| 纯度 | >90%SDS-PAGE. |
| 种属 | E. coli |
| 靶点 | metC |
| Uniprot No | P06721 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-392aa |
| 氨基酸序列 | MADKKLDTQLVNAGRSKKYTLGAVNSVIQRASSLVFDSVEAKKHATRNRA NGELFYGRRGTLTHFSLQQAMCELEGGAGCVLFPCGAAAVANSILAFIEQ GDHVLMTNTAYEPSQDFCSKILSKLGVTTSWFDPLIGADIVKHLQPNTKI VFLESPGSITMEVHDVPAIVAAVRSVVPDAIIMIDNTWAAGVLFKALDFG IDVSIQAATKYLVGHSDAMIGTAVCNARCWEQLRENAYLMGQMVDADTAY ITSRGLRTLGVRLRQHHESSLKVAEWLAEHPQVARVNHPALPGSKGHEFW KRDFTGSSGLFSFVLKKKLNNEELANYLDNFSLFSMAYSWGGYESLILAN QPEHIAAIRPQGEIDFSGTLIRLHIGLEDVDDLIADLDAGFA |
| 预测分子量 | 47 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metC重组蛋白的3篇参考文献的简要列举(注：文献信息为模拟示例，非真实存在)：
1. **标题**：Expression and purification of recombinant MetC from *Escherichia coli* for enzymatic characterization
**作者**：Smith A, et al.
**摘要**：研究报道了通过大肠杆菌表达系统克隆并纯化MetC(胱硫醚-β-裂解酶)，优化了诱导条件与纯化步骤，并验证其催化胱硫醚分解为丙酮酸、氨和半胱氨酸的活性。
2. **标题**：Structural analysis of MetC in *Salmonella typhimurium* using recombinant protein technology
**作者**：Lee H, et al.
**摘要**：通过重组蛋白技术获得高纯度沙门氏菌MetC，利用X射线晶体学解析其三维结构，揭示了底物结合位点及催化机制，为抗生素靶点研究提供依据。
3. **标题**：Functional metC gene heterologous expression in *Bacillus subtilis* and its role in methionine biosynthesis
**作者**：Chen L, et al.
**摘要**：将大肠杆菌metC基因异源表达于枯草芽孢杆菌中，证明重组蛋白可恢复甲硫氨酸营养缺陷型菌株的生长能力，阐明其在细菌代谢补偿途径中的应用潜力。
**Background of metC Recombinant Protein**
The *metC* gene encodes cystathionine β-lyase (CBL), a key enzyme in the methionine biosynthesis pathway, primarily in bacteria. This pyridoxal 5'-phosphate (PLP)-dependent enzyme catalyzes the cleavage of cystathionine to produce homocysteine, cysteine, and α-ketobutyrate, linking sulfur metabolism to amino acid synthesis. In *Escherichia coli*, *metC* is part of the *met regulon*, regulated by methionine availability, and is critical for survival under sulfur-limiting conditions.
Recombinant MetC protein is produced via heterologous expression systems, often using *E. coli* as a host. The gene is cloned into expression vectors under inducible promoters (e.g., T7 or lac), allowing controlled overexpression. Post-induction, the protein is purified using affinity chromatography (e.g., His-tag systems) and validated via SDS-PAGE or Western blot.
Studying MetC has biotechnological and medical relevance. It serves as a model for understanding PLP-dependent enzyme mechanisms and microbial sulfur metabolism. Additionally, since methionine biosynthesis is absent in mammals, MetC is explored as a potential antimicrobial target. Inhibitors targeting this enzyme could disrupt bacterial growth without affecting human cells, offering avenues for novel antibiotics.
Structurally, MetC forms homotetramers with conserved active sites. Research has characterized its kinetic properties and substrate specificity, aiding in enzyme engineering for industrial applications, such as biocatalysis in amino acid production. MetC homologs in pathogens (e.g., *Salmonella*, *Staphylococcus*) are also studied for their role in virulence and persistence.
Overall, MetC recombinant protein is a valuable tool for both basic research and applied microbiology, bridging gaps between metabolic studies, drug discovery, and bioprocess optimization.
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