GST S. Japonicum, His
Escherichia Coli.
Glutathione S-Transferase class-mu 26 kDa isozyme, Sj26 antigen, SjGST, Glutathione S-Transferase class-mu 26 kDa isozyme Glutathione S Transferase.
Greater than 95.0% as determined by SDS-PAGE.
Description
GST S. Japonicum Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 244 amino acids (1-218) and having a molecular mass of 28.3 kDa.
GST S. Japonicum is fused to a 26 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Product Specs
Glutathione S-transferase (GST) is a family of detoxification enzymes. These proteins catalyze the conjugation of glutathione to a diverse range of acceptor molecules, including drugs, carcinogens, and products of oxidative stress, forming S-substituted glutathione. GST plays roles in detoxification by conjugating glutathione to toxins, and in transport. Originally isolated from Schistosoma japonicum, GST is now commonly produced from E. coli.
Recombinant GST from Schistosoma japonicum, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 244 amino acids (residues 1-218), resulting in a molecular weight of 28.3 kDa. The protein is fused with a 26 amino acid His-Tag at the N-terminus and purified using proprietary chromatographic methods.
The GST S. Japonicum protein solution is provided at a concentration of 1mg/ml in Phosphate-Buffered Saline (pH 7.4) with 10% glycerol.
Repeated freezing and thawing of the product should be avoided.
The purity of the protein is greater than 95.0% as determined by SDS-PAGE analysis.
The specific activity of the enzyme is greater than 10 units/mg. One unit of activity is defined as the amount of enzyme required to conjugate 1.0 µmol of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 and 25°C.
Glutathione S-Transferase class-mu 26 kDa isozyme, Sj26 antigen, SjGST, Glutathione S-Transferase class-mu 26 kDa isozyme Glutathione S Transferase.
Escherichia Coli.
MGSSHHHHHH SSGLVPRGSH MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID GDVKLTQSMA IIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALD VVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPKSD
LVPR
Product Science Overview
Glutathione S-Transferase (GST) is an enzyme that plays a crucial role in the detoxification process within cells. It is involved in the conjugation of the reduced form of glutathione (GSH) to xenobiotic substrates, facilitating their excretion from the body. The GST from Schistosoma japonicum (SjGST) is particularly notable for its use in recombinant protein expression systems.
The GST enzyme from Schistosoma japonicum is a 26 kDa protein that functions as a dimer in aerobic organisms . Each monomer consists of two domains: one that binds GSH and another that binds the hydrophobic substrate. This enzyme is essential for reducing lipid hydroperoxides and detoxifying lipid peroxidation end products such as 4-hydroxynonenal (4-HNE) .
Recombinant SjGST is often fused with a His-tag, a sequence of histidine residues, to facilitate purification. The His-tag allows the recombinant protein to be purified using affinity chromatography, specifically nickel or cobalt-based resins that bind to the histidine residues . This fusion protein retains the enzymatic activity of GST and can be used in various biochemical and molecular biology applications.
The GST fusion protein expression system is widely used for several purposes:
- Protein Purification: The His-tagged GST fusion proteins can be easily purified using affinity chromatography .
- Protein-Protein Interactions: GST fusion proteins are used to study protein-protein interactions by immobilizing the GST-tagged protein on a glutathione resin and incubating it with potential interacting partners .
- Crystallization: The GST fusion system is also employed in protein crystallization studies to determine the three-dimensional structure of proteins .
- Vaccine Development: Recombinant SjGST has been explored as a potential vaccine candidate against Schistosoma japonicum infections .
