| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ChAT |
| Uniprot No | P28329 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 120-733aa |
| 氨基酸序列 | AAKTPSSEESGLPKLPVPPLQQTLATYLQCMRHLVSEEQFRKSQAIVQQFGAPGGLGETLQQKLLERQEKTANWVSEYWLNDMYLNNRLALPVNSSPAVIFARQHFPGTDDQLRFAASLISGVLSYKALLDSHSIPTDCAKGQLSGQPLCMKQYYGLFSSYRLPGHTQDTLVAQNSSIMPEPEHVIVACCNQFFVLDVVINFRRLSEGDLFTQLRKIVKMASNEDERLPPIGLLTSDGRSEWAEARTVLVKDSTNRDSLDMIERCICLVCLDAPGGVELSDTHRALQLLHGGGYSKNGANRWYDKSLQFVVGRDGTCGVVCEHSPFDGIVLVQCTEHLLKHVTQSSRKLIRADSVSELPAPRRLRWKCSPEIQGHLASSAEKLQRIVKNLDFIVYKFDNYGKTFIKKQKCSPDAFIQVALQLAFYRLHRRLVPTYESASIRRFQEGRVDNIRSATPEALAFVRAVTDHKAAVPASEKLLLLKDAIRAQTAYTVMAITGMAIDNHLLALRELARAMCKELPEMFMDETYLMSNRFVLSTSQVPTTTEMFCCYGPVVPNGYGACYNPQPETILFCISSFHSCKETSSSKFAKAVEESLIDMRDLCSLLPPTESKPL |
| 预测分子量 | 76.1 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ChAT(胆碱乙酰转移酶)重组蛋白研究的3篇代表性文献示例，包含文献名称、作者及摘要概括：
1. **文献名称**：*Expression and purification of recombinant human choline acetyltransferase in Escherichia coli*
**作者**：Smith A, et al.
**摘要**：本研究利用大肠杆菌表达系统成功表达并纯化了具有高活性的重组人源ChAT蛋白，优化了诱导条件与纯化步骤，证实其酶活性可用于体外乙酰胆碱合成研究。
2. **文献名称**：*Structural insights into choline acetyltransferase by cryo-EM: Implications for catalytic mechanism*
**作者**：Zhang L, et al.
**摘要**：通过冷冻电镜解析了ChAT重组蛋白的三维结构，揭示了其底物结合位点及催化关键残基，为理解乙酰胆碱合成的分子机制提供了结构基础。
3. **文献名称**：*Functional characterization of ChAT mutants in neurodegenerative models using recombinant protein*
**作者**：Wang Y, et al.
**摘要**：构建了ChAT重组蛋白的多种突变体，在细胞模型中验证了其酶活变化与神经退行性疾病(如阿尔茨海默病)中胆碱能功能异常的关联性。
注：以上文献为示例，实际引用需根据具体研究内容选择真实发表的论文。建议通过PubMed或Web of Science以关键词“recombinant ChAT protein”检索最新文献。
Choline acetyltransferase (ChAT) is a critical enzyme in the nervous system, responsible for synthesizing the neurotransmitter acetylcholine (ACh) by catalyzing the transfer of an acetyl group from acetyl-CoA to choline. ACh plays a central role in mediating synaptic transmission in both the central and peripheral nervous systems, influencing processes such as memory, learning, and muscle contraction. Dysregulation of ChAT activity or expression has been implicated in neurological disorders, including Alzheimer’s disease, Parkinson’s disease, and myasthenic syndromes, making it a target for therapeutic research.
Recombinant ChAT protein is produced using genetic engineering techniques, where the *ChAT* gene is cloned into expression vectors and expressed in heterologous systems like *E. coli*, insect cells, or mammalian cell lines. This approach enables large-scale production of highly purified, functional ChAT protein for experimental and clinical applications. Recombinant ChAT retains enzymatic activity, allowing researchers to study its kinetic properties, structure-function relationships, and interactions with inhibitors or modulators *in vitro*. It is also used to develop assays for drug screening, investigate pathological mechanisms in neurodegenerative diseases, and engineer cell-based therapies to restore ACh signaling.
The availability of recombinant ChAT has advanced diagnostic and therapeutic innovations. For example, it aids in producing antibodies for immunohistochemistry to map cholinergic neurons or quantify ChAT levels in disease models. Additionally, recombinant ChAT is explored in gene therapy strategies to compensate for ACh deficiency in neurological conditions. Its standardized production ensures reproducibility in research, addressing challenges associated with isolating the native protein from tissues. Overall, recombinant ChAT serves as a vital tool for both basic neuroscience and translational studies aiming to modulate cholinergic signaling pathways.
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