| Description: | The PRCP protein functions as an enzyme capable of cleaving C-terminal amino acids linked to proline in peptides, including angiotensin II, III, and des-Arg9-bradykinin. This cleavage activity is notable for its occurrence at acidic pH, although enzymatic activity is maintained with certain substrates even under neutral pH conditions. The specific cleavage of proline-linked C-terminal amino acids highlights PRCP's role in modulating the bioactivity of peptide substrates, particularly those involved in regulatory pathways such as the renin-angiotensin and bradykinin systems. The ability of PRCP to operate in both acidic and neutral pH environments further emphasizes its versatility in influencing peptide metabolism under various physiological conditions. PRCP Protein, Human (HEK293, His) is the recombinant human-derived PRCP protein, expressed by HEK293 , with C-6*His labeled tag. The total length of PRCP Protein, Human (HEK293, His) is 475 a.a., with molecular weight of 60-90 kDa. |
