|Calculated MW||38.9 kDa|
|Other Names||Aldo-keto reductase family 1, member C 1, 20-alpha-HSD, DD1/DD2, HBAB, DDH, DDH1|
|Sequence||MGSSHHHHHH SSGLVPRGSH MDSKYQCVKL NDGHFMPVLG FGTYAPAEVP KSKALEATKL AIEAGFRHID SAHLYNNEEQ VGLAIRSKIA DGSVKREDIF YTSKLWCNSH RPELVRPALE RSLKNLQLDY VDLYLIHFPV SVKPGEEVIP KDENGKILFD TVDLCATWEA VEKCKDAGLA KSIGVSNFNR RQLEMILNKP GLKYKPVCNQ VECHPYFNQR KLLDFCKSKD IVLVAYSALG SHREEPWVDP NSPVLLEDPV LCALAKKHKR TPALIALRYQ LQRGVVVLAK SYNEQRIRQN VQVFEFQLTS EEMKAIDGLN RNVRYLTLDI FAGPPNYPFS DEY|
|Storage||-80°C; 0.5 mg/ml solution in 20 mM Tris-HCl buffer (pH 8.0) containing 1 mM DTT and 20% glycerol.|
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Provided below are standard protocols that you may find useful for product applications.
Aldo-keto reductase family 1 member C1 in humans is encoded by the AKR1C1 gene. AKR1C1 transfers progesterone to its inactive state or in other words catalyzes the reaction of 20-alpha-hydroxy progesterone (20-alpha-OHP) in the liver and intestine. AKR1C1 transfers bile and monitors the intrahepatic bile acid concentration though it has a low bile-binding ability. AKR1C1 participates in myelin formation. AKR1C1 is part of the aldo/keto reductase superfamily, which has over 40 known enzymes which catalyze the conversion of aldehydes and ketones to their corresponding alcohols by utilizing NADH and/or NADPH as cofactors thus display overlapping but distinct substrate specificity.
Stolz A.,et al.J. Biol. Chem. 268:10448-10457(1993).
Lou H.,et al.J. Biol. Chem. 269:8416-8422(1994).
Ciaccio P.J.,et al.J. Biol. Chem. 269:15558-15562(1994).
Khanna M.,et al.J. Steroid Biochem. Mol. Biol. 53:41-46(1995).
Nishizawa M.,et al.Genes Cells 5:111-125(2000).
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