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Recombinant Glutathione S-Transferase His Tag

Synonyms    Glutathione S-Transferase, GST, Glutathione S-transferase class-mu 28 kDa isozyme, GST 28, EC 2.5.1.18, Sj28GST, Sj28 antigen.
Introduction    Antioxidant enzyme Glutathione S- Transferase (GST) is thought to do the primary cellular defense mechanism against reactive oxygen species. GST reduces lipid hydroperoxides through its Se-independent glutathione peroxidase activity. The enzyme also detoxifies lipid peroxidation end products such as 4-hydroxynonenal (4-HNE).
The soluble GST is a 26 kDa protein which occurs as a dimer in all aerobic organisms. Each monomer has two domains, one that binds GSH and is an /-structure similar to thioredoxin and the other, all helical, that binds the hydrophobic substrate. The GST -fusion protein expression system is a widely used recombinant protein expression system that allows a peptide or a regulatory protein domain to be expressed as a fusion to the C-terminus of Schistosoma japonicum GST. Fusion proteins also possess GST -enzymatic activity and can undergo dimerization similar to in vivo. The fusion protein can be purified via GST -affinity column chromatography. In most cases, the desired peptides or domains are removed from GST by applying a specific protease that recognizes and cleaves the linker between the protein domain and GST. The technique has been widely used to generate different kinds of proteins for crystallization, molecular immunology studies, the production of vaccines and studies involving protein-protein and protein-DNA interactions.
Description    Recombinant Schistosoma japonicum GST full length protein contains 244 amino acids(1-224 a.a.) expressed in E.coli, having a molecular mass of 28.3kDa.
The GST protein is fused to 20 amino acid His-Tag at N-terminus.
The GST protein is purified by proprietary chromatographic techniques.
Source    Escherichia Coli.
Physical Appearance    Sterile Filtered clear solution.
Formulation    GST is supplied in PBS pH 7.4 & 10% glycerol.
Stability    Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months.
Please prevent freeze-thaw cycles.
Purity    Greater than 95% as determined by SDS-PAGE.
Sequence    MGSSHHHHHH SSGLVPRGSH MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID GDVKLTQSMAIIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALDVVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPKSD LVPR.
Biological Activity    2.8-3.3 units/mg, & is defined as the amount of enzyme that conjugate 1.0 u mole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH-6.5 at 25C.
Usage    CHI'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.

Cat No. Description Unit Price Order
7-02875 Recombinant Glutathione S-Transferase His Tag 10 µg $ 103.17 
7-02876 Recombinant Glutathione S-Transferase His Tag 50 µg $ 268.25 
7-02877 Recombinant Glutathione S-Transferase His Tag 1 mg $ 4285.71 
Ordering Information
Email:order@chiscientific.com
Tel:800.986.6008
Fax:978.897.5462
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