Recombinant human DPP4/CD26 protein

Specific activity is > 200unit/mg, One unit produces 1.0 umole of p-Nitroaniline from Gly-Pro- p-Nitroaniline per minute at pH 8.0 at 37C.

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.

Baculovirus

Enzymes & Proteases

85.4 kDa (737aa) confirmed by MALDI-TOF