| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | catA |
| Uniprot No | P07773 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-311aa |
| 氨基酸序列 | MEVKIFNTQDVQDFLRVASGLEQEGGNPRVKQIIHRVLSDLYKAIEDLNITSDEYWAGVAYLNQLGANQEAGLLSPGLGFDHYLDMRMDAEDAALGIENATPRTIEGPLYVAGAPESVGYARMDDGSDPNGHTLILHGTIFDADGKPLPNAKVEIWHANTKGFYSHFDPTGEQQAFNMRRSIITDENGQYRVRTILPAGYGCPPEGPTQQLLNQLGRHGNRPAHIHYFVSADGHRKLTTQINVAGDPYTYDDFAYATREGLVVDAVEHTDPEAIKANDVEGPFAEMVFDLKLTRLVDGVDNQVVDRPRLAV |
| 预测分子量 | 50.3 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CatA重组蛋白研究的模拟参考文献示例(注：CatA为假设蛋白名称，实际文献需根据具体研究领域检索)：
1. **《Heterologous Expression and Characterization of Recombinant CatA Protein in E. coli》**
- 作者：Zhang L., et al.
- 摘要：研究利用大肠杆菌系统表达CatA重组蛋白，优化诱导条件并采用镍柱亲和层析纯化，证实重组蛋白具有酶活性，可用于后续功能研究。
2. **《Structural Analysis of CatA Recombinant Protein and Its Role in Oxidative Stress Response》**
- 作者：Wang Y., et al.
- 摘要：解析CatA重组蛋白的晶体结构，揭示其通过清除活性氧(ROS)调控氧化应激的分子机制，为抗氧化治疗提供理论依据。
3. **《High-Yield Production of CatA in Pichia pastoris and Its Application in Industrial Biocatalysis》**
- 作者：Kim S., et al.
- 摘要：在毕赤酵母中实现CatA的高效分泌表达，纯化蛋白在高温和极端pH条件下保持稳定性，展示其在工业生物催化中的潜力。
4. **《Functional Characterization of Recombinant CatA in Plant Pathogen Resistance》**
- 作者：Fernández R., et al.
- 摘要：证实植物病原体中的CatA重组蛋白可通过降解宿主防御分子增强致病性，为抗病基因工程提供新靶点。
**提示**：若CatA为特定领域蛋白(如过氧化氢酶变体或病原体抗原)，建议结合具体研究背景使用PubMed或Google Scholar检索准确文献，或检查蛋白名称拼写一致性。
**Background of Recomcombinant catA Protein**
Recombinant catA protein, a genetically engineered variant of the native catA enzyme, has garnered significant attention in biochemical and biotechnological research due to its versatile applications and enhanced production efficiency. The native catA, typically derived from microbial or eukaryotic sources, belongs to a class of enzymes involved in critical metabolic pathways, such as detoxification, substrate modification, or signaling. Its recombinant form is synthesized by cloning the catA gene into expression vectors (e.g., plasmid systems), followed by heterologous expression in host organisms like *Escherichia coli*, yeast, or mammalian cell lines. This approach allows scalable production, improved purity, and customization (e.g., affinity tags for purification).
Structurally, catA often features conserved catalytic domains or binding motifs essential for its enzymatic activity. Recombinant technology enables site-directed mutagenesis to optimize stability, substrate specificity, or thermotolerance, broadening its utility. For instance, engineered catA variants are explored in industrial biocatalysis for synthesizing fine chemicals, pharmaceuticals, or bioremediation agents. In therapeutic contexts, recombinant catA may serve as a therapeutic enzyme replacement or a diagnostic biomarker in diseases linked to enzymatic deficiencies.
Quality control during production involves techniques like SDS-PAGE, Western blotting, and activity assays to confirm fidelity. Challenges include minimizing inclusion body formation in prokaryotic hosts or ensuring post-translational modifications in eukaryotic systems. Despite these hurdles, recombinant catA exemplifies the synergy between protein engineering and industrial demand, offering a sustainable alternative to traditional enzyme extraction methods. Ongoing research focuses on CRISPR-based optimization and AI-driven design to further enhance its functional repertoire, positioning recombinant catA as a pivotal tool in modern biotechnology.
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