Analytical Data
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基因名
Ribonuclease
- Application
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别名
/
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种属
Bacillus amyloliquefaciens
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表达系统
E. coli
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标签
C- His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P00648
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表达区间
48-157aa
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分子量
13.3 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
Ribonuclease (RNase) is an enzyme that plays a crucial role in RNA metabolism by catalyzing the degradation of RNA molecules. The study of recombinant RNase proteins has gained significant attention due to their potential applications in various fields, including molecular biology, biomedicine, and biotechnology. Recombinant DNA technology allows for the expression of RNase proteins in host systems, such as bacteria, yeast, or mammalian cells, enabling researchers to produce large quantities of the enzyme for detailed studies. Understanding the structure-function relationship of RNase is vital, as it can provide insights into its catalytic mechanisms and specificity towards different RNA substrates. Additionally, recombinant RNases have been explored for their therapeutic potential, particularly in the treatment of RNA virus infections and in cancer therapies, where they can selectively degrade the RNA of cancer cells. The ability to engineer RNases through mutations or modifications further enhances their efficacy and specificity, opening new avenues for drug development. Overall, the research on recombinant RNase proteins not only advances our understanding of fundamental biological processes but also paves the way for innovative applications in medicine and biotechnology.
