| 纯度 | > 95 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | CALB2 |
| Uniprot No | P22676 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-271aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MAGPQQQPPY LHLAELTASQ FLEIWKHFDA DGNGYIEGKE LENFFQELEK ARKGSGMMSK SDNFGEKMKE FMQKYDKNSD GKIEMAELAQ ILPTEENFLL CFRQHVGSST EFMEAWRKYD TDRSGYIEAN ELKGFLSDLL KKANRPYDEP KLQEYTQTIL RMFDLNGDGK LGLSEMSRLL PVQENFLLKF QGMKLTSEEF NAIFTFYDKD RSGYIDEHEL DALLKDLYEK NKKEMNIQQL TNYRKSVMSL AEAGKLYRKD LEIVLCSEPP M |
| 预测分子量 | 34 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CALB2重组蛋白的3篇参考文献示例(注：文献信息为模拟生成，仅供参考)：
1. **文献名称**：Expression and Purification of Recombinant Human CALB2 in Escherichia coli
**作者**：Zhang Y, et al.
**摘要**：研究利用大肠杆菌系统高效表达CALB2重组蛋白，优化了诱导条件与纯化工艺，通过His标签亲和层析获得高纯度蛋白，适用于后续功能研究。
2. **文献名称**：Structural Characterization of CALB2 by X-ray Crystallography
**作者**：Li H, Wang T.
**摘要**：解析了重组CALB2蛋白的晶体结构，揭示其钙离子结合域的关键氨基酸残基，为探究其神经保护机制提供结构基础。
3. **文献名称**：CALB2 Recombinant Protein Attenuates Neurodegeneration in Cellular Models
**作者**：Smith J, et al.
**摘要**：通过体外实验验证重组CALB2蛋白对神经元氧化应激损伤的保护作用，表明其可能通过调控钙信号通路延缓神经退行性疾病进程。
4. **文献名称**：High-Yield Production of CALB2 in Mammalian Cells for Functional Assays
**作者**：Chen L, et al.
**摘要**：采用哺乳动物细胞表达系统制备重组CALB2.验证其翻译后修饰及生物活性，为疾病相关分子机制研究提供工具蛋白。
(实际文献请通过PubMed或Web of Science以关键词“CALB2 recombinant protein”检索获取。)
**Background of CALB2 Recombinant Protein**
Carboxylesterase 2 (CALB2), also known as CES2. is a serine hydrolase enzyme belonging to the carboxylesterase family. It plays a critical role in metabolizing endogenous esters, amides, and thioesters, as well as xenobiotics, including prodrugs and environmental toxins. CALB2 is expressed in various tissues, notably the liver, intestines, and kidneys, where it contributes to lipid homeostasis, drug detoxification, and bioactivation. Its substrate versatility and high catalytic efficiency make it a valuable target for pharmaceutical and biotechnological applications.
The recombinant CALB2 protein is produced via genetic engineering, typically using microbial expression systems like *E. coli* or yeast. This approach ensures high purity, scalability, and consistency, overcoming limitations of native tissue extraction. Recombinant CALB2 retains the enzymatic activity of its natural counterpart, enabling its use in *in vitro* studies, drug discovery, and industrial biocatalysis.
In research, CALB2 is employed to investigate metabolic pathways, enzyme kinetics, and inhibitor screening. Industrially, it serves as a green catalyst in organic synthesis, particularly for producing chiral intermediates in pharmaceuticals, agrochemicals, and fine chemicals. Its ability to perform enantioselective reactions under mild conditions aligns with sustainable chemistry goals.
Structural studies of CALB2 have elucidated its catalytic mechanism, involving a serine-histidine-glutamate triad and a hydrophobic substrate-binding pocket. Engineering efforts, such as directed evolution or rational design, aim to enhance its stability, substrate range, or stereoselectivity for tailored applications.
Overall, CALB2 recombinant protein bridges fundamental biochemistry and applied biotechnology, offering tools for advancing therapeutic development and eco-friendly manufacturing processes.
×
