| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | gtfB |
| Uniprot No | P08987 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 426-597aa |
| 氨基酸序列 | WLHFLMNFGNIYANDPDANFDSIRVDAVDNVDADLLQIAGDYLKAAKGIHKNDKAANDHLSILEAWSDNDTPYLHDDGDNMINMDNKLRLSLLFSLAKPLNQRSGMNPLITNSLVNRTDDNAETAAVPSYSFIRAHDSEVQDLIRDIIKAEINPNVVGYSFTMEEIKKAFEI |
| 预测分子量 | 26.8 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gtfB重组蛋白的3篇参考文献示例(内容为虚构，仅作格式参考)：
1. **文献名称**: "重组变形链球菌gtfB蛋白的表达与酶活性分析"
**作者**: 李明等
**摘要**: 本研究在大肠杆菌中成功表达并纯化了重组gtfB蛋白，验证其能够催化蔗糖合成水不溶性葡聚糖，为研究龋齿致病机制提供了工具。
2. **文献名称**: "Streptococcus mutans gtfB结构与功能关系的晶体学研究"
**作者**: Smith J, et al.
**摘要**: 通过X射线晶体学解析了gtfB重组蛋白的三维结构，揭示了其底物结合域和催化活性位点，为抑制酶活性的药物设计奠定基础。
3. **文献名称**: "基于gtfB重组蛋白的防龋疫苗免疫效果评估"
**作者**: 王芳等
**摘要**: 利用毕赤酵母表达系统制备gtfB重组蛋白，动物实验表明其能诱导特异性抗体产生，显著降低大鼠龋齿发生率，具有疫苗开发潜力。
**Background of gtfB Recombinant Protein**
The *gtfB* gene encodes glucosyltransferase-B (GTF-B), a key enzyme produced primarily by *Streptococcus mutans*, a cariogenic bacterium associated with dental plaque formation and tooth decay. GTF-B catalyzes the synthesis of water-insoluble glucans from sucrose, facilitating bacterial adhesion to tooth surfaces and promoting biofilm development. These glucans enhance the structural integrity and virulence of dental plaque, creating an environment conducive to acid production and enamel demineralization.
Recombinant GTF-B protein is generated through molecular cloning, where the *gtfB* gene is expressed in heterologous systems like *Escherichia coli* or yeast. This allows large-scale production of the enzyme for functional and structural studies. Researchers utilize recombinant GTF-B to dissect its mechanism of action, including substrate binding, catalytic activity, and interaction with inhibitors or antibodies. Its structural domains—such as the catalytic site responsible for glucan synthesis and the glucan-binding domain—are critical targets for anti-caries strategies.
Interest in GTF-B stems from its role in dental caries pathogenesis, making it a potential target for therapeutic interventions. Studies explore inhibitors to block glucan synthesis, vaccines to neutralize its activity, or engineered enzymes with modified functions. Beyond dentistry, recombinant GTF-B has applications in biotechnology, such as modifying polysaccharides for industrial use.
Overall, recombinant GTF-B serves as a vital tool for understanding bacterial virulence and developing novel approaches to combat biofilm-related infections, highlighting its significance in both medical and biotechnological fields.
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