Recombinant Human AKR1C2 Protein

Name: Recombinant Human AKR1C2 Protein
Brand: Beta LifeScience
SKU: BL-2047NP
Availability: InStock

BL-2047NP: Greater than 90% as determined by reducing SDS-PAGE. (QC verified)

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Aldo-Keto Reductase Family 1 Member C2 is produced by our E.coli expression system and the target gene encoding Met1-Tyr323 is expressed.
Accession	P52895
Synonym	Aldo-Keto Reductase Family 1 Member C2; 3-Alpha-HSD3; Chlordecone Reductase Homolog HAKRD; Dihydrodiol Dehydrogenase 2; DD-2; DD2; Dihydrodiol Dehydrogenase/Bile Acid-Binding Protein; DD/BABP; Trans-1; 2-Dihydrobenzene-1; 2-Diol Dehydrogenase; Type III 3-Alpha-Hydroxysteroid Dehydrogenase; AKR1C2; DDH2
Gene Background	Aldo-Keto Reductase Family 1 Member C2 (AKR1C2) plays a role in concert with the 5-α/5-β-Steroid Reductases to convert Steroid hormones into the 3-α/5-α and 3-α/5-β-Tetrahydrosteroids. AKR1C2 catalyzes the inactivation of the most potent androgen 5-α-Dihydrotestosterone (5-α-DHT) to 5-α-Androstane-3-α, 17-β-diol (3-α-diol).
Molecular Mass	36.74 KDa
Apmol Mass	35 KDa, reducing conditions
Formulation	Supplied as a 0.2 μm filtered solution of 20mM Tris-HCl, 100mM NaCl, 1mM DTT, pH 8.0.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 90% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution
Storage	Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping	The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	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.
Subcellular Location	Cytoplasm, cytosol.
Protein Families	Aldo/keto reductase family
Database References	HGNC: 385 OMIM: 600450 KEGG: hsa:1646 STRING: 9606.ENSP00000370129 UniGene: 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

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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Recombinant Human AKR1C2 Protein

Recombinant Human AKR1C2 Protein

Product Overview

Target Details

FAQs