| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CMBL |
| Uniprot No | Q96DG6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-245aa |
| 氨基酸序列 | ANEAYPCPC DIGHRLEYGG LGREVQVEHI KAYVTKSPVD AGKAVIVIQD IFGWQLPNTR YIADMISGNG YTTIVPDFFV GQEPWDPSGD WSIFPEWLKT RNAQKIDREI SAILKYLKQQ CHAQKIGIVG FCWGGTAVHH LMMKYSEFRA GVSVYGIVKD SEDIYNLKNP TLFIFAENDV VIPLKDVSLL TQKLKEHCKV EYQIKTFSGQ THGFVHRKRE DCSPADKPYI DEARRNLIEW LNKYM |
| 预测分子量 | 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CMBL(羧甲基纤维素酶)重组蛋白的3篇代表性文献示例，涵盖不同研究方向：
1. **文献名称**: "Heterologous Expression and Characterization of a Novel Carboxymethylcellulase (CMBL) from Thermophilic Bacteria in E. coli"
**作者**: Zhang Y., et al. (2021)
**摘要**: 本研究从嗜热菌中克隆了CMBL基因，并成功在大肠杆菌中实现可溶性表达。纯化后的重组酶在70℃下表现出最高活性，且对羧甲基纤维素底物具有高特异性，适用于生物燃料生产中的高温降解工艺。
2. **文献名称**: "Optimization of CMBL Production in Pichia pastoris and Its Application in Textile Bio-polishing"
**作者**: Lee S., Kim J. (2020)
**摘要**: 通过优化毕赤酵母表达系统的培养条件(如pH、温度、甲醇诱导策略)，显著提高了CMBL重组蛋白的产量。实验证明，该酶能有效去除棉织物表面的纤维绒毛，在纺织工业中展现出环保型生物抛光潜力。
3. **文献名称**: "Structural Insights into CMBL from Marine Microbes: A Molecular Dynamics Study"
**作者**: Wang X., et al. (2022)
**摘要**: 结合X射线晶体学与分子模拟，解析了海洋来源CMBL的三维结构，揭示了其底物结合口袋中关键氨基酸残基(Asp156/Glu189)的催化机制，为理性设计耐盐性纤维素酶提供了理论依据。
注：以上文献为示例性内容，实际研究中需根据具体实验需求检索真实文献(可通过PubMed/Web of Science以关键词"recombinant CMBL"或"carboxymethylcellulase expression"查询最新研究)。
CMBL (Carboxymethylenebutenolidase Homolog) recombinant protein is a genetically engineered version of the CMBL enzyme, derived from its natural homolog found in various organisms, including humans. The native CMBL enzyme belongs to the amidase family and plays a role in hydrolyzing cyclic metabolites, particularly endogenous compounds like lactoylglutathione and methylglyoxal derivatives, which are linked to cellular stress and detoxification pathways. Its activity is associated with metabolic regulation, redox balance, and potential roles in mitigating oxidative damage.
Recombinant CMBL is produced using biotechnological systems, such as *E. coli*, yeast, or mammalian cell cultures, to ensure high purity and scalability. This approach allows researchers to study the enzyme's structure-function relationships, substrate specificity, and catalytic mechanisms in controlled settings. Interest in CMBL stems from its implication in metabolic disorders, aging-related diseases, and detoxification processes. For instance, it may influence pathways relevant to diabetes, neurodegenerative conditions, or drug metabolism.
The recombinant form enables precise biochemical assays, drug discovery screens, and structural studies (e.g., X-ray crystallography) to explore therapeutic targeting. Its production often involves codon optimization for expression efficiency, fusion tags for purification, and validation via enzymatic activity assays. Current research focuses on elucidating its physiological roles, interactions with cellular metabolites, and potential as a biomarker or therapeutic agent. By providing a standardized, abundant protein source, recombinant CMBL accelerates both basic science and translational applications in metabolic health and disease.
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