AKR7A2 Human

Aldo-Keto Reductase Family 7 Member A2 Human Recombinant
Cat. No.
BT16866
Source
Escherichia Coli.
Synonyms
Aflatoxin B1 aldehyde reductase member 2, AFAR, AFAR1, AFB1-AR1, AKR7, Succinic semialdehyde reductase, SSA reductase, AFB1 aldehyde reductase 1, Aldoketoreductase 7, AKR7A2.
Appearance
Sterile Filtered clear colorless solution.
Purity
Greater than 90.0% 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

AKR7A2 Human Recombinant fused to a 39 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 398 amino acids (1-359 a.a) and having a molecular mass of 44 kDa. The AKR7A2 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Aldo-keto reductase family 7 member A2 (AKR7A2) is an enzyme that plays a crucial role in detoxifying aldehydes and ketones. It catalyzes the reduction of succinic semialdehyde to gamma-hydroxybutyrate, utilizing NADPH as a cofactor. This reaction is significant as it produces gamma-hydroxybutyrate (GHB), a neuromodulator. Notably, AKR7A2 exhibits broad substrate specificity, demonstrating NADPH-dependent aldehyde reductase activity towards various substrates, including 2-carboxybenzaldehyde, 2-nitrobenzaldehyde, and pyridine-2-aldehyde in laboratory settings. Additionally, it can reduce 1,2-naphthoquinone and 9,10-phenanthrenequinone in vitro. AKR7A2 also plays a critical role in detoxifying aflatoxin B1 (AFB1), a potent liver carcinogen, by reducing its dialdehyde protein-binding form to the non-binding AFB1 dialcohol. Therefore, AKR7A2 contributes to protecting the liver against AFB1's toxic and carcinogenic effects.
Description
Recombinant human AKR7A2, fused with a 39 amino acid His Tag at its N-terminal, is produced in E. coli. This protein is a single, non-glycosylated polypeptide chain consisting of 398 amino acids, with a molecular weight of 44 kDa. Purification of AKR7A2 is achieved through proprietary chromatographic methods.
Physical Appearance
A clear, colorless solution that has undergone sterile filtration.
Formulation
The AKR7A2 solution is formulated in a buffer consisting of 20mM Tris-HCl (pH 8), 1mM DTT, and 20% glycerol.
Stability
For short-term storage (up to 4 weeks), keep at 4°C. For long-term storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for extended storage. Avoid repeated freezing and thawing.
Purity
The purity of the AKR7A2 protein is determined to be greater than 90% using SDS-PAGE analysis.
Biological Activity
The specific activity of the enzyme is approximately 0.25-0.3 units per mg of protein. Enzymatic activity is determined by measuring the amount of enzyme required to oxidize 1 micromole of NADPH per minute at 25°C. The specific activity is then expressed as units per mg of protein.
Synonyms
Aflatoxin B1 aldehyde reductase member 2, AFAR, AFAR1, AFB1-AR1, AKR7, Succinic semialdehyde reductase, SSA reductase, AFB1 aldehyde reductase 1, Aldoketoreductase 7, AKR7A2.
Source
Escherichia Coli.
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSELEM LSAASRVVSR AAVHCALRSP PPEARALAMS RPPPPRVASV LGTMEMGRRM DAPASAAAVR AFLERGHTEL DTAFMYSDGQ SETILGGLGL GLGGGDCRVK IATKANPWDG KSLKPDSVRS QLETSLKRLQ CPQVDLFYLH APDHGTPVEE TLHACQRLHQ EGKFVELGLS NYASWEVAEI CTLCKSNGWI LPTVYQGMYN ATTRQVETEL FPCLRHFGLR FYAYNPLAGG LLTGKYKYED KDGKQPVGRF FGNSWAETYR NRFWKEHHFE AIALVEKALQ AAYGASAPSV TSAALRWMYH HSQLQGAHGD AVILGMSSLE QLEQNLAATE EGPLEPAVVD AFNQAWHLVA HECPNYFR.

Product Science Overview

Introduction

Aldo-Keto Reductase Family 7 Member A2 (AKR7A2) is a protein-coding gene that belongs to the aldo/keto reductase (AKR) superfamily. This superfamily is involved in the detoxification of aldehydes and ketones. AKR7A2, in particular, plays a significant role in the reduction of succinic semialdehyde to gamma-hydroxybutyrate, an important neuromodulator .

Function and Importance

AKR7A2 is known for its broad substrate specificity. It catalyzes the NADPH-dependent reduction of various aldehydes, including 2-carboxybenzaldehyde, 2-nitrobenzaldehyde, and pyridine-2-aldehyde . This enzyme is crucial in detoxifying harmful compounds such as aflatoxin B1, a potent hepatocarcinogen . Additionally, AKR7A2 may play a role in protecting the liver from the toxic and carcinogenic effects of aflatoxin B1 .

Synthetic Routes and Reaction Conditions

The recombinant form of AKR7A2 is typically expressed in Escherichia coli (E. coli). The protein is produced as a single, non-glycosylated polypeptide chain containing 398 amino acids and has a molecular mass of approximately 44 kDa . The expression system involves the use of a 39 amino acid His Tag at the N-terminal, which aids in the purification process through proprietary chromatographic techniques .

Industrial Production Methods

For industrial production, AKR7A2 is expressed in E. coli and purified using chromatographic techniques. The protein is formulated in a solution containing 20 mM Tris-HCl (pH 8), 1 mM dithiothreitol (DTT), and 20% glycerol . The specific activity of the enzyme is measured by the oxidation of NADPH, with activity expressed as units per milligram of protein .

Types of Reactions

AKR7A2 catalyzes the reduction of aldehydes and ketones to their corresponding alcohols. This reaction involves the use of a reduced nicotinamide cofactor (NADPH) and follows an ordered bi-bi kinetic mechanism with general acid-base catalysis . The enzyme’s broad substrate specificity allows it to participate in various metabolic pathways, including the detoxification of reactive aldehydes and the metabolism of endogenous and exogenous compounds .

Common Reagents and Conditions

The common reagents used in the reactions catalyzed by AKR7A2 include NADPH as a cofactor and various aldehyde substrates. The enzyme operates optimally in a buffer solution containing Tris-HCl (pH 8) and DTT to maintain its stability and activity . The reactions are typically carried out at 25°C to ensure optimal enzymatic activity .

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