Analytical Data
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Gene name
WARS1
- Application
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Alternative Names
WARS1；IFI53；WARS；WRS；Tryptophan--tRNA ligase. cytoplasmic
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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
P23381
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Expression Region
2-471aa
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AA Sequence
PNSEPASLLELFNSIATQGELVRSLKAGNASKDEIDSAVKMLVSLKMSYKAAAGEDYKADCPPGNPAPTSNHGPDATEAEEDFVDPWTVQTSSAKGIDYDKLIVRFGSSKIDKELINRIERATGQRPHHFLRRGIFFSHRDMNQVLDAYENKKPFYLYTGRGPSSEAMHVGHLIPFIFTKWLQDVFNVPLVIQMTDDEKYLWKDLTLDQAYSYAVENAKDIIACGFDINKTFIFSDLDYMGMSSGFYKNVVKIQKHVTFNQVKGIFGFTDSDCIGKISFPAIQAAPSFSNSFPQIFRDRTDIQCLIPCAIDQDPYFRMTRDVAPRIGYPKPALLHSTFFPALQGAQTKMSASDPNSSIFLTDTAKQIKTKVNKHAFSGGRDTIEEHRQFGGNCDVDVSFMYLTFFLEDDDKLEQIRKDYTSGAMLTGELKKALIEVLQPLIAEHQARRKEVTDEIVKEFMTPRKLSFDFQ
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Molecular Weight
56.7 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
WARS1, or Tryptophanyl-tRNA synthetase 1, is an enzyme that plays a crucial role in the translation process by catalyzing the attachment of the amino acid tryptophan to its corresponding tRNA molecule. This process is essential for protein synthesis in all living organisms. Recent studies have highlighted the importance of WARS1 beyond its biochemical function, suggesting its involvement in various cellular processes and signaling pathways. Abnormal expression or mutations in the WARS1 gene have been implicated in several diseases, including neurodegenerative disorders and certain types of cancer. Researchers are increasingly focused on the recombinant expression of WARS1 to better understand its structure, function, and potential as a therapeutic target. By creating recombinant proteins, scientists aim to elucidate the intricate mechanisms by which WARS1 operates, investigate its interactions with other cellular components, and evaluate its role in disease pathology. This research is vital not only for the fundamental understanding of protein synthesis but also for the development of novel therapeutic strategies targeting WARS1-related diseases. The ongoing investigations into WARS1 recombinant proteins promise to yield valuable insights into both its biological significance and its potential applications in medicinal chemistry and protein engineering.
