| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | STIM1 |
| Uniprot No | Q13586-1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-213aa |
| 氨基酸序列 | MDVCVRLALW LLWGLLLHQG QSLSHSHSEK ATGTSSGANS EESTAAEFCR IDKPLCHSED EKLSFEAVRN IHKLMDDDAN GDVDVEESDE FLREDLNYHD PTVKHSTFHG EDKLISVEDL WKAWKSSEVY NWTVDEVVQW LITYVELPQY EETFRKLQLS GHAMPRLAVT NTTMTGTVLK MTDRSHRQKL QLKALDTVLF GPPLLTRHNH LKD |
| 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STIM1重组蛋白的3篇代表性文献的简要信息：
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1. **文献名称**：*STIM1. an essential and conserved component of store-operated Ca²⁺ channel function*
**作者**：Roos, J., et al. (2005)
**摘要**：该研究首次鉴定STIM1为内质网钙库操纵的钙通道(SOCE)关键调控因子。通过重组蛋白表达技术，证实STIM1通过感知内质网钙浓度变化，直接激活细胞膜上的Orai1通道，介导钙离子内流。
2. **文献名称**：*Structural and mechanistic insights into STIM1-mediated initiation of store-operated calcium entry*
**作者**：Zhou, Y., et al. (2013)
**摘要**：利用重组STIM1蛋白的晶体结构和突变分析，揭示了其C端抑制性α-螺旋的结构功能，阐明了STIM1在钙库耗竭后发生构象变化，并通过寡聚化激活Orai1通道的分子机制。
3. **文献名称**：*A cytosolic STIM1 pre-activation mechanism for store-operated calcium entry*
**作者**：Muik, M., et al. (2011)
**摘要**：通过重组STIM1片段与荧光共振能量转移(FRET)技术，证明STIM1在静息状态下以单体存在，钙库耗竭后其胞内结构域发生寡聚化，并通过与Orai1的直接结合触发钙信号通路。
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**说明**：上述文献均涉及STIM1重组蛋白在钙信号机制研究中的应用，涵盖功能鉴定、结构解析及动态调控机制。如需具体文献来源(期刊、卷号等)，建议通过PubMed或Sci-Hub输入标题或作者信息进一步查询。
STIM1 (stromal interaction molecule 1) is a key transmembrane protein located primarily in the endoplasmic reticulum (ER) membrane, where it functions as a calcium sensor and regulator of store-operated calcium entry (SOCE). Discovered in 2005. STIM1 monitors ER luminal calcium levels via its N-terminal EF-hand domain. Depletion of ER calcium stores triggers STIM1 oligomerization and translocation to ER-plasma membrane junctions, where it interacts with ORAI1. a plasma membrane calcium channel, to mediate extracellular calcium influx. This process is critical for maintaining cellular calcium homeostasis and driving downstream signaling pathways involved in immune response, muscle contraction, and gene expression.
Recombinant STIM1 protein, produced through heterologous expression systems (e.g., HEK293 or insect cells), enables researchers to study its structure-function relationships, post-translational modifications, and interaction partners. The protein typically includes functional domains: the canonical EF-hand, a sterile alpha motif (SAM) domain supporting oligomerization, and a C-terminal polybasic region for membrane targeting. Purification tags (e.g., GST, His-tag) are often added to facilitate isolation. Applications range from in vitro reconstitution of SOCE machinery and RNAi rescue experiments to drug screening for calcium-related disorders. Dysregulated STIM1 is implicated in immunodeficiency syndromes, cardiovascular diseases, and cancer metastasis, making its recombinant form valuable for both basic research and therapeutic development. Recent studies also explore engineered STIM1 variants to modulate calcium signaling with spatiotemporal precision.
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