protein

L-xylulose reductase/DCXR Protein, Human (His)

HY-P70082

5 μg;10 μg;50 μg;100 μg

47;80;225;380 USD

L-xylulose reductase/DCXR Protein, Human (His)

proteins

E. coli

5 μg;10 μg;50 μg;100 μg

47;80;225;380 USD

L-xylulose reductase, encoded by the DCXR gene, plays a vital role in cellular metabolism by catalyzing the NADPH-dependent reduction of various pentoses, tetoses, trisaccharides, α-dicarbonyl compounds, and L-xylulose role. This enzyme is actively involved in the uronic acid cycle of glucose metabolism. L-xylulose reductase/DCXR Protein, Human (His) is the recombinant human-derived L-xylulose reductase/DCXR protein, expressed by E. coli , with N-6*His labeled tag. The total length of L-xylulose reductase/DCXR Protein, Human (His) is 244 a.a., with molecular weight of ~28.0 kDa.

Human

L-xylulose reductase, encoded by the DCXR gene, is a versatile enzyme that catalyzes the NADPH-dependent reduction of various pentoses, tetroses, trioses, alpha-dicarbonyl compounds, and specifically L-xylulose. As part of the uronate cycle in glucose metabolism, this enzyme participates in diverse biochemical reactions, contributing to the cellular processing of different sugars. Notably, L-xylulose reductase is implicated in water absorption and cellular osmoregulation in the proximal renal tubules. By producing xylitol, an osmolyte, this enzyme helps prevent osmolytic stress within the renal tubules, showcasing its potential role in maintaining cellular homeostasis in the kidney. The multifunctionality of L-xylulose reductase underscores its significance in both sugar metabolism and cellular osmoregulation, providing insights into its broader physiological impact.

rHuL-xylulose reductase/DCXR, His; L-Xylulose Reductase; XR; Carbonyl Reductase II; Dicarbonyl/L-Xylulose Reductase; Kidney Dicarbonyl Reductase; kiDCR; Sperm Surface Protein P34H; DCXR

Greater than 90% as determined by reducing SDS-PAGE

Supplied as a 0.2 μm filtered solution of 50 mM Tris, 300 mM NaCl, 30% Glycerol, pH 7.4.

Shipping with dry ice.