Glutathione S-transferase (GST) represents a major group of detoxification enzymes. It acts by catalyzing the reaction of glutathione with an acceptor molecule to form an S-substituted glutathione (S=sulfur). The reactions utilizing glutathione contribute to the transformation of a wide range of compounds, including carcinogens, therapeutic drugs, and products of oxidative stress. Apart from its enzymatic activities, GST may also bind toxins and function as a transport protein. Recombinant protein corresponding to aa1-224 from Schistosoma japonicum GST, fused to His-tag at N-terminus, expressed in E. coli. Uniprot/Accession: P09792 Molecular Weight: ~28.3kD (244aa, aa1-224 + NT His Tag) Biological Activity: 2.8-3.3units/mg, defined as the amount of enzyme that conjugates 1u mole of 1-chloro-2, 4-dinitrobenzene (CDNB) with reduced glutathione/minute at pH 6.5 at 25C. Amino Acid Sequence: MGSSHHHHHH SSGLVPRGSH MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID GDVKLTQSMAIIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALDVVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPKSD LVPR Storage and Stability: May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing.. Store at -20C. Aliquots are stable for 6 months after receipt at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
