Recombinant Human AKR1C2 Protein (His Tag)
Beta LifeScience SKU/CAT #: BLPSN-0118
Recombinant Human AKR1C2 Protein (His Tag)
Beta LifeScience SKU/CAT #: BLPSN-0118
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.
|AKR1C-pseudo, AKR1C2, BABP, DD, DD-2, DD/BABP, DD2, DDH2, HAKRD, HBAB, MCDR2, SRXY8, TDD
|AKR1C2 is a member of the aldo/keto reductase superfamily, which consists of more than 4 known enzymes and proteins. These enzymes catalyze the conversion of aldehydes and ketones to their corresponding alcohols using NADH and/or NADPH as cofactors. The enzymes display overlapping but distinct substrate specificity. This enzyme binds bile acid with high affinity, and shows minimal 3-alpha-hydroxysteroid dehydrogenase activity. AKR1C2 gene shares high sequence identity with three other gene members and is clustered with those three genes at chromosome 1p15-p14. Three transcript variants encoding two different isoforms have been found for AKR1C2 gene.
|A DNA sequence encoding the mature form of human AKR1C2 (P52895-1) (Met1-Tyr323) was expressed with a His tag at the N-terminus.
|Predicted N Terminal
|The recombinant human AKR1C2 consists of 338 a.a. and predicts a molecular mass of 38.6 KDa. It migrates as an approximately 37 KDa band in SDS-PAGE under reducing conditions.
|>90% as determined by SDS-PAGE
|Please contact us for more information.
|Please contact us for detailed information
|Lyophilized from sterile PBS, pH 7.4..
|The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
|For Research Use Only
|Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
|Cytosolic aldo-keto reductase that catalyzes the NADH and NADPH-dependent reduction of ketosteroids to hydroxysteroids. Most probably acts as a reductase in vivo since the oxidase activity measured in vitro is inhibited by physiological concentrations of NADPH. Displays a broad positional specificity acting on positions 3, 17 and 20 of steroids and regulates the metabolism of hormones like estrogens and androgens. Works in concert with the 5-alpha/5-beta-steroid reductases to convert steroid hormones into the 3-alpha/5-alpha and 3-alpha/5-beta-tetrahydrosteroids. Catalyzes the inactivation of the most potent androgen 5-alpha-dihydrotestosterone (5-alpha-DHT) to 5-alpha-androstane-3-alpha,17-beta-diol (3-alpha-diol). Also specifically able to produce 17beta-hydroxy-5alpha-androstan-3-one/5alphaDHT. May also reduce conjugated steroids such as 5alpha-dihydrotestosterone sulfate. Displays affinity for bile acids.
|Aldo/keto reductase family
|46,XY sex reversal 8 (SRXY8)
|Expressed in fetal testes. Expressed in fetal and adult adrenal glands.
Gene Functions References
- Curcumin treatments considerably increased the expression of AKR1C2 in prostate cancer cell lines. PMID: 29369461
- We identified two powerful genes in the liver cancer metastasis process, AEG-1 and AKR1C2. PMID: 26318406
- Identify two novel factors, AKR1C2 (positive factor) and NF1 (negative factor), as the AEG-1 downstream players in the process of metastasis in liver cancer. PMID: 26351209
- The endogenous HMOX1 gene but not the AKR1C2 gene is strongly repressed by Bach1 in HaCaT keratinocytes. PMID: 26244607
- In model cell lines of endometrial cancer, AKR1C2 and SRD5A1 have crucial roles in progesterone metabolism. PMID: 25463305
- Significantly higher levels of SRD5A1, AKR1C2, AKR1C3, and HSD17B10 mRNA were however found in bone metastases than in non-malignant and/or malignant prostate tissue PMID: 24244276
- The V54L mutation significantly decreases the 3alpha-hydroxysteroid dehydrogenase activity of DDH2 for the reduction of dihydrotestosterone. PMID: 24434280
- DDH2 expression might be a potential predictor and monitor of cisplatin efficacy in advanced NSCLC patients. PMID: 22534668
- Data suggest that modulation of AKR1C2 by glucocorticoids (dexamethasone in this study) locally modifies exposure of adipose cells to endogenous androgens; thus, AKR1C2 activation/inactivation may be involved in regional fat deposition. PMID: 22275760
- role of AKR1C2 in the metabolism of testosterone and progesterone via the 5beta-reductase pathway. PMID: 21521174
- The folding initiation mechanism of human bile acid-binding protein (BABP) has been examined by (19) F NMR. PMID: 21280124
- Overexpression of aldo-keto reductase 1C2 is associated with disease progression in patients with prostatic cancer PMID: 20840669
- We investigated associations between single nucleotide polymorphisms in genes HSD3B1, SRD5A1/2, and AKR1C2 and prostate cancer risk PMID: 20056642
- human ileal bile acid binding protein binds two molecules of glycocholic acid with low intrinsic affinity but an extraordinarily high degree of positive cooperativity PMID: 11854486
- The kinetics of 3-alpha-HSD type III indicates an ordered ternary complex mechanism characterized by allopregnanolone formation, with NAD cofactor binding before the steroid substrate and dissociating after release of the steroid product. PMID: 12416991
- in prostate cells AKR1C2 acts as a 3-ketosteroid reductase to eliminate 5alpha-DHT and prevents activation of the androgen receptor. PMID: 12810547
- Glaucomatous optic nerve head astrocytes express a higher level of 3alpha-HSD isoform AKR1C2 and its mRNA than normal astrocytes. PMID: 13678667
- expression and activity of type 5 17beta-hydroxysteroid dehydrogenase and type 3 3alpha-hydroxysteroid dehydrogenase in female subcutaneous tissue and omental adipose tissue and in preadipocytes PMID: 14671194
- Akr1c2 which is up-regulated in esophageal squamous cell carcinoma probably plays an important role in tumor development of esophagus and may be proposed as a potential molecular target treatments. PMID: 15188492
- metabolizes tibolone PMID: 15383625
- Results suggest that 17beta-hydroxysteroid dehydrogenase (17beta-HSD) type 3 might play slightly different roles in zebrafish compared with human although testosterone itself is likely to have similar functions in both organisms. PMID: 16216911
- human ileal bile acid binding protein has a high degree of selectivity in its interactions with glycocholate and glycochenodeoxycholate brought on by the conformation of its ternary complex PMID: 16411748
- The regulation of AKR1C2 by antioxidant response element suggests that AKR1C2 detoxifies products of reactive oxidant injury. PMID: 16478829
- continual intake of arsenic in drinking water might provoke AKR1C2 expression that could in turn induce drug resistance in bladder cancer, and AKR1C2 may have a role in development of bladder cancer PMID: 17203165
- Wild-type ileal BABP undergoes a slow conformational change after both bile-salt binding sites become occupied, a kinetic step that is missing in mutants that lack positive cooperativity. PMID: 17432832
- The inhibition of activation of the beta-catenin/TCF-signaling pathway is believed to be one mechanism by which AKR1C2 siRNA exerts a gatekeeper function during hepatocarcinogenesis. PMID: 18251165
- Higher mRNA levels of enzymes synthesizing and inactivating androgens are found in differentiated adipocytes, consistent with higher androgen-processing rates in these cells. PMID: 18984855
- The results show that several naturally occurring single nucleotide polymorphisms in AKR1C2 result in reduced enzyme activities. These variant AKR1C2 alleles may represent one factor involved in the variable degradation of dihydrotestosterone in vivo. PMID: 19258517
- The disulfide bridge does not modify the protein-binding stoichiometry, but has a key role in modulating recognition at both sites, inducing site selectivity for glycocholic and glycochenodeoxycholic acid. PMID: 19754879
- The researchers found an increased risk of breast cancer in women with AKR1C2 who carried 1 or 2 alleles and who used estrogen-progesterone therapy. PMID: 19846565