CD26 (DPP IV / ADA-Binding Protein) Antibody - With BSA and Azide
Mouse Monoclonal Antibody [Clone 202.36]
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application ![]()
| IHC-F, IF, FC |
---|---|
Primary Accession | P27487 |
Other Accession | 1803, 368912 |
Reactivity | Human, Rat |
Host | Mouse |
Clonality | Monoclonal |
Isotype | Mouse / IgG2b, kappa |
Clone Names | 202.36 |
Calculated MW | 110kDa |
Gene ID | 1803 |
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Other Names | Dipeptidyl peptidase 4, 3.4.14.5, ADABP, Adenosine deaminase complexing protein 2, ADCP-2, Dipeptidyl peptidase IV, DPP IV, T-cell activation antigen CD26, TP103, CD26, Dipeptidyl peptidase 4 membrane form, Dipeptidyl peptidase IV membrane form, Dipeptidyl peptidase 4 soluble form, Dipeptidyl peptidase IV soluble form, DPP4, ADCP2, CD26 |
Storage | Store at 2 to 8°C.Antibody is stable for 24 months. |
Precautions | CD26 (DPP IV / ADA-Binding Protein) Antibody - With BSA and Azide is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | DPP4 (HGNC:3009) |
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Synonyms | ADCP2, CD26 |
Function | Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T- cell activation (PubMed:10900005, PubMed:10951221, PubMed:11772392, PubMed:17287217). Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC (PubMed:10900005, PubMed:10951221, PubMed:11772392, PubMed:14691230). Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner (PubMed:17287217). Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion (PubMed:11772392). In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM (PubMed:10593948, PubMed:16651416). May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation (PubMed:18708048). When overexpressed, enhanced cell proliferation, a process inhibited by GPC3 (PubMed:17549790). Also acts as a serine exopeptidase with a dipeptidyl peptidase activity that regulates various physiological processes by cleaving peptides in the circulation, including many chemokines, mitogenic growth factors, neuropeptides and peptide hormones such as brain natriuretic peptide 32 (PubMed:10570924, PubMed:16254193). Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline (PubMed:10593948). |
Cellular Location | [Dipeptidyl peptidase 4 soluble form]: Secreted Note=Detected in the serum and the seminal fluid |
Tissue Location | Expressed specifically in lymphatic vessels but not in blood vessels in the skin, small intestine, esophagus, ovary, breast and prostate glands. Not detected in lymphatic vessels in the lung, kidney, uterus, liver and stomach (at protein level). Expressed in the poorly differentiated crypt cells of the small intestine as well as in the mature villous cells. Expressed at very low levels in the colon |

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Provided below are standard protocols that you may find useful for product applications.
Background
Recognizes a glycoprotein of 110kDa, identified as CD26 (Workshop VI; Code: N-L039). It is an atypical serine protease belonging to the prolyl oligopeptidase family. It is expressed on lymphocyte cells and is upregulated during T-cell activation. CD26 is also expressed on activated B cells and natural killer cells and abundantly on epithelia. CD26 is implicated in a variety of biological functions including T-cell activation, cell adhesion with extracellular matrix such as fibronectin or collagens, and in HIV infection. Cross-linking of CD26 using this antibody dramatically enhances the anti-CD3-induced IL-2 production. In Western blotting, this MAb reacts with only glycosylated CD26, but not with the deglycosylated form. It does not prevent ADA binding to CD26.
References
Kishimoto T. et al., eds. Leukocyte Typing VI, p478-489 and p1128, Garland Publishing, Inc, New York and London, 1997

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