| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SVIP |
| Uniprot No | Q8NHG7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-77aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMGLCFPC PGESAPPTPD LEEKRAKLAE AAERRQKEAA SRGILDVQSV QEKRKKKEKI EKQIATSGPP PEGGLRWTVS |
| 预测分子量 | 11 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SVIP重组蛋白的3篇示例参考文献(内容为虚构示例，仅供参考)：
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1. **文献名称**：*Expression and Functional Analysis of Recombinant SVIP in Regulating VCP-Dependent Protein Degradation*
**作者**：Smith, J. et al. (2015)
**摘要**：本研究利用大肠杆菌表达系统成功纯化SVIP重组蛋白，证实其与Valosin-Containing Protein (VCP)的相互作用，并证明SVIP通过调控VCP的泛素-蛋白酶体活性参与错误折叠蛋白的降解。
2. **文献名称**：*SVIP Recombinant Protein Modulates ER Stress and Autophagy in Mammalian Cells*
**作者**：Zhang, L. et al. (2018)
**摘要**：通过哺乳动物细胞表达SVIP重组蛋白，发现其过表达可缓解内质网应激，并增强自噬通量，提示SVIP在细胞应激响应中通过协调蛋白降解途径维持内质网稳态。
3. **文献名称**：*Structural Insights into SVIP-VCP Complex via Crystallography of Recombinant SVIP*
**作者**：Johnson, R. et al. (2021)
**摘要**：解析SVIP重组蛋白的晶体结构，揭示其与VCP结合的关键结构域，为开发靶向VCP-SVIP相互作用的神经退行性疾病治疗策略提供分子基础。
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**注**：以上文献为示例性内容，实际引用时请以真实发表的论文为准。如需查找真实文献，建议在PubMed、Web of Science等平台检索关键词“SVIP recombinant protein”或“SVIP VCP interaction”。
SVIP (Small Vault Protein Interacting Protein) is a multifunctional protein encoded by the SVIP gene, initially identified as a binding partner of vault proteins—large ribonucleoprotein complexes found in eukaryotic cells. Structurally, SVIP contains a coiled-coil domain and a transmembrane region, enabling interactions with cellular machinery involved in membrane trafficking and protein sorting. It localizes primarily to the endoplasmic reticulum (ER) and Golgi apparatus, where it plays a regulatory role in vesicular transport and ER-associated degradation (ERAD).
SVIP gained attention for its dual role in cellular quality control. It acts as a co-chaperone, modulating the activity of valosin-containing protein (VCP/p97), a key ATPase in ERAD that extracts misfolded proteins for proteasomal degradation. Paradoxically, SVIP also inhibits the formation of autophagosomes, suggesting cross-talk between ERAD and autophagy pathways. This balance influences cellular responses to stress, impacting diseases like cancer and neurodegenerative disorders.
Recombinant SVIP is engineered using expression systems (e.g., E. coli or mammalian cells) to study its biochemical properties and therapeutic potential. Its applications span basic research—elucidating protein quality control mechanisms—and drug development. For instance, SVIP overexpression has been shown to reduce aggregation of toxic proteins (e.g., mutant huntingtin in Huntington’s disease), highlighting its neuroprotective potential. Conversely, inhibiting SVIP could enhance autophagy in cancers reliant on ERAD for survival.
Despite progress, SVIP's pleiotropic effects and context-dependent roles require further exploration. Current studies focus on optimizing recombinant SVIP delivery and targeting its interactions in disease models, aiming to translate its regulatory functions into clinical interventions.
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