Recombinant Schistosoma japonicum Glutathione S-transferase class-mu 26 kDa isozyme CSB-YP357414SXP
Specifications
| 20ug / 100ug / 500ug price = 100ug |
Alternative Name(s):
Sj26 antigen (SjGST) (GST 26)
Species: (Organism)
Schistosoma japonicum (Blood fluke)
Gene Names:
N/A
Tag info:
N-terminal 6xHis-tagged
Target Protein AA Sequence:
MSPILGYWKIKGLVQPTRLLLEYLEEKYEEHLYERDEGDKWRNKKFELGLEFPNLPYYIDGDVKLTQSMAIIRYIADKHNMLGGCPKERAEISMLEGAVLDIRYGVSRIAYSKDFETLKVDFLSKLPEMLKMFEDRLCHKTYLNGDHVTHPDFMLYDALDVVLYMDPMCLDAFPKLVCFKKRIEAIPQIDKYLKSSKYIAWPLQGWQATFGGGDHPPKSDLEVLFQGPLGSPEFPGRLERPHRD
Expression Region:
2-218aa
Subcellular Location:
Tissue Specificity:
Protein Length:
Full Length of Mature Protein
Pathway:
Mol. Weight:
30.4 kDa
Purity:
Greater than 90% as determined by SDS-PAGE.
Form:
Liquid or Lyophilized powder
Buffer:
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Research Areas:
Others
Function:
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.; FUNCTION
Involvement in disease:
Relevance:
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.
Reconstitution:
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Protein Families:
GST superfamily, Mu family
Reference:
"Insights into dynein motor domain function from a 3.3-A crystal structure." Schmidt H., Gleave E.S., Carter A.P. Nat. Struct. Mol. Biol. 19:492-497(2012)
