Composition comprising an antibody which binds to human IGF2BP1 present on the cell surface of a target cell

Abstract

The present invention provides a pharmaceutical composition comprising a monoclonal antibody which binds to human IGF2BP1 present on the cell surface of a target cell and optionally a pharmaceutically acceptable carrier, diluent or excipient, wherein said target cell is a non-permeabilized cell or a living cell. The present invention further provides said pharmaceutical composition for use in an in-vivo imaging method or in a method for the treatment of cancer in a human subject. Further is provided a method for determining whether a human subject may suffer from cancer, comprising determining whether IGF2BP1 is present on the cell surface of cancer cells and / or determining whether IGF2BP1 is present on the surface of extracellular vesicles. Additionally, an antibody which binds to human IGF2BP1 present on the cell surface of a target cell and / or which binds to human IGF2BP1 present on the surface of an extracellular vesicle is provided. The present invention also provides a method of killing a target cell having IGF2BP1 present on the cell surface using an antibody. Furthermore, an antibody is provided, which binds to human IGF2BP1 present on the cell surface of a target cell for use in a method for the treatment of cancer in a subject, comprising, prior to the treatment of cancer in said subject, determining whether a target cell of said subject has IGF2BP1 present on the cell surface.

Description

COMPOSITION COMPRISING AN ANTIBODY WHICH BINDS TO HUMAN IGF2BP1 PRESENT ON THE CELL SURFACE OF A TARGET CELLCROSS-REFERENCE TO RELATED APPLICATIONThe present application claims the benefit of priority of EP Patent Application No. 23 216 945.8 filed 15 December 2023, the content of which is hereby incorporated by reference in its entirety for all purposes.TECHNICAL FIELD OF THE INVENTIONThe present invention provides a pharmaceutical composition comprising a monoclonal antibody which binds to human IGF2BP1 present on the cell surface of a target cell and optionally a pharmaceutically acceptable carrier, diluent or excipient, wherein said target cell is a non-permeabilized cell or a living cell. The present invention further provides said pharmaceutical composition for use in a method for the treatment of cancer in a human subject or in an in-vivo imaging method. Further is provided a method for determining whether a human subject may suffer from cancer, comprising determining if IGF2BP1 is present on the surface of cells and / or on the surface of extracellular vesicles. Additionally, an antibody which binds to human IGF2BP1 present on the cell surface of a target cell and / or on the surface of an extracellular vesicle is provided. The present invention further provides an antibody, which binds to human IGF2BP1 present on the cell surface of a target cell for use in a method of killing said target cell having IGF2BP1 present on the cell surface. Further, a method of killing a target cell having IGF2BP1 present on the cell surface of said target cell, comprising administering an antibody, which binds to human IGF2BP1 present on the cell surface of said target cell is provided. The present invention further relates to an antibody, which binds to human IGF2BP1 present on the cell surface of a target cell for use in a method for the treatment of cancer in a subject, comprising, prior to the treatment of cancer in said subject, determining whether a target cell of said subject has IGF2BP1 present on the cell surface.BACKGROUND ARTIt has long been known that tumor cells carry proteins on their surfaces that are only found inside and / or are secreted in non-tumor cells. In normal cells, these proteins are often located in the membranes of the Golgi apparatus or of the endoplasmic reticulum (ER). It is not known why and for what purpose tumor cells carry them on their surface (Weidle et al., 2011 ). Little is known about the function of such proteins on the surface of tumor cells. On the other hand, these proteins can be of interest as target structures for certain applications, as they may represent tumor-associated or -specific antigens that can be controlled with various methods. These include, e.g., antibodies such as can be used for the detection or treatment of (tumor) diseases.Insulin-like growth factor 2 mRNA-binding protein 1 (IGF2BP1 ; UniProt Q9NZI8) is an RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA- mediated degradation. IGF2BP1 preferentially binds to N6-methyladenosine (m6A)- containing mRNAs and increases their stability (Huang et al., 2018; Zhu et al., 2020) and is therefore often referred to as an ‘m6A reader’. During intestinal wound repair, IGF2BP1 interacts with and stabilizes PTGS2 transcript. PTGS2 mRNA stabilization may be crucial for colonic mucosal wound healing. IGF2BP1 binds to the 3'-UTR of IGF2 mRNA by a mechanism of cooperative and sequential dimerization and regulates IGF2 mRNA subcellular localization and translation.It is known that IGF2BP1 plays an important role in cancer. IGF2BP1 is aberrantly overexpressed in a number of tumor types. Its elevated expression has been found to directly correlate with poor prognosis in most cancer types (Dimitriadis E et al., 2007; Bell JL et al., 2015). Several reports have demonstrated that IGF2BP1 stabilizes the mRNA of pro-proliferative or tumor-promoting genes, including c-myc, |3TrCP1 , GLI1 , MITF, MDR1 (Vikesaa J et al., 2006; Elcheva I et al., 2009; Goswami S et al., 2015; Noubissi FK ef al., 2006; Noubissi FK ef al., 2009, Sparanese D et al., 2007; Leeds P et al., 1997). For example, IGF2BP1 binds to MYC mRNA in the coding region instability determinant (CRD) of the open reading frame (ORF), hence preventing MYC cleavage byendonucleases and possibly microRNA targeting MYC-CRD. This binding to MYC mRNA of IGF2BP1 is enhanced by m6A-modification of the CRD (Huang et al., 2018). IGF2BP1 is also involved in posttranscriptional regulation of transcripts encoding proteins for cell adhesion, invasion, cytoplasmic spreading, and matrix remodeling (Stohr N et al., 2012).Using different colorectal cancer cells, it was furthermore shown that IGF2BP1 enters extracellular vesicles (EVs) of some of the cell lines in vitro using Western-Blot and Immuno-Electron Microscopy (Kuhn et al., 2022). In another study, it was shown that the knock-out of IGF2BP1 reduces the induction of melanoma metastasis via EVs compared to EVs from wild type melanoma cells in a mouse model by modulating the EV cargo (Ghoshal et al., 2019).The prior art document CN 115837079 A discloses the use of agents for targeting IGF2BP1 e.g. for cancer treatment. Such an agent could be a siRNA, an iRNA, a small molecule inhibitor BTYNB, or an antibody. However, only commercially available antibodies were used. The only disclosure of a specific IGF2BP1 antibody is in an experiment for analyzing the expression of IGF2BP1 in esophageal squamous cell carcinoma tissue and adjacent normal squamous epithelium using the IGF2BP1 antibody ab 184305 from Abeam (cf. paragraph

[0068] ). For this analysis the tissues were fixed with formalin and embedded in paraffin (cf. paragraph

[0067] ). The inventors found a cytoplasmic expression of IGF2BP1 in the tumor tissue and no expression in normal tissue (cf. paragraph

[0069] ). The inventors detected IGF2BP1 only in the cytoplasm of the tumor tissue cells and not on the cell surface.The prior art document CN 115961043 A discloses the use of a substance binding to IGF2BP1 or its target for diagnosis and treatment of multiple myeloma. Besides others, such a substance may be a small molecule chemical drug, an anti-IGF2BP1 antibody, or an antibody which binds to an IGF2BP1 target, especially an anti-CDC5L antibody. In Example 10, a cross-linking immunoprecipitation is described. Therein NCI-H929 cells were crosslinked by UV irradiation, lysed and the cell debris was removed. The resulting supernatant was incubated with the IGF2BP1 antibody NBP1 -79024 from Novus. The protein-antibody complex was then precipitated using Protein A / G Dynabeads, and the immunoprecipitated protein-RNA complexes released from the beads. No further IGF2BP1 specific antibody is mentioned in this application. A statement regarding a cellular localization of the IGF2BP1 bound by the used antibody is not possible.As said, IGF2BP1 plays a role in cancer and is therefore prima facie a potential target. However, due to its intracellular location, IGF2BP1 is prima facie not available as target for, e.g. antibodies. Accordingly, the prior art suggested, e.g. small molecules or molecules targeting IGF2BP1 mRNA.The pharmaceutical industry though is constantly looking for new targets for antibodybased therapies including chimeric antigen receptor-equipped immune cells for treating cancer. Indeed, there is a need in the art for the treatment of cancer by targeting new cancer targets.The present invention addresses this need and provides as a solution therefor a new cancer target for an antibody-based therapy as defined in the claims, described herein, exemplified in the Examples and illustrated in the Figures. The new cancer target for an antibody-based therapy is IGF2BP1 which was neither shown to be present on intact / non- permeabilized target cells nor thought to be accessible for an antibody-based therapy, since it is pursuant to common general knowledge an intracellularly located protein. Indeed, as described above, it was only detectable by antibodies if cells were lysed or permeabilized, i.e. , if cells were no longer intact or alive.SUMMARY OF THE INVENTIONThe present invention provides a pharmaceutical composition comprising a monoclonal antibody which binds to human IGF2BP1 present on the cell surface of a target cell and optionally a pharmaceutically acceptable carrier, diluent or excipient, wherein said target cell is a non-permeabilized cell or a living cell.Said antibody which binds to human IGF2BP1 present on the cell surface is not one of the antibodies 2C1 , 5H5, 10G7, 11 F2, 13B2, 15F11 , 17A10, 18G8, 19H9 (19G9), and 24B7 as published in WO 2022 / 123001 A1 . Antibody 19H9 was sometimes referred to as antibody 19G9 in WO 2022 / 123001 A1 and therefore mentioned herein as “19H9 (19G9)”.In one embodiment of the pharmaceutical composition of the present invention, said antibody has cytotoxic activity.In one further embodiment of the pharmaceutical composition of the present invention, said antibody has ADCC or CDC.In one embodiment of the pharmaceutical composition of the present invention, said antibody is conjugated with a cytotoxic substance or a substance used for in-vivo imaging.In one embodiment of the pharmaceutical composition of the present invention, said antibody is internalized from the target cell after binding to IGF2BP1 present on the cell surface.In one further embodiment of the pharmaceutical composition of the present invention, said antibody or a portion thereof is part of a chimeric antigen receptor (CAR). For said embodiment, it is preferred that said CAR is comprised by a T cell, NK cell, NK-T cell or macrophage.In one embodiment of the pharmaceutical composition of the present invention, said antibody is less than 20 % cross-reactive with IGF2BP1 -related proteins.In one further embodiment of the pharmaceutical composition of the present invention, said antibody is an antibody comprising a heavy chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 2.In one embodiment of the pharmaceutical composition of the present invention, said antibody is an antibody comprising a heavy chain variable region comprising heavy chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 3, heavy chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 4, and heavy chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 5, and a light chain variable region comprising light chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 6, light chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 7, and light chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 8.In one embodiment of the pharmaceutical composition of the invention, wherein the CAR mentioned above comprises the heavy chain variable region and the light chain variable region mentioned before or one or more of the CDR as mentioned before.In a further aspect, the present invention provides the pharmaceutical composition according to the present invention for use in an in-vivo diagnostic imaging method for diagnosing cancer.In a further aspect, the present invention provides the pharmaceutical composition according to the present invention for use in a method for the treatment of cancer in a human subject. It is preferred for said aspects that said cancer is characterized by cells, wherein human IGF2BP1 is present on their cell surface. It is also preferred for said aspects that said cancer is breast cancer, ovarian cancer, brain cancer, melanoma, non- small-cell-lung cancer, pancreatic cancer, colon cancer, colorectal cancer, mesenchymal cancer, Hodgkin lymphoma, B cell lymphomas, acute myeloid leukemia (AML) or acute lymphatic leukemia (ALL) of the T cell type. It is also preferred that said cancer is cervical cancer, colorectal adeno carcinoma, laryngeal squamous cell carcinoma, lung cancer, pancreatic adenocarcinoma, ovarian cancer, ovarian clear-cell carcinoma, acute myeloid leukemia (AML) or acute lymphatic leukemia (ALL) of the T cell type.In a further aspect, the present invention provides a method for determining whether a human subject may suffer from cancer, comprising determining in a sample obtained from said human subject whether IGF2BP1 is present on the cell surface of cells comprised by said sample. In further embodiments the used cells are non-permeabilized cells and / or living cells.In a further aspect, the present invention provides a method for determining whether a human subject may suffer from cancer, comprising determining in a sample obtained from said human subject whether IGF2BP1 is present on the surface of extracellular vesicles comprised by said sample.In a further aspect, the present invention provides an antibody which binds to human IGF2BP1 present on the cell surface of a target cell, wherein said antibody is an antibody comprising a heavy chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variableregion having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 2.In one embodiment of the said antibody of the present invention, said target cell is a non- permeabilized cell.In one embodiment of the said antibody of the present invention, said target cell is a living cell.In a further aspect, the present invention provides an antibody which binds to human IGF2BP1 present on the surface of an extracellular vesicle, wherein said antibody is an antibody comprising a heavy chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 2.In a further aspect, the present invention provides an antibody which binds to human IGF2BP1 present on the cell surface of a target cell comprising an antibody comprising a heavy chain variable region comprising heavy chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 3, heavy chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 4, and heavy chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 5, and a light chain variable region comprising light chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 6, light chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 7, and light chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 8.In one embodiment of the said antibody of the present invention, said target cell is a non- permeabilized cell.In one embodiment of the said antibody of the present invention, said target cell is a living cell.In a further aspect, the present invention provides an antibody which binds to human IGF2BP1 present on the surface of an extracellular vesicle comprising an antibody comprising a heavy chain variable region comprising heavy chain CDR1 having the aminoacid sequence as set forth in SEQ ID NO: 3, heavy chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 4, and heavy chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 5, and a light chain variable region comprising light chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 6, light chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 7, and light chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 8.In a further aspect, the invention relates to an antibody, which binds to human IGF2BP1 present on the cell surface of a target cell for use in a method of killing said target cell having IGF2BP1 present on the cell surface.In one embodiment, the antibody is an antibody comprising a heavy chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 2.In a further embodiment the antibody is an antibody comprising a heavy chain variable region comprising heavy chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 3, heavy chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 4, and heavy chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 5, and a light chain variable region comprising light chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 6, light chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 7, and light chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 8.In a further aspect the invention relates to a method of killing a target cell having IGF2BP1 present on the cell surface, comprising administering an antibody, which binds to human IGF2BP1 present on the cell surface of said target cell.In one embodiment of the method, said antibody is an antibody comprising a heavy chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 2.In a further embodiment of the method, said antibody is an antibody comprising a heavy chain variable region comprising heavy chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 3, heavy chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 4, and heavy chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 5, and a light chain variable region comprising light chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 6, light chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 7, and light chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 8.In a further aspect the invention relates to an antibody, which binds to human IGF2BP1 present on the cell surface of a target cell for use in a method for the treatment of cancer in a subject, comprising, prior to the treatment of cancer in said subject, determining whether a target cell of said subject has IGF2BP1 present on the cell surface.In one embodiment said antibody is an antibody comprising a heavy chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 2.In a further embodiment said antibody is an antibody comprising a heavy chain variable region comprising heavy chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 3, heavy chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 4, and heavy chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 5, and a light chain variable region comprising light chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 6, light chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 7, and light chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 8.In all the above aspects and embodiments, the antibody may be a monoclonal antibody.Furthermore, in all the above aspects and embodiments the antibody is not one of the antibodies 2C1 (Seq ID NO. 21 to 26 of WO 2022 / 123001 A1), 5H5 (SEQ ID NO. 27 to 32 of WO2022 / 123001 A1), 10G7 (SEQ ID NO. 33 to 38 of WO 2022 / 123001 A1), 11 F2 (SEQ ID NO. 39 to 44 of WO 2022 / 123001 A1), 13B2 (SEQ ID NO. 45 to 50 of WO 2022 / 123001 A1), 15F11 (SEQ ID NO. 51 to 56 of WO 2022 / 123001 A1), 17A10 (SEQ ID NO. 57 to 62 of WO 2022 / 123001 A1), 18G8 (SEQ ID NO. 63 to 68 of WO 2022 / 123001 A1), 19H9 (19G9) (SEQ ID NO. 69 to 74 of WO 2022 / 123001 A1), and 24B7 (SEQ ID NO. 75 to 80 of WO 2022 / 123001 A1) as published in WO 2022 / 123001 A1.BRIEF DESCRIPTION OF THE DRAWINGSFigure 1 shows that the antibody 12G5 precipitates IGF2BP1. Cyanogen bromide beads coupled with antibody 12G5 or with an isotype control antibody (negK) were incubated overnight with lysates from UWB1.289 ovarian cancer cells. After precipitation of the beads and incubation in Laemmli buffer, eluates were analyzed by mass spectrometry, which revealed a clear enrichment of IGF2BP1 with 12G5 as compared to the isotype control antibody (iso2a).Figure 2 shows that the antibody 12G5 precipitates IGF2BP1. Jurkat cell lysate were incubated overnight with 12G5 or an M BP-specific antibody (Iso contr.) coupled to cyanogen bromide beads. After precipitation of the beads and incubation in Laemmli buffer, eluates were separated by PAGE and an immunoblot with a commercial anti- IGF2BP1 antibody (#PA5-44886; Thermo Scientific) was performed, followed by incubation with an anti-rabbit HRP-labeled secondary antibody. The blot was developed with ECL.Figure 3 shows the surface expression of IGF2BP1 on various cancer cell lines, on primary cancer cells isolated from ascites of a patient with ovarian cancer (AS 77), and on primary T-cell acute lymphoblastic leukemia and acute myeloid leukemia cancer cells.(A) Cancer cell lines (A549, HT29, U251 , DAN, ES-2, HeLa, Capan-1 , and PCI-1 ) and primary cancer cells (AS 77) were incubated with12G5 (solid lines) or an isotype control antibody (gray histograms). Cells were then washed and incubated with an Alexa647 labeled anti-rat IgG antibody. Fluorescence was then measured by flow cytometry on a FACS Canto.(B) Primary cancer cells from patients with T-cell acute lymphoblastic leukemia (T-ALL; left) or acute myeloid leukemia (AML; right) were incubated with 12G5 (black line) or anisotype control antibody (tinted gray histograms). Cells were then washed and incubated with an Alexa647 labeled anti-rat IgG antibody. Fluorescence was finally measured by flow cytometry on a FACS Canto.(C) Primary hepatocytes and primary PBMCs were treated and analyzed as in (A). These normal cells do not express surface IGF2BP1 .Figure 4 shows that the level of IGF2BP1 on the surface of cancer cells is increased by hypoxia. HeLa cervical cancer cells and ES-2 and SK-OV-3 ovarian cancer cells were incubated in a humified atmosphere with 5% CO2 at normoxia (approx. 18% O2) or hypoxia (1 % O2) in standard cell culture medium for 72 hours. Then, surface IGF2BP1 was quantified by flow cytometry. For this, cells were incubated with 12G5 or an isotype control antibody, washed and then incubated with an Alexa647 labeled anti-rat IgG antibody. Finally, fluorescence was measured by flow cytometry (BD FACS Canto). Dashed line = hypoxia; solid line = normoxia, tinted grey histogram = isotype control.Figure 5 shows that 12G5 is IGF2BP1 -specific. Recombinant IGF2BP1 with a FLAGTAG protein (lane 1 ) and, as controls, recombinant ZG16B (lane 2) and recombinant BSA with a FLAG-TAG (lane 3) were separated by PAGE and blotted onto a PVDF membrane. The membrane was incubated with either antibody 12G5 (A) or with an anti-FLAG antibody (B), followed by incubation with an HRP-coupled suitable secondary antibody and finally developed with ECL.Figure 6 shows that 12G5 is IGF2BP1 -specific. 12G5 was coupled to beads and incubated with lysates from HEK293 cells transfected with an expression plasmid encoding IGF2BP1 -FLAG (lane 1 ) or with purified IGF2BP1 -FLAG protein (lane 3) and immunoprecipitated. As a control, lysates were incubated with an isotype antibody coupled to beads (lane 2). After precipitation, eluates in Laemmli buffer were separated by PAGE and blotted onto a PVDF membrane. The membrane was incubated with an anti-FLAG antibody, followed by incubation with an HRP-coupled anti-mouse secondary antibody and finally developed with ECL.Figure 7 shows that 12G5 is IGF2BP1 -specific. (A) wells of a polystyrene 96-well cluster plate were coated with 12G5 (5 pg / ml), a GST-specific control antibody, or with PBS, only, overnight at 4 °C. Then, wells were blocked with 3% bovine serum albumin (BSA), followed by addition of 10pg / well of recombinant IGF2BP1 protein with a FLAG-tag(IGF2BP1 -FLAG). The plate was then incubated at 4 °C for 3 h. Then, wells were washed several times with TBS / 0.1 % Tween and incubated with a FLAG-specific murine antibody (M2; Millipore) for 2 h, followed by incubation with an HRP-labeled anti-mouse antibody. Finally, wells were developed with TMB; the reaction was stopped with H2SO4 and the optical density (OD) at 450 nm was measured. (B) a 96-well cluster plate were coated with a serial dilution of either IGF2BP1 -FLAG or BSA-FLAG, blocked, and then incubated with 12G5 for 2 h, followed by incubation with a peroxidase-labeled anti-rat antibody. Finally, wells were developed with TMB; the reaction was stopped with H2SO4 and the optical density (OD) at 450 nm was measured.Figure 8 shows that 12G5 is IGF2BP1 -specific. SK-OV-3 cells were transfected with IGF2BP1 -specific siRNAs. Three days later, binding of the antibody 12G5 to knockdown and wildtype cells was measured by flow cytometry. For this, SK-OV-3 Wildtype (gray histogram; median fluorescence: 3.002) and the IGF2BP1 knockdown (bold line; median fluorescence: 768) were incubated with 12G5. Then, cells were washed and incubated with an Alexa647 labeled anti-rat secondary antibody. Fluorescence was then measured on a FACS Canto. An isotype control antibody was included as a negative control (dashed line).Figure 9 shows that 12G5 binds to the surface of living ovarian cancer cells.Figure 9 A: UWB1.289 cells were grown on microscope slides, washed in PBS, and incubated with the antibody 12G5 (left) or with Membrite 568 (Biotium Inc.; Fremont, CA) to stain cell surface proteins. Thereafter, cells were fixed with 4 % paraformaldehyde and, in the case of 12G5, incubated with an Alexa647-coupled suitable anti-rat IgG secondary antibody. Surface staining with 12G5 and a partial co-localization with Membrite 568 are clearly visible.Figure 9 B: SK-OV-3 cells were grown on microscope slides, washed in PBS, and incubated with the antibody 12G5 (left) or with Membrite 568 (Biotium Inc.; Fremont, CA) to stain cell surface proteins. Thereafter, cells were fixed with 4 % paraformaldehyde and, in the case of 12G5, incubated with an Alexa647-coupled suitable anti-rat IgG secondary antibody. Surface staining with 12G5 and a partial co-localization with Membrite 568 are clearly visible.Figure 9C shows that 12G5 co-localizes with the surface molecule CD81 . SK-OV-3 cells were cultivated on a cover slip, washed, and incubated with the antibodies 12G5 (left) and a commercial antibody targeting the membrane protein CD81 (right). Cells were thenfixed with 4% paraformaldehyde and analyzed by confocal fluorescence microscopy.Surface staining with 12G5 is clearly visible.Figure 10 shows that IGF2BP1 is released from tumor tissue on the surface of extracellular vesicles.Figure 10 A shows that IGF2BP1 is released via extracellular vesicles (EVs). EVs isolated from ascites fluid from four patients with ovarian cancer were isolated by established technologies comprising differential centrifugation, ultracentrifugation, and density gradient purification. 2 pl each of these EV preparations were then spotted onto pieces of nitrocellulose membrane and incubated with an anti-CD63 antibody (left) or 12G5 (right) at 4 °C overnight. After washing, the membrane was incubated with a secondary antibody (goat anti-rat IgG, coupled with horseradish peroxidase) for 2 hours and developed with ECL. It is evident that at least EVs from ascites #1 and #3) contain IGF2BP1.Figure 10 B shows that IGF2BP1 is expressed on the surface of extracellular vesicles (EVs). EVs contained in ascites fluid from patients with ovarian cancer were isolated via standard protocols for EV isolation via differential centrifugation (400 x g; 2,500 x g; 100,000 x g) followed by a purification by floatation into a density gradient. The wells of a polystyrene 96-well cluster plate were coated with 12G5 (5 pg / ml), a GST-specific control antibody (5 pg / ml) overnight at 4 °C. Then, wells were blocked with 3% bovine serum albumin (BSA), followed by addition of 10pg / well of EVs from 3 different donors. The plate was again incubated overnight at 4 °C. Then, wells were washed several times with TBS / 0.1 % Tween and incubated with an anti-CD63 antibody (CD63 is a protein expressed on most types of EVs), coupled with HRP. Finally, wells were developed with TMB; the reaction was stopped with H2SO4 and the optical density (OD) at 450 nm was measured.Figure 11 shows that the antibody 12G5 is internalized over time upon binding to cells. SK-OV-3 ovarian cancer cells were incubated with 12G5 at room temperature for 10 min and then washed to remove excess free antibody. Cell samples were then incubated at 37 °C for one to five hours or placed on ice (= 0 hour). Cells were then stained with an Alexa647-coupled secondary anti-rat IgG antibody and fluorescence was measured by flow cytometry. The decrease in fluorescence over time is indicative for the internalization of the IGF2BP1 -12G5 complex. The fluorescence measured after 0 hours at 37 °C wasset to 100%. Non-internalized antibodies can be used to e.g. deposit radionuclides at target cells over a long period of time.Figure 12 shows that 12G5 binds surface IGF2BP1 whereas commercial antibodies don’t. Human A549 cells analyzed by flow cytometry for the binding of the antibodies indicated above the histograms. Upper panel: do show binding to surface IGF2BP1 , living A549 cells were incubated with the indicated antibodies (black lines) or a suitable isotype control antibody (gray tinted histograms), followed by incubation with a suitable Alexa- 647 labeled secondary antibody. Finally, cells were analyzed by flow cytometry. Lower panel: do show binding to intracellular IGF2BP1 , A549 cells were fixed and permeabilized (Fix & Perm Cell Permeabilization Kit; Life Technologies) before staining with antibodies as above, followed by flow cytometric analysis.Figure 13 shows that the 12G5 Fab fragment is functional. A549 cells were incubated with the 12G5 Fab fragment (black line) or an isotype control Fab fragment (gray tinted histograms). Cells were then washed and incubated with an Alexa647 labeled anti-rat IgG antibody. Fluorescence was then measured by flow cytometry on a FACS Canto.)DESCRIPTION OF THE INVENTIONThe present invention provides in a first aspect a pharmaceutical composition comprising an antibody which binds to human IGF2BP1 present on the cell surface of a target cell and optionally a pharmaceutically acceptable carrier, diluent or excipient.The present invention thus comprises the finding that IGF2BP1 is present on the cell surface of (cancer) cells, especially on a non-permeabilized cell and / or living cell. Accordingly, a new therapy concept is possible. Until now the prior art characterizes IGF2BP1 as a cytoplasmic RNA binding protein.The rat monoclonal antibody (mAb) 12G5 against human IGF2BP1 was developed from immunizations using cancer cell derived extracellular vesicles (cf. example 1 ) that were carried out by the inventors in cooperation with the core facility 'Monoclonal Antibodies' at the Helmholtz Center Munich (HMGU). The inventors have proven the specificity of this mAb in various experiments of the present invention and much to their surprise this antibody was found to bind to the surface of various human tumor cell lines.Thus, the present invention is the first time that IGF2BP1 is described to be exposed on the surface of tumor cells. The mentioned antibody 12G5 specifically recognizes the IGF2BP1 on the surface of tumor cells and identifies IGF2BP1 as a novel tumor-specific target molecule for cancer therapy and detection. This finding paves the way for specifically targeting tumor cells and thus treating cancer which express IGF2BP1 on their cell surface, because otherwise IGF2BP1 is intracellularly localized and, thus, not amenable for an antibody-based therapy. Without being bound by theory, such an approach has the potential to be specific and / or provide for less undesired side effects, because in theory cells not expressing IGF2BP1 on their cell surface would not be targeted.This specific binding of the antibody 12G5 to human IGF2BP1 on the cell surface is confirmed in the experimental examples. Importantly, only the 12G5 antibody binds to IGF2BP1 on the cell surface in contrast to commercially available IGF2BP1 antibodies, e.g. the IGF2BP1 antibodies mentioned in CN 115961043 A and CN 115837079 A (cf. example 10 and figure 12). Thus, the commercially available antibodies tested fail to bind to IGF2BP1 on the cell surface of intact cells. That being so, the commercially available antibodies tested were able to bind to IGF2BP1 when cells were permeabilized (see figure 12). Without being bound by theory, the commercially available antibodies seem to bind to different epitopes compared to the 12G5 antibody.The antibodies 2C1 (Seq ID NO. 21 to 26 of WO 2022 / 123001 A1 ), 5H5 (SEQ ID NO. 27 to 32 of WO 2022 / 123001 A1 ), 10G7 (SEQ ID NO. 33 to 38 of WO 2022 / 123001 A1 ), 11 F2 (SEQ ID NO. 39 to 44 of WO 2022 / 123001 A1 ), 13B2 (SEQ ID NO. 45 to 50 of WO 2022 / 123001 A1 ), 15F11 (SEQ ID NO. 51 to 56 of WO 2022 / 123001 A1 ), 17A10 (SEQ ID NO. 57 to 62 of WO 2022 / 123001 A1 ), 18G8 (SEQ ID NO. 63 to 68 of WO 2022 / 123001 A1 ), 19H9 (19G9) (SEQ ID NO. 69 to 74 of WO 2022 / 123001 A1 ), and 24B7 (SEQ ID NO. 75 to 80 of WO 2022 / 123001 A1 ) as published in WO 2022 / 123001 A1 are no antibodies of the invention and not part of this invention. Thus, the antibodies 2C1 , 5H5, 10G7, 11 F2, 13B2, 15F11 , 17A10, 18G8, 19H9 (19G9), and 24B7 as published in WO 2022 / 123001 A1 are explicit disclaimed from the content of this invention.That said, once it is known, thanks to the present invention, that IGF2BP1 is present on the cell surface of cancer cells, it is possible to provide further antibodies againstIGF2BP1 present on the cell surface of cancer cells. Indeed, prior to the present invention it was common general knowledge that IGF2BP1 is intracellularly located. Hence, a skilled person would not have looked for IGF2BP1 on the cell surface. However, and indeed, those antibodies which were available in the prior art did not bind to IGF2BP1 on the cell surface as shown by the present inventors herein. Thus, even though a skilled person could have looked for IGF2BP1 on the cell surface of a cell, he would not have been able to do so, because the available antibodies would have failed to bind to IGF2BP1 on the cell surface.That said, once it is known that IGF2BP1 is present on the cell surface of cancer cells and, thanks to the present invention, antibodies are provided which bind to IGF2BP1 on the cell surface, it is not only possible to target IGF2BP on the cell surface of target cells, e.g. cancer cells, but it is also possible to provide further such antibodies. For example, cancer cells known to have IGF2BP1 present on their cell surface can be used for immunization of, e.g. rats or mice. Likewise, membrane fractions of such cell may be used for the immunization.The amino acid sequence of IGF2BP1 is known in the art (UniProt Q9NZI8). For example, the amino acid sequence of human IGF2BP1 is as set forth in SEQ ID NO: 9.The IGF2BP1 protein used in the present invention may be an IGF2BP1 protein having the sequence described above or may be a modified protein having an amino acid sequence derived from the sequence described above by the modification of one or more amino acids. Examples of the modified protein having a sequence derived from the sequence described above by the modification of one or more amino acids can include polypeptides having 70 % or more, preferably 80 % or more, more preferably 90 % or more, even more preferably 95 % or more homology to the amino acid sequence as set forth in SEQ ID NO: 9. Alternatively, partial peptides of these IGF2BP1 proteins may be used.Homology comparisons can be conducted by eye, or more usually, with the aid of readily available sequence comparison programs. These commercially available computer programs can calculate % homology between two or more sequences.% homology may be calculated over contiguous sequences, i.e. one sequence is aligned with the other sequence and each amino acid in one sequence is directly compared with the corresponding amino acid in the other sequence, one residue at a time. This is called an “ungapped” alignment. Typically, such ungapped alignments are performed only over a relatively short number of residues (for example, less than 50 contiguous amino acids).The IGF2BP1 protein used in the present invention is not limited by its origin and is preferably a human IGF2BP1 protein.The term “antibody” as used herein and in the context of the present invention may comprise chimeric antibodies, humanized antibodies, monovalent antibodies, polyvalent antibodies, low-molecular antibodies, a diabody, a Fab fragment, or a scFv.Chimeric antibodies refer to antibodies comprising variable and constant regions of different origins ligated with each other. For example, mouse-human heterogeneous chimeric antibodies are antibodies comprising the heavy and light chain variable regions of a mouse antibody and the heavy and light chain constant regions of a human antibody. Mouse antibody variable region-encoding DNAs are ligated with human antibody constant region-encoding DNAs, and the ligation products can be incorporated into expression vectors to prepare chimeric antibody-expressing recombinant vectors. Cells transformed with these vectors (recombinant cells) can be cultured for the expression of the DNA insert to obtain the chimeric antibodies produced during the culture.In general, the chimeric antibodies comprise non-human animal-derived antibody variable regions and human antibody-derived constant regions. By contrast, the humanized antibodies comprise non-human animal-derived antibody complementarity-determining regions (CDRs), human antibody-derived framework regions (FRs), and human antibody- derived constant regions. The humanized antibodies are also called reshaped human antibodies. Specifically, for example, humanized antibodies comprising non-human animal (e.g., mouse) antibody CDRs grafted in human antibodies are known in the art. The humanized antibodies are useful as active ingredients for a therapeutic agent of the present invention, owing to their reduced antigenicity in the human body.Each antibody variable region usually comprises 3 CDRs flanked by 4 FRs. The CDR regions substantially determine the binding specificity of the antibody. The CDRs havediverse amino acid sequences. On the other hand, amino acid sequences constituting the FRs often exhibit high homology among antibodies having different binding specificities. Therefore, in general, the binding specificity of a certain antibody can allegedly be transplanted to other antibodies through CDR grafting.The antibody present in a pharmaceutical composition of the present invention may encompass bivalent antibodies typified by IgG (lgG1 , lgG2, lgG-4, etc.) and also monovalent antibodies or polyvalent antibodies typified by IgM as long as these antibodies bind to the IGF2BP1 protein. The polyvalent antibody that may be present in the pharmaceutical composition of the present invention may encompass polyvalent antibodies having antigen-binding sites, all of which are the same as each other or some or all of which are different from each other.The antibody present in the pharmaceutical composition of the present invention may also be a low-molecular antibody that encompasses an antibody fragment deficient in a portion of the whole antibody (e.g., whole IgG). Such partial deficiency of the antibody molecule is accepted as long as the resultant antibody fragment is capable of binding to the IGF2BP1 . It is preferred that the antibody fragment employed in the pharmaceutical composition according to the present invention should contain one or both of heavy chain variable (VH) and light chain variable (VL) regions. It is also preferred that the antibody fragment employed in the pharmaceutical composition according to the present invention should contain CDRs. The number of CDRs contained in the antibody fragment employed in the pharmaceutical composition of the present invention is not particularly limited and is preferably at least 6 CDRs: heavy chain CDR1 , CDR2, and CDR3 and light chain CDR1 , CDR2, and CDR3.The amino acid sequence of VH or VL can contain one or more substitution, deletion, addition, and / or insertion. Furthermore, the antibody or antibody fragment that may be employed in the pharmaceutical composition of the present invention may be deficient in a portion of one or both of VH and VL as long as the resultant antibody fragment is capable of binding to the human IGF2BP1. Moreover, its variable region may be chimerized or humanized. Specific examples of the antibody fragment can include Fab, Fab’, F(ab’)2, and Fv. Moreover, specific examples of the low-molecular antibody can include Fab, Fab’, F(ab’)2, Fv, scFv (single chain Fv), diabody, sc(Fv)2 (single chain (Fv)2), and scFv-Fc. In the present invention, the low-molecular antibody is preferably adiabody or sc(Fv)2. These antibody multimers (e.g., dimers, trimers, tetramers, and polymers) are also encompassed by the low-molecular antibody that may be employed in the pharmaceutical composition of the present invention.The term “diabody” as used herein and in the context of the present invention may refer to a bivalent antibody fragment constructed by gene fusion. The diabody is a dimer comprising two polypeptide chains. Usually, each of the polypeptide chains constituting the dimer comprises heavy and light chain variable regions linked via a linker on the same chain. The linker in the diabody is generally too short to allow paring between heavy and light chain variable regions on the same chain. Specifically, the number of amino acid residues constituting the linker is, for example, approximately 5 residues. Therefore, heavy and light chain variable regions encoded on the same polypeptide chain cannot together form a single chain variable region fragment. Instead, they form a dimer by pairing with another single chain variable region fragment. As a result, the diabody has two antigen-binding sites.The scFv, as used in the context of the present invention, may be obtained by linking heavy and light chain variable regions of the antibody. In the scFv, the heavy and light chain variable regions are linked via a linker, preferably, a peptide linker. The heavy and light chain variable regions in the scFv can be derived from any of the antibodies described in the present specification. The peptide linker that links the variable regions is not particularly limited. For example, an arbitrary single chain peptide of approximately 3 to 25 residues can be used as the linker.The antibody as used in the pharmaceutical composition and the antibody according to the present invention may also encompass binding entities, such as lipocalins, an aptamer or an anticalin.The antibody, which binds to human IGF2BP1 , used in the present invention can have various formats. However, it needs to bind to the IGF2BP1 protein and is not particularly limited by its origin, type, shape, etc., but may have a cytotoxic activity. Specifically, an antibody can be used, such as a non-human animal-derived antibody (e.g., a mouse, rat, or camel antibody), a human-derived antibody, a chimeric antibody, or a humanized antibody as described above. The antibody, which binds to human IGF2BP1 used in the present invention is a monoclonal antibody.The antibody which binds to human IGF2BP1 used in the present invention can be obtained as a polyclonal or monoclonal antibody using means known in the art. The antibody used in the present invention is in particular preferably a mammal-derived monoclonal antibody. The mammal-derived monoclonal antibody encompasses, for example, those produced by hybridomas and those produced by hosts transformed with expression vectors containing an antibody gene by a genetic engineering approach.The antibody which binds to human IGF2BP1 on the cell surface may be modified with various molecules such as polyethylene glycol (PEG). Further, the antibody which binds to human IGF2BP1 may also be modified with a chemotherapeutic agent, a radioactive chemical, or the like, having a cytotoxic activity. The antibody which binds to human IGF2BP1 may be also modified with a substance used for diagnostic purposes, e.g. a radioactive chemical, a magnetic chemical, or a fluorescence moiety.The antibody which binds to human IGF2BP1 on the cell surface and which is used in the present invention is not one of the antibodies 2C1 , 5H5, 10G7, 11 F2, 13B2, 15F11 , 17A10, 18G8, 19H9 (19G9), and 24B7 as published in WO 2022 / 123001 A1.Specific examples of the antibody used in the present invention, which recognizes IGF2BP1 present on the cell surface of a target cell and binds thereto, may include the antibodies given and described herein. However, such an antibody is not one of the antibodies 2C1 , 5H5, 10G7, 11 F2, 13B2, 15F11 , 17A10, 18G8, 19H9 (19G9), and 24B7 as published in WO 2022 / 123001 A1.As described above, the antibody of the present invention or as used in the pharmaceutical composition of the present invention including the substitution, deletion, addition, and / or insertion of one or more amino acids is also incorporated in the scope of the present invention and may be prepared or occur naturally. Examples of a method for introducing a mutation in the polypeptide include site-directed mutagenesis (Hashimoto- Gotoh, T. et al., 1995) (Zoller, MJ, and Smith, M., 1983) (Kramer, W. et al., 1984) (Kramer W, and Fritz HJ, 1987) (Kunkel, TA, 1985). This is one of the methods well known by those skilled in the art for preparing a polypeptide functionally equivalent to a certain polypeptide. Those skilled in the art can appropriately introduce a mutation in the antibody of the present invention or the antibody as used in the composition of the presentinvention using such a method and thereby prepare an antibody functionally equivalent to such antibody. Moreover, amino acid mutations may occur in the natural world. Such an antibody that has an amino acid sequence derived from the amino acid sequence of the antibody of the present invention or the antibody as used in the composition of the present invention comprising the mutation of one or more amino acids, is functionally equivalent or a variant to the antibody and is also encompassed by the antibody of the present invention or the antibody as used in the pharmaceutical composition of the present invention.The number of amino acids mutated in such a variant is usually within 50 amino acids, preferably within 30 amino acids, more preferably within 10 amino acids (e.g., within 5 amino acids).For amino acid residues to be mutated, it is preferred that this mutation should be performed conservatively between amino acids having the same side chain property. For example, the following classification based on the properties of amino acid side chains has been established: hydrophobic amino acids (A, I, L, M, F, P, W, Y, and V), hydrophilic amino acids (R, D, N, C, E, Q, G, H, K, S, and T), amino acids having an aliphatic side chain (G, A, V, L, I, and P), amino acids having a hydroxy group-containing side chain (S, T, and Y), amino acids having a sulfur atom-containing side chain (C and M), amino acids having a side chain containing carboxylic acid and amide (D, N, E, and Q), amino acids having a base-containing side chain (R, K, and H), and amino acids having an aromatic group-containing side chain (H, F, Y, and W) (all symbols within the parentheses represent single letter codes of amino acids).A polypeptide having an amino acid sequence modified from a certain amino acid sequence by the deletion and / or addition of one or more amino acid residue(s) and / or the substitution thereof by other amino acids is already known to maintain the biological activity of the original polypeptide (Mark, DF et al., 1984; Wang, A. et al., 1984; Dalbadie- McFarland G. et a / ., 1982; Zoller MJ et al., 1982). Specifically, when amino acids in an amino acid sequence constituting a certain polypeptide are substituted by amino acids classified in the same group thereas, it is generally said that the polypeptide is likely to maintain its activity. In the present invention, the substitution between amino acids within the same amino acid group described above is referred to as conservative substitution.The term “surface” or specifically “cell surface” as used herein means the cell membrane. The cell membrane, which may also be known as plasma membrane, is the thin membrane that surrounds every living cell, delimiting the cell from the environment around it. Enclosed by this cell membrane are the cell’s constituents, often large, water- soluble, highly charged molecules such as proteins, nucleic acids, carbohydrates, and substances involved in cellular metabolism. The cell membrane, therefore, has two functions: first, to be a barrier keeping the constituents of the cell in and unwanted substances out and, second, to be a gate allowing transport into the cell of essential nutrients and removal of waste products from the cell. ER-derived vesicles may also participate in the building or formation of the cell membrane.The term “target cell”, as used within the context of the present invention, is preferably a cancer cell, especially a non-permeabilized cell and / or living cell. The term “cancer”, as used herein, can comprise any one or more of the following: acute lymphocytic leukemia (ALL), acute myeloid leukemia (AML), adrenocortical cancer, anal cancer, bladder cancer, blood cancer, bone cancer, brain tumor, breast cancer, cancer of the female genital system, cancer of the male genital system, central nervous system lymphoma, cervical cancer, childhood rhabdomyosarcoma, childhood sarcoma, chronic lymphocytic leukemia (CLL), chronic myeloid leukemia (CML), colon and rectal cancer, colon cancer, endometrial cancer, endometrial sarcoma, esophageal cancer, eye cancer, gallbladder cancer, gastric cancer, gastrointestinal tract cancer, hairy cell leukemia, head and neck cancer, hepatocellular cancer, Hodgkin’s disease, hypopharyngeal cancer, Kaposi’s sarcoma, kidney cancer, laryngeal cancer, leukemia, liver cancer, lung cancer, malignant fibrous histiocytoma, malignant thymoma, melanoma, mesothelioma, multiple myeloma, myeloma, nasal cavity and paranasal sinus cancer, nasopharyngeal cancer, nervous system cancer, neuroblastoma, non-Hodgkin’s lymphoma, oral cavity cancer, oropharyngeal cancer, osteosarcoma, ovarian cancer, pancreatic cancer, parathyroid cancer, penile cancer, pharyngeal cancer, pituitary tumor, plasma cell neoplasm, primary CNS lymphoma, prostate cancer, rectal cancer, respiratory system, retinoblastoma, salivary gland cancer, skin cancer, small intestine cancer, soft tissue sarcoma, stomach cancer, testicular cancer, thyroid cancer, urinary system cancer, uterine sarcoma, vaginal cancer, vascular system, Waldenstrom’s macroglobulinemia and Wilms’ tumor. Preferred as target cells are cancer cells from breast cancer, ovarian cancer, brain cancer, melanoma, non-small-cell-lung cancer, pancreatic cancer, colon cancer, colorectal cancer, mesenchymal cancer, Hodgkin lymphoma, B cell lymphomas, acute myeloidleukemia (AML) or acute lymphatic leukemia (ALL) of the T cell type. Also preferred as target cells are cancer cells from cervical cancer, colorectal adeno carcinoma, laryngeal squamous cell carcinoma, lung cancer, pancreatic adenocarcinoma, ovarian cancer, ovarian clear-cell carcinoma, acute myeloid leukemia (AML) or acute lymphatic leukemia (ALL) of the T cell type.The term “pharmaceutically acceptable carrier, diluent or excipient” as used in the context of the present invention, may comprise any pharmaceutically acceptable carrier, diluent or excipient for a pharmaceutical composition known by the person skilled in the art. It will be understood that such antibodies or pharmaceutical composition as described herein may be mixed with carriers or diluents, which will not interfere with the intended purpose of the present invention. For example, such a carrier as used within the present invention may be a carrier protein, such as bovine serum albumin (BSA) or keyhole limpet hemocyanin (KLH).In one embodiment of the pharmaceutical composition of the present invention, said antibody has cytotoxic activity.In the context of the present invention, the phrase “cytotoxic activity” refers to having an IGF2BP1 binding activity and may also include to have an activity equivalent to that of the antibody of the present invention. In the present invention, the equivalent activity is not necessarily required to be an identical activity and may be, for example, 50% or more, preferably 70% or more, more preferably 90% or more activity compared with the activity of the antibodies (a) or (b) as described herein. Examples of the upper limit of the activity can include, but is not particularly limited to, 1000% or less, 500% or less, 300% or less, 150% or less, and 100% or less.In one further embodiment of the pharmaceutical composition of the present invention, said antibody has ADCC or CDC.Thus, examples of the cytotoxic activity according to the present invention can include ADCC and CDC activities. In the context of the present invention, the ADCC activity means the activity of damaging target cells through the binding of Fey receptor-bearing cells (immunocytes, etc.) via the Fey receptors to the Fc domains of antibodies specifically attached to the cell surface antigens of the target cells. On the other hand, the CDC activity means a cytotoxic activity mediated by the complement system. Whether or notthe antibody has an ADCC activity or has a CDC activity can be determined by a method known in the art.Thus, the antibody employed in the pharmaceutical composition of the present invention may have activities such as an ADCC activity and as such, may be useful as a pharmaceutical drug, preferably, an anti-cancer agent, wherein the cancer is e.g. breast cancer, ovarian cancer, brain cancer, melanoma, non-small-cell-lung cancer, pancreatic cancer, colon cancer, colorectal cancer, mesenchymal cancer, Hodgkin lymphoma, B cell lymphomas, cervical cancer, colorectal adeno carcinoma, laryngeal squamous cell carcinoma, lung cancer, pancreatic adenocarcinoma, ovarian clear-cell carcinoma, acute myeloid leukemia (AML) or acute lymphatic leukemia (ALL) of the T cell type.In one embodiment of the pharmaceutical composition of the present invention, said antibody is conjugated with a cytotoxic substance or a substance used for in-vivo imaging.In one preferred embodiment of the pharmaceutical composition, the antibody may be conjugated with a cytotoxic substance, such as a chemotherapeutic agent, a toxic peptide, or a radioactive chemical. Such a modified antibody (hereinafter, referred to as an antibody conjugate) can be obtained by chemically modifying the obtained antibody. A method for the antibody modification has already been established in the art.Examples of the chemotherapeutic agent whose cytotoxic activity functions through the conjugation to the antibody that binds IGF2BP1 can include the following chemotherapeutic agents: azaribine, anastrozole, azacytidine, bleomycin, bortezomib, bryostatin-1 , busulfan, camptothecin, 10-hydroxycamptothecin, carmustine, celebrex, chlorambucil, cisplatin, irinotecan, carboplatin, cladribine, cyclophosphamide, cytarabine, dacarbazine, docetaxel, dactinomycin, daunomycin glucuronide, daunorubicin, dexamethasone, diethylstilbestrol, doxorubicin, doxorubicin glucuronide, epirubicin, ethinyl estradiol, estramustine, etoposide, etoposide glucuronide, floxuridine, fludarabine, flutamide, fluorouracil, fluoxymesterone, gemcitabine, hydroxyprogesterone caproate, hydroxyurea, idarubicin, ifosfamide, leucovorin, lomustine, mechlorethamine, medroxyprogesterone acetate, megestrol acetate, melphalan, mercaptopurine, methotrexate, mitoxantrone, mithramycin, mitomycin, mitotane, phenylbutyrate, prednisone, procarbazine, paclitaxel, pentostatin, semustine, streptozocin, tamoxifen, taxanes, taxol, testosterone propionate, thalidomide, thioguanine, thiotepa, teniposide, topotecan, uracil mustard, vinblastine, vinorelbine, vincristine.The chemotherapeutic agent is preferably a low-molecular chemotherapeutic agent. The low-molecular chemotherapeutic agent is unlikely to interfere with the antibody even after its conjugation to the antibody. The low-molecular chemotherapeutic agent usually has a molecular weight of 100 to 2000, preferably 200 to 1000. All of the chemotherapeutic agents exemplified above are low-molecular chemotherapeutic agents. These chemotherapeutic agents encompass prodrugs that are converted in vivo to active chemotherapeutic agents. The prodrug activation may be an enzymatic conversion or a non-enzymatic conversion. Examples of toxic peptides are snake venom peptides comprising Three-Finger Toxins (3FTxs), a disintegrin, a Kunitz-type inhibitor, a natriuretic peptide, or a Sarafotoxin as reviewed in Munawar et al., 2018. Further examples are a trypsin inhibitor, an islanditoxin, a pallotoxin, or an amatoxin as mentioned in Khan et al., 2018.Examples of a radioactive chemical are chemicals having a cytotoxic radionuclide, such radionuclide could be for example iodine-131 , indium-111 , yttrium-90, lutetium-177, actinium-225, gallium-68, or bismuth-213 as reviewed in Hofland et al., 2022 and Martiniova et al., 2022. The antibody coupled to the cytotoxic substance could be used for delivering the cytotoxic substance specifically to the target cell which may reduce unwanted side effects.The antibody could also be coupled to a substance used for in-vivo imaging. Such substances are for example diagnostic used radionuclides, like technetium-99m, fluor-18, carbon-11 , nitrogen-13, oxygen-15, or iodide-124 (cf. e.g. Bhattacharyya et al., 2011 , Martiniova etal., 2022). Further examples of such substances are gadolinium, a magnetic metal particle, or a fluorophore.In one embodiment of the pharmaceutical composition of the present invention, said antibody is internalized by the target cell after binding to IGF2BP1 present on the cell surface. This feature of the antibody gives interesting therapy options. For example, the antibody coupled with the cytotoxic substance, like a drug or a radionuclide, could be used to deliver the cytotoxic substance into the target cell after binding to IGF2BP1 on the surface of the target cell.In one further embodiment of the pharmaceutical composition of the present invention, said antibody or a part thereof is part of a chimeric antigen receptor (CAR). This means,that the heavy and light chain variable region or one or more of the CDR sequences of the antibody may be used for constructing the CAR. For said embodiment, it is preferred that said CAR is comprised by a T cell, NK cell, NK-T cell or macrophage. Chimeric antigen receptors (CARs, also known as chimeric immunoreceptors, chimeric T cell receptors or artificial T cell receptors) are receptor proteins that have been engineered to give T cells, NK cells, NK-Ts cell or macrophages the ability to target a specific protein.In one embodiment of the pharmaceutical composition of the present invention, said antibody is less than 20% cross-reactive with IGF2BP1 -related proteins. This means preferably that said antibody is less than 20 % cross-reactive with other IGF2 binding proteins such as IGF2BP2 or IGF2BP3. More preferably, said antibody is less than 15 % cross-reactive with IGF2BP1 -related proteins, e.g. IGF2BP2 or IGF2BP3. Even more preferably, said antibody is less than 10 % cross-reactive with IGF2BP1 -related proteins, e.g. IGF2BP2 or IGF2BP3. Even more preferably, said antibody is less than 5 % cross- reactive with IGF2BP1 -related proteins, e.g. IGF2BP2 or IGF2BP3. Even more preferably, said antibody is less than 3 % cross-reactive with IGF2BP1 -related proteins, e.g. IGF2BP2 or IGF2BP3. Even more preferably, said antibody is less than 2 % cross- reactive with IGF2BP1 -related proteins, e.g. IGF2BP2 or IGF2BP3. Even more preferably, said antibody is less than 1 % cross-reactive with IGF2BP1 -related proteins, e.g. IGF2BP2 or IGF2BP3.In one embodiment of the pharmaceutical composition of the present invention, said antibody is an antibody comprising a heavy chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 2.In one preferred embodiment of the pharmaceutical composition of the present invention, said antibody is an antibody comprising a heavy chain variable region having an amino acid sequence with at least 90% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 90% identity to the amino acid sequence shown in SEQ ID NO: 2.In one more preferred embodiment of the pharmaceutical composition of the present invention, said antibody is an antibody comprising a heavy chain variable region havingan amino acid sequence with at least 95% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 95% identity to the amino acid sequence shown in SEQ ID NO: 2.In one even more preferred embodiment of the pharmaceutical composition of the present invention, said antibody is an antibody comprising a heavy chain variable region having an amino acid sequence with at least 99% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 99% identity to the amino acid sequence shown in SEQ ID NO: 2.In one embodiment of the pharmaceutical composition of the present invention, said antibody is an antibody comprising a heavy chain variable region comprising heavy chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 3, heavy chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 4, and heavy chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 5, and a light chain variable region comprising light chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 6, light chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 7, and light chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 8.The antibody as used in the pharmaceutical composition of the present invention and as described herein may contain constant regions. The constant regions used are not particularly limited, and any constant region may be used. Preferable examples of the constant regions used in the present invention can include human-derived constant regions. For example, a human lgG1 -derived, human lgG2-derived, human lgG3-derived, or human lgG4-derived constant region can be used as a heavy chain constant region. Also, for example, human K chain-derived or human A chain-derived constant region can be used as a light chain constant region. The constant regions used in the present invention may be constant regions having a native sequence or may be modified constant regions having a sequence derived from the native sequence by the modification of one or more amino acids.The antibody as used in the pharmaceutical composition of the present invention and as described herein may also contain FRs. The FRs used are not particularly limited, and any FR may be used as long as the resulting antibody maintains its binding activity to human IGF2BP1 present on the cell surface of a target cell. Preferable examples of theFRs used in the present invention can include human antibody-derived FRs. Since the technique of FR replacement with the antigen binding activity of an antibody maintained is known in the art, those skilled in the art can appropriately select FRs. The FRs used in the present invention may be FRs having a native sequence or may be FRs having a sequence derived from the native sequence by the modification of one or more amino acids.Provided that a candidate antibody can bind to human IGF2BP1 present on the cell surface of a target cell by at least 80%, preferably at least 85%, more preferably at least 90%, even more preferably at least 95%, compared to the binding activity obtained in a control test performed in the absence of the candidate antibody, this candidate antibody is determined as an antibody that binds to substantially the same epitope as that to which the antibody of the present invention binds or to which the antibody used in the pharmaceutical composition binds.In a further aspect, the present invention provides the pharmaceutical composition according to the present invention for use in an in-vivo diagnostic imaging method for diagnosing cancer. The imaging method comprises the binding of the antibody of the invention to IGF2BP1 on the cell surface. Since a tissue, like a cancer tissue, comprises cells, e.g. cancer cells, it is possible to detect IGF2BP1 on the surface of these cancer cells in a human body by using known diagnostic imaging methods and the inventive antibody. Such imaging methods may be a scintigraphy, a single photon emission computed tomography (SPECT), a positron emission tomography (PET), or a use of a gamma camera wherein the antibody according to the invention coupled to a suitable radionuclide is used. A further exemplary imaging method is magnetic resonance imaging (MRI) using the antibody according to the invention coupled to a gadolinium or a magnetic metal particle. Another exemplary imaging method is image-guided surgery using the antibody of the invention coupled for example to a fluorescence moiety or a radionuclide. The methods mentioned above maybe coupled with a computer tomography (CT). Said cancer is preferred a breast cancer, an ovarian cancer, a brain cancer, melanoma, a non- small-cell-lung cancer, a pancreatic cancer, a colon cancer, a colorectal cancer, a mesenchymal cancer, a Hodgkin lymphoma, B cell lymphomas, an acute myeloid leukemia (AML) or an acute lymphatic leukemia (ALL) of the T cell type. It is further preferred that said cancer is cervical cancer, colorectal adeno carcinoma, laryngeal squamous cell carcinoma, lung cancer, pancreatic adenocarcinoma, ovarian cancer, orovarian clear-cell carcinoma, acute myeloid leukemia (AML) or acute lymphatic leukemia (ALL) of the T cell type.In a further aspect, the present invention provides the pharmaceutical composition according to the present invention for use in a method for the treatment of cancer in a human subject. It is preferred for said embodiment that said cancer is characterized by cells, wherein human IGF2BP1 is present on their cell surface. It is also preferred for said embodiment that said cancer is breast cancer, ovarian cancer, brain cancer, melanoma, non-small-cell-lung cancer, pancreatic cancer, colon cancer, colorectal cancer, mesenchymal cancer, Hodgkin lymphoma, B cell lymphomas, acute myeloid leukemia (AML) or acute lymphatic leukemia (ALL) of the T cell type. It is further preferred that said cancer is cervical cancer, colorectal adeno carcinoma, laryngeal squamous cell carcinoma, lung cancer, pancreatic adenocarcinoma, ovarian cancer, or ovarian clearcell carcinoma, acute myeloid leukemia (AML) or acute lymphatic leukemia (ALL) of the T cell type.The pharmaceutical composition according to the present invention can be administered by standard routes. These include, but are not limited to: oral, rectal, ophthalmic (including intravitreal or intracameral), nasal, topical (including buccal and sublingual), intrauterine, vaginal or parenteral (including subcutaneous, intraperitoneal, intramuscular, intravenous, intradermal, intracranial, intratracheal, and epidural) transdermal, intraperitoneal, intracranial, intracerebroventricular, intracerebral, intravaginal, intrauterine, or parenteral (e.g., intravenous, intraspinal, subcutaneous or intramuscular) routes.The present invention also comprises a method of treating cancer, wherein the method comprises administering a therapeutically effective amount of the pharmaceutical composition according to the present invention to a human subject. It is preferred for said embodiment that said cancer is characterized by cells, wherein human IGF2BP1 is present on their cell surface. It is also preferred for said embodiment that said cancer is breast cancer, ovarian cancer, brain cancer, melanoma, non-small-cell-lung cancer, pancreatic cancer, colon cancer, colorectal cancer, mesenchymal cancer, Hodgkin lymphoma, B cell lymphomas, acute myeloid leukemia (AML) or acute lymphatic leukemia (ALL) of the T cell type. It is further preferred that said cancer is cervical cancer, colorectal adeno carcinoma, laryngeal squamous cell carcinoma, lung cancer, pancreaticadenocarcinoma, ovarian cancer, ovarian clear-cell carcinoma, acute myeloid leukemia (AML) or acute lymphatic leukemia (ALL) of the T cell type.Further, the present invention comprises a method of treating cancer, wherein the method comprises administering a therapeutically effective amount of the antibody used in the pharmaceutical composition according to the present invention to a human subject. It is preferred for said embodiment that said cancer is characterized by cells, wherein human IGF2BP1 is present on their cell surface. It is also preferred for said embodiment that said cancer is breast cancer, ovarian cancer, brain cancer, melanoma, non-small-cell-lung cancer, pancreatic cancer, colon cancer, colorectal cancer, mesenchymal cancer, Hodgkin lymphoma, B cell lymphomas, acute myeloid leukemia (AML) or acute lymphatic leukemia (ALL) of the T cell type. It is further preferred that said cancer is cervical cancer, colorectal adeno carcinoma, laryngeal squamous cell carcinoma, lung cancer, pancreatic adenocarcinoma, ovarian cancer, ovarian clear-cell carcinoma, acute myeloid leukemia (AML) or acute lymphatic leukemia (ALL) of the T cell type.The present invention also provides a method of treating cancer, wherein the method comprises administering a therapeutically effective amount of the antibody according to the present invention as described herein to a human subject. It is preferred for said embodiment that said cancer is characterized by cells, wherein human IGF2BP1 is present on their cell surface. It is also preferred for said embodiment that said cancer is breast cancer, ovarian cancer, brain cancer, melanoma, non-small-cell-lung cancer, pancreatic cancer, colon cancer, colorectal cancer, mesenchymal cancer, Hodgkin lymphoma, B cell lymphomas, acute myeloid leukemia (AML) or acute lymphatic leukemia (ALL) of the T cell type. It is further preferred that said cancer is cervical cancer, colorectal adeno carcinoma, laryngeal squamous cell carcinoma, lung cancer, pancreatic adenocarcinoma, ovarian cancer, ovarian clear-cell carcinoma, acute myeloid leukemia (AML) or acute lymphatic leukemia (ALL) of the T cell type. The antibodies 2C1 , 5H5, 10G7, 11 F2, 13B2, 15F11 , 17A10, 18G8, 19H9 (19G9), and 24B7 as published in WO 2022 / 123001 A1 are no antibodies according to the present invention.The term “therapeutically effective amount” refers to an amount of the antibody or pharmaceutical composition according to the present invention or drug effective to “treat” cancer in the human subject. Specifically, in the case of cancer, the therapeutically effective amount of the antibody / pharmaceutical composition / drug can reduce thenumber of cancer cells; reduce the tumor size; inhibit or stop cancer cell infiltration into peripheral organs; inhibit and stop tumor metastasis; inhibit and stop tumor growth; relieve to some extent one or more of the symptoms associated with the cancer, or a combination of such effects on cancer cells. To the extent the antibody / pharmaceutical composition / drug prevents the growth and / or kills existing cancer cells, it can be referred to as cytostatic and / or cytotoxic.The present invention also covers the use of the pharmaceutical composition according to the present invention for the manufacture of a medicament for the treatment of cancer.In one embodiment, the present invention also covers the use of an antibody of the pharmaceutical composition according to the present invention and as described herein for the manufacture of a medicament for the treatment of cancer. The antibodies 2C1 , 5H5, 10G7, 11 F2, 13B2, 15F11 , 17A10, 18G8, 19H9 (19G9), and 24B7 as published in WO 2022 / 123001 A1 are no antibodies according to the present invention.In one further embodiment, the present invention also covers the use of an antibody according to the present invention and as described herein for the manufacture of a medicament for the treatment of cancer. The antibodies 2C1 , 5H5, 10G7, 11 F2, 13B2, 15F11 , 17A10, 18G8, 19H9 (19G9), and 24B7 as published in WO 2022 / 123001 A1 are no antibodies according to the present invention.Terms such as “treating” or “treatment” or “to treat” refer to both 1 ) therapeutic measures that cure, slow down, lessen symptoms of, and / or halt progression of a diagnosed pathologic condition or disorder and 2) prophylactic or preventative measures that prevent or slow the development of a targeted pathologic condition or disorder. Thus, those in need of treatment include those already with the disorder; those prone to have the disorder; and those in whom the disorder is to be prevented. A subject is successfully “treated” according to the methods of the present invention or with the pharmaceutical composition or antibody according to the present invention if the patient shows one or more of the following: a reduction in the number of or complete absence of cancer cells; a reduction in the tumor size; inhibition of or an absence of cancer cell infiltration into peripheral organs including the spread of cancer into soft tissue and bone; inhibition of or an absence of tumor metastasis; inhibition or an absence of tumor growth; relief of oneor more symptoms associated with the specific cancer; reduced morbidity and mortality; and improvement in quality of life.The antibody to be administered to humans can also be converted to a genetically recombinant antibody that has been engineered artificially, for example, for the purpose of reducing heteroantigenicity in humans. The genetically recombinant antibody encompasses, for example, chimeric antibodies and humanized antibodies as defined herein. These engineered antibodies can be produced using a method known in the art. The antibodies 2C1 , 5H5, 10G7, 11 F2, 13B2, 15F11 , 17A10, 18G8, 19H9 (19G9), and 24B7 as published in WO 2022 / 123001 A1 are no antibodies to be administered according to the present invention.In a further aspect, the present invention provides a method for determining whether a human subject may suffer from cancer, comprising determining in a sample obtained from said human subject whether IGF2BP1 is present on the cell surface of cells comprised by said sample.Said method for determining whether a human subject may suffer from cancer may comprise to determine in a sample obtained from said human subject whether IGF2BP1 is present on the cell surface of cells comprised by said sample.This method may comprise the following steps:- providing a sample obtained from said human subject,- determining in said sample obtained from said human subject whether IGF2BP1 is present on the cell surface of cells comprised by said sample,- correlating the presence of IGF2BP1 on the cell surface of cells comprised by said sample with determining whether the human subject may suffer from cancer.A “subject” or “human subject” in the context of the present invention is a human being. For example, the subject may be a patient being suspected of having a disease or clinical condition associated with cancer or being diagnosed with such a disease or clinical condition.Said “sample” obtained from said human subject is preferably selected from the group consisting of a blood sample, a serum sample, a plasma sample, a cerebrospinal fluid sample, a saliva sample, a solubilized tissue sample and a urine sample or an extract ofany of the aforementioned samples. Preferably, the sample is a serum sample or a plasma sample. Most preferably, the sample is a serum sample for determining whether a human subject may suffer from cancer. The cells comprised in said sample may be non-permeabilized cells and / or living cells.The step of “determining in said sample obtained from said human subject whether IGF2BP1 is present on the cell surface of cells comprised by said sample” may comprise to determine the presence of IGF2BP1 or the fragments thereof by contacting the sample with at least one IGF2BP1 binder. The at least one binder may, for example, be the antibody according to the present invention. It is preferred that at least one binder is less than 20 % cross-reactive with other proteins, particularly other IGF2 binding proteins such as IGF2BP2 and IGF2BP3, more preferably less than 15 %, more preferably less than 10 %, more preferably less than 5 %, even more preferably less than 3 %, even more preferably less than 2 % and even more preferably less than 1 % cross reactive. The antibodies 2C1 , 5H5, 10G7, 11 F2, 13B2, 15F11 , 17A10, 18G8, 19H9 (19G9), and 24B7 as published in WO 2022 / 123001 A1 are no antibodies according to the present invention.In a further aspect, the present invention provides a method for determining whether a human subject may suffer from cancer, comprising determining in a sample obtained from said human subject whether IGF2BP1 is present on the surface of extracellular vesicles comprised by said sample.Said method may comprise the following steps:- providing a sample obtained from said human subject,- separating or isolating extracellular vesicles from said sample by methods known to the skilled person,- determining in said sample obtained from said human subject whether IGF2BP1 is present on the surface of extracellular vesicles comprised by said sample,- correlating the presence of IGF2BP1 on the surface of extracellular vesicles comprised by said sample with determining whether the human subject may suffer from cancer.The same definitions as above apply here, with the following exception. The step of “determining in said sample obtained from said human subject whether IGF2BP1 is present on the surface of extracellular vesicles comprised by said sample” may comprise to determine the presence of IGF2BP1 or the fragments thereof by contacting the sample with at least one IGF2BP1 binder. The at least one binder may, for example, be the antibody according to the present invention. It is preferred that at least one binder is lessthan 20 % cross-reactive with other proteins, particularly other IGF2 binding proteins such as IGF2BP2 and IGF2BP3, more preferably less than 15 %, more preferably less than 10 %, more preferably less than 5 %, even more preferably less than 3 %, even more preferably less than 2 % and even more preferably less than 1 % cross reactive. The antibodies 2C1 , 5H5, 10G7, 11 F2, 13B2, 15F11 , 17A10, 18G8, 19H9 (19G9), and 24B7 as published in WO 2022 / 123001 A1 are no antibodies according to the present invention.The present invention also provides an antibody which binds to human IGF2BP1 present on the cell surface of a target cell, wherein said antibody is an antibody comprising a heavy chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 2.In one preferred embodiment of the antibody, which binds to human IGF2BP1 present on the cell surface of a target cell, said antibody is an antibody comprising a heavy chain variable region having an amino acid sequence with at least 90% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 90% identity to the amino acid sequence shown in SEQ ID NO: 2.In one more preferred embodiment of the antibody, which binds to human IGF2BP1 present on the cell surface of a target cell, said antibody is an antibody comprising a heavy chain variable region having an amino acid sequence with at least 95% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 95% identity to the amino acid sequence shown in SEQ ID NO: 2.In one even more preferred embodiment of the antibody, which binds to human IGF2BP1 present on the cell surface of a target cell, said antibody is an antibody comprising a heavy chain variable region having an amino acid sequence with at least 99% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 99% identity to the amino acid sequence shown in SEQ ID NO: 2.The present invention also provides an antibody which binds to human IGF2BP1 present on the surface of an extracellular vesicle, wherein said antibody is an antibody comprising a heavy chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 2.In one preferred embodiment of the antibody, which binds to human IGF2BP1 present on the surface of an extracellular vesicle, said antibody is an antibody comprising a heavy chain variable region having an amino acid sequence with at least 90% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 90% identity to the amino acid sequence shown in SEQ ID NO: 2.In one more preferred embodiment of the antibody, which binds to human IGF2BP1 present on the surface of an extracellular vesicle, said antibody is an antibody comprising a heavy chain variable region having an amino acid sequence with at least 95% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 95% identity to the amino acid sequence shown in SEQ ID NO: 2.In one even more preferred embodiment of the antibody, which binds to human IGF2BP1 present on the surface of an extracellular vesicle, said antibody is an antibody comprising a heavy chain variable region having an amino acid sequence with at least 99% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 99% identity to the amino acid sequence shown in SEQ ID NO: 2.In a further aspect, the present invention provides an antibody which binds to human IGF2BP1 present on the cell surface of a target cell, which comprises an antibody comprising a heavy chain variable region comprising heavy chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 3, heavy chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 4, and heavy chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 5 anda light chain variable region comprising light chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 6, light chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 7, and light chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 8.In a further aspect, the present invention provides an antibody which binds to human IGF2BP1 present on the surface of an extracellular vesicle, which comprises an antibody comprising a heavy chain variable region comprising heavy chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 3, heavy chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 4, and heavy chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 5 and a light chain variable region comprising light chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 6, light chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 7, and light chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 8.The present invention also provides the use of the antibody of the present invention in the manufacture of a medicament for the treatment of cancer. The antibodies 2C1 , 5H5, 10G7, 11 F2, 13B2, 15F11 , 17A10, 18G8, 19H9 (19G9), and 24B7 as published in WO 2022 / 123001 A1 are no antibodies of the present invention.The invention additionally provides the antibody of the present invention for use in a method of treating cancer and / or for use in in-vivo diagnostic imaging methods. The antibodies 2C1 , 5H5, 10G7, 11 F2, 13B2, 15F11 , 17A10, 18G8, 19H9 (19G9), and 24B7 as published in WO 2022 / 123001 A1 are no antibodies of the present invention.In some embodiments, the antibody of the present invention may contain human Fc regions that are modified to enhance effector function, for example, antigen-dependent cell-mediated cytotoxicity (ADCC) and / or complement dependent cytotoxicity (CDC). This can be achieved by introducing one or more amino acid substitutions in a Fc region of the antibody. For example, cysteine residue(s) can be introduced in the Fc region to allow interchain disulfide bond formation in this region to improve complement-mediated cell killing and antibody-dependent cellular cytotoxicity (ADCC). Homodimeric antibodies with enhanced anti-tumor activity can also be prepared using heterobifunctional cross-linkers as known to the person skilled in the art. Alternatively, an antibody may be engineeredwhich has dual Fc regions. The antibodies 2C1 , 5H5, 10G7, 11 F2, 13B2, 15F11 , 17A10, 18G8, 19H9 (19G9), and 24B7 as published in WO 2022 / 123001 A1 are no antibodies of the present invention.Furthermore, the antibody as described above may has substitution, deletion, addition and / or insertion of one or more amino acids in their CDR sequences as long as the resulting antibodies are functionally equivalent to the antibody. The term "functionally equivalent" refers to being comparable in avidity for IGF2BP1 and cytotoxicity. The term "equivalent" refers to having at least 50 %, preferably having at least 60 %, more preferably having at least 70 %, more preferably having at least 80 %, even more preferably at least 90 %, even more preferably at least 95 % and even more preferably at least 99 % activity, compared with the antibody. The upper limit of the activity is not particularly limited and may be higher than that of the antibody. The avidity or cytotoxicity can be assayed by a method generally known by those skilled in the art.The present invention further relates to an antibody, which binds to human IGF2BP1 present on the cell surface of a target cell for use in a method of killing said target cell having IGF2BP1 present on the cell surface. The antibodies 2C1 , 5H5, 10G7, 11 F2, 13B2, 15F11 , 17A10, 18G8, 19H9 (19G9), and 24B7 as published in WO 2022 / 123001 A1 are no antibodies within this meaning.In one embodiment of the antibody for use in the method of killing said target cell having IGF2BP1 present on the cell surface, said antibody is an antibody comprising a heavy chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 2.In one embodiment of the antibody for use in the method of killing said target cell having IGF2BP1 present on the cell surface, said antibody is an antibody comprising a heavy chain variable region having an amino acid sequence with at least 90% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 90% identity to the amino acid sequence shown in SEQ ID NO: 2.In one embodiment of the antibody for use in the method of killing said target cell having IGF2BP1 present on the cell surface, said antibody is an antibody comprising a heavy chain variable region having an amino acid sequence with at least 95% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 95% identity to the amino acid sequence shown in SEQ ID NO: 2.In one embodiment of the antibody for use in the method of killing said target cell having IGF2BP1 present on the cell surface, said antibody is an antibody comprising a heavy chain variable region having an amino acid sequence with at least 99% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 99% identity to the amino acid sequence shown in SEQ ID NO: 2.In one embodiment of the antibody for use in the method of killing said target cell having IGF2BP1 present on the cell surface, said antibody is an antibody comprising a heavy chain variable region comprising heavy chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 3, heavy chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 4, and heavy chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 5, and a light chain variable region comprising light chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 6, light chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 7, and light chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 8.All embodiments, which have been described herein for the pharmaceutical composition of the present invention and the antibody, which binds to human IGF2BP1 present on the cell surface of a target cell of the present invention and the methods of the present invention as described herein as well as the respective definitions as described above, also apply for the antibody for use in the method of killing said target cell having IGF2BP1 present on the cell surface of the present invention as described herein.The present invention also relates to a method of killing a target cell having IGF2BP1 present on the cell surface of said target cell, comprising administering an antibody, which binds to human IGF2BP1 present on the cell surface of said target cell. The antibodies 2C1 , 5H5, 10G7, 11 F2, 13B2, 15F11 , 17A10, 18G8, 19H9 (19G9), and 24B7 as publishedin WO 2022 / 123001 A1 are no antibodies to be used in this method according to the invention.In one embodiment of the method of killing a target cell having IGF2BP1 present on the cell surface of said target cell, said antibody is an antibody comprising a heavy chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 2.In one embodiment of the method of killing a target cell having IGF2BP1 present on the cell surface of said target cell, said antibody is an antibody comprising a heavy chain variable region having an amino acid sequence with at least 90% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 90% identity to the amino acid sequence shown in SEQ ID NO: 2.In one embodiment of the method of killing a target cell having IGF2BP1 present on the cell surface of said target cell, said antibody is an antibody comprising a heavy chain variable region having an amino acid sequence with at least 95% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 95% identity to the amino acid sequence shown in SEQ ID NO: 2.In one embodiment of the method of killing a target cell having IGF2BP1 present on the cell surface of said target cell, said antibody is an antibody comprising a heavy chain variable region having an amino acid sequence with at least 99% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 99% identity to the amino acid sequence shown in SEQ ID NO: 2.In one embodiment of the method of killing a target cell having IGF2BP1 present on the cell surface of said target cell, said antibody is an antibody comprising a heavy chain variable region comprising heavy chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 3, heavy chain CDR2 having the amino acid sequence as set forthin SEQ ID NO: 4, and heavy chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 5, and a light chain variable region comprising light chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 6, light chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 7, and light chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 8.All embodiments, which are described herein for the pharmaceutical composition of the present invention, the antibody, which binds to human IGF2BP1 present on the cell surface of a target cell of the present invention, the method of determining whether a human subject may suffer from cancer of the present invention as described herein as well as the respective definitions as described above, also apply for the method of killing a target cell having IGF2BP1 present on the cell surface of said target cell as described herein. Especially the term “target cell”, as used within the context of the present invention, is preferably a cancer cell, especially a non-permeabilized cell and / or living cell. The term “cancer”, as used herein, can comprise any one or more of the following: acute lymphocytic leukemia (ALL), acute myeloid leukemia (AML), adrenocortical cancer, anal cancer, bladder cancer, blood cancer, bone cancer, brain tumor, breast cancer, cancer of the female genital system, cancer of the male genital system, central nervous system lymphoma, cervical cancer, childhood rhabdomyosarcoma, childhood sarcoma, chronic lymphocytic leukemia (CLL), chronic myeloid leukemia (CML), colon and rectal cancer, colon cancer, endometrial cancer, endometrial sarcoma, esophageal cancer, eye cancer, gallbladder cancer, gastric cancer, gastrointestinal tract cancer, hairy cell leukemia, head and neck cancer, hepatocellular cancer, Hodgkin’s disease, hypopharyngeal cancer, Kaposi’s sarcoma, kidney cancer, laryngeal cancer, leukemia, liver cancer, lung cancer, malignant fibrous histiocytoma, malignant thymoma, melanoma, mesothelioma, multiple myeloma, myeloma, nasal cavity and paranasal sinus cancer, nasopharyngeal cancer, nervous system cancer, neuroblastoma, non-Hodgkin’s lymphoma, oral cavity cancer, oropharyngeal cancer, osteosarcoma, ovarian cancer, pancreatic cancer, parathyroid cancer, penile cancer, pharyngeal cancer, pituitary tumor, plasma cell neoplasm, primary CNS lymphoma, prostate cancer, rectal cancer, respiratory system, retinoblastoma, salivary gland cancer, skin cancer, small intestine cancer, soft tissue sarcoma, stomach cancer, testicular cancer, thyroid cancer, urinary system cancer, uterine sarcoma, vaginal cancer, vascular system, Waldenstrom’s macroglobulinemia and Wilms’ tumor. Preferred as target cells are cancer cells from breast cancer, ovarian cancer, brain cancer, melanoma, non-small-cell-lung cancer, pancreatic cancer, colon cancer, colorectalcancer, mesenchymal cancer, Hodgkin lymphoma, B cell lymphomas, acute myeloid leukemia (AML) or acute lymphatic leukemia (ALL) of the T cell type. Also preferred as target cells are cancer cells from cervical cancer, colorectal adeno carcinoma, laryngeal squamous cell carcinoma, lung cancer, pancreatic adenocarcinoma, ovarian cancer, ovarian clear-cell carcinoma, acute myeloid leukemia (AML) or acute lymphatic leukemia (ALL) of the T cell type. The antibodies 2C1 , 5H5, 10G7, 11 F2, 13B2, 15F11 , 17A10, 18G8, 19H9 (19G9), and 24B7 as published in WO 2022 / 123001 A1 are no antibodies according to the present invention.The present invention further relates to an antibody, which binds to human IGF2BP1 present on the cell surface of a target cell for use in a method for the treatment of cancer in a subject, comprising, prior to the treatment of cancer in said subject, determining whether a target cell of said subject has IGF2BP1 present on the cell surface. The antibodies 2C1 , 5H5, 10G7, 11 F2, 13B2, 15F11 , 17A10, 18G8, 19H9 (19G9), and 24B7 as published in WO 2022 / 123001 A1 are no antibodies for use in method for the treatment.In one embodiment of the antibody for use in a method for the treatment of cancer in a subject, comprising, prior to the treatment of cancer in said subject, determining whether a target cell of said subject has IGF2BP1 present on the cell surface, said antibody is an antibody comprising a heavy chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 2.In one embodiment of the antibody for use in a method for the treatment of cancer in a subject, comprising, prior to the treatment of cancer in said subject, determining whether a target cell of said subject has IGF2BP1 present on the cell surface, said antibody is an antibody comprising a heavy chain variable region having an amino acid sequence with at least 90% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 90% identity to the amino acid sequence shown in SEQ ID NO: 2.In one embodiment of the antibody for use in a method for the treatment of cancer in a subject, comprising, prior to the treatment of cancer in said subject, determining whethera target cell of said subject has IGF2BP1 present on the cell surface, said antibody is an antibody comprising a heavy chain variable region having an amino acid sequence with at least 95% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 95% identity to the amino acid sequence shown in SEQ ID NO: 2.In one embodiment of the antibody for use in a method for the treatment of cancer in a subject, comprising, prior to the treatment of cancer in said subject, determining whether a target cell of said subject has IGF2BP1 present on the cell surface, said antibody is an antibody comprising a heavy chain variable region having an amino acid sequence with at least 99% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 99% identity to the amino acid sequence shown in SEQ ID NO: 2.In one embodiment of the antibody for use in a method for the treatment of cancer in a subject, comprising, prior to the treatment of cancer in said subject, determining whether a target cell of said subject has IGF2BP1 present on the cell surface, said antibody is an antibody comprising a heavy chain variable region comprising heavy chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 3, heavy chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 4, and heavy chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 5, and a light chain variable region comprising light chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 6, light chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 7, and light chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 8.All embodiments, which are described herein for the pharmaceutical composition of the present invention, the antibody, which binds to human IGF2BP1 present on the cell surface of a target cell of the present invention, and which is not one of the antibodies 2C1 , 5H5, 10G7, 11 F2, 13B2, 15F11 , 17A10, 18G8, 19H9 (19G9), and 24B7 as published in WO 2022 / 123001 , the method of determining whether a human subject may suffer from cancer of the present invention as described herein as well as the respective definitions as described above, also apply for the antibody for use in a method for the treatment of cancer in a subject, comprising, prior to the treatment of cancer in said subject, determining whether a target cell of said subject has IGF2BP1 present on the cell surface as described herein. Especially the term “cancer”, as used herein, can comprise any oneor more of the following: acute lymphocytic leukemia (ALL), acute myeloid leukemia (AML), adrenocortical cancer, anal cancer, bladder cancer, blood cancer, bone cancer, brain tumor, breast cancer, cancer of the female genital system, cancer of the male genital system, central nervous system lymphoma, cervical cancer, childhood rhabdomyosarcoma, childhood sarcoma, chronic lymphocytic leukemia (CLL), chronic myeloid leukemia (CML), colon and rectal cancer, colon cancer, endometrial cancer, endometrial sarcoma, esophageal cancer, eye cancer, gallbladder cancer, gastric cancer, gastrointestinal tract cancer, hairy cell leukemia, head and neck cancer, hepatocellular cancer, Hodgkin’s disease, hypopharyngeal cancer, Kaposi’s sarcoma, kidney cancer, laryngeal cancer, leukemia, liver cancer, lung cancer, malignant fibrous histiocytoma, malignant thymoma, melanoma, mesothelioma, multiple myeloma, myeloma, nasal cavity and paranasal sinus cancer, nasopharyngeal cancer, nervous system cancer, neuroblastoma, non-Hodgkin’s lymphoma, oral cavity cancer, oropharyngeal cancer, osteosarcoma, ovarian cancer, pancreatic cancer, parathyroid cancer, penile cancer, pharyngeal cancer, pituitary tumor, plasma cell neoplasm, primary CNS lymphoma, prostate cancer, rectal cancer, respiratory system, retinoblastoma, salivary gland cancer, skin cancer, small intestine cancer, soft tissue sarcoma, stomach cancer, testicular cancer, thyroid cancer, urinary system cancer, uterine sarcoma, vaginal cancer, vascular system, Waldenstrom’s macroglobulinemia and Wilms’ tumor. Preferred as target cells are cancer cells from breast cancer, ovarian cancer, brain cancer, melanoma, non-small- cell-lung cancer, pancreatic cancer, colon cancer, colorectal cancer, mesenchymal cancer, Hodgkin lymphoma, B cell lymphomas, acute myeloid leukemia (AML) or acute lymphatic leukemia (ALL) of the T cell type. Also preferred as target cells are cancer cells from cervical cancer, colorectal adeno carcinoma, laryngeal squamous cell carcinoma, lung cancer, pancreatic adenocarcinoma, ovarian cancer, ovarian clear-cell carcinoma, acute myeloid leukemia (AML) or acute lymphatic leukemia (ALL) of the T cell type.The antibody according to the present invention may be capable of binding to an IGF2BP1 polypeptide extracellularly. In other words, an antibody as described herein may be capable of binding to IGF2BP1 when it is outside the cell, which also comprises IGF2BP1 to be specifically on the surface of the cell.The description of the sequences, shown in the sequence listing and as used in the context of the present invention, is as follows:SEQ ID NO: 1 shows the amino acid sequence of the VH-region of antibody 12G5.SEQ ID NO: 2 shows the amino acid sequence of the VL-region of antibody 12G5.SEQ ID NO: 3 shows the amino acid sequence of the VH-CDR1 of antibody 12G5.SEQ ID NO: 4 shows the amino acid sequence of the VH-CDR2 of antibody 12G5. SEQ ID NO: 5 shows the amino acid sequence of the VH-CDR3 of antibody 12G5.SEQ ID NO: 6 shows the amino acid sequence of the VL-CDR1 of antibody 12G5.SEQ ID NO: 7 shows the amino acid sequence of the VL-CDR2 of antibody 12G5.SEQ ID NO: 8 shows the amino acid sequence of the VL-CDR3 of antibody 12G5.SEQ ID NO: 9 shows the amino acid sequence of human IGF2BP1 .overview of the SEQ ID NOs and detailed sequences, as used in the context of the present invention, is given in the following Table 1 : le 1 :AEVWPRDQTPDENDQVIVKIIGHFYASQMAQRKIRDILAQVKQQHQKGQSNQAQARRK following ab were used in the context of the present invention: VH = variable heavy chain; VH = variable heavy chain; VL =iable light chain; CDR = complementarity determining region; VH-CDR = CDR of a variable heavy region; VL-CDR = CDR of a variablet region; CDRs can be determined by, e.g. http: / / abysis.org / abysis / * * * * *It is noted that as used herein, the singular forms “a”, “an”, and “the”, include plural references unless the context clearly indicates otherwise. Thus, for example, reference to “a reagent” includes one or more of such different reagents and reference to “the method” includes reference to equivalent steps and methods known to those of ordinary skill in the art that could be modified or substituted for the methods described herein.Unless otherwise indicated, the term "at least" preceding a series of elements is to be understood to refer to every element in the series. Those skilled in the art will recognize or be able to ascertain using no more than routine experimentation, many equivalents to the specific embodiments of the invention described herein. Such equivalents are intended to be encompassed by the present invention.The term "and / or", wherever used herein, includes the meaning of "and", "or" and "all or any other combination of the elements connected by said term".The term “less than” or in turn “more than” does not includes the concrete number.For example, “less than 20” means less than the number indicated. Similarly, “more than” or “greater than” means more than or greater than the indicated number, e.g. “more than 80 %” means more than or greater than the indicated number of 80 %.Throughout this specification and the claims which follow, unless the context requires otherwise, the word “comprise”, and variations such as “comprises” and “comprising”, will be understood to imply the inclusion of a stated integer or step or group of integers or steps, but not the exclusion of any other integer or step or group of integer or step. When used herein the term “comprising” can be substituted with the term “containing” or “including” or sometimes, when used herein, with the term “having”. When used herein, “consisting of' excludes any element, step, or ingredient not specified.The term “including” means “including but not limited to”, “Including” and “including but not limited to” are used interchangeably.It should be understood that this invention is not limited to the particular methodology, protocols, material, reagents, and substances, etc., described herein and as such can vary. The terminology used herein is for the purpose of describing particular embodiments, only, and is not intended to limit the scope of the present invention, which is defined solely by the claims.All publications cited throughout the text of this specification (including all patents, patent application, scientific publications, instructions, etc.), whether supra or infra, are hereby incorporated by reference in their entirety. Nothing herein is to be construed as an admission that the invention is not entitled to antedate such disclosure by virtue of prior invention. To the extent the material incorporated by reference contradicts or is inconsistent with this specification, the specification will supersede any such material.The content of all documents and patent documents cited herein is incorporated by reference in their entirety.A better understanding of the present invention and of its advantages will be had from the following examples, offered for illustrative purposes only. The examples are not intended to limit the scope of the present invention in any way.The invention is further characterized by the following items:1. Pharmaceutical composition comprising an antibody, preferably a monoclonal antibody, which binds to human IGF2BP1 present on the cell surface of a target cell and optionally a pharmaceutically acceptable carrier, diluent or excipient.2. The pharmaceutical composition of item 1 , wherein said target cell is a non- permeabilized cell.3. The pharmaceutical composition of item 1 , wherein said target cell is a living cell.4. The pharmaceutical composition of any one of the preceding items, wherein said antibody has cytotoxic activity.5. The pharmaceutical composition of any one of the preceding items, wherein said antibody has ADCC or CDC.6. The pharmaceutical composition of any one of the preceding items, wherein said antibody is conjugated with a cytotoxic substance or a substance used for in-vivo imaging.7. The pharmaceutical composition of any one of the preceding items, wherein said antibody is internalized from the target cell after binding to IGF2BP1 present on the cell surface.8. The pharmaceutical composition of any one of the preceding items, wherein said antibody or a part thereof is part of a chimeric antigen receptor (CAR).9. The pharmaceutical composition of item 8, wherein said CAR is comprised by a T cell, NK cell, NK-T cell or macrophage.10. The pharmaceutical composition of any one of the preceding items, wherein said antibody is less than 20% cross-reactive with IGF2BP1 -related proteins.11 . The pharmaceutical composition of any one of the preceding items, wherein said antibody is(a) an antibody comprising a heavy chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 2; or(b) an antibody which binds to the same epitope as that in the human IGF2BP1 protein to which the antibody (a) binds.12. The pharmaceutical composition of any one of the preceding items, wherein said antibody is(a) an antibody comprising a heavy chain variable region comprising heavy chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 3,heavy chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 4, and heavy chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 5, and a light chain variable region comprising light chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 6, light chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 7, and light chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 8; or.(b) an antibody which binds to the same epitope as that in the human IGF2BP1 protein to which the antibody (a) binds.13. The pharmaceutical composition of any one of the preceding items for use in an in-vivo diagnostic imaging method for diagnosing cancer.14. The pharmaceutical composition of any one of the preceding items for use in a method for the treatment of cancer in a human subject.15. The pharmaceutical composition for the use of item 13 or 14, wherein said cancer is characterized by cells, wherein human IGF2BP1 is present on their cell surface.16. The pharmaceutical composition for the use of items 13 to 15, wherein said cancer is breast cancer, ovarian cancer, brain cancer, melanoma, non-small-cell- lung cancer, pancreatic cancer, colon cancer, colorectal cancer, mesenchymal cancer, Hodgkin lymphoma, B cell lymphomas, acute myeloid leukemia (AML) or acute lymphatic leukemia (ALL) of the T cell type.17. The pharmaceutical composition for the use of items 13 to 15, wherein said cancer is cervical cancer, colorectal adeno carcinoma, laryngeal squamous cell carcinoma, lung cancer, pancreatic adenocarcinoma, ovarian cancer, ovarian clear-cell carcinoma, acute myeloid leukemia (AML) or acute lymphatic leukemia (ALL) of the T cell type.18. A method for determining whether a human subject may suffer from cancer, comprising determining in a sample obtained from said human subject whether IGF2BP1 is present on the cell surface of cells comprised by said sample.19. The method of item 18, wherein said cells are non-permeabilized cells.20. The method of item 18, wherein said cells are living cells.21. A method for determining whether a human subject may suffer from cancer, comprising determining in a sample obtained from said human subject whether IGF2BP1 is present on the surface of extracellular vesicles comprised by said sample.22. An antibody which binds to human IGF2BP1 present on the cell surface of a target cell wherein said antibody is(a) an antibody comprising a heavy chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 2; or(b) an antibody which binds to the same epitope as that in the human IGF2BP1 protein to which the antibody (a) binds.23. The antibody of item 22, wherein said target cell is a non-permeabilized cell.24. The antibody of item 22, wherein said target cell is a living cell.25. An antibody which binds to human IGF2BP1 present on the surface of an extracellular vesicle, wherein said antibody is(a) an antibody comprising a heavy chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 2; or(b) an antibody which binds to the same epitope as that in the human IGF2BP1 protein to which the antibody (a) binds.An antibody which binds to human IGF2BP1 present on the cell surface of a target cell comprising(a) an antibody comprising a heavy chain variable region comprising heavy chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 3, heavy chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 4, and heavy chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 5, and a light chain variable region comprising light chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 6, light chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 7, and light chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 8; or(b) an antibody which binds to the same epitope as that in the human IGF2BP1 protein to which the antibody (a) binds. The antibody of item 26, wherein said target cell is a non-permeabilized cell. The antibody of item 26, wherein said target cell is a living cell. An antibody which binds to human IGF2BP1 present on the surface of an extracellular vesicle comprising(a) an antibody comprising a heavy chain variable region comprising heavy chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 3, heavy chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 4, and heavy chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 5, and a light chain variable region comprising light chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 6, light chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 7, and light chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 8; or(b) an antibody which binds to the same epitope as that in the human IGF2BP1 protein to which the antibody (a) binds.30. An antibody, which binds to human IGF2BP1 present on the cell surface of a target cell for use in a method of killing said target cell having IGF2BP1 present on the cell surface.31 . The antibody according to item 30, wherein said antibody is(a) an antibody comprising a heavy chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 2; or(b) an antibody, which binds to the same epitope as that in the human IGF2BP1 protein to which antibody (a) binds.32. The antibody according to item 30 or 31 , wherein said antibody is(a) an antibody comprising a heavy chain variable region comprising heavy chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 3, heavy chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 4, and heavy chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 5, and a light chain variable region comprising light chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 6, light chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 7, and light chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 8; or(b) an antibody, which binds to the same epitope as that in the human IGF2BP1 protein to which antibody (a) binds.33. A method of killing a target cell having IGF2BP1 present on the cell surface, comprising administering an antibody, which binds to human IGF2BP1 present on the cell surface of said target cell.34. The method of item 33, wherein said antibody is(a) an antibody comprising a heavy chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acidsequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 2; or(b) an antibody, which binds to the same epitope as that in the human IGF2BP1 protein to which antibody (a) binds. The method of item 33 or 34, wherein said antibody is(a) an antibody comprising a heavy chain variable region comprising heavy chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 3, heavy chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 4, and heavy chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 5, and a light chain variable region comprising light chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 6, light chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 7, and light chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 8; or(b) an antibody, which binds to the same epitope as that in the human IGF2BP1 protein to which antibody (a) binds. An antibody, which binds to human IGF2BP1 present on the cell surface of a target cell for use in a method for the treatment of cancer in a subject, comprising, prior to the treatment of cancer in said subject, determining whether a target cell of said subject has IGF2BP1 present on the cell surface. The antibody according to item 36, wherein said antibody is(a) an antibody comprising a heavy chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 2; or(b) an antibody, which binds to the same epitope as that in the human IGF2BP1 protein to which antibody (a) binds. The antibody according to item 36 or 37, wherein said antibody is(a) an antibody comprising a heavy chain variable region comprising heavy chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 3, heavy chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 4, and heavy chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 5, and a light chain variable region comprising light chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 6, light chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 7, and light chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 8; or(b) an antibody, which binds to the same epitope as that in the human IGF2BP1 protein to which antibody (a) binds.EXAMPLESMaterials and methods:Cells and culture conditions:Cells were cultured in DMEM / F12 medium (Gibco BRL, Karlsruhe, Germany), supplemented with 8 % v / v fetal bovine serum, 1 % v / v L-Glutamine and 1 % v / v penicillin-streptomycin). All cells were incubated in a humidified CO2 incubator at 37 °C, 18.3 % O2 and 5 % CO2. Hypoxic cells were incubated at 1 % O2.Transfection of SK-OV-3 and HEK293 cells:SK-OV-3 and HEK293 cells were transfected with expression plasmids, coding for human IGF2BP1 or mutants thereof using Lipofectamine™ 2000 transfection reagent (ThermoFisher Scientific, Menzel, Germany) according to manufacturer’s instructions. IGF2BP1 specific siRNAs were transfected using Lipofectamine. Where appropriate, cells were selected for positive transfected cells with 80 pg / ml Hygromycin C and further cultured in normal growth medium supplemented with 80 pg / ml Hygromycin C.Flow cytometry:For flow cytometric analysis of IGF2BP1 expression, cells were stained with 12G5 or any other IGF2BP1 -specific antibody in FACS-buffer (PBS + 2 % FCS) or with an isotype control antibody for 20 min followed by staining with an anti-rat-Alexa Fluor®647 secondary antibody (Jackson Immuno Research). All stainings were performed on ice.Western blotting analysis:For analysis of IGF2BP1 expression by western blotting, whole cell lysates were prepared. Adherent cells were washed with PBS, detached by trypsin and pelleted. The cell pellet was washed in PBS. After that, cells were resuspended in RIPA buffer with protease inhibitors (Roche Diagnostics) and incubated on ice for 20 min. Cell fragments were centrifuged for 20 min at 4 °C at max speed. The supernatant was transferred to a new tube and the protein content was determined by Bradford assay (Bio-Rad). 20 pg of cell lysate were used for SDS-PAGE. Gels were electroblotted on a nitrocellulose membrane and blocked with 5 % milk in TBST. Following primary antibodies were used for Western blotting: antibody 12G5, anti-FLAG antibody (B). All primary antibodies were incubated at 4 °C over night. The membrane was washed and incubated with HRP-conjugated secondary antibodies at room temperature for 2 h. The following secondary antibodies were used: anti-rat IgG-HRP (Cell Signaling), antimouse IgG-HRP (Cell Signaling Technology, Frankfurt a. Main, Germany) and antirabbit IgG-HRP (Cell Signaling). Detection of proteins was performed with the ECL system (GE Healthcare, Freiburg, Germany).Immunoprecipitation:Immunoprecipitation was performed using CNBr beads (CNBr-activated Sepharose 4 Fast Flow, GE Healthcare). 1 g beads were solved in 10 ml 1 mM HCI and incubated at room temperature for 20 min. After that beads were spin down for 1 min at 3,000 x g and washed 15 x. Then, a subclass specific mouse anti-rat lgG2a antibody was coupled to the beads (2 mg antibody in coupling buffer 0.3 M NaHCOs, 1.5 M NaCI, pH 8.3) for 1 h at room temperature. After that, beads were washed in coupling buffer and all remaining binding sites blocked with 1 M ethanolamine (1 M) for 2 h at room temperature. After washing in wash buffer (0,1 M Tris / HCI, 0.5 M NaCI, pH 4) and in NaOAc buffer (0.1 M NaOAc, 0.5 M NaCI) coupled beads were resuspended in PBS and used for coupling with 12G5. Therefore, 500 pl 12G5 hybridoma supernatant was incubated with 60 pl anti-subclass specific beads over night at 4 °C.Beads were then washed in PBS and incubated with 2 mg cell lysate at 4 °C over night. After that, beads were washed in RIPA buffer with protease inhibitors, PBS+ (PBS, 0.5% N-laurylsarcosine, 0.1 % SDS) and in PBS. The supernatant was discarded, beads resuspended in 3x Laemmli buffer and incubated at room temperature for 3 min.Confocal Microscopy:1 x 105cells were seeded on cover slips and grown over night. The medium was removed, and cells were washed with PBS, fixed in 4 % PFA for 10 min, permeabilized with PBS containing 0.3 % Tween20 and finally blocked with 3 % BSA in TBS with 0.1 % Tween 20. For staining, cells were incubated with the 1 st antibody, diluted in TBS with 1 % BSA and 0.1 % Tween20 for 1 hour at room temperature. Then, cells were washed three times before incubation with the secondary antibody (goat anti-rat-Alexa 647) in the dark for 40 min. After a final washing step, nuclei were stained with DAPI, a mounting medium (Vectashield) was added, and cover slips were mounted upsidedown on a microscope slide. Slides were analyzed on a Leica SP8X STED microscope using the Leica LAS X software.Isolation of extracellular vesicles:Extracellular vesicles (EV) were isolated from ascites fluid or conditioned cell culture medium by standard technologies. In brief, the fluids were centrifuged at 100.000 x g for 2 hours, the supernatant was carefully removed, and the pelleted material was resuspended in 1.5 ml PBS, centrifuged again as described above, and finally resuspended in approx. 100 pl of PBS. The EVs were quantified by nanoparticle tracking analysis (NTA) and routinely checked by dot blots for the presence of EV marker proteins (CD63, Alix, tsg101 ).Sandwich-ELISA using extracellular vesicles:Extracellular vesicles contained in ascites fluid from patients with ovarian cancer were isolated via standard protocols for EV isolation via differential centrifugation (400 x g; 2,500 x g; 100,000 x g) followed by a purification by floatation into a density gradient. The wells of a polystyrene 96-well cluster plate were coated with 12G5 (5 pg / ml), a GST-specific control antibody (5 pg / ml) overnight at 4 °C. Then, wells were blocked with 3% bovine serum albumin (BSA), followed by addition of 10pg / well of EVs from 3 different donors. The plate was again incubated overnight at 4 °C. Then, wells were washed several times with TBS / 0.1 % Tween and incubated with an anti-CD63 antibody (CD63 is a protein expressed on most types of EVs), coupled with HRP.Finally, wells were developed with TMB; the reaction was stopped with H2SO4 and the optical density (OD) at 450 nm was measured.Generation and testing of the 12G5 Fab fragment:2 mg of antibody 12G5 were digested with papain using the Pierce™ Fab Preparation Kit (Thermo Scientific, Cat. #44985) according to the manufacturer’s instructions. Function of the Fab fragment was tested by flow cytometry. For this, A549 cells were incubated with the 12G5 Fab fragment (black line) or an isotype control Fab fragment (gray tinted histograms). Cells were then washed and incubated with an Alexa647 labeled anti-rat IgG antibody. Fluorescence was then measured by flow cytometry on a FACS Canto.Experimental examples:Example 1 : Generation of antibodies using extracellular vesiclesA Lou / c rat was immunized with a mixture of extracellular vesicles, which were derived from the cancer cell lines A549, SKOV-3, HeLa, and Capan-1 and isolated from conditioned supernatants by serial centrifugation. Briefly, conditioned FCS-free supernatants were collected, subjected to repeated centrifugations at increasing centrifugal force (10 min at 300 x g, 4 °C, and 20 min at 5,000 x g, 4 °C), filtrated (pore size 0.45 pm) and finally precipitated at 100,000 x g, 4 °C for 2 h in a SW28 rotor. Pelleted vesicles were resuspended in 100 pl of PBS and injected i.p. and s.c. with CpG as adjuvant. A boost injection was given five months later, and spleen cells were fused with myeloma cell line P3x63Ag8.653 (ATCC, CRL-1580). Hybridoma supernatants were screened ten days later for IgG production, and positive clones were further expanded and subcloned at least twice by limiting dilution to obtain stable monoclonal cell lines.Example 2: Immunoprecipitation of IGF2BP1 with antibody 12G5 and ovarian cancer cellsCyanogen bromide beads coupled with 12G5 or with an isotype control antibody (negK) were incubated overnight with lysates from UWB1.289 ovarian cancer cells. After precipitation of the beads and incubation in Laemmli buffer, eluates were analyzed by mass spectrometry, which revealed a clear enrichment of IGF2BP1 with 12G5 as compared to the isotype control antibody (iso2a) as shown in figure 1.Example 3: Immunoprecipitation of IGF2BP1 with antibody 12G5 and Jurkat cells Jurkat cell lysate were incubated overnight with 12G5 or an M BP-specific antibody (Iso contr.) coupled to cyanogen bromide beads. After precipitation of the beads and incubation in Laemmli buffer, eluates were separated by PAGE and an immunoblot with a commercial anti-IGF2BP1 antibody (#PA5-44886; Thermo Scientific) was performed, followed by incubation with an anti-rabbit HRP-labeled secondary antibody. The blot was developed with ECL. The results are depicted in Figure 2, which shows a clear band in the 12G5 lane.Example 4: Flow-Cytometry reveals expression of IGF2BP1 on the surface of different cancer cell lines and primary cancer cellsCancer cell lines A549, HT29, 11251 , DAN, ES-2, HeLa, Capan-1 , and PCI-1 , cancer cells isolated from ascites of a patient with ovarian cancer (AS 77), primary cancer cells from patients with T-cell acute lymphoblastic leukemia (T-ALL) or acute myeloid leukemia (AML), primary hepatocytes, and primary PBMCs were incubated with the antibody 12G5 or an isotype control antibody. Cells were then washed and incubated with an Alexa647 labeled anti-rat IgG antibody. Fluorescence was then measured by flow cytometry on a FACS Canto. The results are shown in Figure 3.Figure 3 A shows that antibody 12G5 bounds to the tested cells from cancer cell lines or ascites (solid lines) compared to the isotype control antibody (gray histograms).Figure 3 B shows that antibody 12G5 bounds to primary cancer cells from patients with T-ALL (left, solid line) or AML (right, solid lines) compared to the isotype control antibody (gray histograms).Whereas antibody 12G5 bounds not to primary hepatocytes and primary PBMCs, which do not express IGF2BP1 on their surface (Figure 3 C).Example 5: IGF2BP1 is a hypoxia-inducible proteinHeLa cervix cancer cells, ES-2, and SK-OV-3 ovarian cancer cells were incubated in a humified atmosphere with 5 % CO2 at normoxia (approx. 18 % O2) or hypoxia (1 % O2) in standard cell culture medium for 72 hours. Then, surface IGF2BP1 was quantified by flow cytometry. For this, cells were incubated with 12G5 or an isotype control antibody, washed and then incubated with an Alexa647 labeled anti-rat IgG antibody. Finally, fluorescence was measured by flow cytometry (BD FACS Canto).Figure 4 shows that the tested cell lines expressed more IGF2BP1 on their surface (bound by 12G5) under hypoxic conditions (dashed line) compared to normoxic conditions (solid line). The isotype control is shown as tinted grey histogram.Example 6: Verification of the specificity of the antibody 12G5 for IGF2BP1Example 6a: Antibody 12G5 is an IGF2BP1 -specific antibody as shown by WesternblotIn a first experiment recombinant IGF2BP1 with a FLAG-TAG protein and, as controls, recombinant zymogen granule protein 16B (ZG16B) and recombinant BSA with a FLAG-TAG were separated by PAGE (lane 1 : IGF2BP1 +FLAG, lane 2: ZG16B, lane 3: BSA+FLAG) and blotted onto a PVDF membrane.The membrane was incubated with either antibody 12G5 (A) or with an anti-FLAG antibody (B), followed by incubation with an HRP-coupled suitable secondary antibody and finally developed with ECL.The 12G5 antibody specific binds to IGF2BP1 , but not to the unrelated proteins ZG16B or BSA or to the FLAG-Tag as shown in Figure 5 A. As a control the anti-FLAG antibody binds to the FLAG-TAGs of IGF2BP1 (lane 1 ) and BSA (lane 3) (Figure 5 B).In a second experiment antibody 12G5 was coupled to beads and incubated with lysates from HEK293 cells transfected with an expression plasmid encoding IGF2BP1 - FLAG or with purified IGF2BP1 -FLAG protein and immunoprecipitated. As a control, lysates were incubated with an isotype antibody coupled to beads. After precipitation, eluates in Laemmli buffer were separated by PAGE (lane 1 : HEK293 cell lysate + IGF2BP1 -FLAG, lane 2: isotype antibody coupled to beads, lane 3: IGF2BP1 -FLAG protein) and blotted onto a PVDF membrane. The membrane was incubated with an anti-FLAG antibody, followed by incubation with an HRP-coupled anti-mouse secondary antibody and finally developed with ECL.Figure 6 shows that cell lysates containing IGF2BP1 -FLAG (lane 1 ) and purified IGF2BP1 -FLAG protein (lane 3) could be specific immunoprecipitated by the antibody 12G5 compared to a bead coupled isotype antibody (lane 2).These results demonstrate the specific binding of the antibody 12G5 to IGF2BP1 .Example 6b: Antibody 12G5 is an IGF2BP1 -specific antibody shown by an ELISAThe wells of a polystyrene 96-well cluster plate were coated with 12G5 (5 pg / ml), a GST-specific control antibody, or with PBS, only, overnight at 4 °C. Then, wells were blocked with 3 % bovine serum albumin (BSA), followed by addition of 10pg / well of recombinant IGF2BP1 protein with a FLAG-tag (IGF2BP1 -FLAG). The plate was incubated for 3 h at 4 °C. Then, wells were washed several times with TBS / 0.1 % Tween and incubated with a FLAG-specific murine antibody (M2; Millipore) for 2 h, followed by incubation with a peroxidase-labeled anti-mouse antibody. Finally, wells were developed with TMB; the reaction was stopped with H2SO4 and the optical density (OD) at 450 nm was measured. Figure 7 A clearly shows that the IGF2BP1 -FLAG protein binds specifically to the antibody 12G5 and not to an unrelated antibody.In a further experiment a 96-well cluster plate were coated with a serial dilution of either IGF2BP1 -FLAG or BSA-FLAG, blocked, and then incubated with 12G5 for 2 h, followed by incubation with a peroxidase-labeled anti-rat antibody. Finally, wells were developed with TMB; the reaction was stopped with H2SO4 and the optical density (OD) at 450 nm was measured. Figure 7 B shows a dose-depended binding of the IGF2BP1 - FLAG to the 12G5 antibody, confirming the specificity of this binding.Example 6c: Antibody 12G5 is an IGF2BP1 -specific antibody as shown by flowcytometrySK-OV-3 cells were transfected with IGF2BP1 -specific siRNAs. Three days later, binding of the antibody 12G5 to knockdown and wildtype cells was measured by flow cytometry. For this, SK-OV-3 Wil dtype and were incubated with 12G5. Then, cells were washed and incubated with an Alexa647 labeled anti-rat secondary antibody. Fluorescence was then measured on a FACS Canto. Figure 8 shows that the 12G5 antibody binds to SK-OV-3 wildtype cells (gray histogram; median fluorescence: 3,002) and to a far less extend to the IGF2BP1 knockdown cells (bold line; median fluorescence: 768), revealing the specificity of 12G5 for IGF2BP1 expressed on the cell surface. An isotype control antibody was included as a negative control (dashed line).These results show the specificity of antibody 12G5 for IGF2BP1 expressed on the surface of SK-OV-3 cancer cells.Example 7: Antibody 12G5 binds to the surface of living ovarian cancer cellsLIWB1 .289 and SK-OV-3 cells were grown on microscope slides, washed in PBS, and incubated with the antibody 12G5 (left) or with Membrite 568 (Biotium Inc.; Fremont, CA) to stain cell surface proteins. Thereafter, cells were fixed with 4 % paraformaldehyde and, in the case of 12G5, incubated with an Alexa647-coupled suitable anti-rat IgG secondary antibody. Figure 9 A shows clearly a surface staining of both LIWB1 .289 cells with 12G5 and a partial co-localization with cell surface stain Membrite 568. Also, the surface of SK-OV-3 cells was stained with 12G5 showing a partial co-localization with Membrite 568 (Figure 9 B).In a further experiment SK-OV-3 cells were cultivated on a cover slip, washed, and incubated with the antibodies 12G5 and a commercial antibody targeting the membrane protein CD81. Cells were then fixed with 4 % paraformaldehyde and analyzed by confocal fluorescence microscopy. Figure 9 C shows a clear surface staining with 12G5 antibody (left) compared to the CD81 antibody (right).Example 8: IGF2BP1 is released via extracellular vesiclesExtracellular vesicles (EVs) isolated from four ascites fluid from four patients with ovarian cancer were isolated by established technologies comprising differential centrifugation, ultracentrifugation, and density gradient purification. 2 pl each of these EV preparations were then spotted onto pieces of nitrocellulose membrane and incubated with an anti-CD63 antibody (left) or 12G5 (right) at 4 °C overnight. After washing, the membrane was incubated with a secondary antibody (goat anti-rat IgG, coupled with horseradish peroxidase) for 2 hours and developed with ECL. Figure 10 A shows on the left part the staining of the transmembrane protein CD63 on the EVs with an anti-CD63 antibody in all tested ascites fluids. On the right part the staining of surface IGF2BP1 on EVs using the antibody 12G5 is shown. At least the EVs from ascites 1 and 3 contain IGF2BP1.Example 9: IGF2BP1 is expressed on the surface of extracellular vesiclesEVs contained in ascites fluid from patients with ovarian cancer were isolated via standard protocols for EV isolation via differential centrifugation (400 x g; 2,500 x g; 100,000 x g) followed by a purification by floatation into a density gradient. The wells of a polystyrene 96-well cluster plate were coated with 12G5 (5 pg / ml), a GST-specific control antibody (5 pg / ml) overnight at 4 °C. Then, wells were blocked with 3% bovine serum albumin (BSA), followed by addition of 10 pg / well of EVs from 3 different donors.The plate was again incubated overnight at 4 °C. Then, wells were washed several times with TBS / 0.1 % Tween and incubated with an anti-CD63 antibody (CD63 is a protein expressed on most types of EVs), coupled with HRP. Finally, wells were developed with TMB; the reaction was stopped with H2SO4 and the optical density (OD) at 450 nm was measured. Figure 10 B shows that intact EVs from ovarian cancer patients previously incubated with the antibody 12G5 shows a higher OD450nm measurement after incubation with anti-CD63 antibody compared to EVs incubated with an unrelated GST antibody. This is especially shown for samples EVs 48 and EVs 43. This finding confirms that IGF2BP1 , to which antibody 12G5 binds, is present on the surface of intact EVs.Example 10: Antibody 12G5 is internalized over time upon binding to SK-OV-3 cells SK-OV-3 ovarian cancer cells were incubated with 12G5 at room temperature for 10 min and then washed to remove excess free antibody. Cell samples were then incubated at 37 °C for one to five hours or placed on ice (= 0 hour). Cells were then stained with an Alexa647-coupled secondary anti-rat IgG antibody and fluorescence was measured by flow cytometry. Figure 11 shows a decrease of the measured fluorescence intensity from 0 to 5 hours, whereby in Figure 11 the fluorescence measured after 0 hours at 37 °C was set to 100 %. This result clearly shows a reduction of fluorescence which is indicative for an internalization of the antibody 12G5 bound to surface IGF2BP1 by SK-OV-3 cancer cells. The decrease in fluorescence over time is indicative for the internalization of the IGF2BP1 -12G5 complex.Example 11 : Comparison of surface IGF2BP1 binding with 12G5 and commercially available IGF2BP1 antibodiesFor this experiment flow cytometry analyses were made with living human A549 cells and with fixed and permeabilized A549 cells using a Fix & Perm Cell Permeabilization Kit from Life Technologies.The living A549 cancer cells and the fixed and permeabilized A549 cells were incubated with the 12G5 antibody, the commercially available IGF2BP1 antibodies from Invitrogen (catalog # PAS-23968), from Abeam (catalog # ab290736 and catalog # ab 184305), Novus (catalog # NBP1 -79024), or a suitable isotype control antibody, followed by incubation with a suitable Alexa-647 labeled secondary antibody. Finally, cells were analyzed by flow cytometry. Figure 12 shows in the upper panel the bindingof the tested antibodies to living A549 cells (solid lines) compared to the control (gray tinted histograms). It is clearly visible that the commercially available IGF2BP1 antibodies failed to bind to IGF2BP1 on the surface of A549 cancer cells and only the antibody 12G5 is able to bind to IGF2BP1 on the surface of A549 cancer cells. Figure 12, lower panel, shows the binding of both the 12G5 antibody and the commercially available antibodies (solid lines) to intracellular IGF2BP1 of fixed and permeabilized A549 cells compared to an antibody control (gray tinted histograms). Thus, both 12G5 and commercially available IGF2BP1 antibodies binds to intracellular IGF2BP1 of permeabilized A549 cancer cells.This finding demonstrates that only the antibody 12G5 (and not commercially available IGF2BP1 antibodies) could bind to IGF2BP1 on the surface of living A549 cancer cells.Example 12: Fab fragment of 12G5 binds to IGF2BP1Fab fragments generated from the antibody 12G5 were incubated with A549 cells or an isotype control antibody. Cells were then washed and incubated with an Alexa647 labeled anti-rat IgG antibody. Fluorescence was measured by flow cytometry on a FACS Canto. As shown in figure 13 the Fab fragment of 12G5 (solid line) binds in the same manner to IGF2BP1 on the surface of cancer cells as the 12G5 antibody and compared to the isotype control antibody (gray histogram).REFERENCESBhattacharyya S, Dixit M. Metallic radionuclides in the development of diagnostic and therapeutic radiopharmaceuticals. 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Claims

ClaimsWhat is claimed:

1. Pharmaceutical composition comprising a monoclonal antibody, which binds to human IGF2BP1 present on the cell surface of a target cell and optionally a pharmaceutically acceptable carrier, diluent or excipient, wherein said target cell is a non-permeabilized cell or a living cell.

2. The pharmaceutical composition of any one of the preceding claims, wherein said antibody has cytotoxic activity.

3. The pharmaceutical composition of any one of the preceding claims, wherein said antibody has ADCC or CDC.

4. The pharmaceutical composition of any one of the preceding claims, wherein said antibody is conjugated with a cytotoxic substance or a substance used for in-vivo imaging.

5. The pharmaceutical composition of any one of the preceding claims, wherein said antibody is internalized from the target cell after binding to IGF2BP1 present on the cell surface.

6. The pharmaceutical composition of any one of the preceding claims, wherein said antibody or a portion thereof is part of a chimeric antigen receptor (CAR).

7. The pharmaceutical composition of claim 6, wherein said CAR is comprised by a T cell, NK cell, NK-T cell or macrophage.

8. The pharmaceutical composition of any one of the preceding claims, wherein said antibody is less than 20% cross-reactive with IGF2BP1 -related proteins.

9. The pharmaceutical composition of any one of the preceding claims, wherein said antibody is an antibody comprising a heavy chain variable region having an aminoacid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 2.

10. The pharmaceutical composition of any one of the preceding claims, wherein said antibody is an antibody comprising a heavy chain variable region comprising heavy chain CDR1 having the amino acid sequence as set forth in SEQ ID NO:3, heavy chain CDR2 having the amino acid sequence as set forth in SEQ ID NO:4, and heavy chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 5, and a light chain variable region comprising light chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 6, light chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 7, and light chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 8.11 . The pharmaceutical composition of any one of claims 6 or 7, wherein the CAR comprises the heavy chain variable region and the light chain variable region of claim 9 or one or more of the CDRs of claim 10.

12. The pharmaceutical composition of any one of the preceding claims for use in an in-vivo diagnostic imaging method for diagnosing cancer.

13. The pharmaceutical composition of any one of the preceding claims for use in a method for the treatment of cancer in a human subject.

14. The pharmaceutical composition for the use of any one of claims 12 or 13, wherein said cancer is characterized by cells, wherein human IGF2BP1 is present on their cell surface.

15. The pharmaceutical composition for the use of any one of claims 11 to 14, wherein said cancer is breast cancer, ovarian cancer, brain cancer, melanoma, non-small-cell-lung cancer, pancreatic cancer, colon cancer, colorectal cancer, mesenchymal cancer, Hodgkin lymphoma, B cell lymphomas, acute myeloid leukemia (AML) or acute lymphatic leukemia (ALL) of the T cell type.

16. The pharmaceutical composition for the use of any one of claims 11 to 14, wherein said cancer is cervical cancer, colorectal adeno carcinoma, laryngeal squamous cell carcinoma, lung cancer, pancreatic adenocarcinoma, ovarian cancer, ovarian clear-cell carcinoma, acute myeloid leukemia (AML) or acute lymphatic leukemia (ALL) of the T cell type.

17. A method for determining whether a human subject may suffer from cancer, comprising determining in a sample obtained from said human subject whether IGF2BP1 is present on the cell surface of cells comprised by said sample, wherein said cells are non-permeabilized cells or living cells.

18. A method for determining whether a human subject may suffer from cancer, comprising determining in a sample obtained from said human subject whether IGF2BP1 is present on the surface of extracellular vesicles comprised by said sample.

19. An antibody which binds to human IGF2BP1 present on the cell surface of a target cell wherein said antibody is an antibody comprising a heavy chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 2; wherein said target cell is a non-permeabilized cell or a living cell.

20. An antibody which binds to human IGF2BP1 present on the surface of an extracellular vesicle, wherein said antibody is an antibody comprising a heavy chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 2.

21. An antibody which binds to human IGF2BP1 present on the cell surface of a target cell comprising an antibody comprising a heavy chain variable region comprising heavy chain CDR1 having the amino acid sequence as set forth inSEQ ID NO: 3, heavy chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 4, and heavy chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 5, and a light chain variable region comprising light chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 6, light chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 7, and light chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 8.

22. The antibody of claim 21 , wherein said target cell is a non-permeabilized cell.

23. The antibody of claim 21 , wherein said target cell is a living cell.

24. An antibody which binds to human IGF2BP1 present on the surface of an extracellular vesicle comprising an antibody comprising a heavy chain variable region comprising heavy chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 3, heavy chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 4, and heavy chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 5, and a light chain variable region comprising light chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 6, light chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 7, and light chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 8.

25. An antibody, which binds to human IGF2BP1 present on the cell surface of a target cell for use in a method of killing said target cell having IGF2BP1 present on the cell surface.

26. The antibody of claim 25, wherein said antibody is an antibody comprising a heavy chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 2.

27. The antibody of any one of claims 25 or 26, wherein said antibody is an antibody comprising a heavy chain variable region comprising heavy chain CDR1 havingthe amino acid sequence as set forth in SEQ ID NO: 3, heavy chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 4, and heavy chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 5, and a light chain variable region comprising light chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 6, light chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 7, and light chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 8.

28. A method of killing a target cell having IGF2BP1 present on the cell surface, comprising administering an antibody, which binds to human IGF2BP1 present on the cell surface of said target cell.

29. The method of claim 28, wherein said antibody is an antibody comprising a heavy chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 2.

30. The method of any one of claims 28 or 29, wherein said antibody is an antibody comprising a heavy chain variable region comprising heavy chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 3, heavy chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 4, and heavy chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 5, and a light chain variable region comprising light chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 6, light chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 7, and light chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 8.

31. An antibody, which binds to human IGF2BP1 present on the cell surface of a target cell for use in a method for the treatment of cancer in a subject, comprising, prior to the treatment of cancer in said subject, determining whether a target cell of said subject has IGF2BP1 present on the cell surface.

32. The antibody of claim 31 , wherein said antibody is an antibody comprising a heavy chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 1 and a light chain variable region having an amino acid sequence with at least 85% identity to the amino acid sequence shown in SEQ ID NO: 2.

33. The antibody of any one of claims 31 or 32, wherein said antibody is an antibody comprising a heavy chain variable region comprising heavy chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 3, heavy chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 4, and heavy chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 5, and a light chain variable region comprising light chain CDR1 having the amino acid sequence as set forth in SEQ ID NO: 6, light chain CDR2 having the amino acid sequence as set forth in SEQ ID NO: 7, and light chain CDR3 having the amino acid sequence as set forth in SEQ ID NO: 8.

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