Analytical Data
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基因名
rpmE
- Application
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别名
rpmE; b3936; JW3907; 50S ribosomal protein L31; Large ribosomal subunit protein bL31-A
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种属
Escherichia coli
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表达系统
E. coli
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标签
N- GST
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P0A7M9
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表达区间
1-70aa
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分子量
34.9 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
Recombinant protein technology has revolutionized the field of molecular biology and biotechnology, allowing for the production of proteins that are otherwise difficult to obtain from natural sources. RPME (Recombinant Protein from E. coli) is a significant focus of research due to its potential applications in various domains, including therapeutics, diagnostics, and industrial processes. The rise of RPME is rooted in its advantages over traditional methods, such as higher yield, lower production costs, and the ability to perform post-translational modifications. As recombinant proteins can be engineered for specific functions, studies on RPME aim to optimize expression systems, purification methods, and functional characterization. Research has shown that RPME can be utilized in vaccine development, enzyme production, and as a research tool in understanding protein interactions and functions. The ability to express complex eukaryotic proteins in prokaryotic systems, such as E. coli, further enhances RPME's versatility. Consequently, ongoing studies continue to explore the molecular mechanisms underlying RPME expression and stability, with the ultimate goal of harnessing its full potential for innovative applications in medicine and industry.
