protein

DPP4 (CD26), 39-766aa, Human,His-tag, Recombinant, Hi-5 cell

MBS203255

0.1 mg

375 USD

Recombinant Protein

DPP4 (CD26), 39-766aa, Human,His-tag, Recombinant, Hi-5 cell

DPP4

DPPIV; ADABP; ADCP2; TP103; Dipeptidyl peptidase-4; DPP4; dipeptidyl-peptidase 4; CD26; dipeptidylpeptidase IV (CD26 adenosine deaminase complexing protein 2); adenosine deaminase complexing protein 2

dipeptidyl peptidase 4; Dipeptidyl peptidase 4; dipeptidyl peptidase 4; ADCP-2; DPP IV; T-cell activation antigen CD26; adenosine deaminase complexing protein 2; dipeptidyl peptidase IV; dipeptidylpeptidase 4; dipeptidylpeptidase IV (CD26, adenosine deaminase complexing protein 2); dipeptidyl-peptidase 4; ADABP; Adenosine deaminase complexing protein 2; ADCP-2; Dipeptidyl peptidase IV; DPP IV; T-cell activation antigen CD26; TP103; CD_antigen: CD26Cleaved into the following 2 chains:Dipeptidyl peptidase 4 membrane formAlternative name(s):Dipeptidyl peptidase IV membrane form

DPP4

DPP4; DPP4; CD26; ADABP; ADCP2; DPPIV; TP103; ADCP2; CD26; ADCP-2; DPP IV

DPP4_HUMAN

ADP[Mature form of DPP-4(Ser 39 –Pro 766)]-SGRLVPRGSHHHHHH

> 95% by SDS - PAGE

Liquid in 20mM Tris-HCl pH 8.0, 100mM NaCl, 1mM EDTA, 10% glycerol

0.5 mg/ml (determined by Absorbance at 280nm)

Can be stored at 4 degree C short term (1-2 weeks). For long term storage, aliquot and store at -20 degree C or -70 degree C. Avoid repeated freezing and thawing cycles.

SDS-PAGE

Antigen Species: Human. Tag: His-tag

Expression System: Hi-5. Bioactivity: Specific activity is > 200 units/mg, One unit produces 1.0 umole of p-Nitroaniline from Gly-Pro- p-Nitroaniline per minute at pH 8.0 at 37 degree C. Endotoxin: < 1.0 Eu per 1 microgram of protein (determined by LAL method)

Enzymes & Proteases

DPP4, dipeptidyl peptidase-4 is a complex enzyme expressed on the surface of most cell types and is a serine exopeptidase that cleaves x-proline dipeptides from the N-terminus of polypeptides. DPP4 protein is associated with intracellular signal transduction, apoptosis and plays an important role in tumor biology. There are at least 63 substrates which can bind specifically to DPP4 enzyme including growth factors, chemokines, neuro peptides. Furthermore, DPP4 plays a major role in glucose metabolism by cleaving incretins such as glucose-dependent insulinotropic polypeptide (GIP) and glucagon-like peptide-1 (GLP-1). Recombinant human DPP4 protein was expressed with c-terminal His-tag in high-5 cells using baculovirus expression system and purified by using conventional chromatography techniques.

Pratley RE and Salsali A. (2007) Curr Med Res Opin. 23(4):919-31. Rosenstock J. and Zinman B. (2007) Curr Opin Endocrino Diabetes Obes.60(11):1454-70. Barnett A. (2006). J.Clin. Pract. 60(11):1454-70.

18765694

NP_001926

NM_001935.3

86.4kDa (746aa), confirmed by MALDI-TOF.

Incretin Synthesis, Secretion, And Inactivation Pathway (187170); Metabolism Of Proteins Pathway (106230); Peptide Hormone Metabolism Pathway (771603); Protein Digestion And Absorption Pathway (172847); Protein Digestion And Absorption Pathway (171868); Synthesis, Secretion, And Inactivation Of Glucagon-like Peptide-1 (GLP-1) Pathway (187171); Synthesis, Secretion, And Inactivation Of Glucose-dependent Insulinotropic Polypeptide (GIP) Pathway (187172)

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]

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; Cell adhesion; EC 3.4.14.5; Protease; Membrane protein, integral. Chromosomal Location of Human Ortholog: 2q24.3. Cellular Component: intercellular canaliculus; cell surface; focal adhesion; membrane; lamellipodium; endocytic vesicle; lysosomal membrane; apical plasma membrane; plasma membrane; integral to membrane; lipid raft. Molecular Function: identical protein binding; protein binding; protein homodimerization activity; protease binding; serine-type peptidase activity; dipeptidyl-peptidase activity; serine-type endopeptidase activity; receptor binding. Biological Process: regulation of cell-cell adhesion mediated by integrin; T cell activation; T cell costimulation; positive regulation of cell proliferation; response to hypoxia; endothelial cell migration; proteolysis

0.1 mg

375 USD

0.5 mg

925