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Validated All-in-One™ qPCR Primer for AKR1B10(NM_020299.4) Search again
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
Summary
This gene encodes a member of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. This member can efficiently reduce aliphatic and aromatic aldehydes, and it is less active on hexoses. It is highly expressed in adrenal gland, small intestine, and colon, and may play an important role in liver carcinogenesis. [provided by RefSeq].
Gene References into function
- role as efficient retinal reductase and consequence in retinoid metabolism
- Z-2 allele of the aldose reductase gene is a risk factor for the development of diabetic retinopathy in a group of Caucasian participants with Type 2 diabetes.
- Aldose reductase might play a role in cell cycle progression of A549 tumor cells.
- Data show tha activation of protein kinase C and tyrosine kinase by 12-O-tetradecanoylphorbol-13-acetate elicits increased promoter activity of aldose reductase gene via nuclear factor kappaB.
- Data show that human aldose reductase increases atherosclerosis in diabetic mice.
- crystallographic analysis of human aldose reductase
- TIMP3, DAPK1 and AKR1B10 are important for squamous cell lung cancer tumorogenesis while AKR1B10 is potential oncogene whereas TIMP3 and DAPK1 are potential tumor suppressor genes.
- Inhibition of aldose reductase prevented TNF-alpha-induced activation of protein kinase C and NF-kappaB which resulted in the abrogation of Cox-2 mRNA and protein expression
- associated with tumor recurrence after surgery and keratinization of squamous cell carcinoma in cervical cancer but not endometrial cancer
- AKR1B10 may regulate cell proliferation and cellular response to additional carbonyl stress
- a tyrosine residue located in the catalytic site (Tyr48) is a likely candidate to act as proton acceptor upon inhibitor binding, as it occurs deprotonated to a remarkable extent if only the cofactor NADP+ is bound
- AKR1B10 regulates the stability of acetyl-CoA carboxylase-alpha and is a novel regulator of the biosynthesis of fatty acid, an essential component of the cell membrane, in breast cancer cells
- structural analysis of the high all-trans-retinaldehyde reductase activity of the tumor marker AKR1B10
- The reaction of C299S mutant AKR1B10 is inhibited by fenofibric acid, but manifests pure non-competitive inhibition kinetics that are different from those demonstrated for the wild-type enzyme.
- AKR1B10 might be useful as a new marker for identification of high lung cancer risk patients in usual interstitial pneumonia.
- Results describe cathepsin D and aldo-keto reductase 1C2 and 1B10 dysregulation in Barrett's esophagus and esophageal adenocarcinoma.
- substrate specificity of AKR1B10 is drastically affected by mutation of residue 299 from Cys to Ser
