Active Recombinant Glutathione S-Transferase

• Cat.No.: GST-113
• Product Overview: Recombinant Glutathione S-Transferase full length protein (1-224a.a.) expressed in E.coli, having a molecular mass of 26kDa. GST was isolated from an E. colistrain that carries the coding sequence for Schistosoma japonicum GST under the control of a T7 promoter. The GST is purified by proprietary chromatographic techniques.

Specification

• Description: 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.
• Source: E.coli
• Form: Sterile Filtered clear solution. GST supplied in Phosphate Buffered Saline pH 7.4.
• Bio-activity: 0.5-2.5 units/mg (please enquire for specific batch value). A unit 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.
• Molecular Mass: 26 kDa
• AA Sequence: MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID GDVKLTQSMA IIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALD VVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPKSD LVPR.
• Purity: Greater than 95% as determined by SDS-PAGE.
• Applications: GST can be used for protein-protein interactions assay and protein-DNA interactions assay.
• Stability: Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

Reviews

05/10/2021

Excellent after-sales service, solving many experimental problems.

12/30/2020

The GST protein I purchased is suitable for WB, and I have obtained satisfactory experimental results.

10/22/2020

The protein composition was stable and concentrated, allowing me to obtain satisfactory experimental results.

Q&As

Where is GST primarily located?

GST is mainly localized in the cytoplasm.

How does GST expression change under stress conditions?

Stress stimuli contributed to the up-regulation of GST gene expression, and GSTs showed higher enzymatic activities under different stress stimuli.

What is the function of GST?

GST plays an important role in phytoremediation, detoxification of xenobiotics, and oxidative stress metabolism.

What is the structure of the GST protein?

GST proteins are usually composed of homo- or heterodimers, and each subunit constituting a dimer contains two structural domains, the N-terminal and C-terminal domains.