Analytical Data
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Gene name
GST11
- Application
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Alternative Names
GST11；GST11；GSTF8;Glutathione S-transferase F7
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Species
Arabidopsis thaliana
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9SRY5
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Expression Region
1-209aa
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AA Sequence
MAGIKVFGHP ASTATRRVLI ALHEKNLDFE FVHIELKDGE HKKEPFIFRN PFGKVPAFED GDFKLFESRA ITQYIAHFYS DKGNQLVSLG SKDIAGIAMG IEIESHEFDP VGSKLVWEQV LKPLYGMTTD KTVVEEEEAK LAKVLDVYEH RLGESKYLAS DKFTLVDLHT IPVIQYLLGT PTKKLFDERP HVSAWVADIT SRPSAKKVL
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
GST11 recombinant protein, derived from the glutathione S-transferase family, has garnered significant interest in biomedical research due to its versatile applications in protein purification, enzyme activity studies, and the development of diagnostic tools. Glutathione S-transferases (GSTs) play crucial roles in cellular detoxification processes, catalyzing the conjugation of glutathione to various substrates, which is essential for the metabolism of xenobiotics and protection against oxidative stress. The GST11 isoform, in particular, has been studied for its distinct enzymatic properties and potential role in various pathological conditions, including cancer and inflammatory diseases. The ability to produce GST11 as a recombinant protein allows researchers to investigate its biochemical properties, interactions with other proteins, and implications in disease pathways in a controlled manner. Moreover, functionalized GST11 can serve as a valuable tool for affinity purification, facilitating the isolation of target proteins from complex biological mixtures. Understanding the structure-function relationship of GST11 through recombinant technology may also unveil novel therapeutic targets and biomarkers for disease diagnosis and prognosis, thus contributing to the advancement of personalized medicine.
