| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | C2 |
| Uniprot No | P07910 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-293aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMASNVTNKTDPRSMNSRVFIGNLNTLVVKK SDVEAIFSKYGKIVGCSVHKGFAFVQYVNERNARAAVAGEDGRMIAGQVL DINLAAEPKVNRGKAGVKRSAAEMYGSSFDLDYDFQRDYYDRMYSYPARV PPPPPIARAVVPSKRQRVSGNTSRRGKSGFNSKSGQRGSSKSGKLKGDDL QAIKKELTQIKQKVDSLLENLEKIEKEQSKQAVEMKNDKSEEEQSSSSVK KDETNVKMESEGGADDSAEEGDLLDDDDNEDRGDDQLELIKDDEKEAEEG EDDRDSANGEDDS |
| 预测分子量 | 35 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篇与C2重组蛋白相关的虚构参考文献示例(仅供格式参考)：
1. **《重组C2结构域蛋白在钙依赖性膜结合中的功能分析》**
- 作者：Zhang L. et al.
- 摘要：研究通过大肠杆菌系统表达C2结构域重组蛋白，验证其钙离子依赖性磷脂结合能力，揭示其在细胞膜修复中的作用机制。
2. **《基于C2重组蛋白的药物递送载体开发》**
- 作者：Kim S. & Patel R.
- 摘要：利用昆虫细胞表达的C2重组蛋白构建靶向载体，证明其可特异性结合病变细胞膜并增强药物递送效率。
3. **《C2重组蛋白晶体结构解析及其与突触结合蛋白的相互作用》**
- 作者：Gomez A. et al.
- 摘要：通过X射线衍射获得高分辨率C2重组蛋白结构，揭示其与突触蛋白SNAP-25的结合界面，为神经信号传导研究提供新依据。
注：以上文献为模拟内容，实际研究中建议通过PubMed或Web of Science检索真实论文。
C2 recombinant proteins are engineered variants derived from the C2 domain, a conserved structural motif found in numerous eukaryotic proteins involved in membrane trafficking, signaling, and lipid interactions. The C2 domain, typically comprising ~130 amino acids, adopts a β-sandwich fold with calcium-binding loops that confer Ca²⁺-dependent phospholipid-binding activity. This domain is prominently featured in proteins like protein kinase C (PKC), synaptotagmins, and phospholipases, where it mediates membrane localization and regulatory functions.
Recombinant C2 proteins are produced using heterologous expression systems (e.g., E. coli, yeast, or mammalian cells) to study structure-function relationships, calcium-dependent lipid interactions, or protein-membrane dynamics. Their modular nature allows researchers to isolate the C2 domain from full-length proteins, enabling precise biochemical and biophysical analyses. For instance, C2 recombinant proteins have been pivotal in deciphering Ca²⁺-triggered membrane fusion mechanisms in neurotransmission and elucidating signaling pathways in diseases such as cancer and neurodegeneration.
Applications extend to drug discovery, where engineered C2 domains serve as biosensors or targeting modules for therapeutic delivery. Additionally, structural studies of recombinant C2 proteins have revealed how mutations disrupt calcium or lipid binding, linking molecular defects to pathologies like bleeding disorders or immune dysregulation. Challenges include maintaining native folding and post-translational modifications in vitro, often addressed via codon optimization or fusion tags.
Overall, C2 recombinant proteins represent versatile tools for probing calcium signaling, membrane biology, and disease mechanisms, bridging molecular insights with translational research.
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