重组人CPE蛋白

人

人胚胎肾细胞（HEK293）

Met 1 - Ser 453

A DNA sequence encoding the human carboxypeptidase E (CPE) precursor (NP_001864.1) (Met 1-Ser 453) was fused with a polyhistidine tag at the C-terminus.

> 90 % as determined by SDS-PAGE

Measured by its ability to cleave a peptide substrate, benzoyl-AR-OH. The product, Arg, is reacted with orthophthaldialdehyde (OPA) to form a fluorescent molecule. The specific activity is >12,000 pmoles/min/μg.

The recombinant human CPE comprises 439 amino acids and predicts a molecular mass of 49.4 kDa. As a result of glycosylation, the apparent molecular mass of rhCPE is approximately 53 kDa in SDS-PAGE under reducing conditions.

R74677; MGC7101; CPH1; CARBOXYPEPTIDASE E; CPH-1; CPH; CPE; FAT

Carboxypeptidase E

Human carboxypeptidase E (CPE), also known as Carboxypeptidase H, is a peripheral membrane protein and a zinc metallocarboxypeptidase, and the conversion of proCPE into CPE occurs primarily in secretory vesicles. The active form of CPE cleaves C-terminal amino acid residues of the peptide, and is thus involved in the biosynthesis of peptide hormones and neurotransmitters including insulin, enkephalin, etc. The enzymatic activity is enhanced by millimolar concentrations of Co2+. It has also been proposed that membrane-associated carboxypeptidase E acts as a sorting receptor for targeting regulated secretory proteins which are mostly prohormones and neuropeptides in the trans-Golgi network of the pituitary and in secretory granules into the secretory pathway.Its interaction with glycosphingolipid-cholesterol rafts at the TGN facilitates the targeting. Mutations in this gene are implicated in type I I diabetes due to impaired glucose clearance and insulin resistance.

Lyophilized from sterile PBS, pH 7.4
1. 5 % trehalose and mannitol are added as protectants before lyophilization.
2. Please contact us for any concerns or special requirements.

< 1.0 EU per μg of the protein as determined by the LAL method

Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.