| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | ompT |
| Uniprot No | P09169 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-317aa |
| 氨基酸序列 | STETLSFTPDNINADISLGTLSGKTKERVYLAEEGGRKVSQLDWKFNNAAIIKGAINWDLMPQISIGAAGWTTLGSRGGNMVDQDWMDSSNPGTWTDESRHPDTQLNYANEFDLNIKGWLLNEPNYRLGLMAGYQESRYSFTARGGSYIYSSEEGFRDDIGSFPNGERAIGYKQRFKMPYIGLTGSYRYEDFELGGTFKYSGWVESSDNDEHYDPGKRITYRSKVKDQNYYSVAVNAGYYVTPNAKVYVEGAWNRVTNKKGNTSLYDHNNNTSDYSKNGAGIENYNFITTAGLKYTF |
| 预测分子量 | 37.5 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3篇与ompT重组蛋白相关的文献及其摘要概要：
1. **《Role of the Escherichia coli OmpT protease in protein degradation during recombinant protein production》**
- 作者：Kramer, R.A., et al.
- 摘要：研究大肠杆菌OmpT蛋白酶在重组蛋白表达过程中的影响，发现OmpT会降解部分外源蛋白，提出通过使用ompT缺陷型宿主菌提高目标蛋白稳定性。
2. **《Cloning and characterization of the ompT gene encoding the outer membrane protease T of Escherichia coli》**
- 作者：Sugimura, K., & Nishihara, T.
- 摘要：报道了ompT基因的克隆与测序，阐明其编码的蛋白酶T的丝氨酸蛋白酶活性，并探讨其在重组蛋白表达中的潜在干扰作用。
3. **《Protease-deficient Escherichia coli strains for protein production》**
- 作者：Dekker, N., et al.
- 摘要：评估多种蛋白酶缺陷型大肠杆菌菌株(包括ΔompT)对重组蛋白产量的影响，证明缺失ompT可显著减少目标蛋白的降解，优化纯化效率。
4. **《Substrate specificity of the OmpT protease: Implications for polyhistidine-tagged protein purification》**
- 作者：Kwon, Y.D., et al.
- 摘要：分析OmpT对聚组氨酸标签蛋白的切割活性，建议在His标签重组蛋白纯化中优先选用ompT突变宿主以避免标签降解。
这些文献涵盖了ompT在重组蛋白生产中的挑战、基因特性、宿主工程优化及纯化策略，可为相关实验设计提供参考。
OmpT is an outer membrane protease originally identified in *Escherichia coli*. Belonging to the omptin family of aspartyl proteases, it plays a role in bacterial pathogenesis by cleaving host defense proteins, such as antimicrobial peptides and plasminogen. Structurally, OmpT is a β-barrel transmembrane protein with a conserved catalytic domain exposed to the extracellular environment. Its enzymatic activity is calcium-dependent and exhibits specificity for cleavage between paired basic residues (e.g., Arg-Arg or Arg-Lys motifs), a feature exploited in biotechnological applications.
Recombinant OmpT refers to the protease produced through genetic engineering, often purified from heterologous expression systems like *E. coli* or yeast. Researchers utilize recombinant OmpT to study its substrate specificity, mechanism of action, and role in bacterial virulence. It has also become a tool in protein engineering, particularly for processing fusion proteins by cleaving at designed sites, enabling the release of target proteins with high precision. However, its presence in *E. coli*-based expression systems can inadvertently degrade recombinant proteins during production, necessitating the use of OmpT-deficient strains for such applications.
In biomedical research, OmpT’s involvement in pathogenicity, including urinary tract infections and sepsis, has made it a potential target for antimicrobial therapies. Studies on recombinant OmpT aim to develop inhibitors that block its proteolytic activity, thereby attenuating bacterial virulence. Additionally, its unique cleavage properties are harnessed in diagnostic assays and synthetic biology for controlled protein processing. Despite its utility, challenges remain in optimizing recombinant OmpT’s stability and activity *in vitro*, driving ongoing research into structural modifications and expression strategies. Overall, OmpT exemplifies how bacterial enzymes can be repurposed as valuable tools in both industrial and therapeutic contexts.
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