GLRX Mouse

Glutaredoxin Mouse Recombinant
Cat. No.
BT24624
Source
Escherichia Coli.
Synonyms

Glutaredoxin-1, Thioltransferase-1, TTase-1, Glrx, Glrx1, Grx, Grx1.

Appearance
Sterile Filtered clear 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

GLRX Mouse  Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids (1-107 a.a) and having a molecular mass of 14.3kDa. GLRX is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
GLRX1, also known as Glutaredoxin 1, is an enzyme with multifaceted roles in cellular redox regulation. It exhibits glutathione-disulfide oxidoreductase activity, utilizing NADPH and glutathione reductase to reduce disulfide bonds in various molecules, including low molecular weight disulfides and proteins. This activity is crucial for maintaining cellular redox balance and protecting against oxidative stress. As a glutathione-dependent hydrogen donor for ribonucleotide reductase, GLRX1 participates in DNA synthesis by supporting the reduction of ribonucleotides to deoxyribonucleotides. Moreover, it contributes to the detoxification of reactive oxygen species (ROS) by directly reducing hydroperoxides and repairing ROS-mediated damage, highlighting its significance in cellular defense mechanisms against oxidative stress.
Description
This product consists of recombinant GLRX protein derived from mouse and produced in E. coli. It is engineered as a single, non-glycosylated polypeptide chain encompassing 130 amino acids, including the 107 amino acids of the GLRX protein (1-107 a.a) and a 23 amino acid His-tag fused at the N-terminus. The molecular weight of the recombinant protein is 14.3 kDa. Purification is achieved through proprietary chromatographic techniques to ensure high purity.
Physical Appearance
The product appears as a clear solution that has been sterilized by filtration.
Formulation
The GLRX protein is supplied in a solution with a concentration of 0.5 mg/ml. The solution is buffered with 20mM MES at pH 5.0 and contains 20% glycerol and 0.1M NaCl for stability.
Stability
For short-term storage (up to 2-4 weeks), the product can be stored at 4°C. For extended storage, freezing at -20°C is recommended. To further enhance stability during long-term storage, the addition of a carrier protein such as HSA or BSA (0.1%) is advisable. It is crucial to avoid repeated freeze-thaw cycles to preserve protein integrity.
Purity
The purity of the GLRX protein is greater than 95.0%, as determined by SDS-PAGE analysis.
Synonyms

Glutaredoxin-1, Thioltransferase-1, TTase-1, Glrx, Glrx1, Grx, Grx1.

Source
Escherichia Coli.
Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH MGSMAQEFVN CKIQSGKVVV FIKPTCPYCR KTQEILSQLP FKQGLLEFVD ITATNNTSAI QDYLQQLTGA RTVPRVFIGK DCIGGCSDLI SMQQTGELMT RLKQIGALQL

Product Science Overview

Introduction

Glutaredoxins (GRXs) are small, ubiquitous proteins that play a crucial role in maintaining cellular redox homeostasis. They are part of the thioredoxin superfamily and are involved in various cellular processes, including DNA synthesis, signal transduction, and defense against oxidative stress. This article focuses on the background of mouse recombinant glutaredoxin, highlighting its structure, function, and significance in biological research.

Structure and Classification

Glutaredoxins are characterized by their conserved active site motif, typically CXXC or CXXS, where “C” stands for cysteine and “X” can be any amino acid. Based on their active sites, GRXs are classified into three subfamilies: CPYC, CGFS, and CC . The CPYC and CGFS subfamilies are present in eukaryotes, while the CC subfamily is exclusive to higher plants .

Expression and Purification

Recombinant mouse glutaredoxin is commonly expressed in Escherichia coli (E. coli) systems due to the ease of genetic manipulation and high yield of protein production . The recombinant protein is typically purified using affinity chromatography techniques, ensuring high purity and biological activity .

Biological Functions

Glutaredoxins are primarily involved in the reduction of disulfide bonds in proteins, utilizing glutathione (GSH) as a cofactor. They play a pivotal role in:

  • Redox Homeostasis: Maintaining the balance between oxidation and reduction within the cell.
  • DNA Synthesis: Supporting ribonucleotide reductase activity, which is essential for DNA synthesis .
  • Signal Transduction: Modulating various signaling pathways by regulating the redox state of target proteins.
  • Oxidative Stress Response: Protecting cells from oxidative damage by reducing reactive oxygen species (ROS) and repairing oxidized proteins .
Research Significance

Recombinant mouse glutaredoxin is widely used in research to study its role in cellular processes and its potential therapeutic applications. It serves as a model to understand the function of GRXs in higher organisms and their involvement in diseases such as cancer and neurodegenerative disorders .

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