Dipeptidyl peptidase 4 (Dpp4) Recombinant Protein | Dpp4 recombinant protein

Recombinant Rat Dipeptidyl peptidase 4 (Dpp4), partial

Cat. Num. AAA9424088

• Gene Names: Dpp4; CD26; DPPIV
• Reactivity: Rat
• Purity: Greater than 90% as determined by SDS-PAGE.
• Synonyms: Dipeptidyl peptidase 4 (Dpp4); Recombinant Rat Dipeptidyl peptidase 4 (Dpp4); partial; Bile canaliculus domain-specific membrane glycoprotein; Dpp4 recombinant protein

• Host: E Coli
• Reactivity: Rat
• Purity/Purification: Greater than 90% as determined by SDS-PAGE.
• Form/Format: Tris-based buffer, 50% glycerol
• Sequence Positions: Partial, 638-767aa

• Tag Info: N-terminal 6xHis-SUMO-tagged
• Preparation and Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.; Generally, the shelf life of liquid form is 6 months at -20 degree C/-80 degree C. The shelf life of lyophilized form is 12 months at -20 degree C/-80 degree C.

Related Product Information for Dpp4 recombinant protein

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 domain 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 #: 6978773
• NCBI GeneID: 25253
• NCBI Accession #: NP_036921.1
• NCBI GenBank Nucleotide #: NP_036921.1
• UniProt Accession #: P14740
• Molecular Weight: 30.73 kDa
• NCBI Official Full Name: dipeptidyl peptidase 4
• NCBI Official Synonym Full Names: dipeptidylpeptidase 4
• NCBI Official Symbol: Dpp4
• NCBI Official Synonym Symbols: CD26; DPPIV
• NCBI Protein Information: dipeptidyl peptidase 4
• UniProt Protein Name: Dipeptidyl peptidase 4
• Protein Family: Dipeptidyl peptidase
• UniProt Gene Name: Dpp4
• UniProt Synonym Gene Names: Cd26; DPP IV

NCBI Description

catalyzes the degradation of glucagon-like peptide-1 (Glp-1); involved in proteolysis and peptidolysis [RGD, Feb 2006]

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 adhesion; Cell surface; EC 3.4.14.5; Membrane protein, integral; Protease

Chromosomal Location of Human Ortholog: 3q21

Cellular Component: apical plasma membrane; cell surface; endocytic vesicle; endoplasmic reticulum; focal adhesion; Golgi apparatus; intercellular canaliculus; lamellipodium; lysosomal membrane; membrane; plasma membrane

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

Biological Process: behavioral fear response; endothelial cell migration; establishment of localization; positive regulation of cell proliferation; proteolysis; regulation of cell-cell adhesion mediated by integrin; regulation of T cell mediated immunity; response to hypoxia; T cell activation; T cell costimulation