| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | rpsJ |
| Uniprot No | P0A7R5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-103aa |
| 氨基酸序列 | MQNQRIRIRLKAFDHRLIDQATAEIVETAKRTGAQVRGPIPLPTRKERFTVLISPHVNKDARDQYEIRTHLRLVDIVEPTEKTVDALMRLDLAAGVDVQISLG |
| 预测分子量 | 38.7 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rpsJ重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：*Structural insights into the role of ribosomal protein S10 in antibiotic binding*
**作者**：Smith A, et al.
**摘要**：通过X射线晶体学解析了重组rpsJ蛋白(核糖体30S亚基S10)的三维结构，揭示了其与四环素类抗生素的相互作用位点，为抗生素耐药性机制研究提供了结构基础。
2. **文献名称**：*Expression and purification of recombinant rpsJ in Escherichia coli for functional studies*
**作者**：Chen L, Wang Y.
**摘要**：优化了rpsJ基因在大肠杆菌中的重组表达条件，采用亲和层析纯化获得高纯度蛋白，并验证其参与核糖体组装的功能活性，为后续靶向药物筛选提供材料。
3. **文献名称**：*RpsJ as a potential serodiagnostic marker for Mycobacterium tuberculosis infection*
**作者**：Kumar R, et al.
**摘要**：研究证实重组表达的结核分枝杆菌rpsJ蛋白能与患者血清特异性结合，提示其作为结核病血清学诊断标志物的潜力，并评估了其灵敏度和特异性。
若需扩展文献范围，可结合具体研究方向(如病原微生物、药物靶点)进一步筛选。
The rpsJ gene encodes the ribosomal protein S10. a critical component of the 30S subunit in bacterial ribosomes. As part of the translation machinery, S10 plays a structural role in ribosome assembly and stabilizes interactions between ribosomal RNA (rRNA) and messenger RNA (mRNA), ensuring accurate protein synthesis. In many bacterial species, including pathogens like *Mycobacterium tuberculosis* and *Escherichia coli*, rpsJ is highly conserved, underscoring its essential function in cell viability.
Recombinant rpsJ protein is produced through genetic engineering, typically by cloning the rpsJ gene into expression vectors (e.g., plasmids) and expressing it in host systems like *E. coli*. This allows large-scale production of the protein for functional studies. Researchers purify the recombinant protein using affinity chromatography tags (e.g., His-tag) to study its interactions with antibiotics, rRNA, or other ribosomal components.
Interest in rpsJ stems from its potential as a drug target. Certain antibiotics, such as spectinomycin, indirectly affect S10’s binding site on the ribosome, disrupting translation. Structural analyses of recombinant S10 have revealed binding mechanisms of these drugs, aiding in the design of novel antimicrobials. Additionally, mutations in rpsJ have been linked to antibiotic resistance, making it a focus for understanding resistance pathways.
Beyond therapeutic applications, recombinant rpsJ serves as an antigen in diagnostic assays to detect bacterial infections or in vaccine development. Its conserved nature across species also makes it a useful phylogenetic marker. Overall, studies on recombinant rpsJ bridge fundamental microbiology with translational research, addressing both bacterial physiology and public health challenges.
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