| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | patZ |
| Uniprot No | P76594 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 724-886aa |
| 氨基酸序列 | ERCLFRPILPEDEPQLQQFISRVTKEDLYYRYFSEINEFTHEDLANMTQIDYDREMAFVAVRRIDQTEEILGVTRAISDPDNIDAEFAVLVRSDLKGLGLGRRLMEKLITYTRDHGLQRLNGITMPNNRGMVALARKLGFNVDIQLEEGIVGLTLNLAQREES |
| 预测分子量 | 26.3 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patZ重组蛋白的虚构参考文献示例(仅供参考)：
1. **文献名称**：Functional Characterization of Recombinant patZ Protein in Bacillus subtilis
**作者**：Smith J, et al.
**摘要**：研究通过大肠杆菌表达系统成功纯化patZ重组蛋白，并验证其在枯草芽孢杆菌孢子形成中的调控作用，揭示了其与转录因子相互作用的分子机制。
2. **文献名称**：Optimization of patZ Expression in E. coli for Industrial Enzyme Production
**作者**：Li X, Wang Y.
**摘要**：报道通过启动子优化和密码子改造提高patZ基因在大肠杆菌中的表达效率，重组蛋白产量提升3倍，为工业化应用奠定基础。
3. **文献名称**：Crystal Structure Analysis of patZ Recombinant Protein Reveals ATP-Binding Motifs
**作者**：Tanaka K, et al.
**摘要**：首次解析patZ重组蛋白的晶体结构，发现其N端存在保守的ATP结合域，突变实验证实该区域对蛋白的催化活性至关重要。
注：以上文献为模拟内容，实际研究中请通过学术数据库(如PubMed、Google Scholar)检索具体文献。
PatZ, a bacterial cell division regulatory protein, has garnered significant attention in molecular microbiology due to its role in modulating the assembly and positioning of the divisome machinery. Originally identified in *Escherichia coli*, PatZ (also termed YgfA) functions as a negative regulator of FtsZ, a tubulin-like protein essential for initiating cytokinesis. PatZ interacts with FtsZ protofilaments, delaying their polymerization and preventing premature septum formation. This regulatory mechanism ensures precise spatiotemporal control over cell division, particularly under stress conditions, thereby maintaining cell viability and genomic stability.
The production of recombinant PatZ protein leverages genetic engineering to express and purify the protein in heterologous systems, typically *E. coli*. The patZ gene is cloned into expression vectors under inducible promoters (e.g., T7 or lacUV5), enabling controlled overexpression. Affinity tags, such as polyhistidine (His-tag) or glutathione-S-transferase (GST), are often fused to PatZ to facilitate purification via nickel or glutathione affinity chromatography. Subsequent steps may include cleavage of the fusion tag and further purification using size-exclusion or ion-exchange chromatography to obtain high-purity, bioactive PatZ.
Recombinant PatZ serves as a critical tool for *in vitro* studies, including structural analysis (e.g., X-ray crystallography, cryo-EM), biochemical assays to dissect FtsZ interaction dynamics, and high-throughput screening for antimicrobial agents targeting cell division. Its role in bacterial cytokinesis makes it a potential target for novel antibiotics, especially amid rising antimicrobial resistance. However, challenges persist in optimizing solubility and stability during recombinant production, often necessitating buffer optimization or co-expression with chaperones. Ongoing research aims to elucidate PatZ's regulatory networks and exploit its mechanistic insights for therapeutic development.
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