Analytical Data
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Gene name
GSTK1
- Application
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Alternative Names
GST-K1; GST13; HDCMD47P; Glutathione S-transferase subunit 13
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Species
Mouse
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q9DCM2
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Expression Region
Ser19~Ala222
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Molecular Weight
27kDa
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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
GSTK1, or Glutathione S-Transferase Kappa 1, is a member of the glutathione transferase family, which plays a crucial role in detoxification processes within cells. This enzyme is responsible for catalyzing the conjugation of glutathione to a variety of electrophilic compounds, thereby facilitating their excretion and reducing cellular toxicity. Research has shown that GSTK1 is involved in the metabolism of several endogenous and exogenous substrates, including drugs and environmental pollutants. Its expression is linked to various physiological and pathological conditions, including cancer and oxidative stress-related diseases. Given the importance of GSTK1 in detoxification pathways, there is growing interest in understanding its structure, function, and potential as a therapeutic target. The recombinant production of GSTK1 allows for in-depth biochemical studies, including enzyme kinetics, substrate specificity, and the investigation of its interaction with potential inhibitors. These studies contribute to a more comprehensive understanding of its role in cellular defense mechanisms. Moreover, this research has implications for drug development and personalized medicine, particularly in optimizing therapeutic strategies for conditions influenced by GSTK1 activity. Exploring the recombinant protein not only enhances our knowledge of its biological functions but also paves the way for novel applications in biomedicine and biotechnology.
