GSTM2 Recombinant Protein

Source : Escherichia Coli. GSTM2 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 238 amino acids (1-218 a.a.) and having a molecular mass of 27.9kDa. The GSTM2 is purified by proprietary chromatographic techniques. Glutathione S-transferase Mu 2 (GSTM2) belongs to the glutathione s-transferase (GST) family of proteins. GSTM2 is a glutathione S-transferase that belongs to the mu class. There are 8 families of GST proteins, specifically: alpha, kappa, mu, omega, pi, sigma, theta and zeta, each of which is composed of proteins that have various functions throughout the cell. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are structured in a gene cluster on chromosome 1p13.3 and are proven to be highly polymorphic. These genetic variants can change an individual''s susceptibility to carcinogens and toxins as well as have an effect on the toxicity and efficacy of several drugs.

Glutathione S-transferase Mu 2||GST class-mu 2||GSTM2-2||GSTM2||GST4||GSTM||GTHMUS||MGC117303.

Greater than 95.0% as determined by SDS-PAGE.

The GSTM2 solution (0.5 mg/mL) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol,0.1M NaCl and 1mM DTT.

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.

Specific activity is < 25 units/mg, and is defined as the amount of enzyme that conjugate 1.0 μmole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25°C.