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|Product Name||AKR1C1, 1-323aa, Human|
|Background||AKR1C1 is member of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. These enzymes catalyze the conversion of aldehydes and ketones to their corresponding alcohols by utilizing NADH and/or NADPH as cofactors. The enzymes display overlapping but distinct substrate specificity. This enzyme catalyzes the reduction of progesterone to the inactive form 20-alpha-hydroxy-progesterone. Recombinant AKR1C1 protein was expressed in E.coli and purified by using conventional chromatography techniques.|
|Synonyms||20-alpha-HSD, DD1/DD2, HBAB, DDH, DDH1, Aldo-keto reductase family 1, member C1 20 alpha (3 alpha) hydroxysteroid dehydrogenase, 20 alpha hydroxysteroid dehydrogenase, 2ALPHAHSD, AK1C1, MBAB, Aldo keto reductase family 1 member C1, C9, Chlordecone reductase homolog, Chlordecone reductase homolog HAKRC, DD1, Dihydrodiol dehydrogenase 1, Dihydrodiol dehydrogenase 1/2, H37, HAKRC, Hepatic dihydrodiol dehydrogenase, High affinity hepatic bile acid-binding protein, Trans-1,2 dihydrobenzene 1,2 diol dehydrogenase, Type II 3 alpha hydroxysteroid dehydrogenase,|
|Amino Acid 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|
|Molecular Weight||26.2 kDa (236aa), confirmed by MALDI-TOF.|
|Concentration||1 mg/ml (determined by Bradford assay)|
|Form||Liquid, in Phosphate Buffered Saline pH7.4 containing 10% glycerol|
|Purity||> 90% by SDS-PAGE|
|NCBI Accession #||NP_001344|
|Storage||Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -20C or -70C. Avoid repeated freezing and thawing cycles.|
|Intended Use||For Research Use Only|
|References||Zhang Y., et al. (2000) J. Mol. Endocrinol. 25:221-228
Zhang Y., et al. (2009) Mol Cell Endicrinol. 298(1-2):76-83
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