| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | degP |
| Uniprot No | P0C0V0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 27-474aa |
| 氨基酸序列 | AETSSATTAQQMPSLAPMLEKVMPSVVSINVEGSTTVNTPRMPRNFQQFFGDDSPFCQEGSPFQSSPFCQGGQGGNGGGQQQKFMALGSGVIIDADKGYVVTNNHVVDNATVIKVQLSDGRKFDAKMVGKDPRSDIALIQIQNPKNLTAIKMADSDALRVGDYTVAIGNPFGLGETVTSGIVSALGRSGLNAENYENFIQTDAAINRGNSGGALVNLNGELIGINTAILAPDGGNIGIGFAIPSNMVKNLTSQMVEYGQVKRGELGIMGTELNSELAKAMKVDAQRGAFVSQVLPNSSAAKAGIKAGDVITSLNGKPISSFAALRAQVGTMPVGSKLTLGLLRDGKQVNVNLELQQSSQNQVDSSSIFNGIEGAEMSNKGKDQGVVVNNVKTGTPAAQIGLKKGDVIIGANQQAVKNIAELRKVLDSKPSVLALNIQRGDSTIYLLMQ |
| 预测分子量 | 48.8 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 **DegP(HtrA)重组蛋白**的3篇参考文献及其摘要概述：
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1. **文献名称**：*Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine*
**作者**：Spiess, C., Beil, A., & Ehrmann, M.
**摘要**：该研究解析了DegP的晶体结构，揭示了其作为蛋白酶和分子伴侣的双重功能。DegP通过形成动态的六聚体结构，在应激条件下选择性降解错误折叠蛋白或辅助其正确折叠，结构中的PDZ结构域对底物识别至关重要。
2. **文献名称**：*Structural basis for regulated protease and chaperone activity of DegP*
**作者**：Krojer, T., et al.
**摘要**：本文通过结构生物学手段，阐明了DegP的变构调控机制。其活性通过pH和底物结合触发，PDZ结构域与蛋白酶结构域的协同作用使DegP能切换“伴侣”与“降解”模式，调控依赖于错误折叠蛋白的累积状态。
3. **文献名称**：*Role of DegP in the elimination of misfolded proteins in Escherichia coli*
**作者**：Iwanczyk, M., et al.
**摘要**：研究利用重组DegP蛋白，证明其在高温或氧化应激下通过形成多聚体复合物清除大肠杆菌内错误折叠蛋白。敲除DegP导致细胞内蛋白聚集，证实其在维持蛋白质稳态中的关键作用。
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以上文献涵盖DegP的结构机制、功能调控及生理作用，均为该领域的经典研究。如需具体期刊或年份信息，可进一步补充查询。
DegP, also known as HtrA (High-temperature requirement A), is a bifunctional protease and chaperone protein originally identified in *Escherichia coli*. It plays a critical role in bacterial stress responses by degrading misfolded proteins or assisting in their refolding under conditions such as heat shock, oxidative stress, or envelope protein dysregulation. Structurally, DegP consists of a trypsin-like protease domain and two PDZ domains that regulate substrate recognition and oligomerization. Its activity is tightly controlled through temperature-dependent conformational changes, transitioning from chaperone-like hexamers at lower temperatures to proteolytically active 12- or 24-mers under stress.
Recombinant DegP (rDegP) is engineered for overexpression and purification in heterologous systems like *E. coli*. This allows detailed study of its dual enzymatic functions, substrate specificity, and structural dynamics. Research highlights its role in bacterial pathogenesis, as DegP homologs in pathogens (e.g., *Salmonella*, *Helicobacter pylori*) contribute to virulence by degrading host defense proteins or maintaining envelope integrity. Biotechnological applications exploit rDegP’s ability to degrade aggregation-prone proteins during recombinant protein production, enhancing yield and purity. Additionally, its stress-responsive properties inspire synthetic biology designs for protein quality control systems. However, uncontrolled proteolysis by DegP can complicate bioprocessing, driving studies on regulatory mechanisms like allosteric PDZ domain interactions. Current efforts also target DegP as a therapeutic candidate, with inhibitors under investigation to disrupt bacterial survival mechanisms. Overall, rDegP serves as a versatile tool for probing bacterial stress adaptation while offering industrial and medical potential.
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