Human CD13 / ANPEP (603 Met/Ile, His Tag) recombinant protein

Human CD13 / ANPEP (603 Met/Ile, His Tag) recombinant protein

• DataSheet
• Material Safety Data Sheets (MSDS)

Aminopeptidase N (ANPEP or APN), also known as CD13, is a cell-surface metalloprotease located in the small-intestinal and renal microvillar membrane, as well as other plasma membranes. It belongs to the peptidase M1 family. CD13 plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases and is involved in the metabolism of regulatory peptides by diverse cell types. CD13/APN is a potent regulator of angiogenesis which is essential for tumor invasion and metastasis, and its transcription in activated endothelial cells is induced by angiogenic growth factors via the RAS/MAPK pathway. In addition, this enzyme has been shown to participate in antigen processing and presentation, and accordingly, defects in this gene appear to be a cause of various types of leukemia or lymphoma and carcinomas.

Alanyl (Membrane) aminopeptidase (Aminopeptidase N, aminopeptidase M, microsomal aminopeptidase, CD13, p150), isoform CRA_a

ANPEP; APN; GP150; CD13; P150; LAP-1; AP-N; AP-M; PEPN; LAP1

Q59E93

ANPEP; hCG_27217

Human Cells

A DNA sequence encoding the metalloprotease domain (Lys 69-Lys 967?603 Met/Ile) of the mature form of human ANPEP (NP_001141.2) was expressed with N-terminal signal peptide and C-terminal polyhistidine tag.

Human

The recombinant human ANPEP protein consists of 910 amino acids and has a predicted molecular mass of 104.2 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rhANPEP is approximately 135-140 kDa due to glycosylation.

> 97 % as determined by SDS-PAGE

Measured by its ability to cleave the fluorogenic peptide substrate, Ala-7-amido-4-methylcoumarin (Ala-AMC).
The specific activity is >2,500 pmoles/min/μg.