Analytical Data
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基因名
RPLP0
- Application
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别名
RPLP0；Large ribosomal subunit Protein uL10
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种属
Human
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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
P05388
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表达区间
2-317aa
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氨基酸序列
MASMTGGQQMGRGHHHHHHENLYFQGGEFPREDRATWKSNYFLKIIQLLD DYPKCFIVGADNVGSKQMQQIRMSLRGKAVVLMGKNTMMRKAIRGHLENN PALEKLLPHIRGNVGFVFTKEDLTEIRDMLLANKVPAAARAGAIAPCEVT VPAQNTGLGPEKTSFFQALGITTKISRGTIEILSDVQLIKTGDKVGASEA TLLNMLNISPFSFGLVIQQVFDNGSIYNPEVLDITEETLHSRFLEGVRNV ASVCLQIGYPTVASVPHSIINGYKRVLALSVETDYTFPLAEKVKAFLADP SAFVAAAPVAAATTAAPAAAAAPAKVEAKEESEESDEDMGFGLFD
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分子量
37 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
RPLP0, also known as ribosomal protein LPO or ribosomal protein P0, is a critical component of the ribosomal structure, playing an essential role in the assembly and function of the ribosome, the cellular machinery for protein synthesis. Research into RPLP0 has gained significance due to its involvement in various cellular processes and its implications in disease states, especially cancer. Alterations in ribosomal proteins, including RPLP0, can disrupt normal ribosome function, leading to aberrations in protein synthesis that are often associated with tumorigenesis. Additionally, RPLP0 is a member of a highly conserved family of proteins, underscoring its fundamental role in cellular biology across species. Investigations into RPLP0 reorganization and its interactions with other ribosomal proteins and translation factors can provide deeper insights into ribosome biogenesis and the regulatory mechanisms governing protein synthesis. Furthermore, understanding the molecular dynamics of RPLP0 may open new avenues for therapeutic interventions, particularly in targeting cancers that exhibit dysregulated ribosomal biogenesis. As ribosomal proteins often undergo complex post-translational modifications, characterizing these modifications in RPLP0 can elucidate their functional impacts on ribosome activity and cellular homeostasis. Thus, the study of RPLP0 not only enhances our understanding of fundamental biological processes but also holds promise for developing novel strategies in cancer treatment and other diseases linked to ribosomal dysfunction.
