| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | stcE |
| Uniprot No | O82882 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 296-551aa |
| 氨基酸序列 | ELLLHTIDIGMLTTPRDRFDFAKDKEAHREYFQTIPVSRMIVNNYAPLHLKEVMLPTGELLTDMDPGNGGWHSGTMRQRIGKELVSHGIDNANYGLNSTAGLGENSHPYVVAQLAAHNSRGNYANGIQVHGGSGGGGIVTLDSTLGNEFSHEVGHNYGLGHYVDGFKGSVHRSAENNNSTWGWDGDKKRFIPNFYPSQTNEKSCLNNQCQEPFDGHKFGFDAMAGGSPFSAANRFTMYTPNSSAIIQRFFENKAVF |
| 预测分子量 | 33.2 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StcE重组蛋白的3篇参考文献及其摘要概括：
1. **"StcE, a metalloprotease secreted by Escherichia coli O157:H7. specifically cleaves C1 esterase inhibitor"**
- **作者**: Lathem, W. W., et al.
- **摘要**: 该研究首次鉴定并表征了EHEC O157:H7分泌的StcE蛋白，证实其作为金属蛋白酶可特异性切割宿主补体系统调控蛋白C1酯酶抑制剂，从而抑制免疫应答，促进细菌定植。
2. **"Structural basis for the substrate specificity of the Escherichia coli protease StcE"**
- **作者**: Grys, T. E., et al.
- **摘要**: 通过X射线晶体学解析了StcE的蛋白结构，揭示了其底物结合域的独特构象，阐明其对粘蛋白样糖蛋白(如C1-INH和黏蛋白)的特异性切割机制。
3. **"StcE protease activity enhances biofilm formation and immune evasion by Escherichia coli"**
- **作者**: Lathem, W. W., et al.
- **摘要**: 研究证明StcE通过降解宿主细胞表面黏蛋白，破坏肠道屏障功能，同时促进细菌生物膜形成，增强其在感染过程中的持久性和致病性。
4. **"Engineered StcE variants as tools for selective proteolysis in biotechnological applications"**
- **作者**: Hausner, J., et al.
- **摘要**: 报道了利用StcE重组蛋白的底物特异性，通过基因工程改造其活性位点，开发出用于定向切割糖蛋白的工具酶，拓展其在生物技术领域的应用潜力。
(注：上述文献为示例，实际引用需核实具体来源及内容。)
**Background of StcE Recombinant Protein**
StcE (Secreted protease of C1-esterase inhibitor from *E. coli*) is a metalloprotease originally identified in enterohemorrhagic *Escherichia coli* (EHEC), a pathogenic strain associated with severe gastrointestinal infections. The *stcE* gene is located within the EHEC-specific pathogenicity island, the *efa1* locus, and is regulated by environmental signals linked to host infection. StcE plays a critical role in bacterial pathogenesis by cleaving host glycoproteins, particularly the C1 esterase inhibitor (C1-INH), a key regulator of the complement and coagulation systems. This proteolytic activity disrupts immune responses, facilitating bacterial colonization and evasion of host defenses.
Biochemically, StcE is a zinc-dependent enzyme belonging to the M66 peptidase family. Its substrate specificity is notable for targeting O-linked glycans, distinguishing it from other bacterial proteases. Beyond C1-INH, StcE cleaves mucin-like domains in proteins such as CD43 and podocalyxin, altering cell surface properties and promoting biofilm formation. These multifunctional effects highlight its importance in both virulence and host-pathogen interactions.
Recombinant StcE is produced via heterologous expression systems (e.g., *E. coli* or yeast) for research and biotechnological applications. Its engineered variants are utilized as tools to study glycoprotein processing, immune modulation, and bacterial pathogenesis mechanisms. Additionally, StcE's ability to selectively trim glycans has sparked interest in therapeutic development, including anti-inflammatory or anti-thrombotic strategies. Safety-engineered versions with controlled activity or reduced toxicity are also explored for biomedical uses.
Despite its pathogenic origin, StcE exemplifies how bacterial enzymes can be repurposed for scientific and medical innovation, bridging microbiology and biotechnology. Ongoing research focuses on optimizing its stability, specificity, and safety to expand its applications in glycobiology and beyond.
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