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Recombinant Schistosoma Japonicum Glutathione S-transferase Class-mu 26 kDa Isoz

Recombinant Schistosoma Japonicum Glutathione S-transferase Class-mu 26 kDa Isoz Recombinant Schistosoma Japonicum Glutathione S-transferase Class-mu 26 kDa Isoz

Instruction Manual!

Product name: Recombinant Schistosoma Japonicum Glutathione S-transferase Class-mu 26 kDa Isoz
Source:E.coli
Purity:Greater than 95% as determined by reducing SDS-PAGE.
Buffer Formulation:Lyophilized from a 0.2 μm filtered solution of PBS, pH7.4.
Applications:Applications:SDS-PAGE; WB; ELISA; IP.
Storage:Avoid repeated freeze/thaw cycles. Store at 2-8 oC for one month. Aliquot and store at -80 oC for 12 months.
UOM:100ug/50ug/200ug/1mg/1g
Source E.coli
Description Recombinant Schistosoma Japonicum Glutathione S-transferase Class-mu 26 kDa Isozyme is produced by our E.coli expression system and the target gene encoding Met1-Lys218 is expressed.
Names Glutathione S-transferase class-mu 26 kDa isozyme; GST 26; Sj26 antigen; SjGST
Accession # P08515
Formulation Lyophilized from a 0.2 μm filtered solution of PBS, pH7.4.
Shipping The product is shipped at ambient temperature.
Reconstitution Always centrifuge tubes before opening. Do not mix by vortex or pipetting.
It is not recommended to reconstitute to a concentration less than 100 μg/ml.
Dissolve the lyophilized protein in ddH2O.
Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage Lyophilized protein should be stored at < -20°C, though stable at room temperature for 3 weeks.
Reconstituted protein solution can be stored at 4-7°C for 2-7 days.
Aliquots of reconstituted samples are stable at < -20°C for 3 months.
Purity Greater than 95% as determined by reducing SDS-PAGE.
Endotoxin Less than 0.1 ng/µg (1 IEU/µg) as determined by LAL test.
Amino Acid Sequence
MSPILGYWKIKGLVQPTRLLLEYLEEKYEEHLYERDEGDKWRNKKFELGLEFPNLPYYIDGDVKL TQSMAIIRYIADKHNMLGGCPKERAEISMLEGAVLDIRYGVSRIAYSKDFETLKVDFLSKLPEML KMFEDRLCHKTYLNGDHVTHPDFMLYDALDVVLYMDPMCLDAFPKLVCFKKRIEAIPQIDKYLKS SKYIAWPLQGWQATFGGGDHPPKSD
Background Glutathione S-transferases (GSTs), previously known as ligandins, comprise a family of eukaryotic and prokaryotic phase II metabolic isozymes best known for their ability to catalyze the conjugation of the reduced form of glutathione (GSH) to xenobiotic substrates for the purpose of detoxification. The GST family consists of three superfamilies: the cytosolic, mitochondrial, and microsomal (MAPEG) proteins. 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. The activity of GSTs is dependent upon a steady supply of GSH from the synthetic enzymes gamma-glutamylcysteine synthetase and glutathione synthetase, as well as the action of specific transporters to remove conjugates of GSH from the cell. The primary role of GSTs is to detoxify xenobiotics by catalyzing the nucleophilic attack by GSH on electrophilic carbon, sulfur, or nitrogen atoms of said nonpolar xenobiotic substrates, thereby preventing their interaction with crucial cellular proteins and nucleic acids.

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