| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | alp1 |
| Uniprot No | P28296 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 102-403aa |
| 氨基酸序列 | EIRKSADVAHVEEDQIWYLDALTTQKGAPWGLGSISHKGQASTDYIYDTSAGAGTYAYVVDSGINVNHVEFESRASLAYNAAGGSHVDSIGHGTHVAGTIGGKTYGVAKKTNLLSVKVFQGESSSTSIILDGFNWAVNDIVSKGRTKKAAINMSLGGGYSYAFNNAVENAFDEGVLSVVAAGNENSDASNTSPASAPNALTVAAINKSNARASFSNYGSVVDIFAPGQDILSAWIGSTTATNTISGTSMATPHIVGLSVYLMGLENLSGPAAVTARIKELATNGVVTNVKGSPNKLAYNGNA |
| 预测分子量 | 38.5 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ALP1重组蛋白的3篇假想参考文献示例(注：ALP1为虚构蛋白名称，实际文献需通过学术数据库查询)：
1. **《Structural characterization of recombinant ALP1 protein from Arabidopsis》**
- 作者：Li, X. et al.
- 摘要：首次报道拟南芥来源的ALP1重组蛋白的晶体结构，揭示其独特的α-螺旋结构域与植物抗逆性的关联。
2. **《ALP1 recombinant protein enhances neuronal regeneration in vitro》**
- 作者：Smith, J. & Patel, R.
- 摘要：证明哺乳动物细胞表达的ALP1重组蛋白通过激活PI3K/AKT通路促进大鼠神经元突触生长，提出其神经修复应用潜力。
3. **《High-yield production of bioactive ALP1 in E. coli expression system》**
- 作者：Kim, S. et al.
- 摘要：优化大肠杆菌表达体系实现ALP1重组蛋白的高效可溶表达，经纯化验证其体外抑制乳腺癌细胞迁移的活性。
(提示：若需真实文献，建议通过PubMed/Google Scholar检索"ALP1 recombinant protein"或结合具体物种/功能关键词查询。)
**Background of ALP1 Recombinant Protein**
ALP1 recombinant protein is a genetically engineered derivative of a native protein, often associated with microbial pathogenesis or cellular signaling. Originating from bacterial species like *Streptococcus mutans*, ALP1 (Antigen L-like Protein 1) belongs to the antigen I/II family, which plays a critical role in bacterial adhesion and biofilm formation. These surface proteins facilitate microbial colonization by binding to host receptors, such as salivary glycoproteins or extracellular matrix components, contributing to virulence in oral and systemic infections.
The recombinant form of ALP1 is produced using heterologous expression systems (e.g., *E. coli* or yeast), enabling scalable and purified protein yields. The gene encoding ALP1 is cloned into expression vectors, followed by transfection, induction, and affinity chromatography-based purification. This process ensures high specificity and minimal contamination, making it suitable for research and therapeutic applications.
ALP1 recombinant protein serves as a vital tool in studying host-pathogen interactions, particularly in dental caries and infective endocarditis. It aids in elucidating mechanisms of immune evasion and bacterial persistence. Additionally, it is employed in vaccine development, where its immunogenic properties are harnessed to elicit protective antibody responses. In diagnostics, ALP1 acts as an antigen in immunoassays to detect pathogen-specific antibodies in clinical samples.
Research on ALP1 also extends to structural biology, where its domains are analyzed to design inhibitors blocking bacterial adhesion. Its role in biofilm formation underscores its potential as a target for antimicrobial therapies. Overall, ALP1 recombinant protein bridges basic science and translational applications, offering insights into microbial virulence and strategies for combating resistant infections.
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