ACE2 Protein, Human (sf9, His)

ACE2, an indispensable counter-regulatory carboxypeptidase within the renin-angiotensin hormone system, plays a pivotal role in maintaining cardiovascular homeostasis by intricately regulating blood volume and systemic vascular resistance. Through its enzymatic activity, ACE2 converts angiotensin I to angiotensin 1-9 and angiotensin II to angiotensin 1-7, exerting anti-hypertrophic effects in cardiomyocytes and acting as a vasodilator with anti-proliferative properties. Beyond its central role in the renin-angiotensin system, ACE2 exhibits broad enzymatic activity, cleaving various vasoactive peptides such as neurotensin, kinetensin, and des-Arg bradykinin. Moreover, ACE2 is proficient in cleaving other biological peptides, including apelins, casomorphins, and dynorphin A. Notably, ACE2's C-terminus, homologous to collectrin, orchestrates the trafficking of the neutral amino acid transporter SL6A19 to the gut epithelial cell membrane, thereby regulating its surface expression and catalytic activity. Importantly, ACE2 also serves as a receptor for human coronaviruses SARS-CoV, SARS-CoV-2, and HCoV-NL63, implicating it in microbial infection pathways. ACE2 Protein, Human (sf9, His) is the recombinant human-derived ACE2 protein, expressed by Sf9 insect cells , with C-His labeled tag. The total length of ACE2 Protein, Human (sf9, His) is 740 a.a., with molecular weight of ~85.1 kDa.

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Recombinant Proteins