Analytical Data
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Gene name
GSTT1
- Application
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Alternative Names
GSTT1;Glutathione S-transferase theta-1
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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
P30711
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Expression Region
2-240aa
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AA Sequence
GLELYLDLLSQPCRAVYIFAKKNDIPFELRIVDLIKGQHLSDAFAQVNPLKKVPALKDGDFTLTESVAILLYLTRKYKVPDYWYPQDLQARARVDEYLAWQHTTLRRSCLRALWHKVMFPVFLGEPVSPQTLAATLAELDVTLQLLEDKFLQNKAFLTGPHISLADLVAITELMHPVGAGCQVFEGRPKLATWRQRVEAAVGEDLFQEAHEVILKAKDFPPADPTIKQKLMPWVLAMIR
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Molecular Weight
34.1 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
Related Products
Protein Description
GSTT1 (Glutathione S-transferase T1) is a member of the GST superfamily of enzymes, which play a crucial role in the detoxification of electrophilic compounds by catalyzing the conjugation of glutathione to these substrates. The GSTT1 gene is notable for its polymorphism, with a significant percentage of the population exhibiting a deletion variant that results in the complete loss of enzyme activity. This deletion has been associated with increased susceptibility to various diseases, including cancers and cardiovascular diseases, as well as altered responses to certain drugs and environmental toxins. Research into GSTT1 recombinant proteins has sought to elucidate the functional roles of the enzyme in metabolic pathways and its implications for individual variations in detoxification processes. By studying GSTT1 through recombinant expression, researchers can investigate the enzyme's kinetics, substrate specificity, and interactions with other biomolecules, providing insights into how GSTT1 contributes to cellular defense mechanisms against oxidative stress and xenobiotic exposure. Additionally, understanding the mechanisms underlying GSTT1 gene polymorphisms may lead to the development of personalized medicine approaches, enabling more effective disease prevention and treatment strategies based on an individual's genetic makeup. Consequently, the study of GSTT1 recombinant proteins is not only vital for basic biochemical research but also for its potential applications in toxicology, pharmacogenomics, and therapeutic interventions.
