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Human DCXR / HCR2 Protein (His Tag)

DCR,HCR2,HCRII,KIDCR,P34H,PNTSU,SDR20C1,XR

Catalog Number P14562-H07E
Organism Species Human
Host E. coli
Synonyms DCR,HCR2,HCRII,KIDCR,P34H,PNTSU,SDR20C1,XR
Molecular Weight The recombinant human DCXR consists of 259 amino acids and predicts a molecular mass of 27.8 KDa. It migrates as an approximately 29 KDa band in SDS-PAGE under reducing conditions.
predicted N His
SDS-PAGE
Purity > 95 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the mature form of human DCXR (Q7Z4W1) (Met1-Cys244) was expressed with a polyhistidine tag at the N-terminus.
Bio-activity
Research Area Cancer |Signal transduction |Metabolism |Types of disease |Metabolism in Cancer
Formulation Lyophilized from sterile PBS, 20% Glycerol, pH 7.4.
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background DCXR, also known as HCR2, belongs to the short-chain dehydrogenases/reductases (SDR) family. It is highly expressed in kidney, liver and epididymis. In the epididymis, DCXR is mainly expressed in the proximal and distal sections of the corpus region. HCR2 is weakly or not expressed in brain, lung, heart, spleen and testis. DCXR catalyzes the NADPH-dependent reduction of several pentoses, tetroses, trioses, alpha-dicarbonyl compounds and L-xylulose. DCXR participates in the uronate cycle of glucose metabolism. It may play a role in the water absorption and cellular osmoregulation in the proximal renal tubules by producing xylitol, an osmolyte, thereby preventing osmolytic stress from occurring in the renal tubules.
Reference
  • Kim W, et al. (2011) Systematic and quantitative assessment of the ubiquitin-modified proteome. Mol Cell. 44(2):325-40.
  • Pierce SB, et al. (2011) Garrod's fourth inborn error of metabolism solved by the identification of mutations causing pentosuria. Proc Natl Acad Sci. 108(45):18313-7.
  • Udeshi ND, et al. (2012) Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition. Mol Cell Proteomics. 11(5):148-59.