| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SSR1 |
| Uniprot No | P43307 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22-207aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSRGGPRGL LAVAQDLTED EETVEDSIIE DEDDEAEVEE DEPTDLVEDK EEEDVSGEPE ASPSADTTIL FVKGEDFPAN NIVKFLVGFT NKGTEDFIVE SLDASFRYPQ DYQFYIQNFT ALPLNTVVPP QRQATFEYSF IPAEPMGGRP FGLVINLNYK DLNGNVFQDA VFNQTVTVIE REDGLDGET |
| 预测分子量 | 23 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SSR1重组蛋白的3篇参考文献示例(内容基于研究领域常见方向，非真实文献，供参考)：
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1. **文献名称**: *"Recombinant Expression and Functional Characterization of SSR1 in Protein Translocation"*
**作者**: Zhang Y, et al.
**摘要**: 研究报道了在大肠杆菌系统中成功表达并纯化重组SSR1蛋白，验证其作为内质网信号序列受体亚基在蛋白质转运中的关键作用，证实其与Sec61复合物的相互作用机制。
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2. **文献名称**: *"Structural Analysis of SSR1 Using Cryo-EM: Implications for Membrane Protein Complex Assembly"*
**作者**: Tanaka K, et al.
**摘要**: 通过冷冻电镜解析重组SSR1蛋白的高分辨率结构，揭示其在内质网膜蛋白复合物组装中的构象变化，为靶向膜蛋白疾病的药物设计提供结构基础。
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3. **文献名称**: *"SSR1 Knockdown and Recombinant Rescue in Arabidopsis Reveals Its Role in Abiotic Stress Response"*
**作者**: Chen L, et al.
**摘要**: 利用重组SSR1蛋白回补拟南芥突变体，证明SSR1通过调节内质网应激通路增强植物对盐胁迫和干旱的耐受性，为作物抗逆性改良提供新靶点。
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注：若需真实文献，建议通过PubMed或Google Scholar以“SSR1 recombinant protein”“Signal Sequence Receptor 1”等关键词检索近年研究。
**Background of SSR1 Recombinant Protein**
SSR1 (Sec61 Subunit Sigma-1 Receptor) is a protein encoded by the *SEC61G* gene, primarily associated with the Sec61 translocon complex in the endoplasmic reticulum (ER). This complex facilitates the translocation of nascent polypeptides during protein biosynthesis and plays a role in maintaining ER membrane integrity. SSR1. also identified as a homolog of the sigma-1 receptor (σ1R), has garnered attention due to its involvement in cellular stress responses, calcium signaling, and modulation of ion channels. Unlike the canonical σ1R, SSR1 is ubiquitously expressed and integrates into ER membranes, influencing protein folding, quality control, and interorganelle communication.
Recombinant SSR1 protein is engineered using genetic engineering techniques, typically expressed in *E. coli* or mammalian cell systems to ensure proper post-translational modifications. Purification methods like affinity chromatography yield high-purity proteins for functional studies. Its recombinant form enables researchers to dissect its molecular interactions, particularly its role in ER-associated degradation (ERAD), autophagy, and cellular adaptation to stress.
SSR1’s relevance extends to disease research, including neurodegenerative disorders (e.g., Alzheimer’s), cancer (where ER stress pathways are dysregulated), and viral infections that exploit ER machinery. Studies also explore its potential as a therapeutic target, given its influence on proteostasis and cell survival. By leveraging recombinant SSR1. scientists aim to unravel its structural dynamics, ligand-binding properties, and crosstalk with other ER-resident proteins, offering insights into novel treatment strategies for ER stress-related pathologies.
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