Dipeptidyl Peptidase 4 / CD26 (DPP4) Peptide
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Description
Dipeptidyl Peptidase 4 / CD26 (DPP4) Peptide is a synthetic peptide.
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Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | Dipeptidyl Peptidase 4 / CD26 (DPP4) |
| Host | Synthetic |
| Recommended Dilution | BL (predicted): 0.5 mg/ml. Optimal dilutions/concentrations should be determined by the end user. |
| Conjugation | Unconjugated |
| Observed MW | Sequence Fragment: Internal region: C-PPHFDKSKKYP |
| Size 1 | 100 µg |
| Form | Lyophilized Reconstitute in deionized water. |
| Tested Applications | P-ELISA |
| Buffer | Prior to lyophilization: Deionized water. |
| Availability | Shipped within 5-10 working days. |
| Storage | Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| Gene ID | 1803, 13482, 25253 |
| NCBI Accession | NP_001926.2 |
| Alias | CD26,ADABP,ADCP2,DPPIV,TP103,Dipeptidyl peptidase 4,Adenosine deaminase complexing protein 2,ADCP-2,Dipeptidyl peptidase IV,T-cell activation antigen CD26 |
| Background | Protein DPP4 |
| Note | This product is for research use only. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
Descripción
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DPP4 antibody
Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor(TCR)-mediated T-cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. 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. May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation. When overexpressed, enhanced cell proliferation, a process inhibited by GPC3. Acts also 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. Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.
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