Analytical Data
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Gene name
GSTp
- Application
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Alternative Names
GSTp；FAEES3；GST3；Glutathione S-transferase P
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Species
Human
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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
P09211
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Expression Region
2-210aa
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AA Sequence
PPYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQEGSLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGLYGKDQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYVKALPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLLIHEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYVNLPINGNGKQ
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Molecular Weight
25.2 kDa
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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
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Protein Description
GSTp (glutathione S-transferase pi) is a member of the glutathione S-transferase (GST) family, known for its role in detoxification processes by conjugating harmful substances with glutathione. Its overexpression in various malignancies has drawn significant attention to its potential as a biomarker for cancer diagnosis and prognosis. Research has highlighted that GSTp is involved in the metabolic processing of xenobiotics and plays a crucial role in cellular defense against oxidative stress and electrophilic damage. Due to its stability and solubility, GSTp has been widely utilized as a fusion partner in recombinant protein production, aiding in the purification and characterization of target proteins. The use of GSTp as a tag allows for the straightforward isolation of proteins expressed in various systems, including bacteria and eukaryotic cells. This versatility has enabled scientists to study numerous cellular processes and protein interactions more effectively. Moreover, investigations into the structure and function of GSTp have revealed insights into its enzymatic mechanisms and interactions with small molecules, underscoring its importance in pharmacology and toxicology. Consequently, ongoing research focuses on understanding the regulatory mechanisms governing GSTp expression and activity, as well as exploring its potential as a target for therapeutic interventions in cancer and other diseases associated with oxidative stress. Overall, the study of GSTp recombinant proteins offers valuable opportunities for advancing both basic research and clinical applications, positioning GSTp as a key player in the interface of biochemistry and medicine.
