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anti-Human AKR1C2 Antibodies:
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Human Monoclonal AKR1C2 Primary Antibody for ELISA, WB - ABIN514927
Takahashi, Bains, Pfeifer, Grigliatti, Reid, Riggs: Aldo-keto reductase 1C2 fails to metabolize doxorubicin and daunorubicin in vitro. in Drug metabolism and disposition: the biological fate of chemicals 2008
Show all 2 Pubmed References
Human Polyclonal AKR1C2 Primary Antibody for WB - ABIN514925
Ebert, Kisiela, Wsól, Maser: Proteasome inhibitors MG-132 and bortezomib induce AKR1C1, AKR1C3, AKR1B1, and AKR1B10 in human colon cancer cell lines SW-480 and HT-29. in Chemico-biological interactions 2011
Human Polyclonal AKR1C2 Primary Antibody for ELISA, WB - ABIN560582
Su, Liao, Huang, Chu, Lin, Chang: Aldo-keto reductase 1C2 is essential for 1-nitropyrene's but not for benzo[a]pyrene's induction of p53 phosphorylation and apoptosis. in Toxicology 2008
Tibolone is metabolized by the 3alpha/3beta-hydroxysteroid dehydrogenase activities of the four human isozymes of the aldo-keto reductase 1C subfamily: inversion of stereospecificity with a delta5(10)-3-ketosteroid.
Curcumin treatments considerably increased the expression of AKR1C2 in prostate cancer cell lines.
Data show that increased levels of AKR1C1/C2 enhanced the sensitivity of esophageal squamous cell carcinoma (ESCC) cells to ethyl-3,4-dihydroxybenzoate (EDHB).
The reduction of DHT obese homozygotic twins could be linked to its increased degradation by AKR1C2 and HSD11B1, and increased estrogen levels could be linked to increased adiposity-related expression of aromatase in adipose tissue.
the present study suggests that AKR1C1, AKR1C2, AKR1C3, and AKR1C4 are closely associated with drug resistance to both CDDP and 5FU, and that mefenamic acid, an inhibitor of AKR1C, restores sensitivity through inhibition of drug-resistance in human cancer cells.
We identified two powerful genes in the liver cancer metastasis process, AEG-1 and AKR1C2.
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.
The endogenous HMOX1 gene but not the AKR1C2 gene is strongly repressed by Bach1 in HaCaT keratinocytes.
In model cell lines of endometrial cancer, AKR1C2 and SRD5A1 have crucial roles in progesterone metabolism.
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
The V54L mutation significantly decreases the 3alpha-hydroxysteroid dehydrogenase activity of DDH2 for the reduction of dihydrotestosterone.
DDH2 expression might be a potential predictor and monitor of cisplatin efficacy in advanced NSCLC patients.
Data suggest that interleukin-1beta facilitates progesterone metabolism in cervical fibroblasts by regulating expression of AKR1C1 and AKR1C2.
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.
role of AKR1C2 in the metabolism of testosterone and progesterone via the 5beta-reductase pathway.
enhanced metabolism of progesterone by SRD5A1 and the 20alpha-HSD and 3alpha/beta-HSD activities of AKR1C1, AKR1C2 and AKR1C3
analysis of single nucleotide polymorphisms of AKR1C1 and AKR1C2
The folding initiation mechanism of human bile acid-binding protein (BABP) has been examined by (19) F NMR.
Overexpression of aldo-keto reductase 1C2 is associated with disease progression in patients with prostatic cancer
We investigated associations between single nucleotide polymorphisms in genes HSD3B1, SRD5A1/2, and AKR1C2 and prostate cancer risk
This gene encodes a member of the aldo/keto reductase superfamily, which consists of more than 40 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. This gene shares high sequence identity with three other gene members and is clustered with those three genes at chromosome 10p15-p14. Three transcript variants encoding two different isoforms have been found for this gene.
, aldo-keto reductase family 1 member C2
, chlordecone reductase homolog HAKRD
, dihydrodiol dehydrogenase 2; bile acid binding protein; 3-alpha hydroxysteroid dehydrogenase, type III
, pseudo-chlordecone reductase
, trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
, type II dihydrodiol dehydrogenase
, 17-alpha-hydroxysteroid dehydrogenase
, 3(or 17)-alpha-hydroxysteroid dehydrogenase
, 3-alpha-hydroxysteroid dehydrogenase
, aldo-keto reductase family 1 member C21
, aldo-keto reductase family 1, member C21