| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RCN1 |
| Uniprot No | Q15293 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 30-331aa |
| 氨基酸序列 | MRGSHHHHHHGMASMTGGQQMGRDLYDDDDKDRWGSELEKPTVRKERVVR PDSELGERPPEDNQSFQYDHEAFLGKEDSKTFDQLTPDESKERLGKIVDR IDNDGDGFVTTEELKTWIKRVQKRYIFDNVAKVWKDYDRDKDDKISWEEY KQATYGYYLGNPAEFHDSSDHHTFKKMLPRDERRFKAADLNGDLTATREE FTAFLHPEEFEHMKEIVVLETLEDIDKNGDGFVDQDEYIADMFSHEENGP EPDWVLSEREQFNEFRDLNKDGKLDKDEIRHWILPQDYDHAQAEARHLVY ESDKNKDEKLTKEEILENWNMFVGSQATNYGEDLTKNHDEL |
| 预测分子量 | 40 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RCN1重组蛋白的3篇模拟参考文献，涵盖不同研究方向：
1. **文献名称**：*Recombinant RCN1 promotes tumor cell migration through integrin-mediated signaling pathways*
**作者**：Chen L, et al.
**摘要**：本研究通过大肠杆菌表达系统制备了重组RCN1蛋白，并发现其通过结合细胞表面整合素αVβ3激活下游FAK/PI3K通路，显著增强乳腺癌细胞的迁移能力，提示RCN1在肿瘤转移中的潜在作用。
2. **文献名称**：*Crystal structure analysis of calcium-binding domains in recombinant human RCN1*
**作者**：Sato K, et al.
**摘要**：利用X射线晶体学解析了重组人源RCN1蛋白的EF-hand钙结合结构域的三维结构，揭示了其与Ca²⁺结合的特异性位点构象变化，为理解RCN1在内质网钙稳态中的功能提供结构基础。
3. **文献名称**：*RCN1 recombinant protein attenuates ER stress-induced apoptosis in neuronal cells*
**作者**：Wang Y, et al.
**摘要**：通过哺乳动物细胞表达系统获得功能性重组RCN1.证明其通过抑制PERK-eIF2α-ATF4通路减轻内质网应激导致的神经元凋亡，提示RCN1在神经退行性疾病中的保护机制。
(注：以上文献为模拟示例，实际研究需查询具体数据库。)
RCN1 (Reticulocalbin 1) is a calcium-binding protein predominantly localized in the endoplasmic reticulum (ER), belonging to the CREC (Cab45/reticulocalbin/ERC-45/calumenin) protein family. First identified in the 1990s, it is encoded by the RCN1 gene in humans and shares structural homology with other ER-resident proteins like calumenin and reticulocalbin-3. Its molecular weight ranges between 32-36 kDa, depending on post-translational modifications.
Structurally, RCN1 contains six conserved EF-hand motifs that enable calcium ion binding, though only a subset exhibits functional calcium-binding capacity. It also features an N-terminal signal peptide for ER localization and six tandem repeat domains resembling epidermal growth factor (EGF)-like motifs. These structural elements suggest roles in calcium homeostasis and protein-protein interactions within the secretory pathway.
Functionally, RCN1 is implicated in multiple cellular processes, including protein folding, calcium storage, and ER stress response. Studies link it to the regulation of store-operated calcium entry (SOCE) through interactions with stromal interaction molecule 1 (STIM1). It also participates in quality control mechanisms for secreted proteins by modulating calcium-dependent chaperone activities.
Recombinant RCN1 protein is typically produced using bacterial (E. coli) or eukaryotic expression systems. The recombinant form enables biochemical studies of its calcium-binding properties, crystallographic analyses, and functional investigations in cell-free systems. Its production has facilitated discoveries about its potential involvement in pathological conditions, including cancer progression (through EMT regulation), neurodegenerative diseases (via ER stress modulation), and cardiovascular disorders (impacting calcium signaling).
Current research focuses on characterizing its post-translational modifications (e.g., glycosylation) and developing RCN1-targeted probes for diagnostic or therapeutic applications in ER stress-related diseases.
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