Analytical Data
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基因名
YARS
- Application
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别名
CMTDIC; TYRRS; YRS; YTS; Tyrosine tRNA Ligase 1,Cytoplasmic
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种属
Human
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表达系统
E. coli
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标签
N-His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P54577
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表达区间
Gly2~Ser528
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分子量
63kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
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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.
