Analytical Data
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Gene name
GRS
- Application
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Alternative Names
BCL2A1;BCL2L5;BFL1;GRS;Bcl-2-related Protein A1
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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
Q16548
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Expression Region
1-152aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMTDCEF GYIYRLAQDY LQYVLQIPQP GSGPSKTSRV LQKVAFSVQK EVEKNLKSCL DNVNVVSVDT ARTLFNQVME KEFEDDIINW GRIVTIFAFE GILIKKLLRQ QIAPDVDTYK EISYFVAEFI MNNTGEWIRQ NGGWENGFVK KFEPKS
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Molecular Weight
20 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
The study of GRS (Glutathione Reductase-like Protein) recombinant protein has gained attention due to its potential roles in various biological processes, particularly in redox biology and oxidative stress response. GRS is involved in maintaining the cellular redox state by catalyzing the reduction of glutathione disulfide to glutathione, thus playing a critical role in protecting cells from oxidative damage. Research into its recombinant form allows for detailed investigations into its enzymatic activity, structure-function relationships, and interactions with other cellular components. Moreover, understanding the GRS protein's mechanisms can provide insights into its involvement in diseases linked to oxidative stress, such as cancer, neurodegenerative disorders, and aging. The production of GRS as a recombinant protein in host systems like bacteria or yeast facilitates large-scale purification and functional characterization, which is essential for elucidating its biochemical properties and therapeutic potential. Additionally, the exploration of GRS variants offers opportunities for engineering proteins with enhanced functions or novel properties, paving the way for advancements in biomedicine and biotechnology. Overall, the research surrounding GRS recombinant protein is crucial for developing strategies to mitigate oxidative stress-related pathologies and for enhancing our understanding of fundamental metabolic processes.
