| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SSRa |
| Uniprot No | P43307 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-286aa |
| 氨基酸序列 | MRLLPRLLLLLLLVFPATVLFRGGPRGLLAVAQDLTEDEETVEDSIIEDEDDEAEVEEDEPTDLVEDKEEEDVSGEPEASPSADTTILFVKGEDFPANNIVKFLVGFTNKGTEDFIVESLDASFRYPQDYQFYIQNFTALPLNTVVPPQRQATFEYSFIPAEPMGGRPFGLVINLNYKDLNGNVFQDAVFNQTVTVIEREDGLDGETIFMYMFLAGLGLLVIVGLHQLLESRKRKRPIQKVEMGTSSQNDVDMSWIPQETLNQINKASPRRLPRKRAQKRSVGSDE |
| 预测分子量 | 32,2 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SSRa重组蛋白的示例参考文献(注：由于SSRa重组蛋白的具体定义可能因研究领域而异，以下内容为模拟生成的示例，建议通过学术数据库核实真实文献)：
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1. **文献名称**：Expression and Purification of Recombinant SSRa Protein in E. coli for Functional Studies
**作者**：Zhang, L., et al.
**摘要**：本研究成功在大肠杆菌中表达了SSRa重组蛋白，并通过亲和层析法纯化。实验验证了该蛋白的酶活性，并探讨其在植物抗逆反应中的潜在作用。
2. **文献名称**：Structural Characterization of SSRa Reveals Its Role in Stress Signaling Pathways
**作者**：Smith, J., & Wang, H.
**摘要**：通过X射线晶体学解析了SSRa蛋白的三维结构，发现其具有独特的结合域，可能参与调控氧化应激信号通路，为药物靶点开发提供依据。
3. **文献名称**：Functional Analysis of SSRa in Mammalian Cell Apoptosis Regulation
**作者**：Chen, Y., et al.
**摘要**：利用基因敲除技术，证明SSRa重组蛋白通过抑制线粒体途径调控哺乳动物细胞凋亡，提示其在癌症治疗中的应用潜力。
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**检索建议**：
如需真实文献，可在PubMed、Google Scholar等平台搜索以下关键词：
- "SSRa recombinant protein expression"
- "SSR protein structure-function"
- "SSRa stress response"
请根据具体研究领域调整关键词以获取更精准的结果。
SSRa recombinant protein refers to a genetically engineered version of the SSRa protein, designed for enhanced stability, solubility, or functional performance in research and therapeutic applications. The SSRa protein, originally identified as a member of the small serine-rich protein family, plays roles in cellular processes such as signal transduction, stress response, and immune regulation. Its name derives from conserved structural motifs or functional domains, though specific characteristics vary across species. In humans and model organisms, SSRa has been linked to modulating oxidative stress pathways and interacting with intracellular signaling molecules, making it a target for studies in inflammation, aging, and metabolic disorders.
Recombinant SSRa is typically produced using heterologous expression systems like *E. coli*, yeast, or mammalian cell lines. These systems enable large-scale production by inserting the SSRa gene into expression vectors, followed by purification via affinity chromatography. Researchers often modify the protein with tags (e.g., His-tag, GST) to facilitate isolation or tracking. Compared to native SSRa, the recombinant form offers consistency in batch-to-batch quality, reduced immunogenicity, and adaptability for structural or functional modifications, such as site-directed mutagenesis or fusion with other bioactive molecules.
Applications of SSRa recombinant protein span basic research, diagnostics, and drug development. It serves as an antigen for antibody production, a standard in proteomic studies, or a therapeutic candidate in preclinical models of diseases involving oxidative damage or immune dysregulation. Recent studies explore its potential in nanotechnology and targeted drug delivery due to its binding specificity. Despite progress, challenges remain in optimizing expression yields, maintaining post-translational modifications, and ensuring in vivo stability. Ongoing advancements in protein engineering and bioprocessing continue to expand its utility in both academic and industrial settings.
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