Recombinant Human AKR1C4 protein is a Human Full Length protein, in the 1 to 323 aa range, expressed in Escherichia coli, with >95% purity, < 0.1 EU/µg endotoxin level and suitable for SDS-PAGE.
M G S S H H H H H H S S G L V P R G S H M D P K Y Q R V E L N D G H F M P V L G F G T Y A P P E V P R N R A V E V T K L A I E A G F R H I D S A Y L Y N N E E Q V G L A I R S K I A D G S V K R E D I F Y T S K L W C T F F Q P Q M V Q P A L E S S L K K L Q L D Y V D L Y L L H F P M A L K P G E T P L P K D E N G K V I F D T V D L S A T W E V M E K C K D A G L A K S I G V S N F N Y R Q L E M I L N K P G L K Y K P V C N Q V E C H P Y L N Q S K L L D F C K S K D I V L V A H S A L G T Q R H K L W V D P N S P V L L E D P V L C A L A K K H K R T P A L I A L R Y Q L Q R G V V V L A K S Y N E Q R I R E N I Q V F E F Q L T S E D M K V L D G L N R N Y R Y V V M D F L M D H P D Y P F S D E Y
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Cytosolic aldo-keto reductase that catalyzes the NADH and NADPH-dependent reduction of ketosteroids to hydroxysteroids. Liver specific enzyme that acts as an NAD(P)(H)-dependent 3-, 17- and 20-ketosteroid reductase on the steroid nucleus and side chain (PubMed:10634139, PubMed:10998348, PubMed:11158055, PubMed:14672942, PubMed:1530633, PubMed:19218247, PubMed:7650035). Displays the ability to catalyze both oxidation and reduction in vitro, but most probably acts as a reductase in vivo since the oxidase activity measured in vitro is inhibited by physiological concentration of NADPH (PubMed:14672942). Acts preferentially as a 3-alpha-hydroxysteroid dehydrogenase (HSD) with a subsidiary 3-beta-HSD activity (PubMed:14672942). Catalyzes efficiently the transformation of the potent androgen 5-alpha-dihydrotestosterone (5alpha-DHT or 17beta-hydroxy-5alpha-androstan-3-one) into the less active form, 5-alpha-androstan-3-alpha,17-beta-diol (3-alpha-diol) (PubMed:10998348, PubMed:11158055, PubMed:14672942). Catalyzes the reduction of estrone into 17beta-estradiol but with low efficiency (PubMed:14672942). Metabolizes a broad spectrum of natural and synthetic therapeutic steroid and plays an important role in metabolism of androgens, estrogens, progestereone and conjugated steroids (PubMed:10998348, PubMed:14672942, PubMed:19218247). Catalyzes the biotransformation of the pesticide chlordecone (kepone) to its corresponding alcohol leading to increased biliary excretion of the pesticide and concomitant reduction of its neurotoxicity since bile is the major excretory route (PubMed:2427522).
CHDR, AKR1C4, Aldo-keto reductase family 1 member C4, 3-alpha-hydroxysteroid dehydrogenase type I, 3alpha-hydroxysteroid 3-dehydrogenase, Chlordecone reductase, Dihydrodiol dehydrogenase 4, HAKRA, 3-alpha-HSD1, CDR, DD-4, DD4
Recombinant Human AKR1C4 protein is a Human Full Length protein, in the 1 to 323 aa range, expressed in Escherichia coli, with >95% purity, < 0.1 EU/µg endotoxin level and suitable for SDS-PAGE.
pH: 8
Constituents: 0.88% Sodium chloride, 0.24% Tris
Cytosolic aldo-keto reductase that catalyzes the NADH and NADPH-dependent reduction of ketosteroids to hydroxysteroids. Liver specific enzyme that acts as an NAD(P)(H)-dependent 3-, 17- and 20-ketosteroid reductase on the steroid nucleus and side chain (PubMed:10634139, PubMed:10998348, PubMed:11158055, PubMed:14672942, PubMed:1530633, PubMed:19218247, PubMed:7650035). Displays the ability to catalyze both oxidation and reduction in vitro, but most probably acts as a reductase in vivo since the oxidase activity measured in vitro is inhibited by physiological concentration of NADPH (PubMed:14672942). Acts preferentially as a 3-alpha-hydroxysteroid dehydrogenase (HSD) with a subsidiary 3-beta-HSD activity (PubMed:14672942). Catalyzes efficiently the transformation of the potent androgen 5-alpha-dihydrotestosterone (5alpha-DHT or 17beta-hydroxy-5alpha-androstan-3-one) into the less active form, 5-alpha-androstan-3-alpha,17-beta-diol (3-alpha-diol) (PubMed:10998348, PubMed:11158055, PubMed:14672942). Catalyzes the reduction of estrone into 17beta-estradiol but with low efficiency (PubMed:14672942). Metabolizes a broad spectrum of natural and synthetic therapeutic steroid and plays an important role in metabolism of androgens, estrogens, progestereone and conjugated steroids (PubMed:10998348, PubMed:14672942, PubMed:19218247). Catalyzes the biotransformation of the pesticide chlordecone (kepone) to its corresponding alcohol leading to increased biliary excretion of the pesticide and concomitant reduction of its neurotoxicity since bile is the major excretory route (PubMed:2427522).
Belongs to the aldo/keto reductase family.
The N-terminus is blocked.
Previously labelled as HSD3a.
AKR1C4 also known as Aldo-keto reductase family 1 member C4 plays a role in the metabolism of steroid hormones. It acts mainly as a ketosteroid reductase involved in the conversion of aldo-keto forms. The protein has a molecular mass of approximately 37 kDa. AKR1C4 is expressed in several tissues with high levels found in the liver. In the liver it contributes to the oxidative inactivation of various steroid hormones thereby maintaining hormonal balance.
AKR1C4 functions to reduce ketosteroids into their respective alcohol forms. This activity is important in steroid metabolism and detoxification processes. AKR1C4 is not part of any major enzyme complexes but its function is essential for processing steroids within cells. It impacts hormonal activity by converting potent steroids into their less active forms facilitating the regulation of physiological responses.
AKR1C4 is part of the steroid hormone metabolic pathway and the bile acid biosynthesis pathway. In steroid hormone metabolism it interacts closely with proteins such as AKR1C3 which also acts on similar substrates. Its activity in bile acid biosynthesis ensures the proper conversion and excretion of bile acids essential for lipid digestion and absorption.
AKR1C4 involvement has been noted in liver diseases and hormone-related disorders. Dysregulation or altered expression of AKR1C4 can contribute to conditions such as hepatic steatosis and endocrine disorders like polycystic ovary syndrome (PCOS). Its interaction with proteins like the androgen receptor is also significant as it modulates androgen availability and activity potentially impacting androgen-sensitive conditions.
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SDS-PAGE gel of ab172176 under reduced (lane 1) and non reduced (lane 2) conditions
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