Recombinant rat ACE-2 protein

QSLIEEKAES FLNKFNQEAE DLSYQSSLAS WNYNTNITEE NAQKMNEAAA KWSAFYEEQS KIAQNFSLQE IQNATIKRQL KALQQSGSSA LSPDKNKQLN TILNTMSTIY STGKVCNSMN PQECFLLEPG LDEIMATSTD YNRRLWAWEG WRAEVGKQLR PLYEEYVVLK NEMARANNYE DYGDYWRGDY EAEGVEGYNY NRNQLIEDVE NTFKEIKPLY EQLHAYVRTK LMEVYPSYIS PTGCLPAHLL GDMWGRFWTN LYPLTTPFLQ KPNIDVTDAM VNQSWDAERI FKEAEKFFVS VGLPQMTPGF WTNSMLTEPG DDRKVVCHPT AWDLGHGDFR IKMCTKVTMD NFLTAHHEMG HIQYDMAYAK QPFLLRNGAN EGFHEAVGEI MSLSAATPKH LKSIGLLPSN FQEDNETEIN FLLKQALTIV GTLPFTYMLE KWRWMVFQDK IPREQWTKKW WEMKREIVGV VEPLPHDETY CDPASLFHVS NDYSFIRYYT RTIYQFQFQE ALCQAAKHDG PLHKCDISNS TEAGQKLLNM LSLGNSGPWT LALENVVGSR NMDVKPLLNY FQPLFVWLKE QNRNSTVGWS TDWSPYADQS IKVRISLKSA LGKNAYEWTD NEMYLFRSSV AYAMREYFSR EKNQTVPFGE ADVWVSDLKP RVSFNFFVTS PKNVSDIIPR SEVEEAIRMS RGRINDIFGL NDNSLEFLGI YPTLKPPYEP PVT

ACE2, also known as angiotensin-converting enzyme 2, is carboxypeptidase which converts angiotensin I to angiotensin 1-9, a peptide of unknown function, and angiotensin II to angiotensin 1-7, a vasodilator. It is able to hydrolyze apelin-13 and dynorphin-13 with high efficiency and may be an important regulator of heart function. Recombinant rat ACE2, fused to His-tag at C-terminus, was expressed in insect cell and purified by using conventional chromatography techniques.

< 1 EU per 1ug of protein (determined by LAL method)

Liquid in. Phosphate-Buffered Saline (pH 7.4) containing 10% glycerol

Li W., et al. (2004) J. Virol. 78:11429-11433.; ; Crackower M., A. et al. (2002) Nature 417:822-828.