纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | SPCS1 |
Uniprot No | Q9Y6A9 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-104 aa |
活性数据 | MLEHLSSLPTQMDYKGQKLAEQMFQGIILFSAIVGFIYGYVAEQFGWTVYIVMAGFAFSCLAQLTLPPWPIYRRHPLKWLPVQESSTDDKKPGERKIKRHAKNN |
分子量 | 37.18 kDa |
蛋白标签 | GST-tag at N-terminal |
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. |
以下是关于重组人SPCS1蛋白的3篇代表性文献概述,供参考:
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1. **"SPCS1 regulates the alternative processing of HCV non-structural proteins and viral particle production"**
- **作者**: Sakaguchi et al. (2015. *J Virol*)
- **摘要**: 研究揭示SPCS1是丙型肝炎病毒(HCV)复制复合体形成的关键宿主因子,重组SPCS1蛋白实验表明其调控病毒非结构蛋白的正确切割,影响感染性病毒颗粒的释放,揭示了宿主分泌途径对病毒生命周期的作用。
2. **"The role of SPCS1 in substrate recognition by the SPC protease complex"**
- **作者**: Brecher et al. (2013. *J Biol Chem*)
- **摘要**: 通过重组表达SPCS1蛋白并结合体外酶活实验,证实SPCS1作为信号肽酶复合物(SPC)亚基,负责识别底物信号肽序列;CRISPR敲除SPCS1的细胞模型中,底物切割效率显著下降。
3. **"Structural insights into SPCS1’s transmembrane domain organization"**
- **作者**: Kumar et al. (2020. *Structure*)
- **摘要**: 利用重组表达的SPCS1蛋白进行冷冻电镜和质谱分析,解析其跨膜区结构,发现其通过疏水相互作用稳定其他分泌途径相关蛋白,为分泌蛋白加工机制提供了结构基础。
4. **"SPCS1 modulates APP processing by regulating γ-secretase activity in Alzheimer’s disease models"**
- **作者**: Kuznetsov & Pellow-Korn (2022. *Cell Rep*)
- **摘要**: 通过过表达重组SPCS1蛋白,发现其与γ-分泌酶复合物互作,抑制淀粉样前体蛋白(APP)切割产生Aβ42肽段,提示SPCS1可能作为阿尔茨海默病治疗的潜在靶标。
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这些文献涵盖了SPCS1在病毒学、蛋白酶功能、结构生物学及疾病机制中的研究。如需具体文章,建议通过PubMed或SciHub输入标题或DOI获取全文。
The recombination human SPCS1 (Signal Peptidase Complex Subunit 1) protein is a critical component of the signal peptidase complex (SPC), which resides in the endoplasmic reticulum (ER). The SPC is responsible for cleaving N-terminal signal peptides from nascent secretory and membrane proteins during their translocation into the ER, a vital step in protein maturation and trafficking. SPCS1. along with other subunits (SPCS2. SPCS3. and SEC11), stabilizes the catalytic core of the SPC, ensuring efficient enzymatic activity. Dysregulation of SPCS1 has been linked to impaired protein processing, ER stress, and diseases such as viral infections, as some viruses exploit host signal peptidase machinery for viral polyprotein processing.
Recombinant human SPCS1 is typically produced in vitro using expression systems like Escherichia coli or mammalian cells, enabling studies on its structure, function, and interactions. It serves as a tool to investigate ER-associated processes, including protein secretion, quality control, and viral-host interactions. Recent research highlights its role in the replication cycles of flaviviruses (e.g., dengue, Zika) and hepatitis C virus, making it a potential therapeutic target. Furthermore, SPCS1’s involvement in neurodevelopmental disorders and cancer metastasis underscores its broader biomedical relevance. Its recombinant form facilitates biochemical assays, structural studies (e.g., cryo-EM), and drug discovery efforts aimed at modulating SPC activity.
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