GSS Human

Glutathione Synthetase Human Recombinant
Cat. No.
BT26450
Source
Escherichia Coli.
Synonyms
Glutathione synthetase, GSH synthetase, GSH-S, Glutathione synthase, GSHS, MGC14098, GSS.
Appearance
Sterile Filtered colorless 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

GSS Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 494 amino acids (1-474 a.a.) and having a molecular mass of 54.5kDa. The GSS is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Glutathione synthetase (GSS) is an essential enzyme in the glutathione biosynthesis pathway, catalyzing the final step of glutathione production. It facilitates the condensation of gamma-glutamylcysteine with glycine to form glutathione. Deficiencies in GSS can lead to glutathione synthetase deficiency, also known as GSS deficiency, 5-oxoprolinuria, or pyroglutamic aciduria. This condition is characterized by increased hemolysis (breakdown of red blood cells) and impaired central nervous system function.
Description
This product consists of recombinant human GSS, expressed in E. coli and fused with a 20 amino acid His tag at its N-terminus. This results in a single, non-glycosylated polypeptide chain containing 494 amino acids (including the His tag, residues 1-474 represent the GSS sequence). The molecular weight of the fusion protein is 54.5kDa. Purification is achieved using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless solution, sterile-filtered.
Formulation
This GSS solution is provided at a concentration of 1mg/ml in a buffer consisting of 20mM Tris-HCl (pH 8.0), 1mM DTT, and 10% glycerol.
Stability
For short-term storage (up to 2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. The addition of 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 95.0% using SDS-PAGE analysis.
Synonyms
Glutathione synthetase, GSH synthetase, GSH-S, Glutathione synthase, GSHS, MGC14098, GSS.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHQH SSGLVPRGSH MATNWGSLLQ DKQQLEELAR QAVDRALAEG VLLRTSQEPT SSEVVSYAPF TLFPSLVPSA LLEQAYAVQM DFNLLVDAVS QNAAFLEQTL SSTIKQDDFT ARLFDIHKQV LKEGIAQTVF LGLNRSDYMF QRSADGSPAL KQIEINTISA SFGGLASRTP AVHRHVLSVL SKTKEAGKIL SNNPSKGLAL GIAKAWELYG SPNALVLLIA QEKERNIFDQRAIENELLAR NIHVIRRTFE DISEKGSLDQ DRRLFVDGQE IAVVYFRDGY MPRQYSLQNW EARLLLERSH AAKCPDIATQ LAGTKKVQQE LSRPGMLEML LPGQPEAVAR LRATFAGLYS LDVGEEGDQA IAEALAAPSR FVLKPQREGG GNNLYGEEMV QALKQLKDSE ERASYILMEK IEPEPFENCL LRPGSPARVV QCISELGIFG VYVRQEKTLV MNKHVGHLLR TKAIEHADGG VAAGVAVLDN PYPV.

Product Science Overview

Introduction

Glutathione synthetase (GSS) is a crucial enzyme in the biosynthesis of glutathione (GSH), a tripeptide composed of glutamate, cysteine, and glycine. GSH is a vital antioxidant that plays a significant role in maintaining cellular redox balance, detoxification, and immune response. The recombinant form of human glutathione synthetase is produced using genetic engineering techniques to express the human enzyme in microbial systems, such as Escherichia coli.

Structure and Function

Glutathione synthetase catalyzes the ATP-dependent condensation of gamma-glutamylcysteine and glycine to form glutathione . This reaction is the second step in the GSH biosynthesis pathway, following the formation of gamma-glutamylcysteine by gamma-glutamylcysteine synthetase. The enzyme is a homodimer in humans, meaning it consists of two identical subunits non-covalently bound to each other .

Genetic and Biochemical Properties

The gene encoding human glutathione synthetase is located on chromosome 20q11.2 . Defects in this gene can lead to glutathione synthetase deficiency, a rare autosomal recessive disorder characterized by metabolic acidosis, 5-oxoprolinuria, increased hemolysis, and neurological dysfunction . The enzyme’s active site binds ATP and the substrates, facilitating the formation of an acylphosphate intermediate, which is then attacked by glycine to form GSH .

Recombinant Production

Recombinant human glutathione synthetase is produced by inserting the human GSS gene into a suitable expression vector, which is then introduced into a host organism, typically E. coli . The host cells are cultured under conditions that promote the expression of the recombinant enzyme. The enzyme is then purified from the host cells using various chromatographic techniques.

Applications

Recombinant human glutathione synthetase has several applications in research and industry. It is used to study the biochemical properties and regulation of GSH biosynthesis. Additionally, it is employed in the production of GSH for pharmaceutical and cosmetic purposes . GSH is widely used for its antioxidant properties, detoxification capabilities, and potential therapeutic benefits in conditions such as oxidative stress, liver diseases, and immune disorders .

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