纯度 | >95%SDS-PAGE. |
种属 | Human |
靶点 | RPL12 |
Uniprot No | P30050 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-165aa |
氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMPPKFDP NEIKVVYLRC TGGEVGATSA LAPKIGPLGL SPKKVGDDIA KATGDWKGLR ITVKLTIQNR QAQIEVVPSA SALIIKALKE PPRDRKKQKN IKHSGNITFD EIVNIARQMR HRSLARELSG TIKEILGTAQ SVGCNVDGRH PHDIIDDINS GAVECPAS |
预测分子量 | 20 kDa |
蛋白标签 | His tag N-Terminus |
缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于RPL12重组蛋白的3篇代表性文献示例(内容为模拟虚构,仅供参考):
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1. **文献名称**:*Expression and Purification of Recombinant Human RPL12 in Escherichia coli*
**作者**:Chen L. et al.
**摘要**:本研究成功构建了人源RPL12基因的原核表达系统,通过优化诱导条件和纯化步骤,获得高纯度重组蛋白,并验证其与核糖体亚基的体外结合活性。
2. **文献名称**:*Structural Insights into RPL12’s Role in Ribosome Biogenesis*
**作者**:Wang Y. et al.
**摘要**:利用X射线晶体学解析了重组RPL12蛋白的三维结构,揭示了其C端结构域在核糖体组装中的关键作用,并发现其突变导致翻译效率下降。
3. **文献名称**:*RPL12 Overexpression Promotes Tumor Progression via p53 Pathway*
**作者**:Kim S. et al.
**摘要**:通过体外重组RPL12蛋白递送至癌细胞,证明其过表达通过调控p53信号通路促进肿瘤细胞增殖,提示RPL12可能成为癌症治疗的潜在靶点。
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注:以上文献信息为示例性模拟,实际研究需通过学术数据库(如PubMed、Web of Science)检索验证。
**Background of Recombinant RPL12 Protein**
RPL12 (ribosomal protein L12) is a component of the 60S subunit of eukaryotic ribosomes, playing critical roles in translation and ribosome biogenesis. As part of the ribosomal stalk, RPL12 facilitates interactions between elongation factors and the ribosome during protein synthesis. Its dynamic structure allows it to act as a molecular switch, coordinating GTP hydrolysis and ensuring translational fidelity. Beyond its canonical role, RPL12 has been implicated in extra-ribosomal functions, including cell cycle regulation, apoptosis, and DNA repair, highlighting its multifaceted importance in cellular homeostasis.
Recombinant RPL12 protein is engineered through molecular cloning, typically expressed in *E. coli* or mammalian systems to ensure proper folding and post-translational modifications. This engineered form retains the functional properties of native RPL12. enabling researchers to study its interactions, structural dynamics, and regulatory mechanisms *in vitro*. The recombinant protein often includes tags (e.g., His-tag) for simplified purification and detection.
Interest in RPL12 has grown due to its dysregulation in diseases. Overexpression of RPL12 is observed in certain cancers, where it may promote tumor progression by enhancing translation efficiency or suppressing apoptosis. Conversely, mutations in RPL12 are linked to ribosomopathies, disorders stemming from impaired ribosome function. Recombinant RPL12 serves as a tool for investigating these pathologies, screening therapeutic agents, and elucidating ribosome-associated pathways.
Additionally, studies leveraging recombinant RPL12 contribute to understanding antibiotic resistance mechanisms, as bacterial homologs of ribosomal proteins are common drug targets. By dissecting RPL12's role in ribosome assembly and function, researchers aim to uncover novel strategies for treating diseases tied to translational dysregulation.
In summary, recombinant RPL12 is a vital resource for probing ribosome biology, disease mechanisms, and therapeutic development.
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