MSRA Human

Methionine Sulfoxide Reductase A Human Recombinant
Cat. No.
BT19453
Source
Escherichia Coli.
Synonyms
Mitochondrial peptide methionine sulfoxide reductase, Peptide-methionine (S)-S-oxide reductase, Peptide Met(O) reductase, Protein-methionine-S-oxide reductase, PMSR, MSRA.
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

MSRA Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (24-235) and having a molecular mass of 26.2kDa.
The MSRA is fused to a 24 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
Methionine sulfoxide reductase A (MSRA), a member of the MsrA Met sulfoxide reductase family, plays a critical role as a repair enzyme for proteins deactivated by oxidation. It catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins back to methionine. MSRA utilizes peptide-L-methionine, thioredoxin disulfide, and H₂O as substrates, producing peptide-L-methionine (R)-S-oxide and thioredoxin. This ubiquitous and highly conserved protein exhibits highest expression levels in kidney and nervous tissues in both humans and animals.
Description
Recombinant human MSRA, produced in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 237 amino acids (residues 24-235), resulting in a molecular weight of 26.2 kDa. This protein features a 24 amino acid His-Tag fused at the N-terminus and is purified using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless solution that has been sterilized by filtration.
Formulation
The MSRA protein solution (0.5 mg/ml) is supplied in a buffer containing 20mM Tris-HCl (pH 8.0), 10% glycerol, 1mM DTT, and 50mM NaCl.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
Purity is determined to be greater than 90.0% by SDS-PAGE analysis.
Synonyms
Mitochondrial peptide methionine sulfoxide reductase, Peptide-methionine (S)-S-oxide reductase, Peptide Met(O) reductase, Protein-methionine-S-oxide reductase, PMSR, MSRA.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMGNSAS NIVSPQEALP GRKEQTPVAA KHHVNGNRTV EPFPEGTQMA VFGMGCFWGA ERKFWVLKGV YSTQVGFAGG YTSNPTYKEV CSEKTGHAEV VRVVYQPEHM SFEELLKVFW ENHDPTQGMR QGNDHGTQYR SAIYPTSAKQ MEAALSSKEN YQKVLSEHGF GPITTDIREG QTFYYAEDYH QQYLSKNPNG YCGLGGTGVS CPVGIKK.

Product Science Overview

Introduction

Methionine Sulfoxide Reductase A (MSRA) is an enzyme that plays a crucial role in the repair of oxidative damage to proteins. This enzyme is responsible for the reduction of methionine sulfoxide (MetO) back to methionine, thereby restoring the normal function of oxidized proteins. The human recombinant form of MSRA is produced using recombinant DNA technology, which allows for the production of large quantities of the enzyme for research and therapeutic purposes.

Structure and Function

MSRA is part of the methionine sulfoxide reductase (Msr) system, which consists of two families of enzymes: MsrA and MsrB. These enzymes are stereospecific, with MsrA reducing the S-form of MetO and MsrB reducing the R-form . The primary function of MSRA is to repair oxidative damage to proteins, which can occur under physiological and pathological conditions due to exposure to reactive oxygen species (ROS) and hydrogen peroxide .

Biological Significance

The reduction of MetO by MSRA is essential for maintaining cellular function and protecting against oxidative stress. Oxidative stress can lead to the accumulation of MetO-modified proteins, which may alter their function or cause the accumulation of toxic proteins in cells . By reducing MetO to methionine, MSRA helps to prevent these detrimental effects and supports cellular homeostasis.

Expression and Localization

Human MSRA is expressed in various tissues, with the highest levels found in the kidney and nervous tissue . The enzyme’s activity is dependent on thioredoxin, a small protein that acts as an electron donor in the reduction process . The subcellular distribution of MSRA can be regulated by alternative splicing of its first exon, which affects its localization within the cell .

Clinical Relevance

MSRA has been implicated in several physiological and pathological processes. For example, it has been shown to play a role in the activation of sulindac, a nonsteroidal anti-inflammatory prodrug, to its active metabolite sulindac sulfide . This activation occurs in human tissues and contributes to the drug’s therapeutic effects. Additionally, MSRA’s role in reducing oxidative damage makes it a potential target for therapeutic interventions aimed at mitigating oxidative stress-related diseases.

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