Analytical Data
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基因名
RPLP0
- Application
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别名
Rplp0; Arbp; 60S acidic ribosomal protein P0; 60S ribosomal protein L10E
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种属
Mouse
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表达系统
E. coli
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标签
N-10*His;C-Myc;N-SUMO
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P14869
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表达区间
M1-D317
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蛋白长度
Full Length
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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
RPLP0, or Ribosomal Protein Lateral Stalk Subunit P0, is a critical component of the ribosomal stalk structure, which plays a fundamental role in protein synthesis in eukaryotic cells. This protein is part of the large ribosomal subunit and is involved in the interactions between the ribosome and various factors during translation, influencing the overall efficiency and regulation of protein synthesis. Research into RPLP0 has gained importance due to its implications in cell growth and proliferation, as well as its potential involvement in cancer biology. Alterations or mutations in ribosomal proteins, including RPLP0, have been linked to various diseases, particularly malignancies, where disruptions in protein synthesis can lead to uncontrolled cell division. Consequently, the study of RPLP0 as a recombinant protein has emerged as a significant area for understanding its structure-function relationship and regulatory mechanisms in ribosomal activity. Furthermore, recombinant RPLP0 can serve as a valuable tool in structural biology and biochemistry, allowing for detailed studies on ribosomal dynamics and the development of therapeutic strategies targeting ribosome-associated pathways. Insights from RPLP0 research may pave the way for novel approaches in cancer treatment and provide a deeper understanding of the fundamental processes of life at the molecular level.
