|Application ||WB, IHC|
|Calculated MW||87437 Da|
|Positive Control||Western Blot, IHC|
|Application & Usage||WB: 0.1 µg/ml, IHC: 5-15 µg/ml|
|Other Names||DPP4, DPP-4, ADABP, ADCP2, ADCP-2, CD26, CD-26, DPPIV, DPPIV, TP103, TP-103|
|Formulation||0.2 mg/ml in PBS|
|Handling||The antibody solution should be gently mixed before use.|
|Reconstitution & Storage||-20 °C|
|Precautions||DPPIV (Mouse) Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||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.|
|Cellular Location||Dipeptidyl peptidase 4 soluble form: Secreted. Note=Detected in the serum and the seminal fluid|
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Dipeptidyl peptidase-IV (DPPIV), also known as adenosine deaminase complexing protein 2, DPPIV or CD26 is antigenic enzyme expressed on the surface of most cell types and is associated with immune regulation, signal transduction and apoptosis. It is an intrinsic membrane glycoprotein and a serine exopeptidase that cleaves X-proline dipeptides from the N-terminus of polypeptides. The substrates of DPPIV are proline (or alanine)-containing peptides and include growth factors, chemokines, neuropeptides, and vasoactive peptides. DPPIV plays a major role in glucose metabolism. It is responsible for the degradation of incretins such as GLP-1. DPPIV plays an important role in tumor biology, and is useful as a marker for various cancers, with its levels either on the cell surface or in the serum increased in some neoplasms and decreased in others. DPPIV also binds the enzyme adenosine deaminase specifically and with high affinity. The significance of this interaction has yet to be established.
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