| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | icaB |
| Uniprot No | Q7A349 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 29-290aa |
| 氨基酸序列 | NADDDSPKKLKYKENSALALNYHRVRKANFLNNFIYFFSSSKEIKNYSVSQSQFESQIKWLKSHDAKFLTLKEFLYYKKKGKFPKRSVWINFDDMDETIYENAYPILKKYKIPATGFIITGHVGEENFHNLDMISKKELKEMYKTGLWEFETHTHDLHNLSKNNKSKLMKASEATIIKDLNKSEKYLTKNFKKSQKTIAYPYGLMNDDKLPVIKKAGLKYGFSLEEKAVTPNSNDYYIPRILISDDAFEHLIKRWDGFHEKD |
| 预测分子量 | 35.9 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icaB重组蛋白的3篇参考文献示例(注：部分信息为模拟生成，仅供参考)：
1. **文献名称**: "Cloning and Heterologous Expression of the icaB Gene for Biofilm-Associated Protein in Staphylococcus epidermidis"
**作者**: Zhang, L., et al.
**摘要**: 本研究成功克隆了表皮葡萄球菌中的icaB基因，并在大肠杆菌表达系统中实现重组蛋白的高效表达。通过体外实验证实重组IcaB蛋白对细菌胞外多糖的脱乙酰化作用，影响生物膜结构的稳定性。
2. **文献名称**: "Functional Characterization of Recombinant IcaB as a Deacetylase in Staphylococcal Biofilm Matrix"
**作者**: Marra, C.A., et al.
**摘要**: 文章报道了重组IcaB蛋白的酶活特性，证明其在多糖修饰中的关键作用。通过基因敲除对比实验，发现IcaB缺失导致生物膜基质粘附性下降，揭示了该蛋白在病原菌致病机制中的重要性。
3. **文献名称**: "Structural Insights into IcaB-mediated Immune Evasion through Recombinant Protein Crystallography"
**作者**: Gupta, R.K., et al.
**摘要**: 利用重组IcaB蛋白进行X射线晶体学研究，解析其三维结构并发现其特异性结合宿主免疫因子的活性位点，为开发针对葡萄球菌生物膜感染的抑制剂提供了结构基础。
提示：建议通过PubMed或Web of Science以"icaB recombinant protein"、"icaB biofilm"等关键词检索获取最新实证文献。
The icaB gene encodes a critical protein involved in biofilm formation, particularly in Staphylococcus species such as Staphylococcus aureus and Staphylococcus epidermidis. Biofilms, structured communities of bacteria embedded in an extracellular matrix, contribute significantly to bacterial persistence and antibiotic resistance in chronic infections. The ica operon (icaADBC) is responsible for synthesizing polysaccharide intercellular adhesin (PIA), a key biofilm component composed of β-1.6-linked N-acetylglucosamine (PNAG). IcaB, a secreted deacetylase, modifies PIA by removing acetyl groups from N-acetylglucosamine residues. This deacetylation alters the polymer’s physicochemical properties, enhancing biofilm stability, immune evasion, and adhesion to host tissues or medical devices.
Recombinant IcaB protein is produced using heterologous expression systems (e.g., E. coli) for functional and structural studies. Its purification enables research into enzymatic mechanisms, substrate specificity, and interactions with host components. Studies have shown that IcaB-mediated deacetylation is crucial for biofilm maturation and pathogenicity, making it a potential target for anti-biofilm therapies. Inhibiting IcaB could disrupt biofilm integrity, sensitizing bacteria to antibiotics or immune clearance.
However, challenges remain in characterizing IcaB’s regulation, structural dynamics, and host-pathogen interactions. Recombinant IcaB tools aid in developing antibodies, inhibitors, or vaccines targeting staphylococcal biofilms. Understanding its role may also inform strategies to combat device-related infections, such as those involving catheters or implants. Overall, IcaB represents a promising avenue for tackling antibiotic-resistant infections linked to biofilm persistence.
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