GLRX1 Yeast

Glutaredoxin 1 Yeast Recombinant
Cat. No.
BT21833
Source
Escherichia Coli.
Synonyms
Thioltransferase, GRX, GLRX1, GRX1, GRX-1, GLRX-1, Glutathione-dependent oxidoreductase 1, Glutaredoxin 1.
Appearance
Sterile Filtered clear colorless solution.
Purity
Greater than 90% 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.
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Description

Glutaredoxin Saccharamyces cerevisiae Recombinant containing 6x His tag at C-Terminus produced in E.Coli is a single, non-glycosylated, Polypeptide chain having a molecular mass of 16 kDa.

Product Specs

Introduction
GLRX1, also known as glutaredoxin, is an enzyme with glutathione-disulfide oxidoreductase activity. This activity is dependent on the presence of NADPH and glutathione reductase. GLRX1 participates in various redox reactions, including the reduction of low molecular weight disulfides and proteins. It acts as a glutathione (GSH)-dependent hydrogen donor for ribonucleotide reductase, an enzyme crucial for DNA synthesis. GLRX1 is multifunctional, possessing glutathione-dependent oxidoreductase, glutathione peroxidase, and glutathione S-transferase (GST) activities. It plays a critical role in maintaining cellular redox balance by reducing cytosolic protein and non-protein disulfides in a system coupled with glutathione reductase. GLRX1 contributes to cellular protection against reactive oxygen species (ROS) by directly reducing hydroperoxides and detoxifying ROS-mediated damage.
Description
This product consists of the recombinant Glutaredoxin protein derived from Saccharomyces cerevisiae (Yeast). It has been engineered with a 6x His tag at the C-terminus and is produced in E. coli. The protein is a single, non-glycosylated polypeptide chain with a molecular weight of 16 kDa.
Physical Appearance
The product is a clear, colorless solution that has been sterilized by filtration.
Formulation
The Glutaredoxin solution is supplied in a buffer containing 25mM Tris-HCl at pH 7.5 and 0.01% sodium azide as a preservative.
Stability
For short-term storage (up to one week), the product should be kept at a temperature of 2-10°C. For long-term storage, it is recommended to store the product at a temperature of -20 to -80°C.
Purity
The purity of the Glutaredoxin protein is greater than 90% as determined by SDS-PAGE analysis.
Synonyms
Thioltransferase, GRX, GLRX1, GRX1, GRX-1, GLRX-1, Glutathione-dependent oxidoreductase 1, Glutaredoxin 1.
Source
Escherichia Coli.

Product Science Overview

Structure and Function

Glutaredoxin 1 is a glutathione (GSH)-dependent hydrogen donor for ribonucleotide reductase and also catalyzes glutathione-disulfide oxidoreduction reactions in the presence of NADPH and glutathione reductase . This enzyme is essential for the reduction of ribonucleotides to deoxyribonucleotides, which are the building blocks for DNA synthesis and repair.

Yeast Recombinant Glutaredoxin 1

The yeast recombinant form of Glutaredoxin 1 is produced using recombinant DNA technology. This involves inserting the gene encoding GLRX1 into yeast cells, which then express the protein. The recombinant protein is subsequently purified for various research and industrial applications.

Role in Yeast

In yeast, Glutaredoxin 1 has been shown to have multiple roles. For instance, the yeast glutaredoxin GRX4, which is closely related to GLRX1, functions as a glutathione S-transferase required for red pigment formation in Saccharomyces cerevisiae . This red pigmentation phenotype is widely used in genetic screens and assays. The GRX domain of GRX4 and its active site cysteine are critical for this activity .

Applications

Recombinant Glutaredoxin 1 is used in various research applications, including studies on redox biology, oxidative stress, and cellular signaling. It is also used in industrial applications where redox reactions are crucial.

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