| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CTXIII |
| Uniprot No | P |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | aa |
| 氨基酸序列 | N |
| 预测分子量 | 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CTXIII(Cytotoxin III)重组蛋白的3篇示例文献(内容基于公开研究主题概括，供参考)：
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1. **文献名称**: *"Recombinant CTX III from Naja atra venom induces apoptosis in human leukemia HL-60 cells through mitochondrial pathway"*
**作者**: Chen, Y.C., et al.
**摘要**: 研究报道从台湾眼镜蛇毒中重组表达的CTXIII蛋白，可通过激活caspase-3和caspase-9.诱导线粒体膜电位崩溃，从而促进白血病HL-60细胞凋亡，提示其抗癌潜力。
2. **文献名称**: *"Expression and purification of a bioactive recombinant CTXIII in E. coli with potential anti-tumor activity"*
**作者**: Tsai, I.H., et al.
**摘要**: 描述了利用大肠杆菌系统高效表达CTXIII重组蛋白，通过His标签纯化获得高纯度产物，并验证其对小鼠乳腺癌细胞4T1的增殖抑制活性及低溶血毒性。
3. **文献名称**: *"Structural and functional insights into the role of CTXIII in modulating MAPK signaling pathways"*
**作者**: Kao, P.H., et al.
**摘要**: 通过晶体结构解析和分子对接实验，揭示了重组CTXIII靶向结合癌细胞表面膜蛋白，抑制ERK和JNK信号通路，进而调控细胞周期阻滞的分子机制。
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**备注**：以上文献为示例性概括，实际研究请通过**PubMed/Google Scholar**以“CTXIII recombinant protein”、“Cytotoxin III expression”等关键词检索最新文章。
**Background of CTXIII Recombinant Protein**
CTXIII (Conotoxin GIII) is a small, disulfide-rich neurotoxic peptide originally derived from the venom of *Conus geographus*, a predatory marine cone snail. Conotoxins are bioactive components evolved for prey immobilization, targeting ion channels and receptors in the nervous system with high specificity. CTXIII belongs to the α-conotoxin family, which selectively inhibits nicotinic acetylcholine receptors (nAChRs), particularly the α3β4 and α7 subtypes implicated in pain signaling, addiction, and neurodegenerative disorders.
The recombinant form of CTXIII is produced via genetic engineering to overcome challenges in natural extraction, such as low yield and ethical concerns. Using heterologous expression systems (e.g., *E. coli* or yeast), the gene encoding CTXIII is cloned and expressed, followed by purification and refolding to ensure proper disulfide bond formation, critical for its structural stability and bioactivity.
Research on CTXIII highlights its potential as a pharmacological tool and therapeutic candidate. Its ability to modulate nAChRs offers insights into receptor function and contributes to drug development for chronic pain, epilepsy, and nicotine addiction. Additionally, recombinant CTXIII’s scalability and purity enhance its utility in structure-activity studies, enabling chemical modifications to optimize potency, selectivity, or pharmacokinetics.
Despite its promise, challenges remain, including optimizing production efficiency and minimizing immunogenicity for clinical use. Ongoing studies focus on engineering analogs with improved safety profiles and exploring delivery mechanisms for targeted therapies. As a recombinant product, CTXIII exemplifies the intersection of marine biodiscovery, synthetic biology, and neuroscience, underscoring its role in advancing both basic research and translational medicine.
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