纯度 | >90%SDS-PAGE. |
种属 | E.coli |
靶点 | albA |
Uniprot No | Q8TZV1 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-93aa |
氨基酸序列 | MAEEHVVYIGKKPVMNYVLAVITQFNEGAKEVSIKARGRAISRAVDVAEIVRNRFLKDTVDIKEIKIGTEELPTADGRTTNTSTIEIVLERKV |
预测分子量 | 26.4 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albA重组蛋白的3篇示例参考文献(注:文献信息为示例性概括,实际引用需根据真实文献调整):
1. **《Functional characterization of the albA gene in biofilm formation》**
- 作者:Branda, S.S. et al.
- 摘要:研究通过重组表达albA蛋白,证实其在枯草芽孢杆菌生物膜形成中的关键作用,缺失albA导致生物膜结构异常,表明其参与胞外基质组装。
2. **《Structural analysis of recombinant AlbA protein from Bacillus subtilis》**
- 作者:Ostrowsky, A. et al.
- 摘要:利用大肠杆菌系统重组表达albA蛋白,通过X射线晶体学解析其三维结构,揭示其独特的β-螺旋折叠模式,为理解其结合疏水分子功能提供结构基础。
3. **《AlbA as a surfactant protein: Applications in microbial enhanced oil recovery》**
- 作者:Kobayashi, K. et al.
- 摘要:评估重组albA蛋白的乳化活性,证明其能稳定油水界面,在石油生物修复和工业乳化剂开发中具潜在应用价值。
提示:上述内容为模拟文献,建议通过PubMed或Web of Science检索真实研究。
AlbA recombinant protein is derived from the AlbA protein, originally identified in *Staphylococcus aureus*, a Gram-positive bacterium associated with opportunistic infections. AlbA, part of the microbial surface components recognizing adhesive matrix molecules (MSCRAMMs) family, plays a role in bacterial adhesion, biofilm formation, and immune evasion. It binds to host proteins like IgG, contributing to pathogenicity by interfering with immune responses.
The recombinant form of AlbA is produced using genetic engineering techniques, typically through heterologous expression in *E. coli* or other host systems. The gene encoding AlbA is cloned into expression vectors, allowing large-scale production and purification. Recombinant AlbA retains functional domains critical for ligand interactions, enabling studies on its structural properties, adhesion mechanisms, and role in bacterial virulence.
Research on AlbA recombinant protein focuses on understanding *S. aureus* pathogenesis, particularly biofilm-related infections and immune evasion strategies. It serves as a tool for developing therapeutic agents, such as antibodies or inhibitors targeting AlbA-mediated adhesion, and vaccines to block bacterial colonization. Additionally, it aids in diagnostic applications, including antibody detection in infected hosts.
Recent studies also explore AlbA’s potential in nanotechnology due to its self-assembling properties. Its recombinant form offers a controlled model for investigating host-pathogen interactions and designing anti-biofilm therapies. Overall, AlbA recombinant protein is a valuable resource in microbiology, immunology, and biomedical engineering.
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