ACE2 Protein, Cynomolgus (HEK293, His-Avi)

ACE2 Protein, 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. 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. ACE2 Protein, Cynomolgus (HEK293, His-Avi) is the recombinant cynomolgus-derived ACE2 protein, expressed by HEK293 , with C-His, C-Avi labeled tag.

Angiotensin-converting enzyme 2 (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^[1][2][3][4].

Cynomolgus

HEK293

C-Avi;C-8*His

A0A2K5X283 (Q18-V739)

102130864  [NCBI]

Partial

QSTIEEQAKTFLDKFNHEAEDLFYQSSLASWNYNTNITEENVQNMNNAGEKWSAFLKEQSTLAQMYPLQEIQNLTVKLQLQALQQNGSSVLSEDKSKRLNTILNTMSTIYSTGKVCNPNNPQECLLLDPGLNEIMEKSLDYNERLWAWEGWRSEVGKQLRPLYEEYVVLKNEMARANHYKDYGDYWRGNYEVNGVDGYDYNRDQLIEDVERTFEEIKPLYEHLHAYVRAKLMNAYPSYISPTGCLPAHLLGDMWGRFWTNLYSLTVPFGQKPNIDVTDAMVNQAWNAQRIFKEAEKFFVSVGLPNMTQGFWENSMLTDPGNVQKVVCHPTAWDLGKGDFRIIMCTKVTMDDFLTAHHEMGHIQYDMAYAAQPFLLRNGANEGFHEAVGEIMSLSAATPKHLKSIGLLSPDFQEDNETEINFLLKQALTIVGTLPFTYMLEKWRWMVFKGEIPKDQWMKKWWEMKREIVGVVEPVPHDETYCDPASLFHVSNDYSFIRYYTRTLYQFQFQEALCQAAKHEGPLHKCDISNSTEAGQKLLNMLKLGKSEPWTLALENVVGAKNMNVRPLLNYFEPLFTWLKDQNKNSFVGWSTDWSPYADQSIKVRISLKSALGDKAYEWNDNEMYLFRSSVAYAMRTYFLEIKHQTILFGEEDVRVADLKPRISFNFYVTAPKNVSDIIPRTEVEEAIRISRSRINDAFRLNDNSLEFLGIQTTLAPPYQSPV

Approximately 95-110 kDa,based on SDS-PAGE under reducing conditions,due to the glycosylation.

≥ 95%, as determined by Bis-Tris PAGE.

<1 EU/μg, determined by LAL method.

• [1]. Wang W, et al. Angiotensin-Converting Enzyme 2 Metabolizes and Partially Inactivates Pyr-Apelin-13 and Apelin-17: Physiological Effects in the Cardiovascular System. Hypertension. 2016 Aug;68(2):365-77.  [Content Brief]

  [2]. Donoghue M, et al. A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9. Circ Res. 2000 Sep 1;87(5):E1-9.  [Content Brief]

  [3]. Vickers C, et al. Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase. J Biol Chem. 2002 Apr 26;277(17):14838-43.  [Content Brief]

  [4]. Li W, et al. Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus. Nature. 2003 Nov 27;426(6965):450-4.  [Content Brief]