Analytical Data
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Gene name
YARS
- Application
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Alternative Names
CMTDIC; TYRRS; YRS; YTS; Tyrosine tRNA Ligase 1,Cytoplasmic
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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 90% as determined by SDS-PAGE.
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Uniprot
P54577
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Expression Region
Gly2~Ser528
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Molecular Weight
63kDa
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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
YARS (tyrosyl-tRNA synthetase) is an essential enzyme involved in protein synthesis, specifically in the attachment of the amino acid tyrosine to its corresponding transfer RNA (tRNA). The study of YARS and its recombinant forms has gained significant attention due to its pivotal role in various biological processes and its implications in disease states. Recent research suggests that YARS is not only crucial for accurate protein synthesis but also plays a role in cell signaling, inflammation, and stress responses. Abnormal YARS expression has been implicated in several diseases, including cancer and autoimmune disorders, making it a potential therapeutic target. The recombinant production of YARS allows for the detailed analysis of its structural and functional characteristics, enabling insights into its enzymatic mechanisms and interactions with other cellular components. Moreover, understanding the post-translational modifications and regulatory mechanisms governing YARS activity may reveal new avenues for drug development. Overall, the exploration of YARS recombinant proteins serves as a promising field that bridges fundamental biochemistry and clinical research, ultimately contributing to our understanding of protein synthesis and its broader implications in health and disease.
