| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ACH |
| Uniprot No | P22607-1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 23-375aa |
| 氨基酸序列 | ESLGTEQRVVGRAAEVPGPEPGQQEQLVFGSGDAVELSCPPPGGGPMGPTVWVKDGTGLVPSERVLVGPQRLQVLNASHEDSGAYSCRQRLTQRVLCHFSVRVTDAPSSGDDEDGEDEAEDTGVDTGAPYWTRPERMDKKLLAVPAANTVRFRCPAAGNPTPSISWLKNGREFRGEHRIGGIKLRHQQWSLVMESVVPSDRGNYTCVVENKFGSIRQTYTLDVLERSPHRPILQAGLPANQTAVLGSDVEFHCKVYSDAQPHIQWLKHVEVNGSKVGPDGTPYVTVLKTAGANTTDKELEVLSLHNVTFEDAGEYTCLAGNSIGFSHHSAWLVVLPAEEELVEADEAGSVYAG |
| 预测分子量 | 40.1 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ACH重组蛋白的虚构参考文献示例(仅供格式参考)：
1. **《High-yield expression and purification of ACH recombinant protein in E. coli》**
- 作者：Smith, J. et al.
- 摘要：研究利用大肠杆菌表达系统高效表达ACH重组蛋白，优化纯化步骤并获得高纯度蛋白，验证其体外生物活性。
2. **《Structural characterization of ACH recombinant protein by X-ray crystallography》**
- 作者：Johnson, R. & Lee, S.
- 摘要：通过X射线晶体学解析ACH重组蛋白的三维结构，揭示其关键功能域构象，为靶向药物设计提供结构基础。
3. **《Functional analysis of ACH recombinant protein in neuronal cell models》**
- 作者：Wang, Y. et al.
- 摘要：探讨ACH重组蛋白在神经元细胞中的信号调控作用，证实其参与乙酰胆碱受体通路并影响突触可塑性。
4. **《Application of ACH recombinant protein in immunotherapy》**
- 作者：Garcia, M. et al.
- 摘要：评估ACH重组蛋白作为免疫治疗靶点的潜力，动物实验显示其可显著增强抗肿瘤免疫应答。
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*注：以上文献为模拟示例，实际研究中请通过PubMed、Google Scholar等平台检索真实发表论文。*
ACH recombinant proteins are engineered proteins produced through genetic engineering techniques, enabling precise modifications for research, therapeutic, or industrial applications. Derived from the term "recombinant," these proteins are synthesized by inserting target DNA sequences into host organisms (e.g., bacteria, yeast, or mammalian cells) to express specific protein products. The development of recombinant protein technology in the 1970s, following breakthroughs in molecular cloning and gene expression systems, revolutionized biotechnology by allowing large-scale production of proteins with tailored functions.
ACH recombinant proteins often emphasize high purity, stability, and bioactivity, making them critical tools in drug development (e.g., monoclonal antibodies, vaccines), disease diagnostics, and functional studies of cellular pathways. For instance, they are used to study protein-protein interactions, enzyme mechanisms, or immune responses. The choice of expression system depends on the protein's complexity; prokaryotic systems like *E. coli* offer cost-effective production but may lack post-translational modifications, while eukaryotic systems (e.g., CHO cells) enable proper folding and glycosylation for therapeutic proteins.
Recent advancements include CRISPR-based gene editing to optimize host cells, cell-free protein synthesis for rapid prototyping, and AI-driven protein design to enhance functionality. Challenges remain in scaling production, minimizing immunogenicity, and ensuring consistent quality. ACH recombinant proteins continue to drive innovations in personalized medicine, biocatalysis, and synthetic biology, reflecting their pivotal role in bridging molecular biology and real-world applications.
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