Analytical Data
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Gene name
GSH
- Application
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Alternative Names
GSH；Glutathione synthetase
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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
P0A6W9
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Expression Region
1-518aa
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AA Sequence
MIPDVSQALAWLEKHPQALKGIQRGLERETLRVNADGTLATTGHPEALGS ALTHKWITTDFAEALLEFITPVDGDIEHMLTFMRDLHRYTARNMGDERMW PLSMPCYIAEGQDIELAQYGTSNTGRFKTLYREGLKNRYGALMQTISGVH YNFSLPMAFWQAKCGDISGADAKEKISAGYFRVIRNYYRFGWVIPYLFGA SPAICSSFLQGKPTSLPFEKTECGMYYLPYATSLRLSDLGYTNKSQSNLG ITFNDLYEYVAGLKQAIKTPSEEYAKIGIEKDGKRLQINSNVLQIENELY APIRPKRVTRSGESPSDALLRGGIEYIEVRSLDINPFSPIGVDEQQVRFL DLFMVWCALADAPEMSSSELACTRVNWNRVILEGRKPGLTLGIGCETAQF PLPQVGKDLFRDLKRVAQTLDSINGGEAYQKVCDELVACFDNPDLTFSAR ILRSMIDTGIGGTGKAFAEAYRNLLREEPLEILREEDFVAEREASERRQQ EMEAADTEPFAVWLEKHA
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Molecular Weight
74 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
Glutathione S-transferase (GST) is a significant family of enzymes involved in detoxification processes, playing a crucial role in cellular defense against oxidative stress and xenobiotic compounds. Recombinant GST proteins have gained increasing attention in biochemical and pharmaceutical research due to their versatile applications. The study of recombinant GSTs not only aids in understanding the mechanisms of drug metabolism and resistance but also facilitates the development of targeted therapies and diagnostic tools. Overexpression of GST genes in various expression systems allows for the production of large quantities of pure proteins, which can be utilized in enzymatic assays, structural studies, and as fusion tags for protein purification. The ability to manipulate GST through genetic engineering has led to the identification of novel enzyme variants with enhanced properties, expanding their applicability in biocatalysis and biotechnology. Furthermore, the exploration of GST structure-function relationships has elucidated critical insights into enzyme activity, thus paving the way for innovative strategies in drug design and therapeutic development. As research progresses, the comprehensive investigation of recombinant GST proteins continues to uncover their pivotal roles in biochemistry and medicine, highlighting their importance as tools not only for scientific advancement but also for clinical applications.
