| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | AchE |
| Uniprot No | P22303 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-640aa |
| 氨基酸序列 | MRPPQCLLHTPSLASPLLLLLVWLLGGGVGAEGREDAELLVTVRGGRLRG IRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVC YQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVIVWIY GGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPG NVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSR GLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTEL VACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAG DFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQ VSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLA AQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEE KIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLE VRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKN QFDTTASRIAAQTCDPGGTPMSSAPPGPLAVYTIYFRAGL |
| 预测分子量 | 97 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AchE(乙酰胆碱酯酶)重组蛋白研究的参考文献示例(内容基于领域内典型研究方向，部分为虚构示例，仅供参考)：
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1. **文献名称**：*Expression and characterization of recombinant human acetylcholinesterase in a baculovirus system*
**作者**：Sussman, J.L., Harel, M., Frolow, F. et al.
**摘要**：研究利用杆状病毒-昆虫细胞表达系统成功表达人源AchE重组蛋白，通过X射线晶体学解析其三维结构，并验证其催化活性与天然蛋白一致，为神经毒剂作用机制研究提供模型。
2. **文献名称**：*Production of functional Torpedo californica acetylcholinesterase in Pichia pastoris*
**作者**：Shafferman, A., Kronman, C., Velan, B.
**摘要**：报道在毕赤酵母中高效表达电鳐来源的AchE重组蛋白，通过优化密码子和发酵条件提升产量，纯化后蛋白表现出高比活性，适用于抑制剂筛选和分子互作研究。
3. **文献名称**：*Development of a recombinant acetylcholinesterase-based biosensor for organophosphate detection*
**作者**：Liu, Y., Yu, D., Zhang, T.
**摘要**：将重组AchE固定于电化学传感器表面，利用其与有机磷农药的特异性结合导致酶活性抑制的原理，建立快速检测方法，灵敏度达纳摩尔级别，适用于环境监测。
4. **文献名称**：*Site-directed mutagenesis enhances the stability of recombinant mouse acetylcholinesterase*
**作者**：Kryger, G., Harel, M., Giles, K. et al.
**摘要**：通过定点突变改造小鼠AchE的疏水核心区域，显著提高重组蛋白的热稳定性和抗变性能力，为长效制剂开发及结构-功能关系研究奠定基础。
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**备注**：以上文献标题及作者为示例性质，实际引用时建议通过PubMed、Web of Science等平台检索最新或领域内高引论文。真实文献可参考以下方向：
- **结构生物学**：Sussman团队对AchE晶体结构的研究;
- **异源表达**：大肠杆菌、昆虫细胞、酵母等系统的优化;
- **应用研究**：生物传感器、药物筛选或毒性机制分析。
Acetylcholinesterase (AChE) is a critical enzyme in the nervous system, responsible for terminating synaptic transmission by rapidly hydrolyzing the neurotransmitter acetylcholine into choline and acetate. Its role in regulating cholinergic signaling makes it a key target for research in neurobiology, toxicology, and pharmacology. Recombinant AChE proteins are engineered versions of this enzyme produced through genetic engineering techniques, typically using expression systems like *E. coli*, yeast, insect cells, or mammalian cell lines. These systems allow large-scale production of AChE with high purity and consistency, overcoming limitations of isolating the enzyme from natural tissues.
The development of recombinant AChE has been driven by its diverse applications. In neuroscience, it aids in studying synaptic function and neurodegenerative diseases like Alzheimer's, where AChE inhibitors are used to enhance cholinergic activity. In toxicology, recombinant AChE serves as a biosensor to detect organophosphate and carbamate pesticides, which inhibit AChE and disrupt nerve function. Additionally, it’s used to develop antidotes for nerve agent poisoning. Structural studies of recombinant AChE have provided insights into its catalytic mechanism, substrate specificity, and interactions with inhibitors, guiding drug design.
Challenges in producing functional recombinant AChE include ensuring proper post-translational modifications (e.g., glycosylation) and correct folding for enzymatic activity. Advances in protein engineering, such as codon optimization and fusion tags, have improved expression efficiency. Recombinant AChE also enables customization, like creating mutant forms to study resistance mechanisms in pests or designing novel therapeutics. Overall, it represents a versatile tool bridging basic research and practical applications in medicine, agriculture, and environmental safety.
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