SDS-Page: Recombinant Bacteria GST Epitope Tag Protein [NBP1-30259] - GST Epitope Tag Protein Glutathione S- Transferase(GST), 28.3 kDa (244aa), confirmed by MALDI-TOF with a purity of 95% by SDS - PAGE
Specific activity is > 10 units/mg, and is defined as the amount of enzyme that conjugate 1.0 umole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25C.
>95% pure by SDS-PAGE
28.3 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Read Publication using NBP1-30259 in the following applications:
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
Phosphate buffered saline (pH 7.4), 10% glycerol
>95% pure by SDS-PAGE
Alternate Names for Recombinant Parasite GST Epitope Tag Protein
glutathione S-transferase M1
glutathione S-transferase mu 1
GST class-mu 1
GST HB subunit 4
HB subunit 4
Glutathione S-transferase (GST) represents a major group of detoxification enzymes. This enzyme acts by catalyzing the reaction of glutathione with an acceptor molecule to form an S-substituted glutathione (S=sulfur). The reactions utilizing glutathione contribute the transformation of a wide range of compounds, including carcinogens, therapeutic drugs, and products of oxidative stress. As well as its enzymatic activities, GST may also bind toxins and function as transport protein. Because of this, an early term for GSTs was ligandin. Glutathione S-transferase was originally separated from Schistosoma japonicum but currently isolated from recombinant E.coli source. Recombinant human GST, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are guaranteed for 3 months from date of receipt.
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