Analytical Data
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Gene name
WARS
- Application
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Alternative Names
WARS；IFI53；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
60.0 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
WARS, or tryptophanyl-tRNA synthetase, is a crucial enzyme that catalyzes the attachment of the amino acid tryptophan to its corresponding tRNA, a key step in protein synthesis. Understanding the structure and function of WARS is essential for comprehending the broader complexities of translation and cellular metabolism. Recent research has highlighted the role of WARS not only in protein synthesis but also in cellular signaling and responses to stress. Dysregulation of WARS has been implicated in various diseases, including cancers and neurodegenerative disorders, which has spurred interest in its potential as a therapeutic target. The development of recombinant WARS proteins allows for detailed biochemical and structural studies, enabling researchers to explore its interactions and regulatory mechanisms at a molecular level. Advances in techniques such as X-ray crystallography and cryo-electron microscopy have provided unprecedented insights into the three-dimensional structure of WARS, revealing functional domains and active sites that inform our understanding of its enzymatic activity. Furthermore, the study of WARS in different organisms helps illuminate evolutionary adaptations in protein synthesis machinery. Overall, the research on WARS and its recombinant forms not only enhances our understanding of fundamental biological processes but also opens new avenues for the development of novel therapeutic strategies aimed at mitigating diseases associated with its malfunction.
