AKR1C4 Human
Aldo-keto reductase family 1 member C4 (chlordecone reductase 3-alpha hydroxysteroid dehydrogenase type I dihydrodiol dehydrogenase 4), 3-alpha-hydroxysteroid dehydrogenase type I, MGC22581, HAKRA, 3 alpha-hydroxysteroid dehydrogenase/dihydrodiol dehydrogenase 4, CDR, DD4, CHDR, 3-alpha-HSD1, C11.
Greater than 90.0% as determined by SDS-PAGE.
Description
AKR1C4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 323 amino acids (1-323aa ) and having a molecular mass of 37kDa.
Product Specs
Aldo-keto reductase family 1 member C4, also known as AKR1C4, belongs to the aldo/keto reductase superfamily, which comprises over 40 proteins and enzymes. This enzyme plays a crucial role in catalyzing the conversion of aldehydes and ketones into their respective alcohols using NADH and/or NADPH as cofactors. In the liver, AKR1C4 is involved in the bioreduction of chlordecone, a harmful organochlorine pesticide, converting it into chlordecone alcohol.
Recombinant human AKR1C4, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 323 amino acids (1-323aa). It has a molecular weight of 37kDa.
The AKR1C4 protein solution is supplied at a concentration of 1mg/ml and is formulated in a buffer containing 20mM Tris-HCl (pH 8.5), 0.1M NaCl, 10% glycerol, and 1mM DTT.
The purity of the protein is determined to be greater than 90.0% using SDS-PAGE analysis.
The enzyme exhibits a specific activity exceeding 700pmol/min/ug. This activity is determined by measuring the rate at which 1.0 picomole of 1-Acenaphthenol is oxidized per minute in the presence of NADP at a pH of 8.8 and a temperature of 25°C.
Aldo-keto reductase family 1 member C4 (chlordecone reductase 3-alpha hydroxysteroid dehydrogenase type I dihydrodiol dehydrogenase 4), 3-alpha-hydroxysteroid dehydrogenase type I, MGC22581, HAKRA, 3 alpha-hydroxysteroid dehydrogenase/dihydrodiol dehydrogenase 4, CDR, DD4, CHDR, 3-alpha-HSD1, C11.
MDPKYQRVEL NDGHFMPVLG FGTYAPPEVP RNRAVEVTKL AIEAGFRHID SAYLYNNEEQ VGLAIRSKIA DGSVKREDIF YTSKLWCTFF QPQMVQPALE SSLKKLQLDY VDLYLLHFPM ALKPGETPLP KDENGKVIFD TVDLSATWEV MEKCKDAGLA KSIGVSNFNC RQLEMILNKP GLKYKPVCNQ VECHPYLNQS KLLDFCKSKD IVLVAHSALG TQRHKLWVDP NSPVLLEDPV LCALAKKHKR TPALIALRYQ LQRGVVVLAK SYNEQRIREN IQVFEFQLTS EDMKVLDGLN RNYRYVVMDF LMDHPDYPFS DEY.
Product Science Overview
Aldo-Keto Reductase Family 1 Member C4, also known as AKR1C4, is a member of the aldo-keto reductase superfamily. This superfamily consists of more than 40 known enzymes and proteins that catalyze the conversion of aldehydes and ketones to their corresponding alcohols by utilizing NADH and/or NADPH as cofactors . AKR1C4 is a protein-coding gene that plays a significant role in various biochemical pathways, including the metabolism of steroid hormones and bile acids .
The AKR1C4 gene is located on chromosome 10p15-p14 and shares high sequence identity with three other gene members clustered in the same region . The gene encodes a protein that consists of 323 amino acids and has a molecular weight of approximately 37 kDa . The protein structure includes a conserved NADPH-binding domain, which is essential for its enzymatic activity .
AKR1C4 catalyzes the bioreduction of chlordecone, a toxic organochlorine pesticide, to chlordecone alcohol in the liver . This enzyme also exhibits 3-alpha-hydroxysteroid dehydrogenase activity, which is crucial for the metabolism of steroid hormones . Specifically, it transforms the potent natural androgen dihydrotestosterone into 5-alpha-androstan-3-alpha,17-beta-diol, a compound with much lower activity .
The enzymatic activities of AKR1C4 are vital for maintaining the balance of steroid hormones and bile acids in the body . It plays a role in the synthesis and clearance of testosterone, thereby influencing various physiological processes . Additionally, AKR1C4 is involved in the metabolism of xenobiotics, which are foreign compounds that enter the body .
Recombinant human AKR1C4 is widely used in research to study its enzymatic properties and potential therapeutic applications . Understanding the function and regulation of this enzyme can provide insights into the treatment of diseases related to steroid hormone imbalances and xenobiotic metabolism .
