AKR1B1 Mouse

Aldose Reductase Mouse Recombinant
Cat. No.
BT15913
Source
E.coli.
Synonyms
Aldose reductase, AKR1B1, AR, Aldehyde reductase, Akr1b3, Aldor1, Aldr1, Akr1b1, Ahr-1, Ahr1, ALR2.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95% 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

AKR1B1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 339 amino acids (1-316a.a.) and having a molecular mass of 38.1kDa.
AKR1B1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
AKR1B1, a member of the aldo/keto reductase superfamily, plays a crucial role in glucose metabolism and is implicated in diabetic complications. It catalyzes the reduction of glucose to sorbitol, potentially contributing to the development of diabetic complications. This enzyme exhibits broad substrate specificity, reducing various carbonyl compounds. Studies using transgenic mice overexpressing human aldose reductase highlight AKR1B1's involvement in ischemic injury and its impact on post-ischemic recovery. Additionally, AKR1B1 is recognized as a crucial mediator in TNF-alpha signaling, influencing adhesion molecule expression and monocyte binding to the endothelium. Notably, it acts as a critical regulator of TNF-alpha-induced apoptosis in endothelial cells.
Description
Recombinant AKR1B1 Mouse protein, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 339 amino acids (1-316a.a.) with a molecular weight of 38.1kDa. A 23 amino acid His-tag is fused to the N-terminus. Purification is achieved using proprietary chromatographic techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The AKR1B1 protein solution is provided at a concentration of 1mg/ml. It is formulated in a buffer consisting of Phosphate buffered saline (pH7.4) and 10% glycerol.
Stability
For short-term storage (up to 2-4 weeks), the product should be kept at 4°C. For extended storage, it is recommended to store the product frozen at -20°C. To ensure optimal stability during long-term storage, the addition of a carrier protein such as HSA or BSA (0.1%) is advisable. It is important to minimize repeated freeze-thaw cycles.
Purity
The purity of the AKR1B1 protein is greater than 95% as determined by SDS-PAGE analysis.
Biological Activity
The specific activity of the enzyme is measured as greater than 500 pmol/min/ug. This is defined as the amount of enzyme required to catalyze the reduction of 1.0 pmole of DL-glyceraldehyde per minute in the presence of NADPH at a pH of 7.0 and a temperature of 37°C.
Synonyms
Aldose reductase, AKR1B1, AR, Aldehyde reductase, Akr1b3, Aldor1, Aldr1, Akr1b1, Ahr-1, Ahr1, ALR2.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMASHLEL NNGTKMPTLG LGTWKSPPGQ VTEAVKVAID LGYRHIDCAQ VYQNEKEVGV ALQEKLKEQV VKRQDLFIVS KLWCTFHDKS MVKGAFQKTL SDLQLDYLDL YLIHWPTGFK PGPDYFPLDA SGNVIPSDTD FVDTWTAMEQ LVDEGLVKTI GVSNFNPLQI ERILNKPGLK YKPAVNQIEC HPYLTQEKLI EYCHSKGIVV TAYSPLGSPD RPWAKPEDPS LLEDPRIKAI AAKYNKTTAQ VLIRFPIQRN LVVIPKSVTP VRIAENLKVF DFEVSSEDMA TLLSYNRNWR VCALMSCAKH KDYPFHAEV.

Product Science Overview

Introduction

Aldose reductase (AR) is a cytosolic monomeric enzyme that belongs to the aldo-keto reductase (AKR) superfamily. This superfamily includes more than 150 NAD(P)(H)-dependent oxidoreductases found in all prokaryotic and eukaryotic kingdoms, including yeast, plants, invertebrates, and vertebrates . The enzyme is known for its role in the polyol pathway, where it catalyzes the reduction of glucose to sorbitol .

Structure and Function

Aldose reductase is a reduced nicotinamide-adenine dinucleotide phosphate (NADPH)-dependent enzyme that catalyzes the reduction of various aldehydes and ketones to their corresponding alcohols . The enzyme consists of 316 amino acid residues and weighs approximately 35,853 Da . The active site pocket of aldose reductase is relatively hydrophobic, lined by several aromatic and non-polar residues .

Role in Diabetic Complications

Aldose reductase has been extensively studied due to its involvement in diabetic complications . Under diabetic conditions, the enzyme converts excess glucose into sorbitol, which is then converted to fructose . This accumulation of sorbitol and fructose can lead to osmotic stress and contribute to various diabetic complications, such as diabetic retinopathy and nephropathy .

Tissue Distribution and Expression

Aldose reductase is ubiquitously expressed in various human organs, including the kidney, lens, retina, nerve, heart, placenta, brain, skeletal muscle, testis, blood vessels, lung, and liver . However, AR-like proteins exhibit tissue-specific patterns of expression . For instance, certain isoforms are enriched in the adrenal gland, enterohepatic, and adipose tissues .

Physiological Functions Beyond Detoxification

Beyond its role in detoxification, recent studies suggest that aldose reductase and its isoforms may have additional physiological functions . These enzymes are capable of modifying or generating signaling molecules, shifting their status from mere scavengers to important messengers . This has implications for their roles in glucido-lipidic metabolism and adipose tissue homeostasis .

Clinical Significance

Aldose reductase is involved in many oxidative stress diseases, cell signal transduction, and cell proliferation processes, including cardiovascular disorders, sepsis, and cancer . Inhibition of aldose reductase has been suggested as a therapeutic strategy to reduce inflammation associated with the activation of retinal microglia .

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