| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | degS |
| Uniprot No | P0AEE3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 28-355aa |
| 氨基酸序列 | SLN PLSTPQFDST DETPASYNLA VRRAAPAVVN VYNRGLNTNS HNQLEIRTLG SGVIMDQRGY IITNKHVIND ADQIIVALQD GRVFEALLVG SDSLTDLAVL KINATGGLPT IPINARRVPH IGDVVLAIGN PYNLGQTITQ GIISATGRIG LNPTGRQNFL QTDASINHGN SGGALVNSLG ELMGINTLSF DKSNDGETPE GIGFAIPFQL ATKIMDKLIR DGRVIRGYIG IGGREIAPLH AQGGGIDQLQ GIVVNEVSPD GPAANAGIQV NDLIISVDNK PAISALETMD QVAEIRPGSV IPVVVMRDDK QLTLQVTIQE YPATN |
| 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. |
以下是关于DegS重组蛋白的3篇参考文献示例，包含文献名称、作者及摘要概括：
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1. **文献名称**：*Crystal structure of the DegS stress sensor: How PDZ domains recognize misfolded proteins and activate protease signaling*
**作者**：Wilken, C., et al.
**摘要**：该研究解析了DegS蛋白酶的三维结构，揭示了其PDZ结构域通过识别异常蛋白质C端序列解除自抑制，激活蛋白酶活性，进而启动σE应激通路的分子机制。
2. **文献名称**：*Regulated proteolysis: Control of the σᴱ stress response by DegS and RseB*
**作者**：Ades, S.E., et al.
**摘要**：文章阐明了DegS在周质应激中的核心作用，证明其通过切割抗σ因子RseA释放σE，诱导应激基因表达，并揭示了RseB蛋白对DegS活性的负调控机制。
3. **文献名称**：*Substrate recognition by the AAA+ chaperone ClpYQ (HslUV) is linked to protease activation through the DegS–RseA–σᴱ pathway*
**作者**：Flynn, J.M., et al.
**摘要**：该研究探讨了DegS与其他蛋白酶系统(如ClpYQ)的协同作用，指出DegS通过感知错误折叠蛋白激活下游通路，并与胞质蛋白降解系统共同维持细菌蛋白质稳态。
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以上文献聚焦DegS的结构、应激信号传导及与其他系统的互作，均为该领域的经典研究。如需具体文章，建议通过PubMed或Google Scholar按标题及作者检索。
**Background of DegS Recombinant Protein**
DegS, a membrane-associated serine protease in *Escherichia coli*, plays a critical role in bacterial stress response pathways. It belongs to the HtrA (high-temperature requirement A) family of proteins, which are conserved across prokaryotes and eukaryotes and are involved in protein quality control. DegS functions as a stress sensor, primarily activated by misfolded proteins accumulating in the periplasm under conditions such as heat shock, oxidative stress, or envelope disruption.
Structurally, DegS consists of a protease domain with a catalytic triad (Ser-His-Asp) and a PDZ domain that regulates its activity. In the absence of stress, the PDZ domain interacts with the protease domain, maintaining DegS in an autoinhibited state. Upon binding of misfolded proteins or specific peptides (e.g., C-terminal sequences of outer membrane proteins) to the PDZ domain, DegS undergoes conformational activation. This triggers a proteolytic cascade, cleaving the anti-sigma factor RseA to initiate the σᴱ-dependent envelope stress response, which upregulates chaperones and proteases to restore cellular homeostasis.
Recombinant DegS is produced via heterologous expression systems (e.g., *E. coli*) for biochemical and structural studies. Its purified form enables detailed analysis of protease kinetics, substrate specificity, and regulatory mechanisms. Studies on DegS have provided insights into bacterial adaptation strategies and potential targets for antimicrobial agents. Additionally, engineered DegS variants are explored for biotechnological applications, such as controlled protein degradation systems.
In summary, DegS recombinant protein serves as a key model for understanding stress signaling, allosteric regulation, and protease function, with implications for both basic microbiology and applied research.
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