Analytical Data
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基因名
Alanyl-tRNA synthetase
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简介
The Alanyl-tRNA synthetase protein facilitates a two-step process, activating alanine with ATP to form Ala-AMP and transferring it to the acceptor end of tRNA(Ala). Additionally, it corrects incorrectly charged tRNA(Ala) through its editing domain. Alanyl-tRNA synthetase Protein, Human (sf9, His) is the recombinant human-derived Alanyl-tRNA synthetase protein, expressed by Sf9 insect cells , with N-His labeled tag.
- Application
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别名
Alanine--tRNA ligase, cytoplasmic; AlaRS; AARS1; AARS
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种属
Human
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表达系统
Baculovirus
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标签
N-10*His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P49588
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表达区间
M1-N968
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蛋白长度
Full Length
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分子量
109.2 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
Alanyl-tRNA synthetase (AlaRS) is a crucial enzyme in the process of protein biosynthesis, responsible for the aminoacylation of tRNA with the amino acid alanine. The accurate functioning of AlaRS is essential for the fidelity of protein translation, as it ensures that the correct amino acid is incorporated into the growing polypeptide chain. Given its vital role in cellular metabolism and protein synthesis, AlaRS has garnered significant attention in research, particularly in the context of antibiotic resistance and the development of novel therapeutic agents. Recombinant expression of AlaRS allows for detailed biochemical studies and structural analyses, facilitating an understanding of its catalytic mechanisms and substrate specificity. By engineering AlaRS from various organisms, scientists aim to elucidate the evolutionary adaptations of this enzyme and its interaction with tRNA and other translation components. Furthermore, the study of AlaRS can provide insights into the development of innovative biotechnological applications, such as in the production of synthetic peptides and proteins with non-canonical amino acids. Overall, the research on recombinant AlaRS not only enhances our comprehension of fundamental biological processes but also holds promising implications for medical and industrial fields.
