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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.
Storage
In lyophilized state for 1 year (4°C); After reconstitution under sterile conditions for 3 months (-70°C). Avoid repeated freeze/thaw cycles.
Reconstitution
Reconstitute in sterile distilled water to a concentration of 0.1-1.0 mg/mL.
Warning
For research use only!
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.
Species
Schistosoma japonicum
Source
E. coli
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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