.

[66] S.D. Shiayan, V.V. Nasonov, N.V. Bovin, L.I. Novikova, V.A. Aleshkin, A.G. Lutov, STUDIES OF N-LINKED OLIGOSACCHARIDE CHAINS OF ALPHA(1)-ACID GLYCOPROTEIN ISOLATED FROM ASCITIC FLUID OF STOMACH-CANCER PATIENTS AND NORMAL SERUM, Eksperimentalnaya Onkologiya, 15 (1993) 53-61.

[67] J. Bones, J.C. Byrne, N. O’Donoghue, C. McManus, C. Scaife, H. Boissin, A. Nastase, P.M. Rudd, Glycomic and glycoproteomic analysis of serum from patients with stomach cancer reveals potential markers arising from host defense response mechanisms, J. Proteome Res., 10 (2010) 1246-1265.

[68] S.H. Lee, S. Jeong, J. Lee, I.S. Yeo, M.J. Oh, U. Kim, S. Kim, S.H. Kim, S.Y. Park, J.H. Kim, S.H. Park, J.H. Kim, H.J. An, Glycomic profiling of targeted serum haptoglobin for gastric cancer using nano LC / MS and LC / MS / MS, Mol. Biosyst., 12 (2016) 3611-3621.

[69] L. Valmu, H. Alfthan, K. Hotakainen, S. Birken, U.H. Stenman, Site-specific glycan analysis of human chorionic gonadotropin beta-subunit from malignancies and pregnancy by liquid chromatography-electrospray mass spectrometry, Glycobiology, 16 (2006) 1207-1218.

[70] T. Kamoto, S. Satomura, T. Yoshiki, Y. Okada, F. Henmi, H. Nishiyama, T. Kobayashi, A. Terai, T. Habuchi, O. Ogawa, Lectin-reactive alpha-fetoprotein (AFP-L3%) curability and prediction of clinical course after treatment of non-seminomatous germ cell tumors, Jpn. J. Clin. Oncol., 32 (2002) 472-476.

[71] S. Ambrose, N. Gordon, J. Goldsmith, W. Wei, M. Zeegers, N. James, M. Knowles, R. Bryan, D. Ward, Use of Aleuria alantia Lectin Affinity Chromatography to Enrich Candidate Biomarkers from the Urine of Patients with Bladder Cancer, Proteomes, 3 (2015) 266.

[72] R. Azevedo, A. Peixoto, C. Gaiteiro, E. Fernandes, M. Neves, L. Lima, L.L. Santos, J.A. Ferreira, Over forty years of bladder cancer glycobiology: Where do glycans stand facing precision oncology?, Oncotarget, 8 (2017) 91734-91764.

[73] E. Pochec, A. Litynska, M. Bubka, A. Amoresano, A. Casbarra, Characterization of the oligosaccharide component of α 3 β 1 integrin from human bladder carcinoma cell line T24 and its role in adhesion and migration, European journal of cell biology, 85 (2006) 47-57.

[74] S. Cotton, R. Azevedo, C. Gaiteiro, D. Ferreira, L. Lima, A. Peixoto, E. Fernandes, M. Neves, D. Neves, T. Amaro, R. Cruz, A. Tavares, M. Rangel, A.M.N. Silva, L.L. Santos, J.A. Ferreira, Targeted O-glycoproteomics explored increased sialylation and identified MUC16 as a poor prognosis biomarker in advanced-stage bladder tumours, Mol. Oncol., 11 (2017) 895-912.

[75] N. Yang, S. Feng, K. Shedden, X.L. Xie, Y.S. Liu, C.J. Rosser, D.M. Lubman, S. Goodison, Urinary Glycoprotein Biomarker Discovery for Bladder Cancer Detection Using LC / MS-MS and Label-Free Quantification, Clin. Cancer Res., 17 (2011) 3349-3359.

[76] Yamashita K, Umetsu K, Suzuki T, Ohkura T (1992) Purification and characterization of a Neu5Ac alpha 2-->6Gal beta 1-->4GlcNAc and HSO3(-)-->6Gal beta 1-->GlcNAc specific lectin in tuberous roots of Trichosanthes japonica. Biochemistry 31 (46):11647-11650.

[77] Debray H, Montreuil J (1989) Aleuria aurantia agglutinin. A new isolation procedure and further study of its specificity various towards glycopeptides and oligosaccharides. Carbohydrate Research 185 (1):15-26.

[78] Kochibe N, Furukawa K (1980) Purification and properties of a novel fucose-specific hemagglutinin of Aleuria aurantia. Biochemistry 19 (13):2841-2846.

[0190] The present invention is also characterized by the following items. 1. An anti-glycoprotein antibody (e.g., an anti-PSA antibody, an anti-AFP antibody, an anti-MUC16 antibody, an anti-WFDC2 antibody, an anti-MUC1 antibody, an anti-ERBB2 antibody, an anti-CEACAM5 antibody, an anti-FUT3 antibody, or an anti-TG antibody, preferably an anti-PSA antibody), or an antigen-binding portion thereof (e.g., a single chain antibody fragment (scAb), scFv, Fab, diabody, DART, domain antibody, or nanobody) immobilized (e.g., conjugated) on a magnetic support (e.g., a magnetic particle, a magnetic bead, a metal nanoparticle or microparticle, a metal oxide nanoparticle or microparticle), wherein the magnetic support further comprises a polypeptide having peroxidase activity (e.g., a polypeptide having EC 1.11.1.7 enzymatic activity, such as microperoxidase-11), and preferably the antibody is selected from the group consisting of the antibodies listed in Table 1 herein. 2. An anti-glycoprotein antibody or an antigen-binding portion thereof according to any one of the preceding paragraphs, wherein the polypeptide having peroxidase activity has a molecular weight of less than 2 kDa (e.g., about 1.5 kDa or about 1.6 kDa or about 1.9 kDa), preferably a molecular weight of 1 kDa to 2 kDa. 3. An anti-glycoprotein antibody or antigen-binding portion thereof according to any one of the preceding clauses, wherein the polypeptide having peroxidase activity is immobilized (e.g. conjugated) on a magnetic carrier. 4. The anti-glycoprotein antibody, or an antigen-binding portion thereof, i) Prostate Specific Antigen (PSA), preferably SEQ ID NO: 1, 2, 3, 4, 5, or 6, more preferably SEQ ID NO: 6; ii) alpha-fetoprotein (AFP), preferably SEQ ID NO: 11 or 12, more preferably SEQ ID NO: 12; iii) Mucin-16 (MUC16), preferably SEQ ID NO: 13; iv) WAP4-disulfide core domain protein 2 (WFDC2), preferably SEQ ID NO: 14, 15, 16, 17, 18, or 19, more preferably SEQ ID NO: 19; v) Mucin-1 (MUC1), preferably SEQ ID NO: 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, or 37, more preferably SEQ ID NO: 37; vi) receptor tyrosine protein kinase erbB-2 (ERBB2), preferably SEQ ID NO: 38, 39, 40, 41, 42, 43, or 44, more preferably SEQ ID NO: 44; vii) carcinoembryonic antigen-related cell adhesion molecule 5 (CEACAM5), preferably SEQ ID NO: 45, 46, or 47, more preferably SEQ ID NO: 47; viii) galactoside 3(4)-L-fucosyltransferase (FUT3), preferably SEQ ID NO: 48; ix) thyroglobulin (TG), preferably SEQ ID NO: 49, 50, or 51; more preferably SEQ ID NO: 51; x) an anti-glycoprotein antibody or antigen-binding portion thereof described in any one of the preceding clauses, which specifically binds to a target polypeptide (e.g., a biomarker) comprising a polypeptide selected from the group consisting of any of the biomarkers described in Table 1 herein (e.g., a target glycoprotein comprises the polypeptide, e.g., an anti-glycoprotein antibody is raised against the polypeptide, e.g., an antigen glycoprotein comprises the polypeptide). 5. The anti-glycoprotein antibody, or antigen-binding portion thereof, according to any one of the preceding clauses, wherein the target polypeptide is prostate specific antigen (PSA) having peptidase activity (e.g. EC 3.4.21.77 enzymatic activity). 6. The anti-glycoprotein antibody or antigen-binding portion thereof is a polypeptide that is i) at least 60% or more (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) identical to the polypeptide sequence of SEQ ID NO:6, preferably the polypeptide has SEQ ID NO:6; ii) at least 60% or more (e.g., at least 65%, at least a polypeptide having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) identical to the polypeptide sequence of SEQ ID NO:1, preferably the polypeptide has SEQ ID NO:1; iii) a polypeptide having at least 60% or more (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, iv) a polypeptide that is at least 60% or more (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) identical to the polypeptide sequence of SEQ ID NO:3, preferably the polypeptide has SEQ ID NO:3; v) a polypeptide that is at least 60% or more (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) identical to the polypeptide sequence of SEQ ID NO:4, preferably the polypeptide has SEQ ID NO:4. vi) a polypeptide that is at least 60% or more (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) identical to the polypeptide sequence of SEQ ID NO:4, preferably the polypeptide has SEQ ID NO:4; vi) a polypeptide that is at least 60% or more (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%,The anti-glycoprotein antibody or antigen-binding portion thereof of any one of the preceding clauses specifically binds to a target polypeptide (e.g., PSA) comprising a polypeptide selected from the group consisting of a polypeptide that is at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the polypeptide of SEQ ID NO: 5, preferably wherein the polypeptide has SEQ ID NO: 5. 7. An anti-glycoprotein antibody or antigen-binding portion thereof according to any one of the preceding clauses, wherein the target polypeptide is human, rabbit, rat or mouse, preferably the target polypeptide is human. 8. The antibody or antigen-binding portion thereof according to any one of the preceding clauses, wherein the polypeptide having peroxidase activity comprises microperoxidase (MP) (e.g. microperoxidase-11), and / or horseradish peroxidase (HRP, e.g. peroxidase C1A having UniProtKB accession number P00433). 9. The antibody or antigen-binding portion thereof according to any one of the preceding clauses, wherein the microperoxidase (MP) is a heme comprising a peptide portion of cytochrome c (e.g., cytochrome c from Equus caballus, shown as SEQ ID NO: 10, NCBI Reference Sequence: NP_001157486.1) that retains peroxidase activity (e.g., EC 1.11.1.7 enzymatic activity, e.g., microperoxidase-11). 10. The antibody or antigen-binding portion thereof according to any one of the preceding clauses, wherein the heme containing cytochrome c peptide moiety is at least 60% or more (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) identical to a polypeptide sequence selected from the group consisting of SEQ ID NO:7 (MP-11 peptide), SEQ ID NO:8 (MP-9 peptide), and SEQ ID NO:9 (MP-8 peptide), and preferably the microperoxidase (MP) peptide is selected from the group consisting of SEQ ID NO:7 (MP-11 peptide), SEQ ID NO:8 (MP-9 peptide), and SEQ ID NO:9 (MP-8 peptide). 11. The antibody or antigen-binding portion thereof according to any one of the preceding clauses, wherein the magnetic carrier is a magnetic particle, a magnetic bead, a metal nanoparticle or a metal microparticle, a metal oxide nanoparticle or a metal oxide microparticle. 12. The anti-glycoprotein antibody or antigen-binding portion thereof according to any one of the preceding clauses, wherein the anti-glycoprotein antibody or antigen-binding portion thereof is capable of binding to the target polypeptide in a sample (e.g., a biomarker selected from the group consisting of PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3, TG, or a biomarker listed in Table 1 herein) and generating a detection signal (e.g., by optical means). 13. The anti-glycoprotein antibody or antigen-binding portion thereof according to any one of the preceding clauses, wherein the anti-glycoprotein antibody or antigen-binding portion thereof is capable of both binding to and concentrating the target polypeptide in a sample (e.g., a biomarker selected from the group consisting of PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3, TG, or a biomarker listed in Table 1 herein) and generating a detection signal (e.g., by optical means). 14. The anti-glycoprotein antibody or antigen-binding portion thereof according to any one of the preceding paragraphs, wherein the anti-glycoprotein antibody or antigen-binding portion thereof is capable of detecting a target polypeptide (e.g., a biomarker selected from the group consisting of PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3, TG, or a biomarker listed in Table 1 herein) in a sample (e.g., a serum sample) having a target polypeptide in an amount corresponding to 0.04 mL or less of undiluted biological sample (e.g., an undiluted serum sample), preferably in the range of 0.01 to 0.04 mL, more preferably in the range of 0.02 to 0.04 mL, and most preferably in the range of 0.02 to 0.04 mL. 15. An anti-glycoprotein antibody or antigen-binding portion thereof according to any one of the preceding clauses, wherein the anti-glycoprotein antibody is a monoclonal antibody. 16. An anti-glycoprotein antibody or antigen-binding portion thereof according to any one of the preceding clauses, wherein the anti-glycoprotein antibody is selected from the group consisting of a chimeric antibody, a humanized antibody, or a human antibody. 17.i) a magnetic support (e.g., magnetic particle, magnetic bead, metal nanoparticle or microparticle, metal oxide nanoparticle or microparticle) comprising an immobilized (e.g., conjugated) anti-glycoprotein antibody (e.g., a monoclonal antibody, a chimeric antibody, a humanized antibody, a human antibody, e.g., an antibody selected from the group consisting of an anti-PSA antibody, an anti-AFP antibody, an anti-MUC16 antibody, an anti-WFDC2 antibody, an anti-MUC1 antibody, an anti-ERBB2 antibody, an anti-CEACAM5 antibody, an anti-FUT3 antibody, an anti-TG antibody, or an antibody described in Table 1 herein), or an antigen-binding portion thereof (e.g., a single chain antibody fragment (scAb), scFv, Fab, diabody, DART, domain antibody, or nanobody); and ii) a polypeptide having peroxidase activity (e.g., EC 1.11.1.7 enzymatic activity, such as microperoxidase-11). 18. A magnetic carrier according to any one of the preceding paragraphs, wherein the polypeptide having peroxidase activity has a molecular weight of less than 2 kDa (e.g., about 1.5 kDa, about 1.6 kDa, or about 1.9 kDa), preferably a molecular weight of 1 kDa to 2 kDa. 19. A magnetic carrier according to any one of the preceding clauses, wherein the polypeptide having peroxidase activity is immobilized (eg, conjugated) onto the magnetic carrier. 20. The anti-glycoprotein antibody, or an antigen-binding portion thereof, i) Prostate Specific Antigen (PSA), preferably SEQ ID NO: 1, 2, 3, 4, 5, or 6, more preferably SEQ ID NO: 6; ii) alpha-fetoprotein (AFP), preferably SEQ ID NO: 11 or 12, more preferably SEQ ID NO: 12; iii) Mucin-16 (MUC16), preferably SEQ ID NO: 13; iv) WAP4-disulfide core domain protein 2 (WFDC2), preferably SEQ ID NO: 14, 15, 16, 17, 18, or 19, more preferably SEQ ID NO: 19; v) Mucin-1 (MUC1), preferably SEQ ID NO: 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, or 37, more preferably SEQ ID NO: 37; vi) receptor tyrosine protein kinase erbB-2 (ERBB2), preferably SEQ ID NO: 38, 39, 40, 41, 42, 43, or 44, more preferably SEQ ID NO: 44; vii) carcinoembryonic antigen-related cell adhesion molecule 5 (CEACAM5), preferably SEQ ID NO: 45, 46, or 47, more preferably SEQ ID NO: 47; viii) galactoside 3(4)-L-fucosyltransferase (FUT3), preferably SEQ ID NO: 48; ix) thyroglobulin (TG), preferably SEQ ID NO: 49, 50, or 51; more preferably SEQ ID NO: 51; x) any of the biomarkers described in Table 1 herein (e.g., a target glycoprotein comprises the polypeptide, e.g., an anti-glycoprotein antibody is raised against the polypeptide, e.g., an antigen glycoprotein comprises the polypeptide), the magnetic carrier described in any one of the preceding paragraphs specifically binding to a target polypeptide comprising a polypeptide selected from the group consisting of: any of the biomarkers described in Table 1 herein (e.g., a target glycoprotein comprises the polypeptide, e.g., an anti-glycoprotein antibody is raised against the polypeptide, e.g., an antigen glycoprotein comprises the polypeptide). 21. The magnetic carrier according to any one of the preceding clauses, wherein the target polypeptide is prostate-specific antigen (PSA) having peptidase activity (eg, EC 3.4.21.77 enzymatic activity). 22. The anti-glycoprotein antibody or antigen-binding portion thereof is a polypeptide that is i) at least 60% or more (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) identical to the polypeptide sequence of SEQ ID NO:6, preferably the polypeptide has SEQ ID NO:6; ii) at least 60% or more (e.g., at least 65%, at least iii) a polypeptide that is at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the polypeptide sequence of SEQ ID NO:1, preferably the polypeptide has SEQ ID NO:2; iii) a polypeptide that is at least 60% or more (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97% identical to the polypeptide sequence of SEQ ID NO:2; iv) a polypeptide that is at least 60% or more (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) identical to the polypeptide sequence of SEQ ID NO:3, preferably the polypeptide has SEQ ID NO:3; v) a polypeptide that is at least 60% or more (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) identical to the polypeptide sequence of SEQ ID NO:4, preferably the polypeptide has SEQ ID NO:4; vi) a polypeptide that is at least 60% or more (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) identical to the polypeptide sequence of SEQ ID NO:4, preferably the polypeptide has SEQ ID NO:4; vi) a polypeptide that is at least 60% or more (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%,The magnetic carrier according to any one of the preceding clauses, which specifically binds to a target polypeptide (e.g., PSA) comprising a polypeptide selected from the group consisting of a polypeptide that is at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identical to the target polypeptide (e.g., a target glycoprotein comprises the polypeptide, e.g., an anti-glycoprotein antibody is raised against the polypeptide, e.g., an antigen glycoprotein comprises the polypeptide), preferably having SEQ ID NO: 5. 23. A magnetic carrier according to any one of the preceding clauses, wherein the target polypeptide is human, rabbit, rat or mouse, preferably the glycoprotein is human. 24. A magnetic carrier according to any one of the preceding clauses, wherein the polypeptide having peroxidase activity comprises microperoxidase (MP) (e.g., microperoxidase-11) and / or horseradish peroxidase (HRP, e.g., peroxidase C1A having UniProtKB accession number P00433). 25. The magnetic carrier according to any one of the preceding clauses, wherein the microperoxidase (MP) is a heme containing a peptide portion of cytochrome c (e.g., cytochrome c from Equus caballus, shown as SEQ ID NO: 10, NCBI Reference Sequence: NP_001157486.1) that retains peroxidase activity (e.g., EC 1.11.1.7 enzyme activity, e.g., microperoxidase-11). 26. The magnetic carrier according to any one of the preceding clauses, wherein the heme containing peptide moiety of cytochrome c is at least 60% or more (e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) identical to a polypeptide sequence selected from the group consisting of SEQ ID NO:7 (MP-11 peptide), SEQ ID NO:8 (MP-9 peptide), and SEQ ID NO:9 (MP-8 peptide), and preferably, the microperoxidase (MP) peptide is selected from the group consisting of SEQ ID NO:7 (MP-11 peptide), SEQ ID NO:8 (MP-9 peptide), and SEQ ID NO:9 (MP-8 peptide). 27. The magnetic carrier according to any one of the preceding paragraphs, wherein the magnetic carrier is a magnetic particle, a magnetic bead, a metal nanoparticle or a metal microparticle, a metal oxide nanoparticle or a metal oxide microparticle. 28. A magnetic carrier according to any one of the preceding clauses, wherein the magnetic carrier is capable of binding to the target polypeptide in a sample (e.g., a biomarker selected from the group consisting of PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3, TG, or a biomarker listed in Table 1 herein) and generating a detection signal (e.g., by optical means). 29. A magnetic carrier according to any one of the preceding clauses, wherein the magnetic carrier is capable of both binding to and concentrating the target polypeptide in a sample (e.g., a biomarker selected from the group consisting of PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3, TG, or a biomarker listed in Table 1 herein) and generating a detection signal (e.g., by optical means). 30. The magnetic carrier according to any one of the preceding paragraphs, wherein the magnetic carrier is capable of detecting a target polypeptide (e.g., a biomarker selected from the group consisting of PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3, TG, or the biomarkers listed in Table 1 of the present specification) in a sample (e.g., a serum sample) having a target polypeptide in an amount corresponding to 0.04 mL or less of an undiluted biological sample (e.g., an undiluted serum sample), preferably in the range of 0.01 to 0.04 mL, more preferably in the range of 0.02 to 0.04 mL, and most preferably in the range of 0.02 to 0.04 mL. 31. The magnetic carrier according to any one of the preceding paragraphs, wherein the anti-glycoprotein antibody is a monoclonal antibody. 32. The magnetic carrier according to any one of the preceding paragraphs, wherein the anti-glycoprotein antibody is selected from the group consisting of a chimeric antibody, a humanized antibody, or a human antibody. 33. A method for producing an anti-glycoprotein antibody (e.g., an anti-glycoprotein antibody described in any one of the preceding paragraphs, e.g., an anti-PSA antibody, an anti-AFP antibody, an anti-MUC16 antibody, an anti-WFDC2 antibody, an anti-MUC1 antibody, an anti-ERBB2 antibody, an anti-CEACAM5 antibody, an anti-FUT3 antibody, an anti-TG antibody, or an antibody selected from the group of antibodies described in Table 1 herein), or an antigen-binding portion thereof (e.g., an antigen-binding portion described in any one of the preceding paragraphs), the method comprising: i) an anti-glycoprotein antibody (e.g., an anti-PSA antibody, an anti-AFP antibody, an anti-MUC16 antibody, an anti-WFDC2 antibody, an anti-MUC1 antibody, an anti-ERBB2 antibody, an anti-CEACAM5 antibody, an anti-FUT3 antibody, an anti-TG antibody, or an antibody selected from the group of antibodies described in Table 1 herein), or an antigen-binding portion thereof as described in any one of the preceding clauses; ii) a polypeptide having peroxidase activity as defined in any one of the preceding clauses. 34. A method for producing a magnetic carrier (e.g., a magnetic carrier described in any one of the above paragraphs), the method comprising: i) an anti-glycoprotein antibody (e.g., an anti-glycoprotein antibody described in any one of the preceding paragraphs, e.g., an anti-PSA antibody, an anti-AFP antibody, an anti-MUC16 antibody, an anti-WFDC2 antibody, an anti-MUC1 antibody, an anti-ERBB2 antibody, an anti-CEACAM5 antibody, an anti-FUT3 antibody, an anti-TG antibody, or an antibody selected from the group of antibodies described in Table 1 herein), or an antigen-binding portion thereof (e.g., an antigen-binding portion described in any one of the preceding paragraphs); ii) a polypeptide having peroxidase activity as defined in any one of the preceding clauses. 35.a)i) a magnetic carrier as described in any one of the preceding clauses, or an anti-glycoprotein antibody (e.g. an anti-PSA antibody, an anti-AFP antibody, an anti-MUC16 antibody, an anti-WFDC2 antibody, an anti-MUC1 antibody, an anti-ERBB2 antibody, an anti-CEACAM5 antibody, an anti-FUT3 antibody, an anti-TG antibody, or an antibody selected from the group of antibodies described in Table 1 herein), or an antigen-binding portion thereof as described in any one of the preceding clauses, ii) providing one or more lectins (e.g., lectins selected from the group of lectins listed in Table 1 herein), preferably the one or more lectins are selected from the group consisting of Maackia amurensis lectin II (MAA II), concanavalin A (Con A) lectin, Aleuria aurantia lectin (AAL), Sambucus nigra (SNA-I) lectin, Wisteria floribunda lectin (WFL), more preferably the one or more lectins include MAA II, most preferably the one or more lectins are two lectins including MAA II, and even more preferably the one or more lectins are selected from the group consisting of aa) AAL (preferably the method has a sensitivity of about 100% and / or the method has a specificity of about 81.3%), or bb) Con A lectin (Con B lectin (Con C lectin (Con D ... A) (preferably the method has a sensitivity of about 100% and / or the method has a specificity of about 93.8%), or cc) two lectins comprising MAA II in combination with SNA-I (preferably the method has a sensitivity of about 100% and / or the method has a specificity of about 93.8%), b) determining the amount, presence or absence of oligosaccharide chains (e.g., glycans) covalently bound to a target polypeptide (e.g., a biomarker) of said anti-glycoprotein antibody (e.g., a target polypeptide described in any one of the preceding paragraphs, e.g., PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3, TG, or a biomarker selected from the group of biomarkers described in Table 1 herein), preferably wherein said target polypeptide is PSA, more preferably wherein said determining comprises the use of a magnetic carrier, and / or an anti-glycoprotein antibody, and / or an antigen-binding portion thereof, and / or one or more lectins, and / or a composition, and / or a kit, e.g., a magnetic carrier, and / or an anti-glycoprotein antibody, and / or an antigen-binding portion thereof, and / or one or more lectins, and / or a composition, and / or a kit, e.g., a magnetic carrier, and / or an anti-glycoprotein antibody, and / or an antigen-binding portion thereof, and / or one or more lectins, and / or a composition, and / or a kit, as described in any one of the preceding or following paragraphs. 36. The method according to any one of the preceding clauses, wherein binding and detection (e.g., by optical means) of the target polypeptide (e.g., a biomarker selected from the group of biomarkers listed in Table 1 herein, e.g., PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3, TG, the group of biomarkers listed in Table 1 herein) are performed together, preferably the target polypeptide is PSA. 37. The method according to any one of the preceding clauses, wherein binding, enrichment and detection (e.g., by optical means) of the target polypeptide (e.g., PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3, TG, or a biomarker selected from the group of biomarkers listed in Table 1 herein) are performed together, preferably the target polypeptide is PSA. 38. The method comprises: i) selective capture and / or enrichment of a target polypeptide (e.g., a biomarker) according to any one of the preceding clauses (e.g., a biomarker selected from the group of biomarkers listed in Table 1 herein, such as PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3, TG, or any of the biomarkers listed in Table 1 herein), preferably wherein the target polypeptide is PSA; ii) selective capture and / or enrichment of a target polypeptide as described in any one of the preceding clauses (e.g. PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3, TG, or a biomarker selected from the group of biomarkers listed in Table 1 herein, preferably the target polypeptide is PSA), wherein the method for selective capture and / or enrichment comprises the use of one or more lectins (e.g. immobilized lectins), preferably the one or more lectins are immobilized at a sample location (e.g. an Enzyme-Linked Immunosorbent Assay (ELISA), Enzyme-Linked Lectin Assay (ELLA), or Magnetic Enzyme-Linked Lectin Assay (MELLA) microplate), iii) glycoprofiling of a target polypeptide (e.g., a biomarker) according to any one of the preceding clauses (e.g., a biomarker selected from the group of biomarkers listed in Table 1 herein, preferably the target polypeptide is PSA), iv) screening and / or analysis of oligosaccharide chains (e.g., glycans) covalently attached to a target polypeptide (e.g., a biomarker) according to any one of the preceding clauses (e.g., a biomarker selected from the group of biomarkers listed in Table 1 herein, preferably the target polypeptide is PSA), v) diagnosis of cancer (e.g., prostate cancer or a cancer selected from the group of cancers listed in Table 1 herein); vi) positive and / or negative prediction of cancer (e.g., prostate cancer or a cancer selected from the group of cancers listed in Table 1 herein); vii) determining the clinical stage of the cancer (e.g., prostate cancer or a cancer selected from the group of cancers listed in Table 1 herein); viii) distinguishing between prostate cancer and metastatic prostate cancer; ix) identification of prostate cancer that may metastasize (e.g., may metastasize to bone), preferably the cancer is selected from the group of cancers listed in Table 1 herein; x) distinguishing between benign prostatic hyperplasia (BPH) and prostate cancer; xi) prevention and / or treatment of cancer (e.g., prostate cancer or a cancer selected from the group of cancers listed in Table 1 herein); xii) differentiation of significant from non-significant tumors by glycoprotein-based (e.g., target polypeptide (e.g., biomarker)-based diagnosis of cancer (e.g., prostate cancer or a cancer selected from the group of cancers listed in Table 1 herein), e.g., based on a biomarker selected from the group of biomarkers listed in Table 1 herein, preferably the target polypeptide is PSA); xiii) differentiation of low-proliferative tumors (e.g., clinically harmless) from high-proliferative tumors (e.g., clinically relevant), for example by glycoprotein-based (e.g., target polypeptide (e.g., biomarker)-based, e.g., based on a biomarker selected from the group of biomarkers listed in Table 1 herein, e.g., PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3, TG, or the group of biomarkers listed in Table 1 herein, preferably the target polypeptide is PSA) diagnosis of cancer (e.g., prostate cancer or a cancer selected from the group of cancers listed in Table 1 herein); xiv) identification of organ-confined and / or potentially curable cancers (e.g., prostate cancer or a cancer selected from the group of cancers listed in Table 1 herein) by glycoprotein-based (e.g., target polypeptide (e.g., biomarker)-based diagnosis of cancer, e.g., based on a biomarker selected from the group of biomarkers listed in Table 1 herein, preferably the target polypeptide is PSA); xv) Compound screening. 39. The method is a method for screening a compound, the method comprising: c) iii) providing a cancer sample (e.g., a prostate cancer sample or a cancer sample selected from the group of cancers listed in Table 1 herein) with a test compound; d) contacting the prostate cancer sample with the test compound; and e) The method of any one of the preceding clauses, further comprising determining the likelihood of metastasis of the prostate cancer cells based on the amount, presence, or absence of determined oligosaccharide chains (e.g., glycans) covalently attached to a target polypeptide in the prostate cancer sample (e.g., a biomarker selected from the group of biomarkers described in any one of the preceding clauses, e.g., PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3, TG, or those described in Table 1 herein, preferably the target polypeptide is PSA) before and after contacting the prostate cancer sample with the test compound. 40. The method according to any one of the preceding clauses, wherein the method is i) for positive prediction of prostate cancer, and / or ii) for distinguishing between benign prostatic hyperplasia (BPH) and prostate cancer, wherein the one or more lectins comprise MAA II or WFL, preferably, the one or more lectins comprise MAA II. 41. The method according to any one of the preceding clauses, wherein the one or more lectins is MAA II and the sensitivity and / or specificity of the method is about 87.5%. 42. The method according to any one of the preceding clauses, wherein the one or more lectins are two lectins comprising: i) Con A (the method has a sensitivity of about 100% and / or the method has a specificity of about 93.8%), or ii) SNA-I (the method has a sensitivity of about 100% and / or the method has a specificity of about 93.8%), or iii) MAA II in combination with AAL (the method has a sensitivity of about 100% and / or the method has a specificity of about 81.3%). 43. The method according to any one of the preceding clauses, wherein the lectin is WFL and the sensitivity of the method is about 50% and / or the specificity of the method is about 75%. 44. The method according to any one of the preceding clauses, wherein the method is i) for negative prediction of prostate cancer, and / or ii) for distinguishing between benign prostatic hyperplasia (BPH) and prostate cancer, and the lectin is selected from the group consisting of Con A, AAL, and SNA-I. 45. The method according to any one of the preceding clauses, wherein the lectin is Con A and the sensitivity of the method is about 50% and / or the specificity of the method is about 75%. 46. ​​The method according to any one of the preceding clauses, wherein the lectin is AAL and the sensitivity of the method is about 50% and / or the specificity of the method is about 75%. 47. The method according to any one of the preceding clauses, wherein the lectin is SNA-I and the sensitivity of the method is about 57% and / or the specificity of the method is about 75%. 48. The method of any one of the preceding clauses, comprising determining a course of treatment based on the amount, presence, or absence of determined oligosaccharide chains (e.g., glycans) covalently attached to a target polypeptide of the anti-glycoprotein antibody (e.g., a target polypeptide described in any one of the preceding clauses, e.g., PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3, TG, or a biomarker selected from the group of biomarkers described in Table 1 herein, preferably the target polypeptide is PSA). 49. The method according to any one of the preceding clauses, wherein the method is for distinguishing between prostate cancer and metastatic prostate cancer in a sample (e.g., in a serum sample), and the one or more lectins are selected from the group consisting of AAL, Con A, MAA II, and SNA-I, preferably selected from the group consisting of AAL, Con A, and MAA II, and more preferably selected from the group consisting of AAL and Con A. 50. The method according to any one of the preceding clauses, wherein the method is performed on a sample. 51. The method according to any one of the preceding clauses, wherein the sample is selected from the group of urine, blood, serum, biopsy specimen, and post-operative tissue sample, preferably a serum sample. 52. A method for determining the glycosylation profile of a protein, comprising: (a) contacting a sample containing the protein with an antibody against the protein to form an antibody-protein complex; (b) isolating the antibody-protein complex obtained in step (a); and (c) contacting the antibody-protein complex with one or more lectins to determine the glycoprofile of the protein. 53. The method according to any one of the preceding clauses, wherein the antibody in step (a) is not immobilized, preferably not immobilized on a solid surface. 54. The method of any one of the preceding clauses, further comprising the step of (d) comparing the glycoprofile of the protein to a control glycoprofile of the protein (e.g., a glycoprofile of the protein under a condition not associated with a disease) to determine whether the glycoprofile of the protein may deviate from the glycoprofile of the control glycoprofile. 55. The method according to any one of the preceding clauses, wherein the protein is a cancer biomarker protein, an autoimmune disease biomarker protein, or an inflammatory disease biomarker protein, preferably the biomarker is selected from the group consisting of the biomarkers listed in Table 1 herein. 56. The method of any one of the preceding clauses, wherein the cancer biomarker protein is an ovarian cancer biomarker protein, a breast cancer biomarker protein, a colorectal cancer biomarker protein, a pancreatic cancer biomarker protein, a prostate cancer biomarker protein, a thyroid cancer biomarker protein, a liver cancer biomarker protein, a lung cancer biomarker protein, a gastric cancer biomarker protein, a testicular cancer biomarker protein, or a bladder cancer biomarker protein, preferably the biomarker is selected from the group consisting of the biomarkers listed in Table 1 herein. 57. Biomarker proteins for ovarian cancer include α1-acid glycoprotein (UniProtKB Accession Nos. P02763 and P19652), C1 esterase inhibitor (UniProtKB Accession Nos. P05155, P00736 and P09871), 2HS glycoprotein (UniProtKB Accession No. P02765), α1-antichymotrypsin (UniProtKB Accession No. P01011), α1-antitrypsin (UniProtKB Accession No. P01009), transferrin (UniProtKB Accession No. P02787), cancer antigen CA125 (CA16) (UniProtKB Accession No. Q8WXI7), and cancer antigen CA15-3 (MUC 1). (UniProtKB Accession No.: P15941), β-haptoglobin (UniProtKB Accession No.: P00738), human epididymis protein 4 (HE4)=WFDC2, hemopexin (UniProtKB Accession No.: P02790), clusterin (UniProtKB Accession No.: P10909), leucine-rich alpha-2-glycoprotein (UniProtKB Accession No.: P02750), or IgG (immunoglobulin G, antibody), preferably said biomarker is selected from the group consisting of the biomarkers listed in Table 1 herein. 58. The method according to any one of the preceding clauses, wherein the breast cancer biomarker protein is cancer antigen CA15-3, cancer antigen CA27.29 (MUC 1, epitope not CA 15-3) (UniProtKB Accession No: P15941), CEA (CEACAM5), Galectin 3 binding protein (UniProtKB Accession No: Q08380), or HER2 / neu (receptor tyrosine-protein kinase erbB-2) (UniProtKB Accession No: P04626), preferably the biomarker is selected from the group consisting of the biomarkers listed in Table 1 herein. 59. The method according to any one of the preceding clauses, wherein the colorectal cancer biomarker protein is β-haptoglobin, CA19-9 (epitope not MUC 1, CA 15-3 and CA 27.29) (UniProtKB Accession No: P15941), CEA (CEACAM5), complement C3 (UniProtKB Accession No: P01024), histidine-rich glycoprotein (UniProtKB Accession No: P04196), or kininogen-1 (UniProtKB Accession No: P01042), preferably the biomarker is selected from the group consisting of the biomarkers listed in Table 1 herein. 60. Pancreatic cancer biomarker proteins include α1-β-glycoprotein (UniProtKB Accession No.: P04217), β-2-glycoprotein 1 (UniProtKB Accession No.: P02749), hemopexin, antithrombin-III (UniProtKB Accession No.: P01008), β-haptoglobin, haptoglobin-associated protein (UniProtKB Accession No.: P00739), amyloid p-component (UniProtKB Accession No.: P02743), serum amyloid p-component = amyloid p-component, clusterin, plasma protease C1 inhibitor = C1 esterase inhibitor, α-1-antichymotrypsin, α-1-antitrypsin, thrombospondin-1 (UniProtKB Accession No.: P07996), MUC1, mucin 4 (CAM 17.1) (UniProtKB Accession No.: P02743). The method according to any one of the preceding clauses, wherein the biomarker is selected from the group consisting of the biomarkers listed in Table 1 herein, such as IL-16 (Accession No. Q99102), MUC5ac (UniProtKB Accession No. P98088), MUC16=CA125 (CA16), or kininogen-1, preferably the biomarker is selected from the group consisting of the biomarkers listed in Table 1 herein. 61. The method according to any one of the preceding clauses, wherein the prostate cancer biomarker protein is beta-haptoglobin, inhibitor of metalloprotease (TIMP-1) (UniProtKB Accession Number: P01033), PSA or tPSA (total or complexed PSA, complexed with alpha1-antichymotrypsin and alpha2-macroglobulin (UniProtKB Accession Number: P01023)), preferably the biomarker is selected from the group consisting of the biomarkers listed in Table 1 herein. 62. The method according to any one of the preceding clauses, wherein the thyroid cancer biomarker protein is thyroglobulin (TG), preferably said biomarker is selected from the group consisting of the biomarkers listed in Table 1 herein. 63. Liver cancer biomarker proteins are α-1-antitrypsin, α-1-antichymotrypsin, α-1-acid glycoprotein 1, and α-fetoprotein (AFP) (UniProtKB Item 11. The method according to any one of the preceding clauses, wherein the biomarker is selected from the group consisting of the biomarkers listed in Table 1 herein. 64. The method according to any one of the preceding clauses, wherein the lung cancer biomarker protein is β-haptoglobin, fibronectin (UniProtKB Accession Number: P02751), α1-acid glycoprotein, or α-1-antitrypsin, preferably the biomarker is selected from the group consisting of the biomarkers listed in Table 1 herein. 65. The method according to any one of the preceding clauses, wherein the gastric cancer biomarker is alpha 1-acid glycoprotein, beta-haptoglobin, or leucine-rich alpha-2-glycoprotein, preferably the biomarker is selected from the group consisting of the biomarkers listed in Table 1 herein. 66. The method according to any one of the preceding clauses, wherein the testicular cancer biomarker is alpha-fetoprotein-L3, or human chorionic gonadotropin-beta (UniProtKB Accession Number: P0DN86), preferably the biomarker is selected from the group consisting of the biomarkers listed in Table 1 herein. 67. The method according to any one of the preceding clauses, wherein the bladder cancer biomarker is MUC1, MUC16, alpha-1-antitrypsin, endoplasmin (UniProtKB Accession No. P14625), Golgi apparatus protein 1 (UniProtKB Accession No. Q92896), prostatic acid phosphatase (UniProtKB Accession No. P15309), Ig gamma-2 chain C region (UniProtKB Accession No. P01859), deoxyribonuclease-2-alpha (UniProtKB Accession No. O00115), or integrin (UniProtKB Accession Nos. P16144 and Q9UKX5), preferably the biomarker is selected from the group consisting of the biomarkers listed in Table 1 herein. 68. The method according to any one of the preceding clauses, wherein the autoimmune disease biomarker protein is IgG (Immunoglobulin G), preferably the biomarker is selected from the group consisting of the biomarkers listed in Table 1 herein. 69. The method according to any one of the preceding clauses, wherein the inflammatory disease biomarker protein is IgG (Immunoglobulin G), IgA (Immunoglobulin A), or C-reactive protein (CRP) (UniProtKB Accession Number: P02741), preferably the biomarker is selected from the group consisting of the biomarkers listed in Table 1 herein. 70. The method of any one of the preceding clauses, wherein the antibody is not directed against a glycan attached to the protein (eg, target polypeptide). 71. The method according to any one of the preceding clauses, wherein the antibody is an antibody or fragment thereof selected from the group consisting of a monoclonal antibody, a chimeric antibody, a humanized antibody, a human antibody, a scFv, a scAb, a Fab, a diabody, a DART, a domain antibody, or a nanobody. 72. The method of any one of the preceding clauses, wherein the antibody is an FN3 scaffold, an adnectin, an affibody, an anticalin, an avimer, a bicyclic peptide, a DARPin, a Kunitz domain, an obody, or an aptamer, such as a DNA, RNA or peptide aptamer. 73. The method according to any one of the preceding clauses, wherein the protein is not released from the antibody when the method is being performed. 74. The method according to any one of the preceding clauses, wherein the antibody comprises beads that allow isolation of the antibody. 75. The method according to any one of the preceding clauses, wherein the beads are agarose beads, latex beads, metal nanoparticles or microparticles, metal oxide nanoparticles or microparticles, or magnetic beads. 76. The method of any one of the preceding clauses, wherein the antibody comprises a detectable label. 77. The method according to any one of the preceding clauses, wherein the detectable label comprises a fluorophore, an enzyme, a radioisotope, a fluorescent protein, a fluorescent dye, or a tag. 78. The enzyme may be a peroxidase (e.g. having EC 1.11.1.7 activity), preferably microperoxidase 11 (MP-11), (MP-9) or (MP-8), alkaline phosphatase (from various sources, preferentially from bovine intestine (UniProtKB accession numbers: P09487 and P19111)), β-galactosidase (from various sources, preferentially from Escherichia coli (UniProtKB accession numbers: P00722, A7ZI91, B1J0T5, B7UJI9, B5Z2P7, Q8X685, A1A831, Q8FKG6, A7ZWZ1, B7N8Q1, B1LIM9, Q1RFJ2, Q0TKT1, Q8VNN2, and P06864), or luciferase (from various sources, preferentially from bovine intestine (UniProtKB Accession Number: P08659)). 79. The one or more lectins are selected from the group consisting of core fucose, antennary fucose, Fucα1-6GlcNAc-N-Asn-containing N-linked oligosaccharides, Fucα1-6 / 3GlcNAc, α-L-Fuc, Fucα1-2Galβ1-4(Fucα1-3)GlcNAc, Fucα1-2Gal, Fucα1-6GlcNAc, Manβ1-4GlcNAcβ1-4GlcNAc, branched N-linked hexasaccharides, Manα1-3Man, α-D-Man, (GlcNAcβ1-4) 2-4 , Galβ1-4GlcNAc, GlcNAcα1-4Galβ1-4GlcNAc, (GlcNAcβ1-4) 2-5, Neu5Ac, Galβ1-3GalNAc-serine / threonine, Galα1-3GalNAc, Galβ1-6Gal, Galβ1-4GlcNAc, Galβ1-3GalNAc, GalNAcα1-3GalNAc, GalNAcα1-3Gal, GalN Acα / β1-3 / 4Gal, α-GalNAc, GalNAcβ1-4Gal, GalNAcα1-3(Fucα1-2)Gal, GalNAcα1-2Gal, GalNAcα1-3GalNAc, GalNAcβ1-3 / 4Gal, GalNAc-Ser / Thr (Tn antigen), Galβ1-3GalNAc-Ser / Thr (T antigen), GalNAcβ1-4GlcNAc (LacdiNAc), α2,3Neu5Ac, α2,6Neu5Ac, α2,8Neu5Ac, sialic acid (α2,3Neu5Ac, α2,6Neu5Ac or α2,8Neu5Ac), Neu5Acα4 / 9-O-Ac-Neu5Ac, Neu5Acα2-3Galβ1-4Glc / GlcNAc, Neu5Acα2-6Gal / GalNAc, N-linked biantennary, N-linked triantennary, branched β1-6GlcNAc, Galα1-3(Fuc α1-2)Galβ1-3 / 4GlcNAc, Galβ1-3(Fucα1-4)GlcNAc, NeuAcα2-3Galβ1-3(Fucα1-4)GlcNAc, Fucα1-2Galβ1-3(Fucα1-4)GlcNAc, Galβ1-4(Fucα1-3)GlcNAc, NeuAcα2-3Galβ1-4(Fucα1-3)GlcNAc, Fucα1-2Galβ1-4(Fucα1-3)GlcNAc, high mannose, sialyl Lewis a Antigen (Sialyl Le a ), Cialis Lewis x Antigen (Sialyl Le x ), Lewis x Antigen (Le x ), sialyl Tn antigen, sialyl T antigen, Lewis y Antigen (Le y ), sulfated core 1 glycan, Tn antigen, T antigen, core 2 glycan, Lewis a Antigen (Le a ), (GlcNAcβ1-4) n, β-D-GlcNAc, GalNAc, Gal-GlcNAc, GlcNAc, Galα1-3Gal, Galβ1-3GalNAc, α-Gal, α-GalNAc, (GlcNAc) n , branched (LacNAc) n The method of any one of the preceding claims, wherein the method is specific for 80. The method according to any one of the preceding clauses, wherein the glycoprofile of PSA and / or tPSA is determined by lectins specific for α2-3Neu5Ac (α2-3 linked sialic acid), α2-6Neu5Ac (α2-6 linked sialic acid), core fucosylation, antennary fucose, biantennary glycans, high mannose glycans, 3 / 4 antennary glycans, LacdiNAc, GalNAc, and / or polysialic acid (Neu5Acα2-8Neu5Ac). 81. Increase in α2-3Neu5Ac (α2-3 linked sialic acid), Decreased α2-6Neu5Ac (α2-6 linked sialic acid), Reduction of core fucose, Increase in antenna-type fucose, Increased core fucose, Increased fucose, Reduction of biantennary glycans, Reduction of high mannose glycans, Increase in 3 / 4 antennary glycans, Increase in LacdiNAc, Increased GalNAc, and / or The presence of polysialic acid (Neu5Acα2-8Neu5Ac), is indicative of prostate cancer. 82. An increase in α2-3Neu5Ac (α2-3 linked sialic acid) as determined by Maackia amurensis agglutinin, anti-α2-3-linked Neu5Ac (α2-3 linked sialic acid) monoclonal antibody, Siglec-1, Siglec-4, or Siglec-8; The reduction of α2-6Neu5Ac (α2-6 linked sialic acid) was determined by Sambucus nigra agglutinin or Trichosanthes japonica agglutinin I. The reduction in core fucose was determined by Pholiota squarrosa lectin or Aspergillus oryzae agglutinin. The increase in antennary fucose was determined by Trichosanthes japonica agglutinin-II, Aleuria aurantia agglutinin, Ulex europaeus I agglutinin, Lens culinaris agglutinin, Pisum sativum agglutinin, Anguilla anguilla agglutinin, and Lotus tetragonolobus agglutinin. The reduction of biantennary glycans was determined by concanavalin A, Galanthus nivalis agglutinin, and Narcissus pseudonarcissus lectin. The reduction of high mannose glycans was determined by concanavalin A, Galanthus nivalis agglutinin, and Narcissus pseudonarcissus (daffodil) lectin. The increase in 2,3 / 4 antennary glycans was determined by Datura stramonium agglutinin, Phaseolus vulgaris hemagglutinin, or Phaseolus vulgaris leukoagglutinin. Increased LacdiNAc was determined by Wisteria floribunda agglutinin. The increase in GalNAc was determined by Wisteria floribunda agglutinin. The method according to any one of the preceding clauses, wherein the presence of polysialic acid (Neu5Acα2-8Neu5Ac) is determined by specific antibodies, Siglec-7, or Siglec-11. 83. A method for diagnosing that a subject may be at risk for or suffer from cancer, comprising: (a) contacting a sample obtained from the subject, the sample containing a cancer biomarker protein, with an antibody against the cancer biomarker protein to form an antibody-cancer biomarker protein complex; (b) isolating the antibody-protein complex obtained in step (a); and (c) contacting the antibody-cancer biomarker protein complex with one or more lectins to determine the glycoprofile of the cancer biomarker protein; A deviation of the glycan profile from a healthy glycan profile of the cancer biomarker protein indicates that the subject may be at risk of cancer or may be afflicted with cancer, preferably the biomarker is selected from the group consisting of the biomarkers set forth in Table 1 herein. 84. The method of any one of the preceding clauses, wherein the cancer biomarker protein is one of those described in any one of the preceding clauses, preferably the biomarker is selected from the group consisting of the biomarkers described in Table 1 herein. 85. A method for diagnosing that a subject may be at risk for or suffer from an autoimmune disease, comprising: (a) contacting a sample obtained from the subject, the sample including an autoimmune disease biomarker protein, with an antibody against the autoimmune disease biomarker protein to form an antibody-autoimmune disease biomarker protein complex; (b) isolating the antibody-protein complex obtained in step (a); and (c) contacting the antibody-autoimmune disease biomarker protein complex with one or more lectins to determine the glycoprofile of the autoimmune disease biomarker protein; A deviation of the glycan profile from a healthy glycan profile of the autoimmune disease biomarker protein indicates that the subject may be at risk for or suffer from an autoimmune disease, preferably the biomarker is selected from the group consisting of the biomarkers set forth in Table 1 herein. 86. The method of any one of the preceding clauses, wherein the autoimmune disease biomarker protein is described in any one of the preceding clauses, preferably the biomarker is selected from the group consisting of the biomarkers described in Table 1 herein. 87. A method for diagnosing that a subject may be at risk for or suffer from an inflammatory disease, comprising: (a) contacting a sample obtained from the subject, the sample including an inflammatory disease biomarker protein, with an antibody against the inflammatory disease biomarker protein to form an antibody-inflammatory disease biomarker protein complex; (b) isolating the antibody-protein complex obtained in step (a); and (c) contacting the antibody-inflammatory disease biomarker protein complex with one or more lectins to determine the glycoprofile of the inflammatory disease biomarker protein; A deviation of the glycan profile from a healthy glycan profile of the inflammatory disease biomarker protein indicates that the subject may be at risk for or suffer from an inflammatory disease, preferably the biomarker is selected from the group consisting of the biomarkers set forth in Table 1 herein. 88. The method of any one of the preceding clauses, wherein the inflammatory disease biomarker protein is described in any one of the preceding clauses, preferably the biomarker is selected from the group consisting of the biomarkers described in Table 1 herein. 89. The method of any one of the preceding clauses (e.g., relating to PSA and prostate cancer), wherein the glycoprofile of PSA is determined by lectins specific for α2-3Neu5Ac (α2-3 linked sialic acid), α2-6Neu5Ac (α2-6 linked sialic acid), core fucosylation, antennary fucose, biantennary glycans, high mannose glycans, 3 / 4 antennary glycans, LacdiNAc, GalNAc, and / or polysialic acid (Neu5Acα2-8Neu5Ac). 90. Increase in α2-3Neu5Ac (α2-3 linked sialic acid), Decreased α2-6Neu5Ac (α2-6 linked sialic acid), Reduction of core fucose, Increase in antenna-type fucose, Increased fucose, Reduction of biantennary glycans, Reduction of high mannose glycans, Increase in 3 / 4 antennary glycans, Increase in LacdiNAc, Increased GalNAc, and / or The presence of polysialic acid (Neu5Acα2-8Neu5Ac), The method of any one of the preceding clauses (e.g., relating to PSA and prostate cancer), wherein: is indicative of prostate cancer. 91. An increase in α2-3Neu5Ac (α2-3 linked sialic acid) as determined by Maackia amurensis agglutinin, anti-α2-3-linked Neu5Ac (α2-3 linked sialic acid) monoclonal antibodies, Siglec-1, Siglec-4, and / or Siglec-8; Reduction of α2-6Neu5Ac (α2-6 linked sialic acid) as determined by Sambucus nigra agglutinin and / or Trichosanthes japonica agglutinin I; The reduction in core fucose was determined by Pholiota squarrosa lectin and / or Aspergillus oryzae agglutinin, The increase in antennary fucose is determined by Trichosanthes japonica agglutinin-II, Aleuria aurantia agglutinin, Ulex europaeus I agglutinin, Lens culinaris agglutinin, Pisum sativum agglutinin, Anguilla anguilla agglutinin, and / or Lotus tetragonolobus agglutinin; The reduction of biantennary glycans was determined by concanavalin A, Galanthus nivalis agglutinin, and Narcissus pseudonarcissus lectin. The reduction of high mannose glycans was determined by concanavalin A, Galanthus nivalis agglutinin, and Narcissus pseudonarcissus (daffodil) lectin. The increase in 2,3 / 4 antennary glycans was determined by Datura stramonium agglutinin, Phaseolus vulgaris hemagglutinin, and / or Phaseolus vulgaris leukoagglutinin. Increased LacdiNAc was determined by Wisteria floribunda agglutinin. The increase in GalNAc is determined by Wisteria floribunda agglutinin, and / or The method of any one of the preceding clauses (e.g., relating to PSA and prostate cancer), wherein the presence of polysialic acid (Neu5Acα2-8Neu5Ac) is determined by specific antibodies, Siglec-7, and / or Siglec-11. 92. The glycan profile of β-haptoglobin is characterized by α2-6Neu5Ac (α2-6-linked sialic acid), core fucosylation, antennary fucose, 3 / 4 antennary glycans, and Lewis a Sugar chain and / or sialyl Lewis x The method of any one of the preceding claims (e.g., for β-haptoglobin and prostate cancer), determined by a lectin specific for a glycan. 93. Increase in α2-6Neu5Ac (α2-6 linked sialic acid), Increased core fucosylation, Increase in antenna-type fucose, Increase in 3 / 4 antennary glycans, Cialis Lewis a Increased glycosylation, and / or Cialis Lewis x Increased glycan The method of any one of the preceding clauses (e.g., regarding β-haptoglobin and prostate cancer), wherein: is indicative of prostate cancer. 94. Increased α2-6Neu5Ac (α2-6 linked sialic acid) as determined by Sambucus nigra prostate and / or Trichosanthes japonica agglutinin I; Increased core fucosylation was determined by Pholiota squarrosa lectin and / or Aspergillus oryzae agglutinin, the increase in antennary fucose is determined by Aleuria aurantia agglutinin, Trichosanthes japonica agglutinin-II, Ulex europaeus I agglutinin, Lens culinaris agglutinin, Pisum sativum agglutinin, Anguilla anguilla agglutinin, and / or Lotus tetragonolobus agglutinin; an increase in 3 / 4 antennary glycans as determined by Phaseolus vulgaris leukoagglutinin, Datura stramonium agglutinin, and / or Phaseolus vulgaris erythrocyte agglutinin; and / or Cialis Lewis a Sugar chain or sialyl Lewis x Increased glycan activity is associated with anti-sialyl Lewis a Carbohydrate antibody, anti-sialyl Lewis x The method of any one of the preceding clauses (e.g., relating to β-haptoglobin and prostate cancer), as determined by glycoantibodies, Sambucus nigra agglutinin, Trichosanthes japonica agglutinin I, Maackia amurensis agglutinin, anti-α2-3-linked Neu5Ac (α2-3 linked sialic acid) monoclonal antibodies, Siglec 1, Siglec 4, and / or Siglec 8. 95. The method of any one of the preceding clauses (eg, relating to TIMP1 and prostate cancer), wherein the glycosylation profile of TIMP1 is determined by a lectin specific for α1-3 / 6 fucose. 96. The method of any one of the preceding clauses (e.g., relating to TIMP1 and prostate cancer), wherein an increase in alpha 1-3 / 6 fucose is indicative of prostate cancer. 97. The method of any one of the preceding clauses (e.g., relating to TIMP1 and prostate cancer), wherein the increase in α1-3 / 6 fucose is determined by AOL, PhoSL, TJA II, UEA-I, LCA, PSL, AAA, and / or LTA. 98. The glycan profile of α1-acid glycoprotein is characterized by 3 / 4 antennary glycans, core fucosylation, α2-6Neu5Ac (α2-6 linked sialic acid), and sialyl Lewis. xThe method of any one of the preceding clauses (e.g., relating to alpha 1-acid glycoprotein and ovarian cancer), as determined by a lectin specific for glycans and / or alpha 2-3Neu5Ac (alpha 2-3 linked sialic acid). Increase in 99.3 / 4 antenna-type glycans, Increased core fucosylation, Increased α2-6Neu5Ac (α2-6 linked sialic acid), Cialis Lewis x Increased glycosylation, and / or Decreased α2-3Neu5Ac (α2-3 linked sialic acid), The method of any one of the preceding clauses (e.g., relating to alpha 1-acid glycoprotein and ovarian cancer), wherein: is indicative of ovarian cancer. The increase in 100.3 / 4 antennary glycans was determined by PHA-1, PHA-E, and / or DSA; Increased core fucosylation is determined by PhoSL and / or AOL, Increase in α2-6Neu5Ac (α2-6 linked sialic acid) as determined by TJA-I and / or SNA; Cialis Lewis a Increased glycan activity is associated with sLe x , SNA, TJA-I, MAA, anti-α2-3-linked Neu5Ac (α2-3-linked sialic acid) antibodies (e.g., HYB4), Siglec-1, Siglec-4, and / or Siglec-8, and / or The method of any one of the preceding clauses (e.g., relating to alpha 1-acid glycoprotein and ovarian cancer), wherein the reduction in alpha 2-3Neu5Ac (alpha 2-3 linked sialic acid) is determined by MAA, anti-alpha 2-3-linked Neu5Ac (alpha 2-3 linked sialic acid) antibodies (e.g., HYB4), Siglec 1, Siglec 4, and / or Siglec 8. 101.The glycan profile of C1 esterase inhibitors is x and / or the method of any one of the preceding paragraphs (e.g., relating to C1 esterase inhibitor and ovarian cancer), as determined by a lectin specific for triantennary glycans. 102. Le xand / or Increase in triantennary glycans, The method of any one of the preceding clauses (e.g., regarding C1 esterase inhibitor and ovarian cancer), wherein: is indicative of ovarian cancer. 103. Le x The increase in Le x and / or as determined by LTA and / or The method of any one of the preceding clauses (e.g., regarding C1 esterase inhibitor and ovarian cancer), wherein the increase in triantennary glycans is determined by DBA, PHA-E, and / or PHA-L. The method of any one of the preceding clauses (e.g., relating to 2-HS glycoprotein and ovarian cancer), wherein the glycan profile of the 104.2-HS glycoprotein is determined by a lectin specific for 3-4 antennary glycans. The method of any one of the preceding clauses (e.g., relating to 2-HS glycoprotein and ovarian cancer), wherein an increase in 105.3-4 antennary glycans is indicative of ovarian cancer. The method of any one of the preceding clauses (e.g., relating to 2-HS glycoprotein and ovarian cancer), wherein the increase in 106.3 / 4 antennary glycans is determined by DBA, PHA-E, and / or PHA-L. 107. The glycan profile of β-haptoglobin is characterized by 3, 4 antennary glycans, Le x , Sialyl Le x The method of any one of the preceding clauses (e.g., relating to β-haptoglobin and ovarian cancer), wherein the level of α2-3Neu5Ac (α2-3 linked sialic acid), α2-6Neu5Ac (α2-6 linked sialic acid), antennary fucose, and / or biantennary glycans is determined by a lectin specific for α2-3Neu5Ac (α2-3 linked sialic acid), α2-6Neu5Ac (α2-6 linked sialic acid), antennary fucose, and / or biantennary glycans. Increase in 108.3 / 4 antennary glycans, Le x Increase in Sialyl Le x Increase in Increased α2-6Neu5Ac (α2-6 linked sialic acid), Decreased α2-3Neu5Ac (α2-3 linked sialic acid), Increased α2-3Neu5Ac (α2-3 linked sialic acid), Decreased α2-6Neu5Ac (α2-6 linked sialic acid), Increase in antennary fucose, and / or Reduction of biantennary glycans, The method of any one of the preceding clauses (e.g., regarding β-haptoglobin and ovarian cancer), wherein: is indicative of ovarian cancer. The increase in 109.3 / 4 antennary glycans is determined by DBA, PHA-E, and / or PHA-L, Le x The increase in Le x and / or LTA, Sialyl Le x The increase in sLe x antibodies against α2-3-linked Neu5Ac (α2-3-linked sialic acid) antibodies (e.g., HYB4), Siglec-1, Siglec-4, and / or Siglec-8; Increase in α2-6Neu5Ac (α2-6 linked sialic acid) as determined by SNA and / or TJA-I; the reduction in α2-3Neu5Ac is determined by MAA, anti-α2-3-linked Neu5Ac (α2-3 linked sialic acid) antibodies (e.g., HYB4), Siglec-1, Siglec-4, and / or Siglec-8; Reduction of α2-6Neu5Ac (α2-6 linked sialic acid) as determined by SNA and / or TJA-I; The increase in antennary fucose is determined by TJA II, AAL, UEA-I, LCA, PSL, AAA, and / or AAL; The reduction of biantennary glycans is determined by Con A and / or GNA, and / or The method of any one of the preceding clauses (e.g., relating to β-haptoglobin and ovarian cancer), wherein the increase in α2-3Neu5Ac (α2-3 linked sialic acid) is determined by MAA, anti-α2-3-linked Neu5Ac (α2-3 linked sialic acid) antibodies (e.g., HYB4), Siglec-1, Siglec-4, and / or Siglec-8. 110. The glycan profile of α-1-antitrypsin is characterized by 4-antennary glycans, Le x The method of any one of the preceding clauses (e.g., with respect to alpha-1-antitrypsin and ovarian cancer), wherein the presence of glycan specificity is determined by a lectin specific for triantennary glycans, alpha 2-3Neu5Ac (alpha 2-3 linked sialic acid), alpha 2-6Neu5Ac (alpha 2-6 linked sialic acid), core fucose, and / or biantennary glycans. Increase in 111.4 antenna-type glycans, Le x Increase in Reduction of 3,4-antennary glycans Decreased α2-3Neu5Ac (α2-3 linked sialic acid), Increased α2-6Neu5Ac (α2-6 linked sialic acid), Increased core fucose, and / or Increase in biantennary glycans, The method of any one of the preceding clauses (e.g., regarding alpha-1-antitrypsin and ovarian cancer), wherein: is indicative of ovarian cancer. The increase in 112.4 antennary glycans is determined by DBA, PHA-E, and / or PHA-L; Le x The increase in Le x and / or LTA, The reduction in tri- and tetraantennary glycans was determined by DBA, PHA-E, and / or PHA-L. a reduction in α2-3Neu5Ac (α2-3 linked sialic acid) as determined by MAA, anti-α2-3-linked Neu5Ac (α2-3 linked sialic acid) antibodies (e.g., HYB4), Siglec-1, Siglec-4, and / or Siglec-8; Increase in α2-6Neu5Ac (α2-6 linked sialic acid) as determined by SNA and / or TJA-I; The increase in core fucose is determined by AOL and / or PhoSL, and / or The method of any one of the preceding clauses, wherein the increase in biantennary glycans is determined by Con A, NPA, and / or GNA (e.g., for alpha-1-antitrypsin and ovarian cancer). 113. The glycan profile of α-1-antichymotrypsin is characterized by tetraantennary glycans, Le x , Sialyl Le x The method of any one of the preceding clauses (e.g., with respect to alpha-1-antichymotrypsin and ovarian cancer), wherein the level of sialic acid is determined by a lectin specific for alpha 2-6Neu5Ac (alpha 2-6 linked sialic acid), and / or alpha 2-3Neu5Ac (alpha 2-3 linked sialic acid). Increase in 114.4 antenna-type glycans, Le x Increase in Sialyl Le x Increase in Increased α2-6Neu5Ac (α2-6 linked sialic acid), and / or Decreased α2-3Neu5Ac (α2-3 linked sialic acid), The method of any one of the preceding clauses (e.g., regarding alpha-1-antichymotrypsin and ovarian cancer), wherein: is indicative of ovarian cancer. The increase in 115.4 antennary glycans is determined by DBA, PHA-E, and / or PHA-L; Le x The increase in Le x and / or LTA, Sialyl Le x The increase in sLe x antibodies against, SNA, TJA-I, MAA, anti-α2-3-linked Neu5Ac (α2-3-linked sialic acid) antibodies (e.g., HYB4), Siglec-1, Siglec-4, or Siglec-8; an increase in α2-6Neu5Ac (α2-6 linked sialic acid) as determined by SNA and / or TJA-I; and / or The method of any one of the preceding clauses (e.g., relating to alpha-1-antichymotrypsin and ovarian cancer), wherein the reduction in 2-3Neu5Ac (alpha 2-3 linked sialic acid) is determined by MAA, anti-alpha 2-3-linked Neu5Ac (alpha 2-3 linked sialic acid) antibodies (e.g., HYB4), Siglec 1, Siglec 4, and / or Siglec 8. 116. The method of any one of the preceding clauses (e.g., relating to transferrin and ovarian cancer), wherein the glycoprofile of transferrin is determined by a lectin specific for triantennary glycans. The method of any one of the preceding clauses (e.g., relating to transferrin and ovarian cancer), wherein a decrease in 117.3 antennary glycans is indicative of ovarian cancer. The method of any one of the preceding clauses (e.g., regarding transferrin and ovarian cancer), wherein the reduction in 118.3 antennary glycans is determined by DBA, PHA-E, and / or PHA-L. 119. The glycan profile of hemopexin is x The method of any one of the preceding claims (e.g., with respect to hemopexin and ovarian cancer), wherein the cancer is determined by a lectin specific for hemopexin. 120. Le x The method of any one of the preceding clauses (e.g., regarding hemopexin and ovarian cancer), wherein an increase in is indicative of ovarian cancer. 121. Le x The increase in Le x The method of any one of the preceding clauses (e.g., with respect to hemopexin and ovarian cancer), as determined by antibodies to and / or LTA. 122. The method according to any one of the preceding clauses (e.g., for IgG and ovarian cancer), wherein the glycoprofile of IgG is determined by a lectin specific for galactose and / or sialic acid. 123. Reduction of galactose, and / or Reduction of sialic acid, The method of any one of the preceding clauses (e.g., regarding IgG and ovarian cancer), wherein: is indicative of ovarian cancer. 124. The reduction of galactose is determined by RCA, RCA120, ABA, Jacalin (DSA), AlloA, ECL and / or PNA, and / or The method of any one of the preceding clauses (e.g., for IgG and ovarian cancer), wherein the reduction in sialic acid is measured by SNA, TJA-I, MAA, anti-α2-3-linked Neu5Ac (sialic acid) antibodies (e.g., HYB4), Siglec-1, Siglec-4, or Siglec-8. 125. The method of any one of the preceding clauses (e.g., relating to CA125 (MUC16) and ovarian cancer), wherein the glycoprofile of CA125 (MUC16) is determined by a lectin specific for the sialyl-Tn antigen and / or the sialyl-T antigen. 126. Increased sialyl-Tn antigen, and / or Increased sialyl T antigen The method of any one of the preceding clauses (e.g., relating to CA125 (MUC16) and ovarian cancer), wherein: is indicative of ovarian cancer. 127. An increase in sialyl-Tn antigen is determined by VVA lectin, SNA, TJA-I, MAA, anti-α2-3 linked Neu5Ac (α2-3 linked sialic acid) antibodies (e.g., HYB4), Siglec-1, Siglec-4, or Siglec-8 after sialidase treatment, and / or The method of any one of the preceding clauses (e.g., for CA125 (MUC16) and ovarian cancer), wherein the increase in sialyl T antigen is determined by anti-carbohydrate IgM antibody 3C9, SNA, TJA-I, MAA, anti-α2-3-linked Neu5Ac (α2-3 linked sialic acid) antibodies (e.g., HYB4), Siglec 1, Siglec 4, and / or Siglec 8 following sialidase detection. 128. The method of any one of the preceding clauses (e.g., relating to CA15-3 (MUC1) and ovarian cancer), wherein the glycoprofile of CA15-3 (MUC1) is determined by lectins specific for sialyl-Tn antigen, core fucose, biantennary glycans, 3 / 4 antennary glycans, and / or antennary fucose. 129. Increased sialyl-Tn antigen Increased core fucose, Increase in biantennary glycans, Reduction in 3 / 4 antennary glycans, and / or Increase in antenna-type fucose, The method of any one of the preceding clauses (e.g., relating to CA15-3 (MUC1) and ovarian cancer), wherein: is indicative of ovarian cancer. 130. Increase in sialyl-Tn antigen is determined by VVA lectin, SNA, TJA-I, MAA, anti-α2-3 linked Neu5Ac (α2-3 linked sialic acid) antibodies (e.g., HYB4), Siglec-1, Siglec-4, or Siglec-8 after detection of sialidase; The increase in core fucose is determined by PhoSL and / or AOL, The increase in biantennary glycans was determined by Con A. The reduction in 3 / 4 antennary glycans is determined by PHA-E, PHA-L and / or DBA, and / or The method of any one of the preceding clauses (e.g., for CA15-3 (MUC1) and ovarian cancer), wherein the increase in antennary fucose is determined by AAL, TJA II, AAL, UEA-I, LCA, PSL, AAA, and / or LTA. 131.The glycan profile of human epididymis protein 4 (HE4) was y The method of any one of the preceding clauses, as determined by a lectin specific for the antigen (e.g., for human epididymis protein 4 (HE4) and ovarian cancer). 132. Le y The method of any one of the preceding clauses, wherein an increase in the antigen is indicative of ovarian cancer (e.g., relating to human epididymis protein 4 (HE4) and ovarian cancer). 133. Le y The increase in antigens is y The method of any one of the preceding claims (e.g., relating to human epididymis protein 4 (HE4) and ovarian cancer) as determined by antibodies against glycans and / or UEA-I. 134. The method of any one of the preceding clauses (eg, relating to clusterin and ovarian cancer), wherein the glycoprofile of clusterin is determined by a lectin specific for α2-6Neu5Ac (α2-6 linked sialic acid). 135. The method of any one of the preceding clauses (eg, relating to clusterin and ovarian cancer), wherein an increase in α2-6Neu5Ac (α2-6 linked sialic acid) is indicative of ovarian cancer. 136. The method according to any one of the preceding clauses (e.g., relating to clusterin and ovarian cancer), wherein the increase in α2-6Neu5Ac (α2-6 linked sialic acid) is determined by SNA and / or TJA-I. 137. The method according to any one of the preceding clauses (e.g., relating to leucine-rich alpha-2-glycoprotein and ovarian cancer), wherein the glycan profile of the leucine-rich alpha-2-glycoprotein is determined by a lectin specific for alpha2-6Neu5Ac (alpha2-6-linked sialic acid). 138. The method of any one of the preceding clauses (e.g., relating to leucine-rich alpha-2-glycoprotein and ovarian cancer), wherein an increase in alpha2-6Neu5Ac (alpha2-6 linked sialic acid) is indicative of ovarian cancer. 139. The method according to any one of the preceding clauses (e.g., relating to leucine-rich alpha-2-glycoprotein and ovarian cancer), wherein an increase in alpha2-6Neu5Ac (alpha2-6 linked sialic acid) is determined by SNA and / or TJA-I. 140. The method of any one of the preceding clauses (e.g., relating to CA15-3 (MUC1) and breast cancer), wherein the glycoprofile of CA15-3 (MUC1) is determined by lectins specific for sulfated core 1 glycans, Tn, sialyl Tn antigen, sialyl T, T antigen, α2-8Neu5Ac (α2-8 linked sialic acid), sialylation, and / or core 2 glycans. 141. Increase in sulfated core 1 glycans Increase in Tn or sialyl-Tn antigens, the presence of sialyl T or T antigen; The presence of α2-8Neu5Ac (α2-8 linked sialic acid), the presence of sialic acid addition, and / or Presence of core 2 glycans, The method of any one of the preceding clauses (e.g., relating to CA15-3 (MUC1) and breast cancer), wherein: is indicative of breast cancer. 142. Increased sulfated core 1 glycans as determined by galectin 4, SBA, ABA, VVA, Jacalin (DSA), BPL, PNA, GSL1, and / or SJA; an increase in Tn or sialyl-Tn antigen is determined by SBA, DBA, VVA, SNA, SNA, TJA-I, MAA, and / or anti-α2-3-linked Neu5Ac (α2-3-linked sialic acid) antibody (e.g., HYB4); the presence of sialyl-Tn or T antigen is determined by SNA, TJA-I, MAA, anti-α2-3-linked Neu5Ac (α2-3 linked sialic acid) antibodies (e.g., HYB4), Siglec-1, Siglec-4, or Siglec-8, SBA, ABA, VVA, BPL, Jacalin, and / or PNA; the presence of α2-8Neu5Ac (α2-8 linked sialic acid) is determined by antibodies against poly(sialic acid), Siglec 7, and / or Siglec 11; The presence of sialylation is determined by SNA, TJA-I, TVA, MAA, anti-α2-3-linked Neu5Ac (α2-3 linked sialic acid) antibodies (e.g., HYB4), Siglec-1, Siglec-4, and / or Siglec-8, and / or The method of any one of the preceding clauses (e.g., for CA15-3 (MUC1) and breast cancer), wherein the presence of core 2 glycan is determined by RCA, RCA120, ABA, Jacalin (DSA), PNA, and / or WGA. 143. The method according to any one of the preceding clauses (eg, relating to CA27.29 and breast cancer), wherein the glycoprofile of CA27.29 is determined by a lectin specific for sialylation. 144. The method of any one of the preceding clauses (e.g., relating to CA27.29 and breast cancer), wherein the presence of sialylation is indicative of breast cancer. 145. The method of any one of the preceding clauses (e.g., relating to CA27.29 and breast cancer), wherein the presence of sialylation is determined by SNA, TJA-I, MAA, anti-α2-3-linked Neu5Ac (α2-3 linked sialic acid) antibodies (e.g., HYB4), Siglec-1, Siglec-4, and / or Siglec-8. 146. The method according to any one of the preceding clauses (eg, relating to HER2 and breast cancer), wherein the glycoprofile of HER2 is determined by a lectin specific for antennary fucose and / or sialylation. 147. Presence of antennary fucose, and / or the presence of sialic acid The method of any one of the preceding clauses (e.g., relating to HER2 and breast cancer), wherein: is indicative of breast cancer. 148. The presence of antennary fucose is determined by UEA, TJA II, AAL, LCA, PSL, AAA, and / or LTA, and / or The method of any one of the preceding clauses (e.g., relating to HER2 and breast cancer), wherein the presence of sialylation is determined by SNA, TJA-I, TVA, MAA, anti-α2-3-linked Neu5Ac (α2-3 linked sialic acid) antibodies (e.g., HYB4), Siglec-1, Siglec-4, and / or Siglec-8. 149. The method according to any one of the preceding clauses (eg, relating to CEA and breast cancer), wherein the glycoprofile of CEA is determined by a lectin specific for tri-, tetra-antennary glycans. 150. The method of any one of the preceding clauses (eg, relating to CEA and breast cancer), wherein the presence of 3, 4 antennary glycans is indicative of breast cancer. 151. The method of any one of the preceding clauses (e.g., relating to CEA and breast cancer), wherein the presence of 3,4 antennary glycans is determined by PHA-E, PHA-L, and / or DBA. 152. The glycan profile of β-haptoglobin is characterized by antennary fucose, biantennary glycan, antennary / core fucose, and dimeric Le. a on Le a The method of any one of the preceding clauses (e.g., relating to β-haptoglobin and colorectal cancer), wherein the IL-10 level is determined by a lectin specific for Gal-β-4-GlcNAc, and / or Gal-β-4-GlcNAc. 153. Increase in antenna-type fucose, Increase in biantennary glycans, Increase in antennary / core fucose, Dimer Le a on Le a and / or Increase in Gal-β1-4-GlcNAc The method of any one of the preceding clauses (e.g., relating to β-haptoglobin and colorectal cancer), wherein: is indicative of colorectal cancer. 154. An increase in antennary fucose is determined by AAL, TJA II, UEA-I, LCA, PSL, AAA, and / or LTA; The increase in biantennary glycans was determined by PHA-E, Con A, PHA-L, and / or DBA. The increase in antennary / core fucose is determined by AAL, AOL, LTA, TJA II, UEA-I, LCA, PSL, AAA, and / or PhoSL; Dimer Le a on Le a The increase in is determined by the mouse monoclonal antibody NCC-ST-421, and / or The method of any one of the preceding clauses (e.g., regarding β-haptoglobin and colorectal cancer), wherein the increase in Gal-β1-4-GlcNAc is determined by galectin 3, ECA, and / or AlloA. 155. The glycosylation profile of carcinoembryonic antigen (CEA) was x, Le y The method of any one of the preceding clauses (e.g., relating to carcinoembryonic antigen (CEA) and colorectal cancer), as determined by lectins specific for α2-3Neu5Ac (α2-3 linked sialic acid), α-D-Man, 3,4 antennary glycans, mannose, fucose, terminal GalNAc, and / or Gal-β1-4-GlcNAc. 156. Le x Increase in Le y Increase in Increased α2-3Neu5Ac (α2-3 linked sialic acid), Increased α-D-Man, Increase in 3- and 4-antennary glycans, Increased mannose and fucose, Reduction of terminal GalNAc, and / or Increase in Gal-β1-4-GlcNAc The method of any one of the preceding clauses (e.g., regarding carcinoembryonic antigen (CEA) and colorectal cancer), wherein: is indicative of colorectal cancer. 157. Le x Increase in LTA and / or sialyl Lewis acid x It is determined by antibodies against glycans. Le y Increase in UEA-I and / or sialyl Lewis y It is determined by antibodies against glycans. an increase in α2-3Neu5Ac (α2-3 linked sialic acid) as determined by MAA, anti-α2-3-linked Neu5Ac (α2-3 linked sialic acid) antibodies (e.g., HYB4), Siglec-1, Siglec-4, or Siglec-8; Increases in α-D-Man were determined by NPA, Con A, and / or GNA. The increase in tri- and tetraantennary glycans is determined by PHA-L, PHA-E, and / or DBA; Increases in mannose and fucose are determined by DC-SIGN, NPA, Con A, GNA, AAL, TJA II, UEA-I, LCA, PSL, AAA, LTA, AOL, and / or PhoSL; The reduction in terminal GalNAc is determined by MGBL, DBA, SBA, VVA, HPA, and / or WFA, and / or The method of any one of the preceding clauses (e.g., with respect to carcinoembryonic antigen (CEA) and colorectal cancer), wherein the increase in Gal-β1-4-GlcNAc is determined by galectin-3. 158. The method of any one of the preceding clauses (e.g., relating to CA 19-9 (MUC1) and colorectal cancer), wherein the glycoprofile of CA19-9 (MUC1) is determined by lectins specific for T antigen, Galβ-1,3GalNAc, antennary fucose, α2-3Neu5Ac (α2-3 linked sialic acid), α2-6Neu5Ac (α2-6 linked sialic acid), 3, 4 branched antennary, and / or terminal GalNAc. 159. Increased T antigen Increase in Galβ1-3GalNAc Increase in antenna-type fucose, Increased α2-3Neu5Ac (α2-3 linked sialic acid), Increased α2-6Neu5Ac (α2-6 linked sialic acid), Reduction of 3- and 4-antennary branching, and / or Increase in terminal GalNAc, The method of any one of the preceding clauses (e.g., relating to CA 19-9 (MUC1) and colorectal cancer), wherein: is indicative of colorectal cancer. 160. The increase in T antigen is determined by SBA and / or ABA, The increase in Galβ1-3GalNAc was determined by PNA, ABA, and / or Jacalin. The increase in antennary fucose is determined by UEA, TJA II, AAL, LCA, PSL, AAA, and / or LTA; an increase in α2-3Neu5Ac (α2-3 linked sialic acid) as determined by MAA, anti-α2-3-linked Neu5Ac (α2-3 linked sialic acid) antibodies (e.g., HYB4), Siglec-1, Siglec-4, or Siglec-8; Increase in α2-6Neu5Ac (α2-6 linked sialic acid) as determined by SNA and / or TJA-I; Reduction in 3 / 4 antenna branching as determined by PHA-E, PHA-L and / or DBA; and / or The method of any one of the preceding clauses (e.g., with respect to CA 19-9 (MUC1) and colorectal cancer), wherein the increase in terminal GalNAc is determined by MGBL, DBA, SBA, HPA, and / or WFA. 161. The method according to any one of the preceding clauses (e.g., relating to complement C3 (UniProtKB: P01024) and colorectal cancer), wherein the glycoprofile of complement C3 (UniProtKB: P01024) is determined by lectins specific for antennary fucose, Galβ1-3GalNAc, α2-3Neu5Ac (α2-3 linked sialic acid), and / or α2-6Neu5Ac (α2-6 linked sialic acid). 162. Increase in antenna-type fucose, Increase in Galβ1-3GalNAc Increased α2-3Neu5Ac (α2-3 linked sialic acid), and / or Increased α2-6Neu5Ac (α2-6 linked sialic acid), The method of any one of the preceding clauses (e.g., relating to complement C3 (UniProtKB: P01024) and colorectal cancer), wherein: is indicative of colorectal cancer. 163. An increase in antennary fucose is determined by AAL, TJA II, UEA-I, LCA, PSL, AAA, and / or LTA; The increase in Galβ1-3GalNAc was determined by PNA, ABA, and / or Jacalin. an increase in α2-3Neu5Ac (α2-3 linked sialic acid) as determined by MAA, anti-α2-3-linked Neu5Ac (α2-3 linked sialic acid) antibodies (e.g., HYB4), Siglec-1, Siglec-4, or Siglec-8; and / or The method of any one of the preceding clauses (e.g., with respect to complement C3 (UniProtKB: P01024) and colorectal cancer), wherein the increase in α2-6Neu5Ac (α2-6 linked sialic acid) is determined by SNA and / or TJA-I. 164. The method according to any one of the preceding clauses (e.g., relating to kininogen-I (UniProtKB: P01042) and colorectal cancer), wherein the glycoprofile of kininogen-I (UniProtKB: P01042) is determined by lectins specific for high mannose, antennary fucose, Galβ1-3GalNAc, α2-3Neu5Ac (α2-3 linked sialic acid), and / or α2-6Neu5Ac (α2-6 linked sialic acid). 165. Increased mannose, Increase in antenna-type fucose, Increase in Galβ1-3GalNAc Increased α2-3Neu5Ac (α2-3 linked sialic acid), and / or Increased α2-6Neu5Ac (α2-6 linked sialic acid), The method of any one of the preceding clauses (e.g., relating to kininogen-I (UniProtKB: P01042) and colorectal cancer), wherein: is indicative of colorectal cancer. 166. Increase in high mannose is determined by Con A, NPA, and / or GNA. The increase in antennary fucose is determined by AAL, TJA II, UEA-I, LCA, PSL, AAA, and / or LTA; The increase in Galβ1-3GalNAc was determined by PNA, ABA, and / or Jacalin. an increase in α2-3Neu5Ac (α2-3 linked sialic acid) as determined by MAA, anti-α2-3-linked Neu5Ac (α2-3 linked sialic acid) antibodies (e.g., HYB4), Siglec-1, Siglec-4, and / or Siglec-8; and / or The method of any one of the preceding clauses (e.g., with respect to kininogen-I (UniProtKB: P01042) and colorectal cancer), wherein the increase in α2-6Neu5Ac (α2-6 linked sialic acid) is determined by SNA and / or TJA-I. 167. The method according to any one of the preceding clauses (e.g., relating to histidine-rich glycoproteins (UniProtKB: P04196) and colorectal cancer), wherein the glycan profile of histidine-rich glycoproteins (UniProtKB: P04196) is determined by a lectin specific for antennary fucose and / or α2-6Neu5Ac (α2-6 linked sialic acid). 168. Increase in antennary fucose, and / or Increased α2-6Neu5Ac (α2-6 linked sialic acid), The method of any one of the preceding clauses (e.g., relating to histidine-rich glycoprotein (UniProtKB: P04196) and colorectal cancer), wherein: is indicative of colorectal cancer. 169. An increase in antennary fucose is determined by TJA II, AAL, UEA-I, LCA, PSL, AAA, and / or LTA, and / or The method of any one of the preceding clauses (e.g., relating to histidine-rich glycoproteins (UniProtKB: P04196) and colorectal cancer), wherein the increase in α2-6Neu5Ac (α2-6 linked sialic acid) is determined by SNA and / or TJA-I. 170. The method according to any one of the preceding clauses (eg, relating to α1-β-glycoprotein and pancreatic cancer), wherein the glycan profile of α1-β-glycoprotein is determined by a lectin specific for Neu5Ac. 171. The method of any one of the preceding clauses (e.g., relating to α1-β-glycoprotein and pancreatic cancer), wherein an increase in Neu5Ac is indicative of pancreatic cancer. 172. The method of any one of the preceding clauses (e.g., relating to α1-β-glycoprotein and pancreatic cancer), wherein the increase in Neu5Ac is determined by SNA, TJA-I, anti-α2-3-linked Neu5Ac (α2-3-linked sialic acid) antibodies (e.g., HYB4), Siglec-1, Siglec-4, and / or Siglec-8. 173. The method according to any one of the preceding clauses (eg, relating to α-amyloid p-component and pancreatic cancer), wherein the glycoprofile of the amyloid p-component is determined by a lectin specific for Neu5Ac. 174. The method of any one of the preceding clauses (eg, relating to alpha amyloid p-component and pancreatic cancer), wherein an increase in Neu5Ac is indicative of pancreatic cancer. 175. The method of any one of the preceding clauses (e.g., relating to alpha amyloid p-component and pancreatic cancer), wherein the increase in Neu5Ac is determined by SNA, TJA-I, anti-alpha 2-3-linked Neu5Ac (alpha 2-3 linked sialic acid) antibodies (e.g., HYB4), Siglec 1, Siglec 4, and / or Siglec 8. 176. The method of any one of the preceding clauses (e.g., relating to β-2-glycoprotein 1 (UniProtKB: P02749) and pancreatic cancer), wherein the glycan profile of β-2-glycoprotein 1 (UniProtKB: P02749) is determined by lectins specific for antennary fucose, α2-3Neu5Ac (α2-3 linked sialic acid), α2-6Neu5Ac (α2-6 linked sialic acid), high mannose, and / or Galβ-1,3GalNAc. 177. Increase in antenna-type fucose, Increased α2-3Neu5Ac (α2-3 linked sialic acid), Increased α2-6Neu5Ac (α2-6 linked sialic acid), Increased high mannose, and / or Increase in Galβ1-3GalNAc The method of any one of the preceding clauses (e.g., relating to beta-2-glycoprotein 1 (UniProtKB: P02749) and pancreatic cancer), wherein: is indicative of pancreatic cancer. 178. An increase in antennary fucose is determined by AAL, TJA II, UEA-I, LCA, PSL, AAA, and / or LTA; an increase in α2-3Neu5Ac (α2-3 linked sialic acid) as determined by MAA, anti-α2-3-linked Neu5Ac (α2-3 linked sialic acid) antibodies (e.g., HYB4), Siglec-1, Siglec-4, or Siglec-8; Increase in α2-6Neu5Ac (α2-6 linked sialic acid) as determined by SNA and / or TJA-I; The increase in high mannose is determined by Con A, NPA, and / or GNA, and / or The method of any one of the preceding clauses (e.g., relating to beta-2-glycoprotein 1 (UniProtKB: P02749) and pancreatic cancer), wherein the increase in Galβ-1,3GalNA is determined by PNA, ABA, and / or jacalin. 179. The method of any one of the preceding clauses (e.g., relating to hemopexin (UniProtKB: P02790) and pancreatic cancer), wherein the glycoprofile of hemopexin (UniProtKB: P02790) is determined by lectins specific for antennary fucose, α2-3Neu5Ac (α2-3 linked sialic acid), α2-6Neu5Ac (α2-6 linked sialic acid), and / or high mannose. 180. Increase in antenna-type fucose, Increased α2-3Neu5Ac (α2-3 linked sialic acid), Increased α2-6Neu5Ac (α2-6 linked sialic acid), and / or Increased high mannose, The method of any one of the preceding clauses (e.g., relating to hemopexin (UniProtKB: P02790) and pancreatic cancer), wherein: is indicative of pancreatic cancer. 181. An increase in antennary fucose is determined by AAL, TJA II, UEA-I, LCA, PSL, AAA, and / or LTA; an increase in α2-3Neu5Ac (α2-3 linked sialic acid) as determined by MAA, anti-α2-3-linked Neu5Ac (α2-3 linked sialic acid) antibodies (e.g., HYB4), Siglec-1, Siglec-4, or Siglec-8; an increase in α2-6Neu5Ac (α2-6 linked sialic acid) as determined by SNA and / or TJA-I; and / or The method of any one of the preceding clauses (e.g., with respect to hemopexin (UniProtKB: P02790) and pancreatic cancer), wherein the increase in high mannose is determined by Con A, NPA, and / or GNA. 182. The method of any one of the preceding clauses (e.g., relating to haptoglobin-associated protein (UniProtKB: P00739) and pancreatic cancer), wherein the glycoprofile of haptoglobin-associated protein (UniProtKB: P00739) is determined by lectins specific for antennary fucose, α2-3Neu5Ac (α2-3 linked sialic acid), α2-6Neu5Ac (α2-6 linked sialic acid), high mannose, and / or Galβ-1,3GalNAc. 183. Increase in antenna-type fucose, Increased α2-3Neu5Ac (α2-3 linked sialic acid), Increased α2-6Neu5Ac (α2-6 linked sialic acid), Increased high mannose, and / or Increase in Galβ1-3GalNAc The method of any one of the preceding clauses (e.g., relating to haptoglobin-related protein (UniProtKB: P00739) and pancreatic cancer), wherein: is indicative of pancreatic cancer. 184. An increase in antennary fucose is determined by AAL, TJA II, UEA-I, LCA, PSL, AAA, and / or LTA; an increase in α2-3Neu5Ac (α2-3 linked sialic acid) as determined by MAA, anti-α2-3-linked Neu5Ac (α2-3 linked sialic acid) antibodies (e.g., HYB4), Siglec-1, Siglec-4, or Siglec-8; Increase in α2-6Neu5Ac (α2-6 linked sialic acid) as determined by SNA and / or TJA-I; The increase in high mannose is determined by Con A, NPA, and / or GNA, and / or The method of any one of the preceding clauses (e.g., relating to haptoglobin-related protein (UniProtKB: P00739) and pancreatic cancer), wherein the increase in Galβ1-3GalNAc is determined by PNA, ABA, and / or jacalin. 185. The method according to any one of the preceding clauses (e.g., relating to serum amyloid p-component (UniProtKB: P02743) and pancreatic cancer), wherein the glycoprofile of serum amyloid p-component (UniProtKB: P02743) is determined by lectins specific for antennary fucose, α2-3Neu5Ac (α2-3 linked sialic acid), α2-6Neu5Ac (α2-6 linked sialic acid), high mannose, and / or Galβ-1-3GalNAc. 186. Increase in antenna-type fucose, Increased α2-3Neu5Ac (α2-3 linked sialic acid), Increased α2-6Neu5Ac (α2-6 linked sialic acid), Increased high mannose, and / or Increase in Galβ1-3GalNAc The method of any one of the preceding clauses (e.g., relating to serum amyloid p-component (UniProtKB: P02743) and pancreatic cancer), wherein: is indicative of pancreatic cancer. 187. An increase in antennary fucose is determined by AAL, TJA II, UEA-I, LCA, PSL, AAA, and / or LTA; an increase in α2-3Neu5Ac (α2-3 linked sialic acid) as determined by MAA, anti-α2-3-linked Neu5Ac (α2-3 linked sialic acid) antibodies (e.g., HYB4), Siglec-1, Siglec-4, or Siglec-8; Increase in α2-6Neu5Ac (α2-6 linked sialic acid) as determined by SNA and / or TJA-I; The increase in high mannose is determined by Con A, NPA, and / or GNA, and / or The method of any one of the preceding clauses (e.g., for serum amyloid p-component (UniProtKB: P02743) and pancreatic cancer), wherein the increase in Galβ-1,3GalNA is determined by PNA, ABA, and / or DSA. 188. The method of any one of the preceding clauses (e.g., relating to clusterin (UniProtKB: P10909) and pancreatic cancer), wherein the glycoprofile of clusterin (UniProtKB: P10909) is determined by lectins specific for antennary fucose, α2-3Neu5Ac (α2-3 linked sialic acid), α2-6Neu5Ac (α2-6 linked sialic acid), and / or Galβ1-3GalNAc. 189. Increase in antenna-type fucose, Increased α2-3Neu5Ac (α2-3 linked sialic acid), Increased α2-6Neu5Ac (α2-6 linked sialic acid), and / or Increase in Galβ1-3GalNAc The method of any one of the preceding clauses (e.g., relating to clusterin (UniProtKB: P10909) and pancreatic cancer), wherein: is indicative of pancreatic cancer. 190. An increase in antennary fucose is determined by AAL, TJA II, UEA-I, LCA, PSL, AAA, and / or LTA; an increase in α2-3Neu5Ac (α2-3 linked sialic acid) as determined by MAA, anti-α2-3-linked Neu5Ac (α2-3 linked sialic acid) antibodies (e.g., HYB4), Siglec-1, Siglec-4, or Siglec-8; an increase in α2-6Neu5Ac (α2-6 linked sialic acid) as determined by SNA and / or TJA-I; and / or The method of any one of the preceding clauses (e.g., relating to clusterin (UniProtKB: P10909) and pancreatic cancer), wherein the increase in Galβ1-3GalNAc is determined by PNA, ABA, and / or jacalin. 191. The method according to any one of the preceding clauses (e.g., relating to antithrombin-III (UniProtKB: P01008) and pancreatic cancer), wherein the glycoprofile of antithrombin-III (UniProtKB: P01008) is determined by lectins specific for antennary fucose, α2-3Neu5Ac (α2-3 linked sialic acid), α2-6Neu5Ac (α2-6 linked sialic acid), high mannose, and / or Galβ-1-3GalNAc. 192. Increase in antenna-type fucose, Increased α2-3Neu5Ac (α2-3 linked sialic acid), Increased α2-6Neu5Ac (α2-6 linked sialic acid), Increased high mannose, and / or Increase in Galβ1-3GalNAc The method of any one of the preceding clauses (e.g., relating to antithrombin-III (UniProtKB: P01008) and pancreatic cancer), wherein: is indicative of pancreatic cancer. 193. An increase in antennary fucose is determined by AAL, TJA II, UEA-I, LCA, PSL, AAA, and / or LTA; an increase in α2-3Neu5Ac (α2-3 linked sialic acid) as determined by MAA, anti-α2-3-linked Neu5Ac (α2-3 linked sialic acid) antibodies (e.g., HYB4), Siglec-1, Siglec-4, or Siglec-8; Increase in α2-6Neu5Ac (α2-6 linked sialic acid) as determined by SNA and / or TJA-I; The increase in high mannose is determined by Con A, NPA, and / or GNA, and / or The method of any one of the preceding clauses (e.g., relating to antithrombin-III (UniProtKB: P01008) and pancreatic cancer), wherein the increase in Galβ1-3GalNAc is determined by PNA, ABA, and / or Jacalin (DSA). 194. The method according to any one of the preceding clauses (e.g., relating to kininogen-I (UniProtKB: P01042) and pancreatic cancer), wherein the glycoprofile of kininogen-I (UniProtKB: P01042) is determined by lectins specific for antennary fucose, α2-3Neu5Ac (α2-3 linked sialic acid), α2-6Neu5Ac (α2-6 linked sialic acid), high mannose, and / or Galβ-1-3GalNAc. 195. Increase in antenna-type fucose, Increased α2-3Neu5Ac (α2-3 linked sialic acid), Increased α2-6Neu5Ac (α2-6 linked sialic acid), Increased high mannose, and / or Increase in Galβ1-3GalNAc The method of any one of the preceding clauses (e.g., relating to kininogen-I (UniProtKB: P01042) and pancreatic cancer), wherein: is indicative of pancreatic cancer. 196. An increase in antennary fucose is determined by AAL, TJA II, UEA-I, LCA, PSL, AAA, and / or LTA; an increase in α2-3Neu5Ac (α2-3 linked sialic acid) as determined by MAA, anti-α2-3-linked Neu5Ac (α2-3 linked sialic acid) antibodies (e.g., HYB4), Siglec-1, Siglec-4, or Siglec-8; Increase in α2-6Neu5Ac (α2-6 linked sialic acid) as determined by SNA and / or TJA-I; The increase in high mannose is determined by Con A, NPA, and / or GNA, and / or The method of any one of the preceding clauses (e.g., relating to kininogen-I (UniProtKB: P01042) and pancreatic cancer), wherein the increase in Galβ1-3GalNAc is determined by PNA, ABA, and / or Jacalin (DSA). 197. The method according to any one of the preceding clauses (e.g., relating to Plasma Protease C1 Inhibitor (UniProtKB:P05155) and pancreatic cancer), wherein the glycan profile of Plasma Protease C1 Inhibitor (UniProtKB:P05155) is determined by a lectin specific for α2-6Neu5Ac (α2-6 linked sialic acid). 198. The method of any one of the preceding clauses, wherein an increase in α2-6Neu5Ac (α2-6 linked sialic acid) is indicative of pancreatic cancer (e.g., plasma protease C1 inhibitor (UniProtKB: P05155 and pancreatic cancer). 199. The method according to any one of the preceding clauses, wherein the increase in α2-6Neu5Ac (α2-6 linked sialic acid) is determined by SNA and / or TJA-I (e.g., plasma protease C1 inhibitor (UniProtKB: P05155 and for pancreatic cancer). 200. The method according to any one of the preceding clauses (eg, relating to β-haptoglobin and pancreatic cancer), wherein the glycan profile of β-haptoglobin is determined by a lectin specific for antennary fucose and / or core fucose. 201. Increase in antenna-type fucose, and / or Increased core fucose, The method of any one of the preceding clauses (e.g., regarding β-haptoglobin and pancreatic cancer), wherein is indicative of pancreatic cancer. 202. An increase in antennary fucose is determined by AAL, TJA II, UEA-I, LCA, PSL, AAA, and / or LTA, and / or The method of any one of the preceding clauses (e.g., relating to β-haptoglobin and pancreatic cancer), wherein the increase in core fucose is determined by AOL and / or PhoSL. 203. The method according to any one of the preceding clauses (eg, relating to α-1-antichymotrypsin and pancreatic cancer), wherein the glycan profile of α-1-antichymotrypsin is determined by a lectin specific for antenna-type fucose. 204. The method of any one of the preceding clauses (e.g., relating to alpha-1-antichymotrypsin and pancreatic cancer), wherein an increase in antennary fucose is indicative of pancreatic cancer. 205. The method of any one of the preceding clauses (e.g., relating to alpha-1-antichymotrypsin and pancreatic cancer), wherein the increase in antennary fucose is determined by AAL, TJA II, UEA-I, LCA, PSL, AAA, and / or LTA. 206. The method of any one of the preceding clauses (eg, relating to thrombospondin-1 and pancreatic cancer), wherein the glycoprofile of thrombospondin-1 is determined by a lectin specific for antennary fucose. 207. The method of any one of the preceding clauses (e.g., relating to thrombospondin-1 and pancreatic cancer), wherein an increase in antennary fucose is indicative of pancreatic cancer. 208. The method of any one of the preceding clauses (e.g., relating to thrombospondin-1 and pancreatic cancer), wherein the increase in antennary fucose is determined by AAL, TJA II, UEA-I, LCA, PSL, AAA, and / or LTA. 209. The method according to any one of the preceding clauses (eg, relating to alpha-1-antitrypsin and pancreatic cancer), wherein the glycan profile of alpha-1-antitrypsin is determined by a lectin specific for antennary fucose. 210. The method of any one of the preceding clauses (e.g., relating to alpha-1-antitrypsin and pancreatic cancer), wherein an increase in antennary fucose is indicative of pancreatic cancer. 211. The method of any one of the preceding clauses (e.g., relating to alpha-1-antitrypsin and pancreatic cancer), wherein the increase in antennary fucose is determined by AAL, TJA II, UEA-I, LCA, PSL, AAA, and / or LTA. 212. The method according to any one of the preceding clauses (e.g., relating to mucin (CAM 17.1) and pancreatic cancer), wherein the glycan profile of mucin (CAM 17.1) is determined by a lectin specific for β-D-GlcNAc and / or Neu5Ac. 213. The method of any one of the preceding clauses (e.g., relating to mucin (CAM 17.1) and pancreatic cancer), wherein an increase in β-D-GlcNAc and / or Neu5Ac is indicative of pancreatic cancer. 214. The method of any one of the preceding clauses (e.g., relating to mucin (CAM 17.1) and pancreatic cancer), wherein the increase in β-D-GlcNAc and / or Neu5Ac is determined by DSA, LEL, WGA, SNA, and / or TJA-I. 215. The method of any one of the preceding clauses (e.g., relating to MUC16 and pancreatic cancer), wherein the glycoprofile of MUC16 is determined by lectins specific for antennary fucose, T antigen, Gal-GlcNAc, GalNAc, GlcNAc and / or mannose. 216. Increase in antenna-type fucose, Decrease in T antigens, Loss of Gal-GlcNAc GalNAc depletion, Decreased GlcNAc, and / or Mannose reduction, The method of any one of the preceding clauses (e.g., regarding MUC16 and pancreatic cancer), wherein: is indicative of pancreatic cancer. 217. An increase in antennary fucose is determined by AAL, TJA II, UEA-I, LCA, PSL, AAA, and / or LTA; The reduction in T antigen is determined by BPL, Jacalin (DSA), PNA, SBA, VVA, ABA, GSL1, and / or SJA; The reduction in Gal-GlcNAc is determined by ECL, PHA-L, PHA-E, AlloA, and / or ECA; GalNA reduction is determined by DBA, GSL1, SBA, VVL, SJA, ABA, BPL, and / or PNA; The reduction in GlcNAc is determined by GSL2, STL, DSA, LEL, and / or WGA, and / or The reduction in mannose is determined by Con A, GNA, and / or NPA, and / or the method of any one of the preceding clauses (e.g., regarding MUC16 and pancreatic cancer). 218. The method of any one of the preceding clauses (e.g., relating to MUC5ac and pancreatic cancer), wherein the glycoprofile of MUC5ac is determined by lectins specific for T antigen, antennary fucose, Gal-GlcNAc, GalNAc, and / or GlcNAc. 219. Increased T antigen Increase in antenna-type fucose, Loss of Gal-GlcNAc GalNAc depletion, and / or GlcNAc Depletion The method of any one of the preceding clauses (e.g., regarding MUC5ac and pancreatic cancer), wherein: is indicative of pancreatic cancer. 220. Increase in T antigen is determined by Jacalin (DSA), SBA, ABA, VVA, BPL, PNA, GSL1, and / or SJA; The increase in antennary fucose is determined by TJA II, AAL, UEA-I, LCA, PSL, AAA, and / or LTA; The reduction in Gal-GlcNAc is determined by ECA, PHA-L, RCA120, PHA-E, and / or RCA; The reduction of GalNA is determined by DBA, VVA, SJA, GSL1, SBA, ABA, BPL, and / or PNA, and / or The method of any one of the preceding clauses (e.g., regarding MUC5ac and pancreatic cancer), wherein the reduction in GlcNAc is determined by DSA, LEL, WGA, GSL2, and / or STL. 221. The method of any one of the preceding clauses (e.g., relating to MUC1 and pancreatic cancer), wherein the glycoprofile of MUC1 is determined by lectins specific for Gal-GlcNAc, tetraantennary glycans, T antigen, GalNAc, Galα-1,3Gal, and / or GlcNAc. 222.Gal-GlcNAc, reduction of tetraantennary glycans, Decrease in T antigens, GalNAc depletion, Increase in Galα1-3Gal, and / or GlcNAc Depletion The method of any one of the preceding clauses (e.g., regarding MUC1 and pancreatic cancer), wherein: is indicative of pancreatic cancer. 223. The reduction of Gal-GlcNAc, tetraantennary glycans is determined by ECA, PHA-L, RCA120, PHA-E, RCA, and / or DBA; The reduction in T antigen is determined by Jacalin (DSA), SBA, ABA, VVA, BPL, PNA, GSL1, and / or SJA; GalNAc reduction is determined by DBA, VVA, SJA, GSL1, SBA, ABA, BPL, and / or PNA; an increase in Galα1-3Gal is determined by GSL 1, and / or The method of any one of the preceding clauses (e.g., regarding MUC1 and pancreatic cancer), wherein the reduction in GlcNAc is determined by DSA, LEL, WGA, GSL2, and / or STL. 224. The method according to any one of the preceding clauses (e.g., relating to thyroglobulin (TG) and thyroid cancer), wherein the glycosylation profile of thyroglobulin (TG) is determined by lectins specific for antennary fucose, terminal galactose, Gal-GlcNAc, triantennary glycans, and / or mannose. 225. Reduction of antenna-type fucose, Increased terminal galactose, Increase in Gal-GlcNAc Increase in triantennary glycans, Increase in antennary fucose, and / or Increased mannose, The method of any one of the preceding clauses (e.g., relating to thyroglobulin (TG) and thyroid cancer), wherein: is indicative of thyroid cancer. 226. A reduction in antennary fucose is determined by LCA, TJA II, AAL, UEA-I, PSL, AAA, and / or LTA; The increase in terminal galactose is determined by RCA, RCA120, ABA, AlloA, Jacalin (DSA), ECL, and / or PNA; The increase in Gal-GlcNAc is determined by ECA, PHA-L, RCA120, PHA-E, and / or RCA; The increase in triantennary glycans is determined by PHA-E, PHA-L, and / or DBA. The increase in antennary fucose is determined by TJA II, AAL, UEA-I, LCA, PSL, AAA, and / or LTA, and / or The method of any one of the preceding clauses, wherein the increase in mannose is determined by Con A, NPA, and / or GNA (e.g., for thyroglobulin (TG) and thyroid cancer). 227. The method according to any one of the preceding clauses (eg, relating to alpha 1-antitrypsin (AAT) and liver cancer), wherein the glycan profile of alpha 1-antitrypsin (AAT) is determined by a lectin specific for antenna-type fucose. 228. The method according to any one of the preceding clauses (e.g., relating to alpha 1-antitrypsin (AAT) and liver cancer), wherein an increase in antennary fucose is indicative of liver cancer. 229. The method according to any one of the preceding clauses (e.g., relating to alpha 1-antitrypsin (AAT) and liver cancer), wherein the increase in antennary fucose is determined by LCA, TJA II, UEA-I, AAL, PSL, AAA, and / or LTA. 230. The method according to any one of the preceding clauses (eg, relating to alpha-fetoprotein (AFP) and liver cancer), wherein the glycan profile of alpha-fetoprotein (AFP) is determined by a lectin specific for antenna-type fucose. 231. The method according to any one of the preceding clauses (e.g., relating to alpha-fetoprotein (AFP) and liver cancer), wherein an increase in antennary fucose is indicative of liver cancer. 232. The method according to any one of the preceding clauses (e.g., relating to alpha-fetoprotein (AFP) and liver cancer), wherein the increase in antennary fucose is determined by LCA, TJA II, UEA-I, AAL, PSL, AAA, and / or LTA. 233. The method according to any one of the preceding clauses (eg, relating to AFP-L3 (AFP) and liver cancer), wherein the glycoprofile of AFP-L3 is determined by a lectin specific for antenna-type fucose. 234. The method according to any one of the preceding clauses (e.g., relating to AFP-L3 (AFP) and liver cancer), wherein an increase in antennary fucose is indicative of liver cancer. 235. The method according to any one of the preceding clauses (e.g., relating to AFP-L3 (AFP) and liver cancer), wherein the increase in antennary fucose is determined by LCA, TJA II, UEA-I, PSL, AAA, and / or LTA. 236. The method according to any one of the preceding clauses (eg, relating to transferrin and liver cancer), wherein the glycosylation profile of transferrin (AFP) is determined by a lectin specific for antennary fucose. 237. The method of any one of the preceding clauses (e.g., relating to transferrin and liver cancer), wherein an increase in antennary fucose is indicative of liver cancer. 238. The method according to any one of the preceding clauses (e.g., relating to transferrin and liver cancer), wherein the increase in antennary fucose is determined by LCA, TJA II, UEA-I, PSL, AAA, and / or LTA. 239. The method according to any one of the preceding clauses (eg, relating to α1-antichymotrypsin (AAT) and liver cancer), wherein the glycan profile of α1-antichymotrypsin (AAT) is determined by a lectin specific for antenna-type fucose. 240. The method according to any one of the preceding clauses (e.g., relating to α1-antichymotrypsin (AAT) and liver cancer), wherein an increase in antennary fucose is indicative of liver cancer. 241. The method according to any one of the preceding clauses (e.g., relating to α1-antichymotrypsin (AAT) and liver cancer), wherein the increase in antennary fucose is determined by AAL, TJA II, UEA-I, LCA, PSL, AAA, and / or LTA. 242. The method according to any one of the preceding clauses (eg, relating to alpha-1-acid glycoprotein and liver cancer), wherein the glycan profile of alpha-1-acid glycoprotein 1 is determined by a lectin specific for antennary fucose. 243. The method of any one of the preceding clauses (e.g., relating to alpha-1-acid glycoprotein 1 and hepatocarcinoma), wherein an increase in antennary fucose is indicative of hepatocarcinoma. 244. The method according to any one of the preceding clauses (e.g., relating to alpha-1-acid glycoprotein 1 and hepatocellular carcinoma), wherein the increase in antennary fucose is determined by AAL, TJA II, UEA-I, LCA, PSL, AAA, and / or LTA. 245. The method according to any one of the preceding clauses (e.g., relating to ceruloplasmin and liver cancer), wherein the glycan profile of ceruloplasmin is determined by a lectin specific for antenna-type fucose. 246. The method of any one of the preceding clauses (e.g., relating to ceruloplasmin and liver cancer), wherein an increase in antennary fucose is indicative of liver cancer. 247. The method according to any one of the preceding clauses (e.g., relating to ceruloplasmin and liver cancer), wherein the increase in antennary fucose is determined by AAL, LCA, TJA II, UEA-I, LCA, PSL, AAA, and / or LTA. 248. The method according to any one of the preceding clauses (eg, relating to alpha-2-macroglobulin and liver cancer), wherein the glycan profile of alpha-2-macroglobulin is determined by a lectin specific for antennary fucose. 249. The method of any one of the preceding clauses (e.g., relating to alpha-2-macroglobulin and liver cancer), wherein an increase in antennary fucose is indicative of liver cancer. 250. The method according to any one of the preceding clauses (e.g., relating to alpha-2-macroglobulin and liver cancer), wherein the increase in antennary fucose is determined by AAL, LCA, TJA II, UEA-I, PSL, AAA, and / or LTA. 251. The method according to any one of the preceding clauses (e.g., relating to alpha-2-HS-glycoprotein and liver cancer), wherein the glycan profile of alpha-2-HS-glycoprotein is determined by a lectin specific for antennary fucose. 252. The method according to any one of the preceding clauses (e.g., relating to alpha-2-HS-glycoprotein and liver cancer), wherein an increase in antennary fucose is indicative of liver cancer. 253. The method according to any one of the preceding clauses (e.g., relating to alpha-2-HS-glycoprotein and liver cancer), wherein the increase in antennary fucose is determined by AAL, TJA II, UEA-I, LCA, PSL, AAA, and / or LTA. 254. The method according to any one of the preceding clauses (eg, relating to fetuin A and liver cancer), wherein the glycoprofile of fetuin A is determined by a lectin specific for antenna-type fucose. 255. The method of any one of the preceding clauses (eg, relating to fetuin A and liver cancer), wherein an increase in antennary fucose is indicative of liver cancer. 256. The method according to any one of the preceding clauses (e.g., relating to fetuin A and liver cancer), wherein the increase in antennary fucose is determined by AAL, TJA II, UEA-I, LCA, PSL, AAA, and / or LTA. 257. The method according to any one of the preceding clauses (e.g., relating to hemopexin and liver cancer), wherein the glycan profile of hemopexin is determined by a lectin specific for antennary fucose. 258. The method of any one of the preceding clauses (e.g., relating to hemopexin and liver cancer), wherein an increase in antennary fucose is indicative of liver cancer. 259. The method according to any one of the preceding clauses (e.g., relating to hemopexin and liver cancer), wherein the increase in antennary fucose is determined by AAL, TJA II, UEA-I, LCA, PSL, AAA, and / or LTA. 260. The method according to any one of the preceding clauses (eg, relating to C3 complement and liver cancer), wherein the glycan profile of C3 complement is determined by a lectin specific for antenna-type fucose. 261. The method of any one of the preceding clauses (e.g., relating to C3 complement and liver cancer), wherein an increase in antennary fucose is indicative of liver cancer. 262. The method according to any one of the preceding clauses (e.g., relating to C3 complement and liver cancer), wherein the increase in antennary fucose is determined by AAL, LCA, TJA II, UEA-I, PSL, AAA, and / or LTA. 263. The method according to any one of the preceding clauses (e.g., relating to histidine-rich glycoproteins and liver cancer), wherein the glycan profile of the histidine-rich glycoprotein is determined by a lectin specific for antenna-type fucose. 264. The method of any one of the preceding clauses (e.g., relating to histidine-rich glycoproteins and liver cancer), wherein an increase in antennary fucose is indicative of liver cancer. 265. The method according to any one of the preceding clauses (e.g., relating to histidine-rich glycoproteins and liver cancer), wherein the increase in antennary fucose is determined by AAL, LCA, TJA II, UEA-I, PSL, AAA, and / or LTA. 266. The method according to any one of the preceding clauses (eg, relating to monocytic differentiation antigen CD14 and liver cancer), wherein the glycoprofile of monocytic differentiation antigen CD14 is determined by a lectin specific for antenna-type fucose. 267. The method of any one of the preceding clauses (eg, relating to monocytic differentiation antigen CD14 and hepatocellular carcinoma), wherein an increase in antennary fucose is indicative of hepatocellular carcinoma. 268. The method according to any one of the preceding clauses (e.g., relating to monocytic differentiation antigen CD14 and hepatocellular carcinoma), wherein the increase in antennary fucose is determined by AAL, LCA, TJA II, UEA-I, PSL, AAA, and / or LTA. 269. The method according to any one of the preceding clauses (eg, relating to hepatocyte growth factor activator and liver cancer), wherein the glycan profile of the hepatocyte growth factor activator is determined by a lectin specific for antenna-type fucose. 270. The method of any one of the preceding clauses (e.g., relating to hepatocyte growth factor activator and liver cancer), wherein an increase in antennary fucose is indicative of liver cancer. 271. The method according to any one of the preceding clauses (e.g., relating to hepatocyte growth factor activator and liver cancer), wherein the increase in antennary fucose is determined by AAL, LCA, TJA II, UEA-I, PSL, AAA, and / or LTA. 272. The glycan profile of β-haptoglobin is characterized by antennary fucose, core fucose, 3 and 4 antennary glycans, α2-6Neu5Ac (α2-6 linked sialic acid), sialyl Le x The method of any one of the preceding claims (e.g., relating to β-haptoglobin and lung cancer), wherein the glycan expression level is determined by a lectin specific for triantennary glycans, and / or sialic acid. 273. Increase in antenna-type fucose, Increased core fucose, Increase in 3- and 4-antennary glycans, Increased α2-6Neu5Ac (α2-6 linked sialic acid), Sialyl Le x Increase in Increased triantennary glycans, and / or Increased sialic acid, The method of any one of the preceding clauses (e.g., regarding β-haptoglobin and lung cancer), wherein: is indicative of lung cancer. 274. An increase in antennary fucose is determined by AAL, TJA II, UEA-I, PSL, AAA, LCA, and / or LTA; The increase in core fucose is determined by AOL and / or PhoSL, The increase in tri- and tetraantennary glycans is determined by PHA-E, PHA-L, and / or DBA; Increase in α2-6Neu5Ac (α2-6 linked sialic acid) as determined by SNA and / or TJA-I; Sialyl Le x the increase is determined by SNA, TJA-I, MAA, anti-α2-3-linked Neu5Ac (α2-3-linked sialic acid) antibodies (e.g., HYB4), Siglec-1, Siglec-4, and / or Siglec-8; The method of any one of the preceding clauses (e.g., relating to β-haptoglobin and lung cancer), wherein the increase in sialic acid is determined by SNA, TJA-I, MAA, anti-α2-3-linked Neu5Ac (α2-3 linked sialic acid) antibodies (e.g., HYB4), Siglec-1, Siglec-4, and / or Siglec-8. 275. The method according to any one of the preceding clauses (eg, relating to fibronectin and liver cancer), wherein the glycosylation profile of fibronectin is determined by a lectin specific for Galβ1-3GalNAc. 276. The method of any one of the preceding clauses (eg, relating to fibronectin and lung cancer), wherein an increase in Galβ1-3GalNAc is indicative of lung cancer. 277. The method of any one of the preceding clauses (e.g., relating to fibronectin and lung cancer), wherein the increase in Galβ1-3GalNAc is determined by PNA, ABA, and / or Jacalin (DSA). 278. The glycan profile of α1-acid glycoprotein is characterized by antennary fucose and / or sialyl Leu. x The method of any one of the preceding claims (e.g., relating to alpha 1-acid glycoprotein and lung cancer), wherein the expression level is determined by a lectin specific for alpha 1-acid glycoprotein. 279. Increase in antennary fucose, and / or Sialyl Le x Increase in The method of any one of the preceding clauses (e.g., relating to alpha 1-acid glycoprotein and lung cancer), wherein: is indicative of lung cancer. 280. An increase in antennary fucose is determined by TJA II, AAL, UEA-I, LCA, PSL, AAA, and / or LTA, and / or Sialyl Le x The increase in sLe x The method of any one of the preceding clauses (e.g., relating to alpha 1-acid glycoprotein and lung cancer), as determined by antibodies to alpha 2-3-linked Neu5Ac (alpha 2-3-linked sialic acid) antibodies (e.g., HYB4), Siglec 1, Siglec 4, and / or Siglec 8. 281. The glycan profile of α-1-antitrypsin is composed of antennary fucose, β-Gal, Galβ1-4GlcNAc, α-Gal and α-GalNAc, (GlcNAc) n , Branched (LacNAc) n The method of any one of the preceding clauses (e.g., with respect to alpha-1-antitrypsin and lung cancer), as determined by a lectin specific for high mannose, Manα1-3Man. 282. Increase in antenna-type fucose, Increase in β-Gal and Galβ1-4GlcNAc Increase in α-Gal and α-GalNAc (GlcNAc) n Increase in Branching (LacNAc) n and / or High mannose, increased Manα1-3Man, The method of any one of the preceding clauses (e.g., relating to alpha-1-antitrypsin and lung cancer), wherein: is indicative of lung cancer. 283. An increase in antennary fucose is determined by AAL, TJA II, UEA-I, LCA, PSL, AAA, and / or LTA; The increase in β-Gal, Galβ1-4GlcNAc is determined by RCA120, RCA, ECL, and / or AlloA; The increase in α-Gal and α-GalNAc is determined by BS-I, DBA, SBA, and / or HPA; (GlcNAc) n The increase is determined by WGA and / or LEL, Branching (LacNAc) n The increase in is determined by PWM and / or The method of any one of the preceding clauses (e.g., relating to alpha-1-antitrypsin and lung cancer), wherein the increase in high mannose, Manα1-3Man, is determined by GNA, Con A, and / or NPA. 284. The glycan profile of α1-acid glycoprotein was characterized by biantennary glycans, galactose, and / or Leu. x The method of any one of the preceding claims (e.g., relating to alpha 1-acid glycoprotein and gastric cancer), wherein the cancer is determined by a lectin specific for alpha 1-acid glycoprotein. 285.2 Increase in antennary glycans, Galactose depletion, and / or Le x Increase in The method of any one of the preceding clauses (e.g., relating to alpha 1-acid glycoprotein and gastric cancer), wherein: is indicative of gastric cancer. The increase in 286.2 antennary glycans was determined by Con A, NPA, and / or GNA; The reduction in galactose is determined by RCA, RCA120, ABA, AlloA, Jacalin (DSA), ECL, and / or PNA; and / or Le x The method of any one of the preceding clauses (e.g., relating to alpha 1-acid glycoprotein and gastric cancer), wherein the increase is determined by LTA. 287. The glycan profile of β-haptoglobin is characterized by sialyl Le x (sLe x ), 3, 4-antennary glycan, antennary fucose, sialyl-Le a (sLe a ), (GlcNAc) nThe method of any one of the preceding clauses (e.g., relating to β-haptoglobin and gastric cancer), wherein the β-haptoglobin level is determined by a lectin specific for high mannose, and / or a lectin specific for high mannose. 288. Sialyl Le x (sLe x ) increase, Increase in 3- and 4-antennary glycans, Increase in antenna-type fucose, Sialyl-Le a (sLe a ) increase, (GlcNAc) n and / or Reduction of high mannose, The method of any one of the preceding clauses (e.g., relating to β-haptoglobin and gastric cancer), wherein: is indicative of gastric cancer. 289. Sialyl Le x (sLe x ) is an increase in anti-sLe x as determined by mouse monoclonal KM93 antibody, SNA, TJA-I, MAA, anti-α2-3 linked Neu5Ac (α2-3 linked sialic acid) antibody (e.g., HYB4), Siglec 1, Siglec 4, or Siglec 8; The increase in tri- and tetraantennary glycans is determined by PHA-E, PHA-L, and / or DBA; The increase in antennary fucose is determined by AAL, TJA II, UEA-I, LCA, PSL, AAA, and / or LTA; Sialyl-Le a (sLe a ) increases with sLe a antibodies against α2-3-linked Neu5Ac (α2-3-linked sialic acid) antibodies (e.g., HYB4), Siglec-1, Siglec-4, and / or Siglec-8; (GlcNAc) n The increase is determined by WGA and / or LEL, and / or The method of any one of the preceding clauses (e.g., regarding β-haptoglobin and gastric cancer), wherein the reduction of high mannose is determined by Con A, NPA, and / or GNA. 290. The glycan profile of leucine-rich-α2-glycoprotein is characterized by sialyl-Le x (sLe x The method of any one of the preceding claims (e.g., relating to leucine-rich-α2-glycoprotein and gastric cancer), wherein the level of leucine-rich-α2-glycoprotein is determined by a lectin specific for leucine-rich-α2-glycoprotein. 291. Sialyl-Le x (sLe x The method of any one of the preceding clauses (e.g., regarding leucine-rich-α2-glycoprotein and gastric cancer), wherein an increase in α2-glycoprotein is indicative of gastric cancer. 292. Sialyl-Le x (sLe x ) is an increase in anti-sLe x Mouse monoclonal KM93 antibody, sLe a The method of any one of the preceding clauses (e.g., relating to leucine-rich-α2-glycoprotein and gastric cancer), as determined by antibodies to, SNA, TJA-I, MAA, anti-α2-3 linked Neu5Ac (α2-3 linked sialic acid) antibodies (e.g., HYB4), Siglec-1, Siglec-4, and / or Siglec-8. 293. The method according to any one of the preceding clauses (e.g., relating to human chorionic gonadotropin-β and testicular cancer), wherein the glycan profile of human chorionic gonadotropin-β is determined by a lectin specific for fucose and / or triantennary glycans. 294. Increased fucose, and / or Increase in triantennary glycans, The method of any one of the preceding clauses (e.g., regarding human chorionic gonadotropin-β and testicular cancer), wherein is indicative of testicular cancer. 295. Increase in fucose is determined by AAL, TJA II, UEA-I, LCA, PSL, AAA, LTA, PhoSL and / or AOL; The method of any one of the preceding clauses (e.g., for human chorionic gonadotropin-β and testicular cancer), wherein the increase in triantennary glycans is determined by PHA-E, PHA-L, and / or DBA. 296. The method according to any one of the preceding clauses (eg, relating to AFP-L3 and testicular cancer), wherein the glycoprofile of AFP-L3 is determined by a lectin specific for antennary fucose. 297. The method of any one of the preceding clauses (e.g., relating to AFP-L3 and testicular cancer), wherein an increase in antennary fucose is indicative of testicular cancer. 298. The method of any one of the preceding clauses (e.g., relating to AFP-L3 and testicular cancer), wherein the increase in antennary fucose is determined by AAL, TJA II, UEA-I, LCA, PSL, AAA, and / or LTA. 299. The method of any one of the preceding clauses (eg, relating to MUC1 and bladder cancer), wherein the glycoprofile of MUC1 is determined by a lectin specific for antennary fucose. 300. The method of any one of the preceding clauses (e.g., relating to MUC1 and bladder cancer), wherein an increase in antennary fucose is indicative of bladder cancer. 301. The method of any one of the preceding clauses (e.g., relating to MUC1 and bladder cancer), wherein the increase in antennary fucose is determined by AAL, TJA II, UEA-I, LCA, PSL, AAA, and / or LTA. 302. The method according to any one of the preceding clauses (e.g., relating to endoplasmin (HSP90B1) and bladder cancer), wherein the glycan profile of endoplasmin (HSP90B1) is determined by a lectin specific for antenna-type fucose. 303. The method of any one of the preceding clauses (e.g., relating to endoplasmin (HSP90B1) and bladder cancer), wherein an increase in antennary fucose is indicative of bladder cancer. 304. The method of any one of the preceding clauses (e.g., relating to endoplasmin (HSP90B1) and bladder cancer), wherein the increase in antennary fucose is determined by AAL, TJA II, UEA-I, LCA, PSL, AAA, and / or LTA. 305. The method of any one of the preceding clauses (e.g., relating to Golgi apparatus protein 1 (GLG1) and bladder cancer), wherein the glycan profile of Golgi apparatus protein 1 (GLG1) is determined by a lectin specific for antennary fucose. 306. The method of any one of the preceding clauses (e.g., relating to Golgi apparatus protein 1 (GLG1) and bladder cancer), wherein an increase in antennary fucose is indicative of bladder cancer. 307. The method of any one of the preceding clauses (e.g., relating to Golgi apparatus protein 1 (GLG1) and bladder cancer), wherein the increase in antennary fucose is determined by AAL, TJA II, UEA-I, LCA, PSL, AAA, and / or LTA. 308. The method according to any one of the preceding clauses (e.g., relating to prostatic acid phosphatase (ACPP) and bladder cancer), wherein the glycosylation profile of prostatic acid phosphatase (ACPP) is determined by a lectin specific for antennary fucose. 309. The method of any one of the preceding clauses (e.g., relating to prostatic acid phosphatase (ACPP) and bladder cancer), wherein an increase in antennary fucose is indicative of bladder cancer. 310. The method according to any one of the preceding clauses (e.g., relating to prostatic acid phosphatase (ACPP) and bladder cancer), wherein the increase in antennary fucose is determined by AAL, TJA II, UEA-I, LCA, PSL, AAA, and / or LTA. 311. The method according to any one of the preceding clauses (e.g., relating to Igγ-2 chain C region (IGHG2) and bladder cancer), wherein the glycan profile of Igγ-2 chain C region (IGHG2) is determined by a lectin specific for antenna-type fucose. 312. The method of any one of the preceding clauses (e.g., relating to Ig gamma-2 chain C region (IGHG2) and bladder cancer), wherein an increase in antennary fucose is indicative of bladder cancer. 313. The method of any one of the preceding clauses (e.g., for Igγ-2 chain C region (IGHG2) and bladder cancer), wherein the increase in antennary fucose is determined by AAL, TJA II, UEA-I, LCA, PSL, AAA, and / or LTA. 314. The method according to any one of the preceding clauses (e.g., relating to DNASE2A and bladder cancer), wherein the glycosylation profile of DNASE2A is determined by a lectin specific for antennary fucose. 315. The method of any one of the preceding clauses (e.g., relating to deoxyribonuclease-2-alpha (DNASE2A) and bladder cancer), wherein an increase in antennary fucose is indicative of bladder cancer. 316. The method of any one of the preceding clauses (e.g., relating to deoxyribonuclease-2-alpha (DNASE2A) and bladder cancer), wherein the increase in antennary fucose is determined by AAL, TJA II, UEA-I, LCA, PSL, AAA, and / or LTA. 317. The method according to any one of the preceding clauses (e.g., relating to integrins and bladder cancer), wherein the glycan profile of the integrin is determined by a lectin specific for sialic acid and / or tetraantennary glycans. 318. Increased sialic acid, and / or Increase in 4-antennary glycans, The method of any one of the preceding clauses (e.g., regarding integrins and bladder cancer), wherein: is indicative of bladder cancer. 319. The increase in sialic acid is determined by SNA, TJA-I, MAA, anti-α2-3-linked Neu5Ac (α2-3-linked sialic acid) antibodies (e.g., HYB4), Siglec-1, Siglec-4, or Siglec-8, and / or The method of any one of the preceding clauses (e.g., relating to integrins and bladder cancer), wherein the increase in tetraantennary glycans is determined by PHA-E, PHA-L, and / or DBA. 320. The method of any one of the preceding clauses (e.g., relating to MUC16 and bladder cancer), wherein the glycoprofile of MUC16 is determined by a lectin specific for sialyl-Tn. 321. The method of any one of the preceding clauses (e.g., relating to MUC16 and bladder cancer), wherein an increase in sialyl-Tn is indicative of bladder cancer. 322. The method of any one of the preceding clauses (e.g., relating to MUC16 and bladder cancer), wherein the increase in sialyl-Tn is determined by SNA, TJA-I, MAA, and / or an anti-α2-3-linked Neu5Ac (α2-3-linked sialic acid) antibody (e.g., HYB4). 323. The glycan profile of α-1-antitrypsin is high in mannose and / or (GlcNAcβ1-4) n The method of any one of the preceding claims (e.g., with respect to alpha-1-antitrypsin and bladder cancer), wherein the cancer is determined by a lectin specific for alpha-1-antitrypsin. 324. Increased mannose levels, and / or (GlcNAcβ1-4) n Increase in The method of any one of the preceding clauses (e.g., regarding alpha-1-antitrypsin and bladder cancer), wherein: is indicative of bladder cancer. 325. The increase in high mannose is determined by Con A, NPA, and / or GNA, and / or (GlcNAcβ1-4) n The method of any one of the preceding clauses (e.g., for alpha-1-antitrypsin and bladder cancer), wherein the increase is determined by WGA and / or LEL. 326. For use in the method according to any one of the preceding clauses, preferably i) for the prediction (e.g., positive or negative) of prostate cancer, preferably the lectin is selected from the group consisting of MAA II, AAL, Con A, SNA-I, and WFA, more preferably the lectin comprises MAA II, most preferably the lectin is two lectins comprising MAA II, and even more preferably the lectin is aa) AAL, or bb) Con A, or cc) comprising MAA II in combination with SNA-I; ii) for distinguishing between benign prostatic hyperplasia (BPH) and prostate cancer, preferably the lectin is selected from the group consisting of MAA II, AAL, Con A, SNA-I, and WFA, more preferably the lectin comprises MAA II, most preferably the lectin is two lectins comprising MAA II, and even more preferably the lectin is aa) AAL, or bb) Con A, or cc) comprising MAA II in combination with SNA-I; iii) A lectin for use in a method selected from the group consisting of: for distinguishing between prostate cancer and metastatic prostate cancer, wherein preferably the lectin is selected from the group consisting of AAL, Con A, MAA II, and SNA-I, more preferably selected from the group consisting of AAL, Con A, and MAA II, and most preferably selected from the group consisting of AAL and Con A. 327. One or more lectins according to any one of the preceding clauses, wherein the one or more lectins are selected from the group consisting of i) Maackia amurensis lectin II (MAA II), ii) concanavalin A (Con A) lectin, iii) Aleuria aurantia lectin (AAL), iv) Sambucus nigra (SNA-I) lectin, v) Wisteria floribunda lectin (WFL), vi) any of the lectins listed in Table 1 herein, preferably the one or more lectins comprise MAA II, more preferably the one or more lectins are two lectins comprising MAA II, and most preferably the one or more lectins are two lectins comprising MAA II in combination with AAL, Con A, or SNA-I. 328. One or more lectins according to any one of the preceding clauses, wherein the one or more lectins are immobilized (e.g., at a sample location, e.g., on a microplate, e.g., an Enzyme-Linked Immunosorbent Assay (ELISA), Enzyme-Linked Lectin Assay (ELLA), or Magnetic Enzyme-Linked Lectin Assay (MELLA) microplate). 329.i) A glycoprotein antibody according to any one of the preceding clauses (e.g., an anti-PSA antibody, or any antibody described in Table 1 herein), or an antigen-binding portion thereof; ii) A magnetic carrier according to any one of the preceding paragraphs; iii) A composition comprising one or more lectins (e.g., any of the lectins listed in Table 1 herein), preferably the one or more lectins are selected from the group consisting of Maackia amurensis lectin II (MAA II), concanavalin A (Con A) lectin, Aleuria aurantia lectin (AAL), Sambucus nigra (SNA-I) lectin, Wisteria floribunda lectin (WFL), more preferably the one or more lectins comprise MAA II, most preferably the one or more lectins are two lectins comprising MAA II, even most preferably the one or more lectins are two lectins comprising MAA II in combination with AAL, Con A, or SNA-I, even most preferably the one or more lectins are one or more lectins listed in any one of the preceding clauses. 330.i) a magnetic carrier according to any one of the preceding clauses, or an anti-glycoprotein antibody according to any one of the preceding clauses (e.g. an anti-PSA antibody, an anti-AFP antibody, an anti-MUC16 antibody, an anti-WFDC2 antibody, an anti-MUC1 antibody, an anti-ERBB2 antibody, an anti-CEACAM5 antibody, an anti-FUT3 antibody, an anti-TG antibody, or any antibody described in Table 1 herein, preferably the target polypeptide is an anti-PSA antibody), or an antigen-binding portion thereof, ii) a composition according to any one of the above clauses comprising one or more lectins (e.g., any lectin listed in Table 1 herein), preferably wherein the one or more lectins are selected from the group consisting of Maackia amurensis lectin II (MAA II), concanavalin A (Con A) lectin, Aleuria aurantia lectin (AAL), Sambucus nigra (SNA-I) lectin, Wisteria floribunda lectin (WFL), more preferably wherein the one or more lectins comprise MAA II, most preferably wherein the one or more lectins are two lectins comprising MAA II, even most preferably wherein the one or more lectins are two lectins comprising MAA II in combination with AAL, Con A, or SNA-I, even most preferably wherein the one or more lectins are one or more lectins listed in any one of the above clauses. 331. A kit comprising an anti-glycoprotein antibody (e.g., an anti-PSA antibody, an anti-AFP antibody, an anti-MUC16 antibody, an anti-WFDC2 antibody, an anti-MUC1 antibody, an anti-ERBB2 antibody, an anti-CEACAM5 antibody, an anti-FUT3 antibody, an anti-TG antibody, or any antibody described in Table 1 herein, preferably an anti-PSA antibody), an antigen-binding portion thereof, a magnetic carrier, one or more lectins, or a composition described in any one of the preceding paragraphs. 332. A kit for performing the method according to any one of the preceding clauses, comprising an antibody specific for a cancer biomarker protein according to any one of the preceding clauses and one or more lectins according to any one of the preceding clauses, preferably wherein the cancer biomarker is selected from the group consisting of the biomarkers listed in Table 1 herein. 333. A kit for performing the method according to any one of the preceding clauses, comprising an antibody specific for an autoimmune disease biomarker protein according to any one of the preceding clauses, and one or more lectins according to any one of the preceding clauses, preferably wherein the biomarkers are selected from the group consisting of the biomarkers listed in Table 1 herein. 334. A kit for performing the method according to any one of the preceding clauses, comprising an antibody specific for an inflammatory disease biomarker protein according to any one of the preceding clauses, and one or more lectins according to any one of the preceding clauses, preferably wherein the biomarkers are selected from the group consisting of the biomarkers listed in Table 1 herein. 335. An anti-glycoprotein antibody (e.g., an anti-PSA antibody, an anti-AFP antibody, an anti-MUC16 antibody, an anti-WFDC2 antibody, an anti-MUC1 antibody, an anti-ERBB2 antibody, an anti-CEACAM5 antibody, an anti-FUT3 antibody, an anti-TG antibody, or any antibody described in Table 1 herein, preferably an anti-PSA antibody), an antigen-binding portion thereof, a magnetic carrier, one or more lectins, or a composition according to any one of the preceding clauses for use as a medicament. 336.i) selective capture and / or enrichment of a target polypeptide as described in any one of the preceding paragraphs (e.g., PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3, TG, or any biomarker as described in Table 1 herein, preferably the target polypeptide is PSA); ii) selective capture and / or enrichment of a target polypeptide as described in any one of the preceding clauses (e.g. PSA, AFP, MUC16, WFDC2, MUC1, ERBB2, CEACAM5, FUT3, TG, or any biomarker described in Table 1 herein, preferably the target polypeptide is PSA), wherein the method for selective capture and / or enrichment comprises the use of one or more lectins (e.g. immobilized lectins), preferably the one or more lectins are immobilized at a sample locati...

Claims

1. 1. A method for determining a glycoprofile of a protein, comprising: (a) contacting a sample containing the protein with an antibody against the protein to form an antibody-protein complex; (b) isolating the antibody-protein complex obtained in step (a); and (c) then contacting the antibody-protein complex with one or more lectins to determine the glycoprofile of the protein; A method, wherein the antibody in step (a) is not immobilized on a solid surface but is instead bound to a magnetic carrier, the protein is not released from the antibody when performing the method, and the one or more lectins are not immobilized at the sample location.

2. 2. The method of claim 1, further comprising the step of: (d) comparing the glycoprofile of the protein to a control glycoprofile of the protein to determine whether the glycoprofile of the protein may deviate from the glycoprofile of the control glycoprofile.

3. The method of claim 1 or 2, wherein the protein is a cancer biomarker protein, an autoimmune disease biomarker protein, or an inflammatory disease biomarker protein.

4. 4. The method of claim 3, wherein the cancer biomarker protein is an ovarian cancer biomarker protein, a breast cancer biomarker protein, a colorectal cancer biomarker protein, a pancreatic cancer biomarker protein, a prostate cancer biomarker protein, a thyroid cancer biomarker protein, a liver cancer biomarker protein, a lung cancer biomarker protein, a gastric cancer biomarker protein, a testicular cancer biomarker protein, or a bladder cancer biomarker protein.

5. The method of claim 4, wherein the prostate cancer biomarker protein is β-haptoglobin, TIMP-1, PSA, fPSA, or tPSA.

6. The method of any one of claims 1 to 5, wherein the antibody comprises beads that allow isolation of the antibody.

7. The one or more lectins may be selected from the group consisting of core fucose, antennary fucose, Fucα1-6GlcNAc-N-Asn-containing N-linked oligosaccharides, Fucα1-6 / 3GlcNAc, α-L-Fuc, Fucα1-2Galβ1-4(Fucα1-3)GlcNAc, Fucα1-2Gal, Fucα1-6GlcNAc, Manβ1-4GlcNAcβ1-4GlcNAc, branched N-linked hexasaccharides, Manα1-3Man, α-D-Man, (GlcNAcβ1-4)2-4, Galβ1-4GlcNAc, GlcNAcα1-4Galβ1-4GlcNAc, (GlcNAc β1-4)2-5, Neu5Ac (sialic acid), Galβ1-3GalNAc-serine / threonine, Galα1-3GalNAc, Galβ1-6Gal, Galβ1-4GlcNAc, Galβ1-3GalNAc, GalNAcα1-3GalNAc, GalNAcα1-3G al, GalNAcα / β1-3 / 4Gal, α-GalNAc, GalNAcβ1-4Gal, GalNAcα1-3(Fucα1-2)Gal, GalNAcα1-2Gal, GalNAcα1-3GalNAc, GalNAcβ1-3 / 4Gal, GalNAc-Ser / Thr (Tn antigen), Galβ1-3GalNAc-Ser / Thr (T antigen), GalNAcβ1-4GlcNAc (LacdiNAc), α-2,3Neu5Ac (α2-3 linked sialic acid), α-2,6Neu5Ac (α2-6 linked sialic acid), α-2,8Neu5Ac (α2-8 linked sialic acid), sialic acid (α-2,3Neu5Ac, α-2,6Neu5Ac or α-2,8Neu5Ac), Neu5Acα4 / 9-O-Ac-Neu5Ac, Neu5Acα2-3Galβ1-4Glc / GlcNAc, Neu5Acα2-6Gal / GalNAc, N-linked biantennary, N-linked triantennary, branched β1-6GlcNAc, Galα1-3(Fucα1-2)Galβ1-3 / 4GlcNAc, Galβ1-3(Fucα1-4)GlcNAc, NeuAcα2-3Galβ1- 3(Fucα1-4)GlcNAc, Fucα1-2Galβ1-3(Fucα1-4)GlcNAc, Galβ1-4(Fucα1-3)GlcNAc, NeuAcα2-3Galβ1-4(Fucα1-3)GlcNAc, Fucα1-2Galβ1-4(Fucα1-3)GlcNAc, high mannose, sialyl Lewis a (sialyl Lea) antigen, sialyl Lewis x (sialyl Lex) antigen, Lewis x (Lex) The method according to any one of claims 1 to 6, which is specific to an antigen, a sialyl Tn antigen, a sialyl T antigen, a Lewis y (Ley) antigen, a sulfated core 1 glycan, a Tn antigen, a T antigen, a core 2 glycan, a Lewis a (Lea) antigen, (GlcNAcβ1-4)n, β-D-GlcNAc, GalNAc, Gal-GlcNAc, GlcNAc, Galα1-3Gal, Galβ1-3GalNAc, α-Gal, α-GalNAc, (GlcNAc)n, or a branched (LacNAc)n.

8. 1. A method for aiding in the diagnosis of a subject being at risk for or suffering from cancer, comprising: (a) contacting a sample obtained from the subject, the sample containing a cancer biomarker protein, with an antibody against the cancer biomarker protein to form an antibody-cancer biomarker protein complex; (b) isolating the antibody-protein complex obtained in step (a); and (c) then contacting the antibody-cancer biomarker protein complex with one or more lectins to determine the glycoprofile of the cancer biomarker protein; the antibody in step (a) is not immobilized on a solid surface but is instead bound to a magnetic carrier, the cancer biomarker protein is not released from the antibody during the method, the antibody is bound to a magnetic carrier, and the one or more lectins are not immobilized at the sample location; The method provides a deviation of the glycan profile from a healthy glycan profile of the cancer biomarker protein as information indicating that the subject is at risk of cancer or is suffering from cancer.

9. 1. A method for aiding in the diagnosis that a subject is at risk for or has an autoimmune disease, comprising: (a) contacting a sample obtained from the subject, the sample including an autoimmune disease biomarker protein, with an antibody against the autoimmune disease biomarker protein to form an antibody-autoimmune disease biomarker protein complex; (b) isolating the antibody-protein complex obtained in step (a); and (c) then contacting the antibody-autoimmune disease biomarker protein complex with one or more lectins to determine the glycoprofile of the autoimmune disease biomarker protein; the antibody in step (a) is not immobilized on a solid surface but is instead bound to a magnetic carrier, the autoimmune disease biomarker protein is not released from the antibody during the method, the antibody is bound to a magnetic carrier, and the one or more lectins are not immobilized at the sample location; The method provides a deviation of the glycan profile from a healthy glycan profile of the autoimmune disease biomarker protein as information indicating that the subject is at risk of or suffering from an autoimmune disease.

10. 1. A method for aiding in the diagnosis that a subject is at risk for or suffering from an inflammatory disease, comprising: (a) contacting a sample obtained from the subject that contains an inflammatory disease biomarker protein with an antibody to the inflammatory disease biomarker protein to form an antibody-inflammatory disease biomarker protein complex; (b) isolating the antibody-protein complex obtained in step (a); and (c) then contacting the antibody-inflammatory disease biomarker protein complex with one or more lectins to determine the glycoprofile of the inflammatory disease biomarker protein; the antibody in step (a) is not immobilized on a solid surface but is instead bound to a magnetic carrier, the inflammatory disease biomarker protein is not released from the antibody during the method, the antibody is bound to a magnetic carrier, and the one or more lectins are not immobilized at the sample location; The method provides a deviation of the glycan profile from a healthy glycan profile of the inflammatory disease biomarker protein as information indicating that the subject is at risk of or suffering from an inflammatory disease.

11. 9. Use of a kit for carrying out the method according to claim 8, comprising an antibody specific for a cancer biomarker protein according to claim 4 and one or more lectins according to claim 7.

12. 10. Use of a kit for carrying out the method of claim 9, comprising an antibody specific for an autoimmune disease biomarker protein that is IgG and one or more lectins as described in claim 7.

13. 11. Use of a kit for carrying out the method of claim 10, comprising an antibody specific for an inflammatory disease biomarker protein, the antibody being IgG, IgA, or CRP, and one or more lectins as described in claim 7.

14. The method of any one of claims 1 to 10, wherein the antibody comprises a detectable label.

15. 15. The method of claim 14, wherein the antibody comprises a fluorophore, an enzyme, a radioisotope, a fluorescent protein, a fluorescent dye, or a tag.

16. The method according to any one of claims 1 to 10, wherein the magnetic carrier is a magnetic bead.

Images