ACE2 Mouse

Angiotensin-converting enzyme 2 (ACE2) is an enzyme found on the surface of cells in various organs, including the intestines, arteries, lungs, heart, and kidneys. ACE2 serves as an entry point for SARS coronaviruses, including SARS-CoV-2. The spike (S) glycoprotein of the coronavirus is a key factor in viral infection. It's a class I viral fusion antigen located on the virion's outer envelope. The S protein identifies and binds to host cell receptors, facilitating the fusion of viral and cellular membranes, thus enabling infection. The S1 domain of the coronavirus S protein has two main parts: the N-terminal domain and the C-terminal domain. Either or both of these domains can act as receptor-binding domains. SARS-CoV and MERS-CoV both use their C-domain to bind to their respective receptors. ACE2 is a transmembrane protein with its N-terminal domain, containing the catalytic site, located outside the cell and its C-terminal tail located inside the cell. ACE2 acts as a mono-carboxypeptidase, an enzyme that cleaves peptide bonds. Specifically, it degrades Angiotensin I to produce Angiotensin 1-9 and Angiotensin II to produce Angiotensin 1-7.

ACE2 Mouse, produced in Sf9 insect cells using a baculovirus expression system, is a single, glycosylated polypeptide chain. It comprises 731 amino acids (specifically, amino acids 18-740) and has a molecular weight of 84.5 kDa. The protein includes a 6-amino acid Histidine tag (His-Tag) attached to its C-terminus to facilitate purification. It is purified using proprietary chromatographic techniques.

The ACE2 solution is buffered in Phosphate-Buffered Saline (pH 7.4) and contains 10% Glycerol as a stabilizing agent.

For short-term storage (up to 2-4 weeks), the ACE2 solution can be stored at 4°C. For extended storage, it is recommended to freeze the solution at -20°C. To further enhance stability during long-term storage, adding a carrier protein such as Albumin (0.1% HSA or BSA) is advised. Repeated freezing and thawing of the solution should be avoided.

The purity of the ACE2 protein is greater than 95%, as determined by SDS-PAGE analysis.

The biological activity of ACE2 is defined as its enzymatic ability to hydrolyze the substrate McaYVADAPK(Dnp)-OH. This ACE2 Mouse product exhibits an activity greater than 200 pmol/min/µg, meaning that 1 µg of the enzyme can hydrolyze more than 200 picomoles of the substrate per minute at a pH of 7.5 and a temperature of 25°C.

ACE2, 2010305L05Rik, Angiotensin I Converting Enzyme, Angiotensin I Converting, Enzyme (Peptidyl-Dipeptidase A), Angiotensin-Converting Enzyme Homolog, Angiotensin-Converting Enzyme, ACE-Related Carboxypeptidase, Metalloprotease MPROT15, Peptidyl-Dipeptidase A, ACEH, EC 3.4.17.23, EC 3.4.17.

QSLTEENAKT FLNNFNQEAE DLSYQSSLAS WNYNTNITEE NAQKMSEAAA KWSAFYEEQS KTAQSFSLQE IQTPIIKRQL QALQQSGSSA LSADKNKQLN TILNTMSTIY STGKVCNPKN PQECLLLEPG LDEIMATSTD YNSRLWAWEG WRAEVGKQLR PLYEEYVVLK NEMARANNYN DYGDYWRGDY EAEGADGYNY NRNQLIEDVE RTFAEIKPLY EHLHAYVRRK LMDTYPSYIS PTGCLPAHLL GDMWGRFWTN LYPLTVPFAQ KPNIDVTDAM MNQGWDAERI FQEAEKFFVS VGLPHMTQGF WANSMLTEPA DGRKVVCHPT AWDLGHGDFR IKMCTKVTMD NFLTAHHEMG HIQYDMAYAR QPFLLRNGAN EGFHEAVGEI MSLSAATPKH LKSIGLLPSD FQEDSETEIN FLLKQALTIV GTLPFTYMLE KWRWMVFRGE IPKEQWMKKW WEMKREIVGV VEPLPHDETY CDPASLFHVS NDYSFIRYYT RTIYQFQFQE ALCQAAKYNG SLHKCDISNS TEAGQKLLKM LSLGNSEPWT KALENVVGAR NMDVKPLLNY FQPLFDWLKE QNRNSFVGWN TEWSPYADQS IKVRISLKSA LGANAYEWTN NEMFLFRSSV AYAMRKYFSI IKNQTVPFLE EDVRVSDLKP RVSFYFFVTS PQNVSDVIPR SEVEDAIRMS RGRINDVFGL NDNSLEFLGI HPTLEPPYQPPVTLEHHHHH H.