Analytical Data
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Gene name
gshA
- Application
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Alternative Names
gshA；gshA；Glutamate--cysteine ligase EgtA
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Species
E.coli
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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
MIPDVSQALAWLEKHPQALKGIQRGLERETLRVNADGTLATTGHPEALGSALTHKWITTDFAEALLEFITPVDGDIEHMLTFMRDLHRYTARNMGDERMWPLSMPCYIAEGQDIELAQYGTSNTGRFKTLYREGLKNRYGALMQTISGVHYNFSLPMAFWQAKCGDISGADAKEKISAGYFRVIRNYYRFGWVIPYLFGASPAICSSFLQGKPTSLPFEKTECGMYYLPYATSLRLSDLGYTNKSQSNLGITFNDLYEYVAGLKQAIKTPSEEYAKIGIEKDGKRLQINSNVLQIENELYAPIRPKRVTRSGESPSDALLRGGIEYIEVRSLDINPFSPIGVDEQQVRFLDLFMVWCALADAPEMSSSELACTRVNWNRVILEGRKPGLTLGIGCETAQFPLPQVGKDLFRDLKRVAQTLDSINGGEAYQKVCDELVACFDNPDLTFSARILRSMIDTGIGGTGKAFAEAYRNLLREEPLEILREEDFVAEREASERRQQEMEAADTEPFAVWLEKHA
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Molecular Weight
74.3 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
GshA, the gene encoding γ-glutamylcysteine synthetase, plays a crucial role in the biosynthesis of glutathione, an essential tripeptide involved in cellular antioxidant defense, detoxification, and maintenance of redox homeostasis. The study of GshA and its recombinant protein is significant due to the pivotal role of glutathione in various biological processes, including the regulation of apoptosis, immune response, and protection against oxidative stress. Alterations in glutathione levels have been linked to numerous diseases, including cancer, neurodegenerative disorders, and metabolic syndromes. Consequently, understanding the structure and function of GshA can aid in elucidating its biological significance and potential therapeutic applications. Recombinant expression of GshA allows for detailed biochemical characterization, enabling researchers to explore its enzymatic mechanisms, substrate specificity, and interactions with other proteins. The development of GshA-based therapeutic strategies or inhibitors could pave the way for novel treatments aimed at restoring glutathione balance in pathological conditions. Furthermore, the use of recombinant GshA in studies investigating the modulation of oxidative stress can provide insights into cellular responses to environmental stressors, enhancing our understanding of the molecular pathways involved in health and disease. Overall, the research on GshA recombinant protein is not only vital for comprehending fundamental biological processes but also holds substantial promise for developing innovative therapeutic solutions.
