BcMag™ GST-tagged Protein Purification Kit

Glutathione-S-transferase (GST) is a highly soluble and stable 26 kDa enzyme that catalyzes the protective mechanisms of Glutathione (GSH). Many eukaryotic proteins are produced as inclusion bodies (insoluble aggregated protein), a malfunctioning protein caused by misfolding, in prokaryotic expression systems such as E. coli. It is usually painful to refold the inclusion body into a functional protein. GST is widely used as a fusion partner that promotes greater expression and solubility of the desired protein by taking advantage of its high stability and solubility to overcome this problem. Moreover, GST has a high affinity toward reduced Glutathione, its natural substrate. Therefore, GST as an affinity tag becomes a versatile tool for single-step purification of active recombinant production in a prokaryotic expression system. Glutathione is a short peptide (Glu-Cys-Gly) that displays a high affinity toward glutathione S-transferase (GST). When the Glutathione is immobilized in a chromatography matrix such as beaded agarose or magnetic beads, the matrix can precisely capture GST-tagged protein via the affinity interaction. The GST tag can be fused to either the C- or N-terminus of a protein by inserting DNA sequence coding for the protein of interest into commercial expression vectors. The protein of interest can be cleaved off the GST tag by site-specific protease if desired. The protease site can be engineered between GST-tag and the protein of interest. Currently, Glutathione is mainly immobilized to the traditional affinity chromatography matrices such as agarose resin or column. These solid matrices make the purification process tedious, time-consuming, unable to handle very tiny samples, and challenging to adapt to the automation system. Bioclone introduces a powerful magnetic beads-based GST–tagged protein system to overcome these problems.

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