| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | BCHE |
| Uniprot No | P06276 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 29-602aa |
| 氨基酸序列 | EDDIIIATKNGKVRGMNLTVFGGTVTAFLGIPYAQPPLGRLRFKKPQSLT KWSDIWNATKYANSCCQNIDQSFPGFHGSEMWNPNTDLSEDCLYLNVWIP APKPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGA LGFLALPGNPEAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAG AASVSLHLLSPGSHSLFTRAILQSGSFNAPWAVTSLYEARNRTLNLAKLT GCSRENETEIIKCLRNKDPQEILLNEAFVVPYGTPLSVNFGPTVDGDFLT DMPDILLELGQFKKTQILVGVNKDEGTAFLVYGAPGFSKDNNSIITRKEF QEGLKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDVVGDYNFIC PALEFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPL ERRDNYTKAEEILSRSIVKRWANFAKYGNPNETQNNSTSWPVFKSTEQKY LTLNTESTRIMTKLRAQQCRFWTSFFPKVLEMTGNIDEAEWEWKAGFHRW NNYMMDWKNQFNDYTSKKESCVGLVDHHHHHH |
| 预测分子量 | 66 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BCHE(丁酰胆碱酯酶)重组蛋白的3篇参考文献，包含文献名称、作者及摘要内容概括：
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1. **文献名称**: "High-level expression of recombinant human butyrylcholinesterase in transgenic plants"
**作者**: Geyer BC et al.
**摘要**: 该研究利用植物表达系统(如烟草)实现了人源BCHE重组蛋白的高效表达，证明其酶活性和稳定性与天然蛋白相似，为大规模生产解毒剂提供新途径。
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2. **文献名称**: "Crystal structure of recombinant human butyrylcholinesterase and its mutants"
**作者**: Nachon F et al.
**摘要**: 通过X射线晶体学解析了重组人BCHE及其突变体的三维结构，揭示了关键活性位点与底物结合机制，为设计新型抑制剂奠定基础。
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3. **文献名称**: "Recombinant butyrylcholinesterase as a detoxifying agent against organophosphate poisoning"
**作者**: Ashani Y et al.
**摘要**: 研究证明重组BCHE蛋白可有效中和有机磷类神经毒剂，并在动物模型中显著提高存活率，验证其作为广谱解毒剂的潜力。
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如需更多文献或具体研究方向，可进一步补充说明。
Butyrylcholinesterase (BChE), also known as pseudocholinesterase, is a serine hydrolase primarily synthesized in the liver and distributed in plasma, the nervous system, and other tissues. It plays a critical role in hydrolyzing esters, including acetylcholine analogs, succinylcholine, and cocaine, thereby contributing to detoxification and metabolic regulation. Unlike acetylcholinesterase (AChE), which is synaptic and neuron-specific, BChE exhibits broader substrate specificity and tissue distribution, making it a versatile biocatalyst and therapeutic target.
Recombinant BChE production emerged to address limitations in sourcing native human BChE from blood, which is scarce and carries contamination risks. Using genetic engineering, the BCHE gene is expressed in heterologous systems like Chinese hamster ovary (CHO) cells, Escherichia coli, or plant-based platforms. Mammalian systems are preferred for producing glycosylated, bioactive forms, while prokaryotic systems enable cost-effective production of non-glycosylated variants for structural studies or biosensor applications.
Recombinant BChE has gained attention for its therapeutic potential. It serves as a bioscavenger against organophosphate poisoning by irreversibly binding to nerve agents before they inhibit AChE. It also detoxifies cocaine overdose and prolongs the effects of neuromuscular-blocking drugs. Additionally, altered BChE activity is linked to neurodegenerative diseases like Alzheimer’s, spurring research into its role in amyloid-beta metabolism.
Challenges remain in scaling production and maintaining enzyme stability. Advances in protein engineering, such as PEGylation or fusion proteins, aim to enhance its pharmacokinetics. Overall, recombinant BChE represents a promising tool for drug development, detoxification therapies, and understanding neurological disorders, bridging biochemistry with clinical innovation.
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