Analytical Data
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基因名
R70M
- Application
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别名
R70M;
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种属
E.coli
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q50927
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表达区间
27-198aa
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氨基酸序列
AGVAEFNDKGELLLPKNYREWVMVGTQVTPNELNDGKAPFTEIMTVYVDPESYAHWKKTGEFRDGTVTVKELVSVGDRKGPGSGNGYFMGDYIGLEASVKDSQRFANEPGNWAFYIFYVPDTPLVAAAKNLPTAECAACHKENAKTDMVFTQFYPVLRAAKATGESGVVAPK
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分子量
34.7 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
The R70M recombinant protein has emerged as a significant focus of research due to its potential implications in various biomedical applications, particularly in the fields of enzyme technology and therapeutic development. This protein variant is characterized by a mutation at the 70th residue, where arginine is replaced by methionine (R70M), which may alter its functional properties and stability compared to the wild-type counterpart. Studies have indicated that such modifications can enhance the protein’s catalytic efficiency or alter its interaction with substrates, making it a valuable subject for protein engineering. Furthermore, understanding the structural and functional consequences of the R70M mutation can provide insights into disease mechanisms, particularly in conditions where enzyme dysfunction is implicated. The exploration of R70M also contributes to the broader field of synthetic biology, where engineered proteins can be designed for specific industrial processes or therapeutic applications. Researchers are actively investigating its properties through a combination of experimental and computational approaches, aiming to elucidate the relationship between its structure and function. This research avenue not only enhances our fundamental understanding of protein behavior but also opens up possibilities for innovative solutions to pressing medical and industrial challenges, positioning R70M as a promising candidate for future studies in protein biochemistry and biotechnology.












