Recombinant Human AKR1C2 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-0118

Recombinant Human AKR1C2 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-0118
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Product Overview

Tag His
Host Species Human
Accession P52895
Synonym AKR1C-pseudo, AKR1C2, BABP, DD, DD-2, DD/BABP, DD2, DDH2, HAKRD, HBAB, MCDR2, SRXY8, TDD
Background 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.
Description A DNA sequence encoding the mature form of human AKR1C2 (P52895-1) (Met1-Tyr323) was expressed with a His tag at the N-terminus.
Source E.coli
Predicted N Terminal His
AA Sequence Met1-Tyr323
Molecular Weight 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.
Purity >90% as determined by SDS-PAGE
Endotoxin Please contact us for more information.
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile PBS, pH 7.4..
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage 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.

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
Associated Diseases 46,XY sex reversal 8 (SRXY8)
Tissue Specificity Expressed in fetal testes. Expressed in fetal and adult adrenal glands.

Gene Functions References

  1. Curcumin treatments considerably increased the expression of AKR1C2 in prostate cancer cell lines. PMID: 29369461
  2. We identified two powerful genes in the liver cancer metastasis process, AEG-1 and AKR1C2. PMID: 26318406
  3. 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
  4. The endogenous HMOX1 gene but not the AKR1C2 gene is strongly repressed by Bach1 in HaCaT keratinocytes. PMID: 26244607
  5. In model cell lines of endometrial cancer, AKR1C2 and SRD5A1 have crucial roles in progesterone metabolism. PMID: 25463305
  6. 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
  7. The V54L mutation significantly decreases the 3alpha-hydroxysteroid dehydrogenase activity of DDH2 for the reduction of dihydrotestosterone. PMID: 24434280
  8. DDH2 expression might be a potential predictor and monitor of cisplatin efficacy in advanced NSCLC patients. PMID: 22534668
  9. 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
  10. role of AKR1C2 in the metabolism of testosterone and progesterone via the 5beta-reductase pathway. PMID: 21521174
  11. The folding initiation mechanism of human bile acid-binding protein (BABP) has been examined by (19) F NMR. PMID: 21280124
  12. Overexpression of aldo-keto reductase 1C2 is associated with disease progression in patients with prostatic cancer PMID: 20840669
  13. We investigated associations between single nucleotide polymorphisms in genes HSD3B1, SRD5A1/2, and AKR1C2 and prostate cancer risk PMID: 20056642
  14. 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
  15. 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
  16. in prostate cells AKR1C2 acts as a 3-ketosteroid reductase to eliminate 5alpha-DHT and prevents activation of the androgen receptor. PMID: 12810547
  17. Glaucomatous optic nerve head astrocytes express a higher level of 3alpha-HSD isoform AKR1C2 and its mRNA than normal astrocytes. PMID: 13678667
  18. 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
  19. 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
  20. metabolizes tibolone PMID: 15383625
  21. 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
  22. 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
  23. The regulation of AKR1C2 by antioxidant response element suggests that AKR1C2 detoxifies products of reactive oxidant injury. PMID: 16478829
  24. 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
  25. 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
  26. 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
  27. 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
  28. 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
  29. 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
  30. 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


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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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