|Other Names||Aldo-keto reductase family 1 member C1, 111-, 20-alpha-hydroxysteroid dehydrogenase, 20-alpha-HSD, Chlordecone reductase homolog HAKRC, Dihydrodiol dehydrogenase 1/2, DD1/DD2, High-affinity hepatic bile acid-binding protein, HBAB, Indanol dehydrogenase, Trans-1, 2-dihydrobenzene-1, 2-diol dehydrogenase, AKR1C1, DDH, DDH1|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Converts progesterone to its inactive form, 20-alpha- dihydroxyprogesterone (20-alpha-OHP). In the liver and intestine, may have a role in the transport of bile. May have a role in monitoring the intrahepatic bile acid concentration. Has a low bile-binding ability. May play a role in myelin formation.|
|Tissue Location||Expressed in all tissues tested including liver, prostate, testis, adrenal gland, brain, uterus, mammary gland and keratinocytes. Highest levels found in liver, mammary gland and brain.|
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Provided below are standard protocols that you may find useful for product applications.
AKR1C1 encodes a 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 reaction of progesterone to the inactive form 20-alpha-hydroxy-progesterone. This protein shares high sequence identity with three other gene members and is clustered with those three genes at chromosome 10p15-p14.
Reding, K.W., et al. Am. J. Epidemiol. 170(10):1241-1249(2009)Chien, C.W., et al. Carcinogenesis 30(10):1813-1820(2009)Davies, N.J., et al. Cancer Res. 69(11):4769-4775(2009)
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