| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | bepA |
| Uniprot No | P66948 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 28-487aa |
| 氨基酸序列 | DSADTLPDMGTSAGSTLSIGQEMQMGDYYVRQLRGSAPLINDPLLTQYINSLGMRLVSHANSVKTPFHFFLINNDEINAFAFFGGNVVLHSALFRYSDNESQLASVMAHEISHVTQRHLARAMEDQQRSAPLTWVGALGSILLAMASPQAGMAALTGTLAGTRQGMISFTQQNEQEADRIGIQVLQRSGFDPQAMPTFLEKLLDQARYSSRPPEILLTHPLPESRLADARNRANQMRPMVVQSSEDFYLAKARTLGMYNSGRNQLTSDLLDEWAKGNVRQQRAAQYGRALQAMEANKYDEARKTLQPLLAAEPGNAWYLDLATDIDLGQNKANEAINRLKNARDLRTNPVLQLNLANAYLQGGQPQEAANILNRYTFNNKDDSNGWDLLAQAEAALNNRDQELAARAEGYALAGRLDQAISLLSSASSQVKLGSLQQARYDARIDQLRQLQERFKPYTKM |
| 预测分子量 | 58.5 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BepA重组蛋白的假设性参考文献(基于常见研究方向，具体文献需核实)：
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1. **文献名称**: *BepA acts as a protease and chaperone in the β-barrel assembly machinery of Escherichia coli*
**作者**: Hizukuri, Y., et al.
**摘要**: 研究揭示BepA在大肠杆菌中具有蛋白酶和分子伴侣双重功能，参与外膜β-桶状蛋白(如OmpA)的正确折叠与质量控制。重组BepA实验表明其通过ATP依赖的蛋白酶活性降解错误折叠蛋白，同时协助膜蛋白组装。
2. **文献名称**: *Structural insights into the bifunctional mechanism of BepA in bacterial outer membrane biogenesis*
**作者**: Tanaka, S., et al.
**摘要**: 通过X射线晶体学解析重组BepA蛋白的三维结构，发现其N端为蛋白酶结构域，C端为底物结合域。该结构解释了BepA如何协同蛋白酶活性和分子伴侣功能维持外膜稳态。
3. **文献名称**: *BepA deletion enhances antibiotic susceptibility in Gram-negative bacteria*
**作者**: Li, X., et al.
**摘要**: 研究显示，敲除bepA基因导致大肠杆菌外膜完整性受损，对庆大霉素等抗生素敏感性显著增加。重组BepA蛋白的体外回补实验证实其通过维持膜蛋白稳定性参与抗生素抗性。
4. **文献名称**: *ATP-dependent protease activity of recombinant BepA: A kinetic analysis*
**作者**: Müller, J., et al.
**摘要**: 在大肠杆菌中表达并纯化重组BepA蛋白，测定其ATP酶活性和底物降解动力学，发现BepA对错误折叠的OMP底物具有特异性切割能力，且活性依赖金属离子辅因子。
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**注**：以上为模拟文献，实际文献需通过PubMed、Google Scholar等平台检索关键词“BepA recombinant protein”或“BepA function”获取。真实文献可能涉及以下研究方向：细菌外膜蛋白组装、蛋白酶-分子伴侣双功能机制、抗生素耐药性等。
**Background of BepA Recombinant Protein**
BepA is a bacterial protease originally identified in *Escherichia coli* as a bifunctional enzyme involved in both quality control of outer membrane proteins (OMPs) and degradation of misfolded β-barrel assembly machinery (BAM) components. It plays a critical role in maintaining outer membrane integrity by selectively removing misassembled OMPs or damaged BAM complexes, thereby ensuring proper membrane biogenesis and bacterial survival under stress conditions. Structurally, BepA belongs to the M48 metalloprotease family, characterized by a conserved zinc-binding motif, and it exhibits both chaperone-like and proteolytic activities.
The recombinant BepA protein is engineered for *in vitro* studies to dissect its dual enzymatic functions and substrate specificity. By expressing BepA in heterologous systems (e.g., *E. coli*), researchers produce purified, active forms of the protein for structural analysis (e.g., crystallography) and biochemical assays. These studies have revealed that BepA interacts with BAM complex subunits, such as BamA, and cleaves specific substrates in a regulated manner.
Interest in BepA also stems from its potential as a therapeutic target. Inhibiting BepA could disrupt bacterial membrane homeostasis, sensitizing pathogens to antibiotics. Additionally, its unique mechanism of coupling chaperone and protease activities provides insights into protein quality control systems, which are conserved across prokaryotes and eukaryotes. Current research focuses on elucidating BepA's regulatory networks, its role in antibiotic resistance, and its application in synthetic biology for engineering stress-resistant bacterial strains. Overall, BepA recombinant protein serves as a vital tool for advancing both basic microbiology and translational drug discovery.
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