DPP4 blocking peptide

DPP4 Antibody (Center) Blocking Peptide

• Gene Names: DPP4; CD26; ADABP; ADCP2; DPPIV; TP103
• Synonyms: DPP4; DPP4 Antibody (Center) Blocking Peptide; Dipeptidyl peptidase 4; 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; ADCP2; DPP4 blocking peptide

• Form/Format: Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.
• Sequence Length: 766

• 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.
• Preparation and Storage: Maintain refrigerated at 2-8 degree C for up to 6 months. For long term storage store at -20 degree C.

Related Product Information for DPP4 blocking peptide

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.

NCBI and Uniprot Product Information

• NCBI GI #: 1352311
• NCBI GeneID: 1803
• UniProt Accession #: P27487; Q53TN1
• Molecular Weight: 88,279 Da
• NCBI Official Full Name: Dipeptidyl peptidase 4
• NCBI Official Synonym Full Names: dipeptidyl peptidase 4
• NCBI Official Symbol: DPP4
• NCBI Official Synonym Symbols: CD26; ADABP; ADCP2; DPPIV; TP103
• NCBI Protein Information: dipeptidyl peptidase 4
• UniProt Protein Name: Dipeptidyl peptidase 4
• Protein Family: Dipeptidyl peptidase
• UniProt Gene Name: DPP4
• UniProt Synonym Gene Names: ADCP2; CD26; ADCP-2; DPP IV
• UniProt Entry Name: DPP4_HUMAN

NCBI Description

The protein encoded by this gene is identical to adenosine deaminase complexing protein-2, and to the T-cell activation antigen CD26. It is an intrinsic membrane glycoprotein and a serine exopeptidase that cleaves X-proline dipeptides from the N-terminus of polypeptides. [provided by RefSeq, Jul 2008]

Uniprot Description

DPP4: 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. Belongs to the peptidase S9B family. DPPIV subfamily.

Protein type: Cell surface; EC 3.4.14.5; Cell adhesion; Membrane protein, integral; Protease

Chromosomal Location of Human Ortholog: 2q24.3

Cellular Component: apical plasma membrane; cell surface; endocytic vesicle; focal adhesion; lamellipodium; lysosomal membrane; membrane; plasma membrane

Molecular Function: dipeptidyl-peptidase activity; identical protein binding; protease binding; protein binding; protein homodimerization activity; receptor binding; serine-type peptidase activity; viral receptor activity

Biological Process: endothelial cell migration; positive regulation of cell proliferation; regulation of cell-cell adhesion mediated by integrin; response to hypoxia; T cell activation; T cell costimulation