GST protein (His tag) (80R-1204)

Purified recombinant Schistosoma japonicum GST protein

Synonyms Sj26 protein protein, Glutathione S-Transferase class-mu 26 kDa isozyme Glutathione S Transferase., SjGST protein
Species Schistosoma japonicum
Protein Type Recombinant
Applications SDS-PAGE
Assay Information 1. Prepare a 1ml 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 DEG C and monitor at A340nm until the value is constant using a spectrophotometer. 3. Add 50ul of recombinant GST protein with various concentrations (1ug, 2ug, 5ug) in 950ul reaction buffer. 4. Mix by inversion and record the increase at A340nm for 5 minutes.

Images

Coomassie Blue stained SDS-PAGE of GST protein (His tag) (80R-1204)

Figure annotation denotes ug of protein loaded and % gel used.

Specifications

Residues 1-224 amino acids: 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
Expression System E.coli
Grade & Purity > 95% pure
Molecular Weight 28.3 kDa (244aa), confirmed by MALDI-TOF.
Tag/Conjugate His tag
Form & Buffer Supplied as a liquid in PBS, pH 7.4, containing 10% glycerol.
Concentration 1 mg/ml

Usage & Assay Information

Bioactivity Specific activity is 2.8-3.3 units/mg, and is defined as the amount of enzyme that conjugate 1.0 uM of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25 DEG C.

Storage & Safety

Storage Store at 4 deg C for short term storage (1/2 weeks). Aliquot and store at -20 deg C or - 70 deg C for long term storage. Avoid repeated freeze/thaw cycles.

General Information

Biological Significance 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 a 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. Recombinant human GST, fused to His-tag at N-terminus, was expressed in E. coli and purified by using conventional chromatography techniques.

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Images

  • Coomassie Blue stained SDS-PAGE of GST protein (His tag) (80R-1204) | Figure annotation denotes ug of protein loaded and % gel used.

Availability: In stock

Price: £176.28
Size: 100 ug
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