Analytical Data
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Gene name
WARS
- Application
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Alternative Names
GAMMA-2; IFI53; IFP53; WRS; TrpRS; hWRS; Tryptophan tRNA Ligase 1,Cytoplasmic; Interferon-induced protein 53; Tryptophanyl-tRNA synthetase
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Species
Human
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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
P23381
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Expression Region
Phe247~Lys458
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Molecular Weight
30kDa
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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
WARS (tryptophan-tRNA synthetase) is an essential enzyme that catalyzes the attachment of the amino acid tryptophan to its corresponding tRNA, a crucial step in protein synthesis. Its role in the translation process makes it a vital component in cellular biology. Beyond its fundamental enzymatic function, WARS has garnered attention for its involvement in various cellular processes, including cellular stress responses and immune regulation. Recent studies have shown that WARS can exhibit non-classical functions, such as contributing to the regulation of inflammatory responses, particularly in autoimmune and neurodegenerative disorders. The research on WARS and its recombinant protein forms has gained momentum due to the therapeutic potential they present. Recombinant WARS proteins can be explored for their regulatory roles, mechanisms of action, and potential as biomarkers or therapeutic targets. Furthermore, the ability to produce WARS in a recombinant form facilitates in-depth biochemical characterization and functional assays, allowing researchers to elucidate its diverse roles in health and disease. Overall, understanding the intricate functions of WARS through recombinant technology holds promise for developing novel therapeutic strategies and enhancing our comprehension of cellular mechanisms.
