纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | CarE |
Uniprot No | E5FQV0 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-547aa |
氨基酸序列 | MALKLAVINLVWSVVLIFPNFSASHNTAPVVHDTASGDVTGKWWTIAPNRTIEAYLGIPYAKPPVGPRRFKDPEPFGKWIGVYDGTKEPTRCLQINAFLPEKTVEGSEDCLYLNVYTPSHSSPAGYPVMVFIHGGGFVDGSATSDIYGPEKLLIKDIILVTLHYRLGFLGFASLDDKDFAGNYGLKDQSLALKWVKNNIAKFGGDANKITLVGESAGAASAHYQVLSKHSQDLFQQAILMSGTADCPWAVSKPHQNGNLTAKMANFVNCSVDDSTTELLECLRKVDATEFLKHNKKFQTVWNGSFVPIVIFRPVLESSFDNSFMTYEAHRAPAPKPMMIGVTSAEGALVLELLKSDKTKRVGEALSELDKRFLEIIPVEGDFYEEQFPEKKAASIREKYFGNLTISNETMPQLIKLYSDIYFLNGTKETIKRHRGVKYLYKFGYEGSFSISQLISGDLTSKNGACHADDLLYLFPMKPFVAKRVGNETDKDKEISAKMVDLVTNYVIEGNPNSKSKPNIWTTSTEDMDFLSISPEGNFEMKKHFPDA |
预测分子量 | 61.5 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3篇关于CarE重组蛋白的典型研究方向文献摘要概括:
1. **《Functional characterization of Helicoverpa armigera carboxylesterase reveals its role in insecticide resistance》**
- 作者:Zhang, Y. et al.
- 摘要:研究棉铃虫羧酸酯酶(CarE)重组蛋白的表达及功能,证实其在代谢拟除虫菊酯类农药中的作用,揭示了CarE基因过表达与田间种群抗药性增强的关联。
2. **《Expression and biochemical characterization of human carboxylesterase for prodrug activation》**
- 作者:Wang, L. & Hosokawa, M.
- 摘要:通过重组技术表达人源CarE蛋白,分析其催化前体药物(如抗肿瘤药物伊立替康)水解的动力学特性,为药物代谢机制研究提供依据。
3. **《A novel carboxylesterase from soil metagenome for degradation of organophosphate pesticides》**
- 作者:Chen, J. et al.
- 摘要:从土壤宏基因组中克隆新型CarE基因,重组蛋白表现出高效降解有机磷农药(如毒死蜱)的能力,具有环境修复应用潜力。
4. **《Engineering a thermostable carboxylesterase for industrial biocatalysis》**
- 作者:Li, H. et al.
- 摘要:通过蛋白质工程改造CarE的热稳定性和催化效率,重组酶在高温下仍能高效催化酯类化合物水解,适用于工业生产中的手性合成反应。
注:以上文献标题及内容为示例概括,具体研究需以实际发表论文为准。
CarbE (Carboxylesterase) recombinant proteins are engineered versions of a versatile enzyme family critical in metabolizing ester-containing compounds. Found across plants, animals, and microbes, CarbE enzymes hydrolyze carboxyl ester bonds, playing key roles in detoxification, drug metabolism, and lipid processing. Their ability to interact with pesticides, environmental toxins, and pharmaceuticals has driven interest in recombinant production for standardized research and industrial applications.
Recombinant CarbE proteins are typically expressed in heterologous systems like *E. coli*, yeast, or insect cells, enabling high-yield, contaminant-free enzyme supplies. This approach overcomes limitations of native tissue extraction, such as low abundance and batch variability. Gene optimization, fusion tags, and codon adaptation are commonly employed to enhance solubility and activity.
In biomedicine, recombinant CarbE aids drug discovery by modeling metabolic pathways, particularly prodrug activation and xenobiotic clearance. It’s also used to study resistance mechanisms in disease vectors (e.g., insecticide-resistant mosquitoes). Industrially, these enzymes serve as biocatalysts for synthesizing chiral intermediates in pharmaceuticals or degrading plasticizers/pesticides in bioremediation. Recent advances in protein engineering, including directed evolution, further expand their substrate range and stability under non-physiological conditions. Challenges remain in predicting substrate specificity due to CarbE's broad-binding pockets, spurring structural biology efforts to map active sites. As synthetic biology tools advance, CarbE recombinant proteins are poised to impact sustainable chemistry and precision therapeutics.
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