Analytical Data
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基因名
Iars1
- Application
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别名
(Isoleucyl-tRNA synthetase)(IRS)(IleRS)
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种属
Mouse
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表达系统
E. coli
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标签
N- His & C- Myc
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q8BU30
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表达区间
732-831aa
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分子量
16.8 kDa
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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
Iars1, or isoleucyl-tRNA synthetase 1, is a vital enzyme that catalyzes the attachment of isoleucine to its corresponding tRNA, a critical step in protein synthesis. The study of Iars1 is significant due to its essential role in cellular metabolism and the potential implications in various diseases, including genetic disorders and cancers. Mutations in the IARS1 gene can lead to severe neurological conditions, emphasizing the need for a thorough understanding of its structure and function. Recent advancements in recombinant protein technology have enabled researchers to produce Iars1 in a laboratory setting, facilitating in-depth biochemical studies. This recombinant Iars1 can be used to elucidate its enzymatic activity, assess its interaction with tRNA and other molecular partners, and explore the effects of specific mutations. Furthermore, understanding Iars1's structure can provide insights into the mechanisms of tRNA charging and aid in the design of potential therapeutic strategies for diseases associated with its dysfunction. The exploration of Iars1 through recombinant protein techniques thus holds promise for advancing our knowledge in molecular biology and developing innovative treatments for related disorders.
