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

SKU AR09284PU-N

GST-Tag (1-224, His-tag) schistosoma recombinant protein, 0.1 mg

Product Data

• Species: Schistosoma
• Expression Host: E. coli
• Expression cDNA Clone or AA Sequence:
  Protein Sequence

  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
• Presentation State: Purified
• Buffer: Presentation State: Purified; State: Liquid purified protein; Buffer System: PBS, pH 7.4, 10% glycerol
• 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)
• 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.
• Shipping: Blue Ice

Reference Data

• Synonyms: Glutathione S-transferase Tag, GST26-Tag
• 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.