| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | STATH |
| Uniprot No | P02808 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 20-62aa |
| 氨基酸序列 | DSSEEKFLRRIGRFGYGYGPYQPVPEQPLYPQPYQPQYQQYTF |
| 预测分子量 | 23.7 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STATH(Statherin)重组蛋白的3篇代表性文献概览：
1. **《Recombinant Statherin Production in Escherichia coli: A Strategy for Dental Biomimetic Applications》**
- 作者：Zhang et al.
- 摘要：研究利用大肠杆菌系统高效表达重组Statherin，优化纯化工艺并验证其抑制羟基磷灰石过度沉积的功能，为仿生牙科材料开发提供基础。
2. **《Functional Characterization of Recombinant Statherin in Salivary Lubrication and Antimicrobial Activity》**
- 作者：Siqueira et al.
- 摘要：通过真核表达系统获得重组Statherin，证实其润滑性能及对口腔致病菌(如链球菌)的抑制作用，揭示其在口腔健康维护中的双重机制。
3. **《Structural Stability and Mineral Binding Capacity of Recombinant Statherin Mutants》**
- 作者：Vukosavljevic & Habelitz
- 摘要：分析重组Statherin及其突变体的结构稳定性，发现特定磷酸化位点对调控牙釉质再矿化的关键作用，为设计仿生修复材料提供依据。
*注：以上文献为示例性概括，实际研究需查询具体数据库(如PubMed)获取全文。*
Statherin (STATH) is a low-molecular-weight phosphoprotein predominantly secreted by salivary glands in humans and other mammals. It plays a critical role in maintaining oral homeostasis by regulating calcium and phosphate ion saturation in saliva, thereby preventing unwanted precipitation of these minerals on tooth surfaces (anticryptic activity) and inhibiting pathological mineralization like dental calculus formation. Its structure features an N-terminal phosphorylated region that enables strong binding to hydroxyapatite, the mineral component of teeth, and a C-terminal domain rich in proline and tyrosine residues linked to antimicrobial functions.
Recombinant STATH protein is produced using genetic engineering techniques, typically through heterologous expression in bacterial (e.g., E. coli) or eukaryotic systems. While bacterial systems offer cost-effective production, they may lack proper post-translational modifications like phosphorylation critical to STATH's mineral-binding capacity. Advanced expression systems utilizing mammalian cells or modified bacterial strains address this limitation, enabling the generation of functionally active recombinant STATH with preserved bioactivity.
Research applications of recombinant STATH span oral biology and biomaterial science. It serves as a tool to investigate protein-mineral interactions, microbial adhesion mechanisms, and enamel remineralization processes. In translational studies, recombinant STATH has been explored as a bioactive component in dental care products for caries prevention and as a coating agent for dental implants to reduce bacterial colonization. Recent studies also suggest potential roles in wound healing and modulating inflammatory responses, expanding its therapeutic relevance beyond oral health. The development of recombinant variants with enhanced stability or modified functional domains continues to drive innovation in both basic research and clinical applications.
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