DCXR Human, Bioactive

Dicarbonyl/L-Xylulose Reductase Human Recombinant, Bioactive
Cat. No.
BT18144
Source
Escherichia Coli.
Synonyms
DCR, HCR2, HCRII, KIDCR, P34H, SDR20C1, Dicarbonyl/L-Xylulose Reductase, EC=1.1.1.10, Carbonyl reductase II, Kidney dicarbonyl reductase, Sperm surface protein P34H.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

DCXR Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 264 amino acids (1-244 a.a.) and having a molecular mass of 28 kDa. The DCXR is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
DCXR, also known as L-xylulose reductase, is an enzyme involved in carbohydrate metabolism. It catalyzes the NADPH-dependent reduction of various sugars, including pentoses, tetroses, trioses, alpha-dicarbonyl compounds, and L-xylulose. DCXR plays a crucial role in the uronate cycle of glucose metabolism. Furthermore, it contributes to water absorption and cellular osmoregulation in the proximal renal tubules by producing xylitol, an osmolyte. This function helps prevent osmolytic stress in the renal tubules.
Description
Recombinant Human DCXR, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 264 amino acids, with the active protein encompassing residues 1-244. The protein has a molecular weight of 28 kDa. A 20 amino acid His-Tag is fused to the N-terminus to facilitate purification, which is carried out using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless solution, sterile-filtered.
Formulation
The DCXR protein is supplied at a concentration of 0.5mg/ml in a buffer consisting of 20mM Tris-HCl (pH 8.0), 1mM DTT, 20% glycerol, and 50mM NaCl.
Stability
For short-term storage (up to 2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to store the protein at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is advised for long-term storage. Avoid repeated freeze-thaw cycles to maintain protein integrity.
Purity
The purity of the DCXR protein is greater than 95%, as determined by SDS-PAGE analysis.
Biological Activity
The specific activity of the enzyme is measured to be greater than 1,800 pmol/min/ug. This is determined by the enzyme's ability to oxidize 1 picomole of xylitol to L-xylulose per minute at pH 10.0 and a temperature of 37°C.
Synonyms
DCR, HCR2, HCRII, KIDCR, P34H, SDR20C1, Dicarbonyl/L-Xylulose Reductase, EC=1.1.1.10, Carbonyl reductase II, Kidney dicarbonyl reductase, Sperm surface protein P34H.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MELFLAGRRV LVTGAGKGIG RGTVQALHAT GARVVAVSRT QADLDSLVRE CPGIEPVCVD LGDWEATERA LGSVGPVDLL VNNAAVALLQ PFLEVTKEAF DRSFEVNLRA VIQVSQIVAR GLIARGVPGA IVNVSSQCSQ RAVTNHSVYC STKGALDMLT KVMALELGPH KIRVNAVNPT VVMTSMGQAT WSDPHKAKTM LNRIPLGKFA EVEHVVNAIL FLLSDRSGMT TGSTLPVEGG FWAC.

Product Science Overview

Introduction

Dicarbonyl/L-Xylulose Reductase (DCXR), also known as Carbonyl Reductase II, is an enzyme that plays a crucial role in the metabolism of various sugars and carbonyl compounds. This enzyme is particularly significant in the reduction of L-xylulose and other dicarbonyl compounds, which are intermediates in the uronate cycle of glucose metabolism .

Structure and Production

The human recombinant form of DCXR is produced in Escherichia coli (E. coli) and is a single, non-glycosylated polypeptide chain consisting of 264 amino acids. The recombinant enzyme includes a 20 amino acid His-Tag at the N-terminus, which facilitates its purification through chromatographic techniques . The molecular mass of the enzyme is approximately 28 kDa .

Function and Mechanism

DCXR catalyzes the NADPH-dependent reduction of a variety of pentoses, tetroses, trioses, alpha-dicarbonyl molecules, and L-xylulose. This reduction process is essential for the conversion of these compounds into their respective alcohol forms, such as xylitol from L-xylulose . The enzyme’s activity is crucial for maintaining cellular osmoregulation and water absorption in the proximal renal tubules by producing xylitol, an osmolyte that prevents osmolytic stress .

Biological Significance

The enzyme’s role in the uronate cycle of glucose metabolism highlights its importance in the broader context of carbohydrate metabolism. By converting L-xylulose to xylitol, DCXR helps regulate the levels of reactive carbonyl species, which can be harmful if accumulated in high concentrations . Additionally, the enzyme’s activity in the kidneys aids in the prevention of osmolytic stress, thereby contributing to overall renal health .

Stability and Storage

The recombinant DCXR enzyme is typically stored in a sterile, filtered, colorless solution containing Tris-HCl buffer, dithiothreitol (DTT), glycerol, and sodium chloride (NaCl). For short-term storage, the enzyme can be kept at 4°C, while long-term storage requires freezing at -20°C with the addition of a carrier protein to prevent degradation . It is important to avoid multiple freeze-thaw cycles to maintain the enzyme’s activity and stability .

Applications

DCXR has various applications in biochemical research and clinical studies. Its ability to reduce a wide range of carbonyl compounds makes it a valuable tool for studying metabolic pathways and the effects of reactive carbonyl species. Additionally, the enzyme’s role in osmoregulation and renal function can be explored in the context of kidney health and disease .

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