Analytical Data
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基因名
rne
- Application
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别名
(RNase E)
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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- His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P21513
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表达区间
35-125aa
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分子量
16.1 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 study of recombinant proteins, particularly those derived from Rne (a key component of RNA processing and degradation), is fundamental to understanding various cellular processes and their implications in health and disease. Over the past few decades, advances in molecular biology techniques have enabled the production of Rne recombinant proteins in various host systems, which are crucial for elucidating their biochemical properties and regulatory mechanisms. Rne plays a critical role in the regulation of RNA stability and turnover, impacting gene expression and cellular responses to environmental signals. Research has shown that disturbances in Rne function can lead to various pathologies, including cancer and neurodegenerative diseases. By utilizing recombinant DNA technology, scientists can produce and purify Rne proteins in sufficient quantities for structural and functional studies. These investigations not only enhance our understanding of Rne's role in RNA metabolism but also pave the way for novel therapeutic strategies targeting RNA-related disorders. Additionally, the ability to engineer Rne proteins with specific modifications opens avenues for developing designer proteins with tailored functions, further expanding the potential applications in biotechnology and medicine. Overall, the exploration of Rne recombinant proteins represents a significant intersection of molecular biology, genetics, and therapeutic innovation, driving forward our knowledge and treatment of RNA-related diseases.












