Lyophilized from sterile PBS, pH 7.5, 5 % trehalose and 5 % mannitol.
Molecular Mass
Recombinant Glutathione S-transferase (GST) consists of 218 amino acids and predicts a molecular mass of 25.5 KDa. It migRates as an approximately 29 KDa band in SDS-PAGE under reducing conditions.
Endotoxin
< 1.0 EU per 1 microgram of protein (determined by LAL method).
Purity
> 95 % by SDS-PAGE.
BACKGROUND
Background
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut.
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