ACE Human
Sf9, Baculovirus cells.
Angiotensin-converting enzyme, ACE, Dipeptidyl carboxypeptidase I, Kininase II, CD_antigen: CD143, DCP, DCP1, ACE1, CD143
Greater than 90.0% as determined by SDS-PAGE.
Description
ACE Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 1235 amino acids (30-1256 a.a.) and having a molecular mass of 142kDa.
ACE is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Product Specs
Angiotensin-converting enzyme, ACE, Dipeptidyl carboxypeptidase I, Kininase II, CD_antigen: CD143, DCP, DCP1, ACE1, CD143
Sf9, Baculovirus cells.
LDPGLQPGNF SADEAGAQLF AQSYNSSAEQ VLFQSVAASW AHDTNITAEN ARRQEEAALL SQEFAEAWGQ KAKELYEPIW QNFTDPQLRR IIGAVRTLGS ANLPLAKRQQ YNALLSNMSR IYSTAKVCLP NKTATCWSLD PDLTNILASS RSYAMLLFAW EGWHNAAGIP LKPLYEDFTA LSNEAYKQDG FTDTGAYWRS WYNSPTFEDD LEHLYQQLEP LYLNLHAFVR RALHRRYGDR YINLRGPIPA HLLGDMWAQS WENIYDMVVP FPDKPNLDVT STMLQQGWNA THMFRVAEEF FTSLELSPMP PEFWEGSMLE KPADGREVVC HASAWDFYNR KDFRIKQCTR VTMDQLSTVH HEMGHIQYYL QYKDLPVSLR RGANPGFHEA IGDVLALSVS TPEHLHKIGL LDRVTNDTES DINYLLKMAL EKIAFLPFGY LVDQWRWGVF SGRTPPSRYN FDWWYLRTKY QGICPPVTRN ETHFDAGAKF HVPNVTPYIR YFVSFVLQFQ FHEALCKEAG YEGPLHQCDI YRSTKAGAKL RKVLQAGSSR PWQEVLKDMV GLDALDAQPL LKYFQPVTQW LQEQNQQNGE VLGWPEYQWH PPLPDNYPEG IDLVTDEAEA SKFVEEYDRT SQVVWNEYAE ANWNYNTNIT TETSKILLQK NMQIANHTLK YGTQARKFDV NQLQNTTIKR IIKKVQDLER AALPAQELEE YNKILLDMET TYSVATVCHP NGSCLQLEPD LTNVMATSRK YEDLLWAWEG WRDKAGRAIL QFYPKYVELI NQAARLNGYV DAGDSWRSMY ETPSLEQDLE RLFQELQPLY LNLHAYVRRA LHRHYGAQHI NLEGPIPAHL LGNMWAQTWS NIYDLVVPFP SAPSMDTTEA MLKQGWTPRR MFKEADDFFT SLGLLPVPPE FWNKSMLEKP TDGREVVCHA SAWDFYNGKD FRIKQCTTVN LEDLVVAHHE MGHIQYFMQY KDLPVALREG ANPGFHEAIG DVLALSVSTP KHLHSLNLLS SEGGSDEHDI NFLMKMALDK IAFIPFSYLV DQWRWRVFDG SITKENYNQE WWSLRLKYQG LCPPVPRTQG DFDPGAKFHI PSSVPYIRYF VSFIIQFQFH EALCQAAGHT GPLHKCDIYQ SKEAGQRLAT AMKLGFSRPW PEAMQLITGQ PNMSASAMLS YFKPLLDWLR TENELHGEKL GWPQYNWTPN SARSEGPLPD SGRVSFLGLD LDAQQARVEH HHHHH
Product Science Overview
Angiotensin Converting Enzyme (ACE) is a crucial enzyme in the renin-angiotensin system (RAS), which regulates blood pressure and fluid balance in the body. The human recombinant form of this enzyme, often referred to as rhACE, has been developed for various therapeutic applications.
ACE is a membrane-bound enzyme that catalyzes the conversion of angiotensin I to angiotensin II, a potent vasoconstrictor . This conversion plays a significant role in the regulation of blood pressure and electrolyte balance. ACE is expressed in various tissues, including the lungs, kidneys, and blood vessels .
Recombinant human ACE (rhACE) has been studied for its potential therapeutic benefits in several conditions:
- Hypertension: By converting angiotensin I to angiotensin II, ACE plays a critical role in blood pressure regulation. Inhibitors of ACE are commonly used to treat hypertension .
- Heart Failure: ACE inhibitors are also used in the management of heart failure, as they help reduce the workload on the heart by lowering blood pressure and decreasing fluid retention .
- Acute Respiratory Distress Syndrome (ARDS): Studies have explored the use of rhACE2, a recombinant form of ACE2, in treating ARDS. This enzyme helps modulate the levels of angiotensin II and its antagonist angiotensin 1-7, which has vasodilatory and anti-inflammatory properties .
Several clinical trials have been conducted to evaluate the safety and efficacy of rhACE in various conditions:
- Pharmacokinetics and Pharmacodynamics: Research has shown that rhACE2 can be administered intravenously with a dose-dependent increase in systemic exposure. The enzyme has a biphasic elimination pattern and a terminal half-life of approximately 10 hours .
- ARDS Treatment: A pilot clinical trial investigated the use of rhACE2 in patients with ARDS. The study found that rhACE2 was well-tolerated and modulated the levels of RAS peptides, although it did not significantly impact acute physiology or clinical outcomes .
