纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | RCN2 |
Uniprot No | Q14257 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 26-317aa |
氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMEELHYPLGERRSDYDREALLGV QEDVD EYVKLGHEEQQKRLQAIIKKIDLDSDGFLTESELSSWIQMSFKHY AMQ EAKQQFVEYDKNSDDTVTWDEYNIQMYDRVIDFDENTALDDAEEESF R KLHLKDKKRFEKANQDSGPGLSLEEFIAFEHPEEVDYMTEFVIQEALEE HDKNGDGFVSLEEFLGDYRWDPTANEDPEWILVEKDRFVNDYDKDNDGR L DPQELLPWVVPNNQGIAQEEALHLIDEMDLNGDKKLSEEEILENPDL FLTSEATDYGRQLHDDYFYHDEL |
预测分子量 | 37 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3篇关于RCN2重组蛋白的示例文献(内容为模拟概括,建议通过学术数据库核实具体文献):
1. **《Recombinant RCN2 promotes cell migration via integrin-mediated signaling pathways》**
- 作者:Chen L. et al.
- 摘要:研究利用大肠杆菌系统表达重组RCN2蛋白,发现其通过整合素-黏着斑激酶(FAK)通路增强肿瘤细胞迁移,提示RCN2在癌症转移中的潜在作用。
2. **《Expression and functional characterization of RCN2 in cardiac fibrosis》**
- 作者:Wang Y. et al.
- 摘要:通过昆虫细胞体系重组表达RCN2.证实其通过调控TGF-β/Smad信号通路加剧心肌纤维化,为心血管疾病治疗提供新靶点。
3. **《Structural insights into calcium-binding properties of recombinant RCN2》**
- 作者:Kim S. et al.
- 摘要:利用X射线晶体学解析重组RCN2蛋白的钙离子结合结构域,揭示其与内质网钙稳态调控相关的分子机制。
4. **《RCN2 recombinant protein attenuates ER stress in neurodegenerative models》**
- 作者:Gonzalez-Reyes A. et al.
- 摘要:在CHO细胞中表达的重组RCN2显示可缓解内质网应激,改善阿尔茨海默病模型中的神经元存活率。
**提示**:以上为模拟文献,实际研究请通过PubMed、Google Scholar等平台以"RCN2 recombinant protein"或"recombinant calumenin"为关键词检索。
Reticulocalbin 2 (RCN2), a member of the reticulocalbin family, is an EF-hand calcium-binding protein predominantly localized in the endoplasmic reticulum (ER). It plays a role in calcium ion binding and secretory pathway regulation, contributing to protein folding, post-translational modifications, and intracellular signaling. Structurally, RCN2 contains six conserved EF-hand motifs that enable calcium-dependent conformational changes, facilitating interactions with client proteins or membranes. Its expression is linked to cellular stress responses, including ER stress, hypoxia, and oxidative damage.
Recombinant RCN2 protein, produced via genetic engineering in systems like Escherichia coli or mammalian cells, retains native functional domains, allowing researchers to study its biochemical properties and interactions. Studies suggest RCN2 is involved in tumor progression, angiogenesis, and drug resistance in cancers, potentially serving as a diagnostic biomarker or therapeutic target. In neurodegenerative diseases, it may modulate ER stress pathways implicated in protein aggregation. Additionally, RCN2's role as a molecular chaperone in collagen secretion highlights its importance in extracellular matrix remodeling.
Despite progress, RCN2's precise mechanisms remain partially elusive due to functional redundancy within its protein family and context-dependent behavior. Current research focuses on elucidating its interactome, calcium-dependent signaling cascades, and disease-specific regulatory networks. Recombinant RCN2 tools are vital for structural studies, antibody development, and high-throughput screening for drug discovery. Challenges include optimizing recombinant protein stability for functional assays and validating in vivo relevance. Further exploration of RCN2's dual roles in homeostasis and pathology may unlock novel therapeutic strategies for cancer and ER-related disorders.
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