Pub Date : 2009-10-26DOI: 10.1089/HYB.2009.0037.MAB
Esin Aslankaraoglu-Akcael, R. Demirgan, K. Yesilbag, F. Yucel
{"title":"MAbs Against Bovine Viral Diarrhea Virus (BVDV)","authors":"Esin Aslankaraoglu-Akcael, R. Demirgan, K. Yesilbag, F. Yucel","doi":"10.1089/HYB.2009.0037.MAB","DOIUrl":"https://doi.org/10.1089/HYB.2009.0037.MAB","url":null,"abstract":"","PeriodicalId":55044,"journal":{"name":"Hybridoma","volume":"28 1","pages":"383-384"},"PeriodicalIF":0.0,"publicationDate":"2009-10-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1089/HYB.2009.0037.MAB","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"61243340","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
B. Sayan, N. Emre, M. B. Irmak, M. Ozturk, R. Cetin-Atalay
Mouse monoclonal antibodies (MAb) were generated against p33ING1b tumor suppressor protein. 15B9 MAb was highly specific in recognizing a single protein band of approximately 33 kDa endogenous p33ING1b protein from HCC cell lines and normal liver tissue by Western blot analysis and by immunoprecipitation. Although p33ING1b mutations are rarely observed in cancer, differential subcellular distribution and nuclear exclusion of p33ING1b were reported in different cancer types. Therefore we analyzed the expression and subcellular localization of p33ING1b in HCC cell lines using 15B9 MAb. So far, p33ING1b mutations or differential subcellular localization are not reported in HCC. In this study, by indirect immunofluorescence using MAb 15B9, we demonstrate that nuclear localization of p33ING1b was highly correlated with well-differentiated HCC cell lines whereas poorly differentiated HCC cells have nuclear exclusion of the protein. Moreover no association was observed between differential subcellular localization of p33ING1b and p53 mutation status of HCC cell lines. Hence our newly produced MAb 15B9 can be used for studying cellular activities of p33ING1b under normal and cancerous conditions.
{"title":"Nuclear exclusion of p33ING1b tumor suppressor protein: explored in HCC cells using a new highly specific antibody.","authors":"B. Sayan, N. Emre, M. B. Irmak, M. Ozturk, R. Cetin-Atalay","doi":"10.1089/hyb.2008.0058","DOIUrl":"https://doi.org/10.1089/hyb.2008.0058","url":null,"abstract":"Mouse monoclonal antibodies (MAb) were generated against p33ING1b tumor suppressor protein. 15B9 MAb was highly specific in recognizing a single protein band of approximately 33 kDa endogenous p33ING1b protein from HCC cell lines and normal liver tissue by Western blot analysis and by immunoprecipitation. Although p33ING1b mutations are rarely observed in cancer, differential subcellular distribution and nuclear exclusion of p33ING1b were reported in different cancer types. Therefore we analyzed the expression and subcellular localization of p33ING1b in HCC cell lines using 15B9 MAb. So far, p33ING1b mutations or differential subcellular localization are not reported in HCC. In this study, by indirect immunofluorescence using MAb 15B9, we demonstrate that nuclear localization of p33ING1b was highly correlated with well-differentiated HCC cell lines whereas poorly differentiated HCC cells have nuclear exclusion of the protein. Moreover no association was observed between differential subcellular localization of p33ING1b and p53 mutation status of HCC cell lines. Hence our newly produced MAb 15B9 can be used for studying cellular activities of p33ING1b under normal and cancerous conditions.","PeriodicalId":55044,"journal":{"name":"Hybridoma","volume":"28 1 1","pages":"1-6"},"PeriodicalIF":0.0,"publicationDate":"2009-02-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1089/hyb.2008.0058","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"61242987","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Hidehiro Takahashi, Y. Kitagawa, Masae Maeda-Satoh, H. Hasegawa, H. Sawa, T. Sata
Telomerase, a ribonucleoprotein enzyme, is a cellular RNA-dependent DNA polymerase that serves to maintain the tandem arrays of telomeric repeats at the eukaryotic chromosomal ends. We previously reported that topoisomerase I dissociates HIV-1 reverse transcriptase from genomic RNAs, and binding of topoisomerase I to RNA template regulates cDNA synthesis. We also found that a monoclonal antibody (MAb) against topoisomerase I, designated as MAb 1, suppresses the reverse transcription efficiency using a detergent-disrupted HIV-1 virion. In this study, we describe how MAb 1 suppresses telomerase activity in cellular lysates. In addition, siRNAs of topoisomerase I has attenuated telomerase activity in culture cells. These results suggest that topoisomerase I is involved in telomerase activity, as well as HIV-1 reverse transcription.
{"title":"Monoclonal antibody and siRNAs for topoisomerase I suppress telomerase activity.","authors":"Hidehiro Takahashi, Y. Kitagawa, Masae Maeda-Satoh, H. Hasegawa, H. Sawa, T. Sata","doi":"10.1089/hyb.2008.0066","DOIUrl":"https://doi.org/10.1089/hyb.2008.0066","url":null,"abstract":"Telomerase, a ribonucleoprotein enzyme, is a cellular RNA-dependent DNA polymerase that serves to maintain the tandem arrays of telomeric repeats at the eukaryotic chromosomal ends. We previously reported that topoisomerase I dissociates HIV-1 reverse transcriptase from genomic RNAs, and binding of topoisomerase I to RNA template regulates cDNA synthesis. We also found that a monoclonal antibody (MAb) against topoisomerase I, designated as MAb 1, suppresses the reverse transcription efficiency using a detergent-disrupted HIV-1 virion. In this study, we describe how MAb 1 suppresses telomerase activity in cellular lysates. In addition, siRNAs of topoisomerase I has attenuated telomerase activity in culture cells. These results suggest that topoisomerase I is involved in telomerase activity, as well as HIV-1 reverse transcription.","PeriodicalId":55044,"journal":{"name":"Hybridoma","volume":"28 1 1","pages":"63-5"},"PeriodicalIF":0.0,"publicationDate":"2009-02-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1089/hyb.2008.0066","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"61243037","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Michael G. K. Jones, V. McLoughlin, J. Connolly, C. Farquhar, I. Macgregor, M. Head
The human prion diseases, such as variant Creutzfeldt-Jakob disease (vCJD), are characterized by the conversion of the normal cellular prion protein (PrP(C)) into an abnormal disease associated form (PrP(Sc)). Monoclonal antibodies (MAbs) that recognize these different PrP isoforms are valuable reagents both in the diagnosis of these diseases and in prion disease research in general but we know of no attempts to raise MAbs against native human PrP(C). We immunized prion protein gene ablated (PrP(-/-)) mice with native human PrP(C) purified from platelets (pHuPrP) generating a predominantly IgG isotype anti-pHuPrP polyclonal antibody response in all mice. Following fusion of splenocytes from the immunized mice with SP2/0 myeloma cells, we were able to identify single cell clone and cryopreserve 14 stable hybridoma cell lines producing MAbs that reacted with pHuPrP. The properties of these MAbs (such as isotype, binding to native/denatured pHuPrP, and HuPrP epitopes recognized) are described. Furthermore, several of these MAbs showed a selectivity in their ability to immunoprecipitate disease associated PrP(Sc) and its corresponding protease resistant core (PrP(res)).
{"title":"Production and characterization of a panel of monoclonal antibodies against native human cellular prion protein.","authors":"Michael G. K. Jones, V. McLoughlin, J. Connolly, C. Farquhar, I. Macgregor, M. Head","doi":"10.1089/hyb.2008.0067","DOIUrl":"https://doi.org/10.1089/hyb.2008.0067","url":null,"abstract":"The human prion diseases, such as variant Creutzfeldt-Jakob disease (vCJD), are characterized by the conversion of the normal cellular prion protein (PrP(C)) into an abnormal disease associated form (PrP(Sc)). Monoclonal antibodies (MAbs) that recognize these different PrP isoforms are valuable reagents both in the diagnosis of these diseases and in prion disease research in general but we know of no attempts to raise MAbs against native human PrP(C). We immunized prion protein gene ablated (PrP(-/-)) mice with native human PrP(C) purified from platelets (pHuPrP) generating a predominantly IgG isotype anti-pHuPrP polyclonal antibody response in all mice. Following fusion of splenocytes from the immunized mice with SP2/0 myeloma cells, we were able to identify single cell clone and cryopreserve 14 stable hybridoma cell lines producing MAbs that reacted with pHuPrP. The properties of these MAbs (such as isotype, binding to native/denatured pHuPrP, and HuPrP epitopes recognized) are described. Furthermore, several of these MAbs showed a selectivity in their ability to immunoprecipitate disease associated PrP(Sc) and its corresponding protease resistant core (PrP(res)).","PeriodicalId":55044,"journal":{"name":"Hybridoma","volume":"28 1 1","pages":"13-20"},"PeriodicalIF":0.0,"publicationDate":"2009-02-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1089/hyb.2008.0067","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"61243160","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"MAb against the small subunit of human ribonucleotide reductase (hRRM2)","authors":"Y. Yen","doi":"10.1089/HYB.2006.25.313","DOIUrl":"https://doi.org/10.1089/HYB.2006.25.313","url":null,"abstract":"","PeriodicalId":55044,"journal":{"name":"Hybridoma","volume":"25 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2006-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1089/HYB.2006.25.313","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"61243200","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2001-08-01DOI: 10.1089/027245701753179785
Alexis Pérez, Josefa Lombardero, Cristina Mateo, G. Mustelier, M. Alfonso, A. Vázquez, Rolando Pérez
The variable regions from P3, a murine monoclonal antibody (MAb) against NeuGc-containing gangliosides, and two anti-idiotype MAbs directed to P3 MAb were cloned and sequenced. Comparisons with previously reported sequences showed that P3 is a germline antibody encoded by genes from the V(H)Q52 and V(kappa)19 families. Analysis of nucleotides at the heavy chain CDR3 (H-CDR3) showed the presence of an extensive 3' N region that contains almost 50% of the nucleotides of this CDR. In addition, amino acid sequence analysis of the H-CDRs of this MAb revealed the presence of three arginines, two of which are present in the H-CDR3, that could be involved in the interaction of P3 MAb with its electronegative epitope on gangliosides. Anti-idiotype 1E10, which seems to define a "regulatory" idiotope on P3 MAb (it induces Id+ Ab3), represents a germline Ab2 that belongs to the V(H)J558 and V(kappa)10 gene families. By contrary, the anti-idiotype 3B11 is an extensively mutated antibody that belongs to the V(H)3660 and V(kappa)4/5 gene families, defining a "private" idiotope on P3 MAb. Even when different V genes contribute to the variable regions of 1E10 and 3B11 MAbs, they share an acidic motif E/D-D-Y/D-Y-D in H-CDR3, suggesting that both Ab2s recognize paratope positive residues on the Ab1. Therefore, complementary electrostatic interactions involving H-CDR3 from both Ab1 and Ab2, might provide a clue to understand the molecular basis for the generation of gamma-type anti-idiotype antibodies to V regions recognizing glycolylated ganglioside antigens.
{"title":"Immunogenetic analysis of variable regions encoding AB1 and gamma-type AB2 antibodies from the NeuGc-containing ganglioside family.","authors":"Alexis Pérez, Josefa Lombardero, Cristina Mateo, G. Mustelier, M. Alfonso, A. Vázquez, Rolando Pérez","doi":"10.1089/027245701753179785","DOIUrl":"https://doi.org/10.1089/027245701753179785","url":null,"abstract":"The variable regions from P3, a murine monoclonal antibody (MAb) against NeuGc-containing gangliosides, and two anti-idiotype MAbs directed to P3 MAb were cloned and sequenced. Comparisons with previously reported sequences showed that P3 is a germline antibody encoded by genes from the V(H)Q52 and V(kappa)19 families. Analysis of nucleotides at the heavy chain CDR3 (H-CDR3) showed the presence of an extensive 3' N region that contains almost 50% of the nucleotides of this CDR. In addition, amino acid sequence analysis of the H-CDRs of this MAb revealed the presence of three arginines, two of which are present in the H-CDR3, that could be involved in the interaction of P3 MAb with its electronegative epitope on gangliosides. Anti-idiotype 1E10, which seems to define a \"regulatory\" idiotope on P3 MAb (it induces Id+ Ab3), represents a germline Ab2 that belongs to the V(H)J558 and V(kappa)10 gene families. By contrary, the anti-idiotype 3B11 is an extensively mutated antibody that belongs to the V(H)3660 and V(kappa)4/5 gene families, defining a \"private\" idiotope on P3 MAb. Even when different V genes contribute to the variable regions of 1E10 and 3B11 MAbs, they share an acidic motif E/D-D-Y/D-Y-D in H-CDR3, suggesting that both Ab2s recognize paratope positive residues on the Ab1. Therefore, complementary electrostatic interactions involving H-CDR3 from both Ab1 and Ab2, might provide a clue to understand the molecular basis for the generation of gamma-type anti-idiotype antibodies to V regions recognizing glycolylated ganglioside antigens.","PeriodicalId":55044,"journal":{"name":"Hybridoma","volume":"20 4 1","pages":"211-21"},"PeriodicalIF":0.0,"publicationDate":"2001-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1089/027245701753179785","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"60499902","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2001-08-01DOI: 10.1089/027245701753179794
W. Loveless, T. Feizi, M. Valeri, R. Day, S. Bay
Monoclonal antibodies (MAbs) directed to Lewis(x) (Le(x)) and related carbohydrate sequences have been invaluable in anticipating biological roles for these oligosaccharides by detecting the remarkable changes that occur in their expression from the earliest stages of embryogenesis, through development and sequential stages of cell differentiation and maturation. A notable impact has been in the molecular dissection of ligand-receptor interactions in key cell adhesion events at the initial stages of leukocyte recruitment in inflammation, and almost certainly in the metastasis of epithelial tumours. Antibodies that recognise Le(x) and the 3'-sialyl forms were observed to identify leukocyte subsets; these were subsequently found to match those recognized by the leukocyte-endothelium adhesion molecules, the E- and P-selectins. We now describe a MAb (rat hybridoma MIN/3/60) raised to 3'-sulpho-Le(x), a carbohydrate sequence which, in vitro, is bound not only by the E-, L-, and P-selectins, but also by the cysteine-rich domain of the macrophage endocytosis receptor. We observe that MIN/3/60 is bispecific, however; it binds 3'-sulpho-Le(a) as well as 3'-sulpho-Le(x). Nevertheless, our exploratory studies reveal that it may be a useful histochemical reagent when used in conjunction with a monospecific antibody to 3'-sulpho-Le(a). The MIN/3/60 antibody reveals a sub-population of epithelial glycans in the crypts of Lieberkühn in normal human colon.
针对Lewis(x) (Le(x))和相关碳水化合物序列的单克隆抗体(mab)在预测这些低聚糖的生物学作用方面是无价的，通过检测它们在胚胎发生的早期阶段，通过发育和细胞分化和成熟的顺序阶段的表达中发生的显著变化。一个值得注意的影响是在炎症中白细胞募集的初始阶段关键细胞粘附事件中的配体-受体相互作用的分子解剖，几乎肯定在上皮肿瘤的转移中。观察到识别Le(x)和3'-sialyl形式的抗体可识别白细胞亚群;这些随后被发现与白细胞内皮粘附分子E-和p -选择素识别的分子相匹配。我们现在描述了一个MAb(大鼠杂杂瘤MIN/3/60)提高到3'-硫- le (x)，这是一个碳水化合物序列，在体外，不仅与E-， L-和p -选择素结合，而且与巨噬细胞内吞作用受体的富含半胱氨酸的结构域结合。我们观察到MIN/3/60是双特异性的;它能结合3'-硫硫- le (a)和3'-硫硫- le (x)。然而，我们的探索性研究表明，当与3'-硫- le (a)的单特异性抗体结合使用时，它可能是一种有用的组织化学试剂。MIN/3/60抗体显示正常人结肠lieberk隐窝中存在上皮聚糖亚群。
{"title":"A monoclonal antibody, MIN/3/60, that recognizes the sulpho-Lewis(x) and sulpho-Lewis(a) sequences detects a sub-population of epithelial glycans in the crypts of human colonic epithelium.","authors":"W. Loveless, T. Feizi, M. Valeri, R. Day, S. Bay","doi":"10.1089/027245701753179794","DOIUrl":"https://doi.org/10.1089/027245701753179794","url":null,"abstract":"Monoclonal antibodies (MAbs) directed to Lewis(x) (Le(x)) and related carbohydrate sequences have been invaluable in anticipating biological roles for these oligosaccharides by detecting the remarkable changes that occur in their expression from the earliest stages of embryogenesis, through development and sequential stages of cell differentiation and maturation. A notable impact has been in the molecular dissection of ligand-receptor interactions in key cell adhesion events at the initial stages of leukocyte recruitment in inflammation, and almost certainly in the metastasis of epithelial tumours. Antibodies that recognise Le(x) and the 3'-sialyl forms were observed to identify leukocyte subsets; these were subsequently found to match those recognized by the leukocyte-endothelium adhesion molecules, the E- and P-selectins. We now describe a MAb (rat hybridoma MIN/3/60) raised to 3'-sulpho-Le(x), a carbohydrate sequence which, in vitro, is bound not only by the E-, L-, and P-selectins, but also by the cysteine-rich domain of the macrophage endocytosis receptor. We observe that MIN/3/60 is bispecific, however; it binds 3'-sulpho-Le(a) as well as 3'-sulpho-Le(x). Nevertheless, our exploratory studies reveal that it may be a useful histochemical reagent when used in conjunction with a monospecific antibody to 3'-sulpho-Le(a). The MIN/3/60 antibody reveals a sub-population of epithelial glycans in the crypts of Lieberkühn in normal human colon.","PeriodicalId":55044,"journal":{"name":"Hybridoma","volume":"20 4 1","pages":"223-9"},"PeriodicalIF":0.0,"publicationDate":"2001-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1089/027245701753179794","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"60500078","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2001-08-01DOI: 10.1089/027245701753179802
G. Hass, J. Meyer, R. Newitt, T. Labuda, L. Brown, R. Aebersold, R. Vessella
The monoclonal antibody (MAb) A6H, originally developed to fetal renal tissues, was found to be highly reactive to renal cell carcinoma and was subsequently demonstrated to co-stimulate a subpopulation of T cells. The A6H antigen had not been identified heretofore. Antigen from detergent extracts of renal cell carcinoma cells (7860) was immunoabsorbed with A6H-agarose, and the resin-bound proteins were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The antigen had a molecular weight of approximately 120 kDa as determined by Western blots. The 120-kDa protein band was excised and subjected to in-gel tryptic digestion, and the resulting peptides were separated and analyzed by liquid chromatography tandem mass spectrometry (LC MSMS). The tandem mass spectra of the eluting peptides were used in combination with the SEQUEST computer program to search a human National Cancer Institute (NCI) protein database for the identity of the protein. The target antigen was shown to be dipeptidyl peptidase IV (DPP IV), which is also known as the cluster differentiation antigen CD26. Flow analysis of the expression of the A6H antigen and of CD26 on 7860 cells and on peripheral blood lymphocytes supported the identification of the A6H antigen as DPP IV. Recognition that the A6H antigen is DPP IV/CD26 afforded the opportunity to compare previous studies on A6H with those on other anti-CD26 antibodies in terms of expression in cancer cell lines and various tissues and as co-stimulators of T-cell activation.
{"title":"Identification of the target of monoclonal antibody A6H as dipeptidyl peptidase IV/CD26 by LC MSMS.","authors":"G. Hass, J. Meyer, R. Newitt, T. Labuda, L. Brown, R. Aebersold, R. Vessella","doi":"10.1089/027245701753179802","DOIUrl":"https://doi.org/10.1089/027245701753179802","url":null,"abstract":"The monoclonal antibody (MAb) A6H, originally developed to fetal renal tissues, was found to be highly reactive to renal cell carcinoma and was subsequently demonstrated to co-stimulate a subpopulation of T cells. The A6H antigen had not been identified heretofore. Antigen from detergent extracts of renal cell carcinoma cells (7860) was immunoabsorbed with A6H-agarose, and the resin-bound proteins were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The antigen had a molecular weight of approximately 120 kDa as determined by Western blots. The 120-kDa protein band was excised and subjected to in-gel tryptic digestion, and the resulting peptides were separated and analyzed by liquid chromatography tandem mass spectrometry (LC MSMS). The tandem mass spectra of the eluting peptides were used in combination with the SEQUEST computer program to search a human National Cancer Institute (NCI) protein database for the identity of the protein. The target antigen was shown to be dipeptidyl peptidase IV (DPP IV), which is also known as the cluster differentiation antigen CD26. Flow analysis of the expression of the A6H antigen and of CD26 on 7860 cells and on peripheral blood lymphocytes supported the identification of the A6H antigen as DPP IV. Recognition that the A6H antigen is DPP IV/CD26 afforded the opportunity to compare previous studies on A6H with those on other anti-CD26 antibodies in terms of expression in cancer cell lines and various tissues and as co-stimulators of T-cell activation.","PeriodicalId":55044,"journal":{"name":"Hybridoma","volume":"20 4 1","pages":"231-6"},"PeriodicalIF":0.0,"publicationDate":"2001-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1089/027245701753179802","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"60500205","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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