ACE2 (18-740) Human

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 virus responsible for COVID-19. The coronavirus spike (S) glycoprotein, a class I viral fusion antigen found on the outer envelope of the virus, plays a crucial role in viral infection. It does this by binding to host cell receptors and facilitating the fusion of viral and cellular membranes. The S1 subunit of the spike protein contains two main domains: the N-terminal domain and the C-terminal domain. One or both of these domains can act as a receptor-binding domain. SARS-CoV and MERS-CoV both utilize their C-domain to bind to their respective receptors. ACE2 is a type I transmembrane protein with an extracellular N-terminal domain containing the catalytic site and an intracellular C-terminal tail. Structurally, ACE2 consists of a signal peptide, a transmembrane domain, and a single metalloproteinase active site containing a HEXXH zinc-binding domain. Functionally, ACE2 acts as a mono-carboxypeptidase, an enzyme that cleaves peptide bonds at the carboxyl terminus of an amino acid. ACE2 degrades Angiotensin I to produce the nonapeptide Angiotensin 1-9 and Angiotensin II to create the heptapeptide Angiotensin 1-7.

This recombinant ACE2 protein is produced in HEK293 cells and corresponds to the human ACE2 protein sequence from amino acids 18 to 740. It is fused to an IgG-His tag at the N-terminus, adding 242 amino acids and resulting in a total molecular weight of 110.8 kDa. This ACE2 protein specifically binds to the receptor-binding domain (RBD) of the SARS-CoV-2 spike protein.

This product is supplied as a 0.5 mg/ml solution of ACE2 Human protein in phosphate-buffered saline (PBS) with a pH of 7.4 and 10% glycerol.

ACE-2 Human Recombinant Protein is shipped with ice packs to maintain a cool temperature during transport. Upon receipt, it should be stored at -20°C (-4°F).

The purity of this protein is greater than 90% as determined by SDS-PAGE analysis.

The biological activity of this protein is determined by its ability to bind to the SARS-CoV-2 Spike RBD in a functional ELISA assay. The ED50 value, representing the concentration at which 50% binding is observed, is less than or equal to 100 ng/ml. The specific activity, defined as the amount of enzyme required to hydrolyze 1.0 picomole of the substrate Mca-YVADAPK(Dnp)-OH per minute at a pH of 7.5 and a temperature of 25°C, is greater than 250 picomoles/min/microgram.

HEK293 Cells

DGS QSTIEEQ AKTFLDKFNH EAEDLFYQSS LASWNYNTNI TEENVQNMNN AGDKWSAFLK EQSTLAQMYP LQEIQNLTVK LQLQALQQNG SSVLSEDKSK RLNTILNTMS TIYSTGKVCN PDNPQECLLL EPGLNEIMAN SLDYNERLWA WESWRSEVGK QLRPLYEEYV VLKNEMARAN HYEDYGDYWR GDYEVNGVDG YDYSRGQLIE DVEHTFEEIK PLYEHLHAYV RAKLMNAYPS YISPIGCLPA HLLGDMWGRF WTNLYSLTVP FGQKPNIDVT DAMVDQAWDA QRIFKEAEKF FVSVGLPNMT QGFWENSMLT DPGNVQKAVC HPTAWDLGKG DFRILMCTKV TMDDFLTAHH EMGHIQYDMA YAAQPFLLRN GANEGFHEAV GEIMSLSAAT PKHLKSIGLL SPDFQEDNET EINFLLKQAL TIVGTLPFTY MLEKWRWMVF KGEIPKDQWM KKWWEMKREI VGVVEPVPHD ETYCDPASLF HVSNDYSFIR YYTRTLYQFQ FQEALCQAAK HEGPLHKCDI SNSTEAGQKL FNMLRLGKSE PWTLALENVV GAKNMNVRPL LNYFEPLFTW LKDQNKNSFV GWSTDWSPYA DQSIKVRISL KSALGDKAYE WNDNEMYLFR SSVAYAMRQY FLKVKNQMIL FGEEDVRVAN LKPRISFNFF VTAPKNVSDI IPRTEVEKAI RMSRSRINDA FRLNDNSLEF LGIQPTLGPP NQPPVSLEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSHEDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQVYTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVMHEALHNHYTQ KSLSLSPGKH HHHHH