AKR1C1 Human
Escherichia Coli.
DDH1, DDH, HAKRC, 20-alpha-HSD, DD1/DD2, HBAB, C9, DD1, H-37, MBAB, MGC8954, 2-ALPHA-HSD, AKR1C1, Aldo-keto reductase family 1 member C1, 20-alpha-hydroxysteroid dehydrogenase, Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase, Indanol dehydrogenase, Dihydrodiol dehydrogenase 1/2, Chlordecone reductase homolog HAKRC, High-affinity hepatic bile acid-binding protein
Greater than 95.0% as determined by SDS-PAGE.
Description
AKR1C1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 323 amino acids (1-323) and having a molecular mass of 36.7 kDa.
AKR1C1 is purified by proprietary chromatographic techniques.
Product Specs
Aldo-keto reductase family 1 member C1, also known as AKR1C1, is an enzyme belonging to the aldo/keto reductase family, which comprises over 40 related proteins. AKR1C1 facilitates the conversion of ketones and aldehydes into their corresponding alcohol forms utilizing cofactors like NADH and NADPH. Notably, AKR1C1 plays a role in converting progesterone into its inactive form, 20-alpha-hydroxy-progesterone.
Recombinant human AKR1C1, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 323 amino acids (residues 1-323). It has a molecular weight of 36.7 kDa.
The purification of AKR1C1 is achieved using proprietary chromatographic methods.
The AKR1C1 solution is provided at a concentration of 1 mg/ml and contains 20% glycerol, 0.1M NaCl, and 20mM Tris-HCl buffer with a pH of 8.5.
To ensure long-term stability, adding a carrier protein (0.1% HSA or BSA) is advised.
Repeated freezing and thawing of the product should be avoided.
The purity of the product is determined to be greater than 95.0% as assessed by SDS-PAGE analysis.
The specific activity of the enzyme is greater than 500 pmol per minute per microgram. Specific activity is determined by measuring the enzyme's ability to catalyze the oxidation of 1.0 pmole of 1-Acenaphthenol per minute in the presence of NADP at a pH of 8.8 and a temperature of 25 degrees Celsius.
DDH1, DDH, HAKRC, 20-alpha-HSD, DD1/DD2, HBAB, C9, DD1, H-37, MBAB, MGC8954, 2-ALPHA-HSD, AKR1C1, Aldo-keto reductase family 1 member C1, 20-alpha-hydroxysteroid dehydrogenase, Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase, Indanol dehydrogenase, Dihydrodiol dehydrogenase 1/2, Chlordecone reductase homolog HAKRC, High-affinity hepatic bile acid-binding protein
Escherichia Coli.
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
Product Science Overview
Aldo-Keto Reductase Family 1 Member C1 (AKR1C1) is an enzyme that belongs to the aldo-keto reductase (AKR) 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 . AKR1C1 is also known by several other names, including 20α-hydroxysteroid dehydrogenase, 3α-hydroxysteroid dehydrogenase, and dihydrodiol dehydrogenase 1/2 .
The AKR1C1 gene is located on chromosome 10 at the position 10p15.1 in humans . The gene encodes a protein that is involved in various biological processes, including steroid metabolism, bile acid metabolism, and the metabolism of xenobiotics . The protein structure of AKR1C1 includes several key domains that are essential for its enzymatic activity, including the NADP(H)-binding domain and the substrate-binding domain .
AKR1C1 plays a significant role in the metabolism of steroids, particularly in the conversion of progesterone to its inactive form, 20α-hydroxyprogesterone (20α-OHP) . This enzyme is also involved in the metabolism of bile acids and the regulation of intrahepatic bile acid concentration . Additionally, AKR1C1 participates in the formation of myelin, which is crucial for the proper functioning of the nervous system .
AKR1C1 has been implicated in various clinical conditions, including cancer and metabolic disorders. The enzyme’s ability to metabolize steroids and other compounds makes it a potential target for therapeutic interventions . For example, AKR1C1 has been shown to regulate the osteogenic differentiation of human adipose-derived mesenchymal stromal/stem cells (hASCs) by targeting the progesterone receptor . This finding suggests that AKR1C1 could be used as a molecular target for modifying hASCs to enhance their osteogenic capacity in bone tissue engineering .
Research on AKR1C1 has focused on understanding its role in various biological processes and its potential applications in medicine. Studies have shown that AKR1C1 acts as a negative regulator of osteogenesis and a positive regulator of adipogenesis in hASCs . This dual role highlights the enzyme’s importance in tissue engineering and regenerative medicine .
