| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | CTXI |
| Uniprot No | P15220 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-36aa |
| 氨基酸序列 | MCMPCFTTRPDMAQQCRACCKGRGKCFGPQCLCGYD |
| 预测分子量 | 4,0 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CTXI(假设为Conotoxin XI)重组蛋白的模拟参考文献示例，涵盖不同研究方向：
1. **文献名称**：*"Efficient Recombinant Expression of Conotoxin CTXI in Escherichia coli for Neuropharmacological Studies"*
**作者**：Zhang, Y. et al.
**摘要**：本研究优化了CTXI在大肠杆菌中的可溶性表达，采用融合标签与肠激酶切割策略，获得高纯度重组CTXI。体外电生理实验证实其能选择性抑制N型钙通道，活性与天然毒素相当。
2. **文献名称**：*"Structural Insights into Recombinant CTXI by NMR: Implications for Calcium Channel Binding"*
**作者**：Lee, S. & Norton, R.S.
**摘要**：通过核磁共振(NMR)解析了重组CTXI的三维结构，发现其β-折叠构象与天然肽一致。突变分析揭示了关键残基(如Arg10)在结合钙通道α1亚基中的作用。
3. **文献名称**：*"Antinociceptive Effects of Recombinant CTXI in Murine Neuropathic Pain Models"*
**作者**：Garcia-Caraballo, S. et al.
**摘要**：重组CTXI通过鞘内注射显著缓解小鼠慢性疼痛模型(坐骨神经损伤)的机械性痛觉超敏，效果优于加巴喷丁，且无运动功能损伤，提示其镇痛潜力。
4. **文献名称**：*"High-Yield Production of Bioactive CTXI in Pichia pastoris: A Scalable Approach for Therapeutic Development"*
**作者**：Wang, H. et al.
**摘要**：利用毕赤酵母系统实现CTXI的高效分泌表达，产量达50 mg/L。纯化产物经质谱验证正确修饰，体外活性测试显示其对神经元钙电流抑制IC50为12 nM，支持其规模化生产可行性。
注：以上文献为模拟内容，实际研究需通过学术数据库检索确认。建议使用关键词“Conotoxin XI recombinant expression”或“CTXI calcium channel”在PubMed、Web of Science等平台查找真实文献。
CTXI (Conotoxin XI), a recombinant protein derived from the venom of cone snails (genus *Conus*), represents a class of bioactive peptides known for their high specificity in modulating ion channels and neurotransmitter receptors. Cone snails, marine predators, produce complex venoms containing hundreds of conotoxins to immobilize prey. These peptides are categorized into gene superfamilies based on conserved signal sequences and cysteine frameworks. CTXI belongs to the O-superfamily, characterized by a specific disulfide bond arrangement (C-C-CC-C-C) that stabilizes its structure and enables precise interactions with targets.
Recombinant CTXI is synthesized using biotechnological methods, such as bacterial or yeast expression systems, to overcome limitations in natural venom extraction, including low yield and ethical concerns. The protein is engineered with affinity tags (e.g., His-tags) to facilitate purification via chromatography. Structural validation through mass spectrometry and NMR ensures fidelity to native conotoxins.
Functionally, CTXI selectively inhibits voltage-gated sodium (Naₐ) channels, particularly subtypes involved in pain signaling (e.g., Naᵥ1.7). This mechanism has drawn interest in neuroscience and pharmacology for developing non-opioid analgesics or neuroprotective agents. Its recombinant form allows scalable production for structure-activity studies, aiding the design of optimized analogs with enhanced stability or reduced toxicity. Additionally, CTXI serves as a molecular tool to probe ion channel physiology, offering insights into neurological disorders like epilepsy or neuropathic pain.
Despite its potential, challenges remain in optimizing pharmacokinetics and minimizing immunogenicity. Ongoing research focuses on conjugation with drug delivery systems (e.g., nanoparticles) to improve therapeutic efficacy. CTXI exemplifies how venomics and recombinant technology converge to bridge natural toxin diversity with biomedical innovation.
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