GST-Tag (1-224, His-tag) Schistosoma Protein

Specifications

Product Data
Species	Schistosoma
Expression Host	E. coli
Expression cDNA Clone or AA Sequence	Protein Sequence (showhide) MGSSHHHHHH SSGLVPRGSH MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID GDVKLTQSMA IIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALD VVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPKSD LVPR
Tag	His-tag
Predicted MW	28.3 kDa
Concentration	lot specific
Purity	>90% by SDS - PAGE
Buffer	Presentation State: Purified State: Liquid purified protein Buffer System: PBS, pH 7.4, 10% glycerol
Preparation	Liquid purified protein
Protein Description	Recombinant GST, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.
Storage	Store undiluted at 2-8°C for up to two weeks or (in aliquots) at -20°C or -80°C for longer. Avoid repeated freezing and thawing.
Stability	Shelf life: one year from despatch.
Bioactivity	Biological: 2.8-3.3 units/mg, defined as the amount of enzyme that conjugate 1.0 umole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25°C. Activity Assay 1. Prepare a 1 ml reaction mix into a suitable container: The final concentrations are 97 mM potassium phosphate, 0.97 mM EDTA, 2.5 mM glutathione, reduced, 1.0 mM 1-chloro-2,4-dinitrobenzene (CDNB), 3.2% (v/v) ethanol. 2. Equilibrate to 25°C and monitor at A340nm until the value is constant using a spectrophotometer. 3. Add 50 ul of recombinant GST protein with various concentrations (1ug, 2ug, 5ug) in 950 ul reaction buffer. 4. Mix by inversion and record the increase at A340nm for 5 minutes.
Endotoxin	< 1 EU per 1ug of protein (determined by LAL method)
Reference Data
Summary	Glutathione S-transferase (GST) represents a major group of detoxification enzymes. This enzyme 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. Glutathione S-transferase was originally separated from Schistosoma japonicum but currently isolated from recombinant E.coli source.

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