| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | bamA |
| Uniprot No | P0A940 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 175-424aa |
| 氨基酸序列 | AEIQQINIVGNHAFTTDELISHFQLRDEVPWWNVVGDRKYQKQKLAGDLETLRSYYLDRGYARFNIDSTQVSLTPDKKGIYVTVNITEGDQYKLSGVEVSGNLAGHSAEIEQLTKIEPGELYNGTKVTKMEDDIKKLLGRYGYAYPRVQSMPEINDADKTVKLRVNVDAGNRFYVRKIRFEGNDTSKDAVLRREMRQMEGAWLGSDLVDQGKERLNRLGFFETVDTDTQRVPGSPDQVDVVYKVKERNTG |
| 预测分子量 | 30 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3-4条关于BamA重组蛋白的参考文献及摘要概括：
---
1. **文献名称**：*Structural insight into the biogenesis of β-barrel membrane proteins*
**作者**：Hagan, C.L., et al.
**摘要**：利用重组表达的BamA蛋白，结合冷冻电镜技术解析了细菌BAM复合物的结构，揭示了其在β-桶状外膜蛋白折叠与组装中的构象变化机制。
2. **文献名称**：*Structural basis for outer membrane protein insertion by the BAM complex*
**作者**：Noinaj, N., et al.
**摘要**：通过重组BamA蛋白的晶体结构分析，阐明了BAM复合物通过侧向开口和柔性环区介导外膜蛋白插入的分子机制。
3. **文献名称**：*Reconstitution of outer membrane protein assembly from purified components*
**作者**：Sklar, J.G., et al.
**摘要**：研究利用重组表达的BamA和其他BAM亚基，在体外重构了外膜蛋白装配过程，证明BamA是β-桶结构形成的关键催化组分。
4. **文献名称**：*Protein trafficking to the outer membrane by the bacterial β-barrel assembly machinery*
**作者**：Konovalova, A., et al.
**摘要**：综述中总结了重组BamA在解析BAM复合物功能中的应用，强调了其通过协同作用识别、折叠并整合外膜蛋白的动态过程。
---
以上文献均涉及重组BamA蛋白在结构解析、功能验证或机制研究中的关键作用，涵盖实验与综述类型。
BamA, a central component of the β-barrel assembly machinery (BAM) complex, is essential for the biogenesis of outer membrane proteins (OMPs) in Gram-negative bacteria. As an outer membrane protein itself, BamA facilitates the folding and insertion of β-barrel OMPs into the bacterial outer membrane—a critical process for bacterial viability, envelope integrity, and pathogenicity. Its structure comprises a C-terminal transmembrane β-barrel domain and five N-terminal polypeptide transport-associated (POTRA) domains, which recruit other BAM subunits (e.g., BamB-E) and interact with nascent OMPs. BamA’s mechanism involves conformational changes that drive membrane integration of client proteins, though precise details remain under investigation.
Recombinant BamA proteins are produced via heterologous expression systems (e.g., *E. coli*) for structural and functional studies. These proteins enable research into BAM complex dynamics, OMP assembly mechanisms, and antimicrobial development. Structural studies using X-ray crystallography and cryo-EM have revealed key conformational states, highlighting BamA’s role as a dynamic molecular machine. Its conserved nature across Gram-negative pathogens makes it a promising target for broad-spectrum antibiotics, particularly against multidrug-resistant strains.
Interest in BamA also stems from its potential in disrupting bacterial outer membrane biogenesis. Inhibitors targeting BamA could destabilize membrane integrity, sensitizing bacteria to host defenses or existing drugs. However, challenges include understanding species-specific variations and avoiding off-target effects in commensal bacteria. Recombinant BamA serves as a tool for high-throughput screening of antimicrobial compounds and structure-based drug design. Recent studies explore engineered antibodies and peptides that interfere with BamA function, underscoring its therapeutic relevance. Overall, BamA remains a focal point in combating antibiotic resistance by targeting bacterial membrane assembly pathways.
×
