| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Statherin / STATH蛋白 |
| Uniprot No | P02808-1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-62aa |
| 氨基酸序列 | MKFLVFAFIL ALMVSMIGAD SSEEKFLRRI GRFGYGYGPY QPVPEQPLYP QPYQPQYQQY TF |
| 预测分子量 | 32 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. |
以下是关于重组Statherin(STATH)蛋白的示例参考文献(文献信息为示例性质，建议通过学术数据库核实具体内容)：
---
1. **"Structural and functional analysis of human salivary Statherin"**
- **作者**: Oppenheim, J.J., Xu, T., McMillian, F.M.
- **摘要**: 研究解析了Statherin的二级结构，发现其N端富含酸性氨基酸，能够抑制羟基磷灰石晶体的过度生长，并讨论了其在口腔内维持牙釉质矿化平衡的作用机制。
2. **"Recombinant Statherin expression in E. coli and its antimicrobial properties"**
- **作者**: Schwartz, S.S., et al.
- **摘要**: 报道了通过大肠杆菌系统成功表达重组Statherin蛋白，并证明其具有抑制口腔致病菌(如变形链球菌)生物膜形成的能力，提示其在龋齿预防中的潜在应用。
3. **"Biomimetic coating of titanium implants with recombinant Statherin to enhance osseointegration"**
- **作者**: Cai, Y., et al.
- **摘要**: 利用重组Statherin蛋白修饰钛合金表面，实验显示其能显著促进成骨细胞黏附与分化，为牙科植入材料的生物活性改良提供了新策略。
4. **"Role of Statherin in maintaining oral lubrication and pH stability"**
- **作者**: Siqueira, W.L., et al.
- **摘要**: 通过体外实验证实重组Statherin可降低唾液摩擦系数，并缓冲酸性环境，强调了其在口腔黏膜保护和预防牙酸蚀症中的双重功能。
---
**注**：以上文献名为示例，实际研究需通过PubMed/Google Scholar等平台检索关键词“Recombinant Statherin”或“STATH protein”获取准确信息。
**Background of Statherin (STATH) Recombinant Protein**
Statherin (STATH) is a low-molecular-weight, intrinsically disordered phosphoprotein primarily secreted by salivary glands, playing a critical role in oral homeostasis. Naturally found in human saliva, it regulates mineral dynamics by inhibiting spontaneous precipitation of calcium phosphate salts (hydroxyapatite) in supersaturated solutions, thus preventing pathological calcification and maintaining tooth enamel integrity. Its N-terminal domain, rich in phosphorylated serine and tyrosine residues, mediates hydroxyapatite binding, while the C-terminal hydrophobic region contributes to bacterial adhesion modulation and antimicrobial activity.
Recombinant statherin is produced using biotechnological platforms (e.g., *E. coli* or mammalian expression systems) to replicate its native structure and post-translational modifications, particularly phosphorylation. Challenges include preserving its disordered conformation and functional motifs during purification. Recombinant variants are often engineered with tags (e.g., His-tag) to facilitate isolation while retaining bioactivity.
Research applications focus on oral health, including enamel remineralization strategies, anti-caries agents, and biomimetic coatings for dental implants. Its antimicrobial and anti-inflammatory properties are explored for treating periodontal diseases. Additionally, statherin’s role in biomineralization inspires bioengineering of synthetic peptides for regenerative dentistry and bone repair. Recent studies also investigate its interactions with oral microbiota and potential in diagnostics. As a multifunctional salivary component, recombinant statherin bridges translational research in dentistry, biomaterials, and therapeutic development.
×
