Analytical Data
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基因名
TEV Protease
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简介
The TEV protease is critical in aphid transmission and has proteolytic activity that cleaves the Gly-Gly dipeptide at its C terminus. In addition to proteolysis, it interacts with virions and aphid stylets, which is critical for aphid transmission. TEV Protease Protein, Tobacco etch virus (S2256N, C-His) is the recombinant Virus-derived TEV Protease protein, expressed by E. coli , with C-6*His labeled tag.
- Application
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别名
Genome polyprotein; Tobacco Etch Virus Protease
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种属
Virus
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表达系统
E. coli
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标签
C-6*His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
NP_062908.1
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表达区间
E2039-Q2279, S2256N
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氨基酸序列
ESLFKGPRDYNPISSTICHLTNESDGHTTSLYGIGFGPFIITNKHLFRRNNGTLLVQSLHGVFKVKNTTTLQQHLIDGRDMIIIRMPKDFPPFPQKLKFREPQREERICLVTTNFQTKSMSSMVSDTSCTFPSSDGIFWKHWIQTKDGQCGSPLVSTRDGFIVGIHSASNFTNTNNYFTSVPKNFMELLTNQEAQQWVSGWRLNADSVLWGGHKVFMNKPEEPFQPVKEATQLMNELVYSQ
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蛋白长度
Partial
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分子量
26 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
TEV protease, derived from the Tobacco Etch Virus, has emerged as a crucial tool in molecular biology and protein engineering due to its high specificity and efficiency in cleaving fusion tags from recombinant proteins. Researchers have focused on characterizing TEV protease because of its unique cleavage site, which allows for precise removal of tags without disrupting the native structure of the target protein. This feature is particularly valuable in the production of therapeutic proteins and structural biology studies, where the integrity and functionality of the protein are paramount. Additionally, TEV protease operates optimally in a variety of conditions, making it versatile for different experimental setups. The development of recombinant TEV protease has enabled large-scale applications, enhancing purification protocols and streamlining biochemical assays. Studies on the enzyme's kinetics, specificity, and stability in different environments have provided deeper insights into its mechanism of action, allowing scientists to optimize its use in various applications, including protein crystallization and functional assays. As a result, TEV protease plays an indispensable role in advancing our understanding of protein interactions and functions, paving the way for innovations in biopharmaceuticals and biotechnology.
