| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SSR4 |
| Uniprot No | P51571 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 24-144aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSEACLEPQ ITPSYYTTSD AVISTETVFI VEISLTCKNR VQNMALYADV GGKQFPVTRG QDVGRYQVSW SLDHKSAHAG TYEVRFFDEE SYSLLRKAQR NNEDISIIPP LFTVSVDHRG TWNG |
| 预测分子量 | 16 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SSR4重组蛋白的3篇示例参考文献(注：以下文献信息为示例性内容，实际文献需通过学术数据库检索获取)：
1. **文献名称**：Structural and Functional Analysis of SSR4 in the TRAP Complex
**作者**：Smith J, et al.
**摘要**：研究通过重组表达纯化了人源SSR4蛋白，解析了其与TRAP复合体其他亚基的相互作用，揭示了SSR4在内质网蛋白质转运中的关键结构域。
2. **文献名称**：Recombinant SSR4 Expression in Mammalian Cells and Its Role in Glycosylation Disorders
**作者**：Lee H, et al.
**摘要**：利用哺乳动物细胞系统表达SSR4重组蛋白，发现其缺失会导致N-连接糖基化异常，为先天性糖基化疾病(CDG)的机制研究提供依据。
3. **文献名称**：SSR4 Knockout Model and Recombinant Protein Rescue in Drosophila
**作者**：Wang Y, et al.
**摘要**：通过果蝇模型证明SSR4基因敲除导致发育缺陷，外源性重组SSR4蛋白可部分恢复表型，表明其在跨膜蛋白分泌中的保守功能。
建议通过PubMed或Web of Science搜索关键词“SSR4 recombinant”“TRAP complex SSR4”获取真实文献。如需具体论文协助，可提供更详细的研究方向(如结构、疾病关联等)。
SSR4 (Signal Sequence Receptor subunit 4) is a key component of the translocon-associated protein (TRAP) complex located in the endoplasmic reticulum (ER) membrane. This evolutionarily conserved protein plays a critical role in protein translocation and post-translational modification processes. Structurally, SSR4 contains multiple transmembrane domains that facilitate its integration into the ER membrane, where it interacts with other TRAP subunits (SSR1. SSR2. SSR3) to form a functional complex. The TRAP complex assists the Sec61 translocon in coordinating the transfer of nascent polypeptides into the ER lumen, particularly for substrates with challenging signal sequences or complex folding requirements.
Research indicates SSR4 contributes to efficient protein glycosylation and quality control mechanisms by maintaining translocon stability. Its involvement extends to the secretion of hormones, immune molecules, and extracellular matrix proteins. Dysregulation of SSR4 has been linked to congenital disorders of glycosylation (CDG), notably CDG1Y caused by SSR4 mutations, which manifests with developmental delays and coagulation abnormalities. Recent studies also suggest potential associations between SSR4 overexpression and cancer progression, possibly through enhanced secretion of tumorigenic factors.
As a recombinant protein, SSR4 is utilized in structural studies to elucidate TRAP complex dynamics and in drug discovery platforms targeting protein secretion pathways. Its recombinant expression in mammalian systems enables investigations into ER-associated degradation (ERAD) and stress responses, providing insights for therapeutic interventions in protein-misfolding diseases.
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