Glutathione S-transferase (GST) Protein

This recombinant Glutathione S-transferase (GST) protein is encoded by the parasitic Schistosoma japonicum GST gene. The parasite GST protein shows ~60% homogy with class Mu isozymes of mammalian GST (EC 2.5.1.18). The mammalian GST super family consists of four classes: Alpha, Mu, Pi, and Theta. GST catalyzes the conjugation of reduced glutathione to electrophiles on many substrates, thus detoxifying endogenous compounds such as lipid peroxides.

Many recombinant proteins are expressed as glutathione S-transferase fusion proteins to facilitate purification. The recombinant GST can be used as a negative control for recombinant growth factors expressed as GST fusion proteins. The C-terminal end of the protein harbors an engineered thrombin cleavage site and a protein kinase A (PKA) phosphorylation site. The protein can therefore be radioactively labeled with 32P-g-ATP and PKA.

From the laboratory of Te-Chung Lee, PhD, University at Buffalo.

The Investigator's Annexe Part of The Investigator's Annexe program.

Catalog Number Product Size AVAILABILITY Price Qty
EBU009
Glutathione S-transferase (GST) Protein, 100ug (0.1mg/mL)
100ug (0.1mg/mL) In stock
Price: $220.00
EBU010
Glutathione S-transferase (GST) Protein, 500ug (5x100ug, 0.1mg/mL)
500ug, 5x100ug (0.1mg/mL) In stock
Price: $772.00
Specifications
Product Type: Protein
Name: Glutathione S-transferase (GST)
Accession ID: M14654
Source: Recombinantly expressed in E. coliBL21
Molecular Weight: 25 kDa
Amino Acid Sequence: MSPILGYWKIKGLVQPTRLLLEYLEEKYEEHLYERDEGDKWRNKKFELGLEFPNLPYYIDGDVKLTQSMAIIRYIADKHNMLGGCPKERAEISMLEGAVLDIRYGVSRIAYSKDFETLKVDFLSKLPEMLKMFEDRLCHKTYLNGDHVTHPDFMLYDALDVVLYMDPMCLDAFPKLVCFKKRIEAIPQIDKYLKSSKYIAWPLQGWQATFGGGDHPPK
Purity: 99%
Buffer: Tris/NaCl/EDTA
Concentration: 0.1mg/mL
Storage: -80C
Shipped: Dry ice
Data

Detection of GST by SDS-PAGE

GST Figure

Purified GST and GST-YAF2 proteins (2 ug each) were fractionated by 12% SDS-PAGE and stained by Coomassie Blue.

Provider
From the laboratory of Te-Chung Lee, PhD, University at Buffalo.
References
  1. Khan TA, Wang X, Maynard JA. Inclusion of an RGD Motif Alters Invasin Integrin-Binding Affinity and Specificity. Biochemistry. 2016 Apr 12;55(14):2078-90. View Article

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