Glutathione S-Transferase (GST) is a family of enzymes involved in detoxification processes by catalyzing the conjugation of the reduced form of glutathione (GSH) to xenobiotic substrates. Among the various classes of GSTs, the Pi class (GSTP) is particularly noteworthy due to its significant role in cellular detoxification and its involvement in various diseases, including cancer.
Glutathione S-Transferase Pi 2 (GSTP2) is a member of the Pi class of GSTs. In mice, GSTP2 is encoded by the Gstp2 gene. This enzyme is predominantly expressed in the liver and plays a crucial role in the detoxification of endogenous and exogenous compounds. GSTP2 has been shown to have anti-inflammatory properties and is involved in the regulation of apoptosis and cellular proliferation .
Recombinant proteins are proteins that are artificially produced through recombinant DNA technology. This involves inserting the gene encoding the protein of interest into an expression system, such as bacteria, yeast, or mammalian cells, to produce the protein in large quantities. Recombinant GSTP2 is produced by cloning the Gstp2 gene into an expression vector, which is then introduced into a suitable host cell for protein expression.
A His tag, or polyhistidine tag, is a string of histidine residues (usually six) added to either the N-terminus or C-terminus of a protein. This tag facilitates the purification of the recombinant protein through affinity chromatography. The His tag binds to metal ions, such as nickel or cobalt, which are immobilized on a chromatography resin. This allows for the selective binding and elution of the His-tagged protein from a mixture of proteins .
The production of GSTP2 mouse recombinant, His tag, involves several steps:
Recombinant GSTP2 with a His tag has several applications in research and biotechnology: