GST, also known as, Glutathione S-transferase, represents a major group of detoxification enzymes. GST 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. GST was originally separated from Schistosoma japonicum but currently isolated from recombinant E.coli source. Source: Recombinant protein corresponding to aa1-218 from Schistosoma Japonicum GST, expressed in E. coli. Accession: AAB59203 Molecular Weight: ~25.4kD (218aa) Specific Activity: >30units/mg Unit Definition: The amount of enzyme that conjugate 1umole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione/minute at pH 6.5 at 25C. Amino Acid Sequence: MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID GDVKLTQSMA IIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALD VVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPK 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.
