| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HTN3 |
| Uniprot No | P15516 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 20-51aa |
| 氨基酸序列 | MSPILGYWKIKGLVQPTRLLLEYLEEKYEEHLYERDEGDKWRNKKFELGL EFPNLPYYIDGDVKLTQSMAIIRYIADKHNMLGGCPKERAEISMLEGAVL DIRYGVSRIAYSKDFETLKVDFLSKLPEMLKMFEDRLCHKTYLNGDHVTH PDFMLYDALDVVLYMDPMCLDAFPKLVCFKKRIEAIPQIDKYLKSSKYIA WPLQGWQATFGGGDHPPKSDLVPRGSENLYFQGHMDSHAKRHHGYKRKFH EKHHSHRGYRSNYLYDN |
| 预测分子量 | 31 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HTN3重组蛋白的示例参考文献(注：以下文献为示例性概括，非真实存在)：
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1. **文献名称**：*Expression and Characterization of Recombinant Human Histatin 3 in Escherichia coli*
**作者**：Smith J, et al.
**摘要**：研究报道了利用大肠杆菌表达系统成功生产重组HTN3蛋白，并通过离子交换层析纯化。功能实验表明，该重组蛋白对白色念珠菌具有显著抗菌活性，提示其在抗真菌治疗中的应用潜力。
2. **文献名称**：*Structural Analysis of Recombinant HTN3 Reveals Key Antifungal Domains*
**作者**：Lee S, et al.
**摘要**：通过核磁共振技术解析重组HTN3的三维结构，发现其C端区域与真菌细胞膜结合的关键氨基酸残基，揭示了其破坏膜完整性以抑制病原体的分子机制。
3. **文献名称**：*Recombinant HTN3-Loaded Nanoparticles for Oral Candidiasis Therapy*
**作者**：Garcia R, et al.
**摘要**：开发了一种基于重组HTN3的纳米递送系统，显著提高了蛋白的稳定性和黏膜黏附性。动物实验显示，该制剂能有效减少口腔念珠菌感染负荷。
4. **文献名称**：*Functional Comparison of Recombinant HTN3 Variants in Salivary Antimicrobial Defense*
**作者**：Zhang W, et al.
**摘要**：对比不同重组HTN3突变体的功能，发现特定磷酸化修饰可增强其抗菌活性，为设计优化抗菌肽提供理论依据。
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如需真实文献，建议通过PubMed或Google Scholar检索关键词“recombinant HTN3”、“histatin 3 expression”等获取具体研究。
The HTN3 gene encodes histatin 3. a small cationic protein predominantly found in human saliva. Histatins are a family of histidine-rich peptides with multifunctional roles in oral biology, including antimicrobial activity, wound healing, and enamel remineralization. Among them, histatin 3 (encoded by HTN3) and its proteolytic cleavage product, histatin 5. are particularly notable for their potent antifungal properties against Candida species, making them critical components of innate oral immunity. Recombinant HTN3 protein is produced using genetic engineering techniques, often expressed in microbial systems like E. coli or yeast to overcome the limitations of natural salivary extraction, such as low yield and compositional variability. This recombinant approach enables scalable production and consistent quality for research and therapeutic applications. Studies on HTN3 recombinant protein focus on elucidating its structure-function relationships, antimicrobial mechanisms, and potential clinical uses, such as developing antifungal agents for oral candidiasis or bioactive coatings for dental materials. Its ability to disrupt microbial membranes and modulate immune responses has also sparked interest in broader biomedical contexts, including wound care and infection control. Despite promising attributes, challenges remain in optimizing stability, delivery, and cost-effectiveness for translational applications. Ongoing research aims to harness HTN3's unique properties while addressing these hurdles, positioning recombinant histatin 3 as a biologically inspired tool bridging oral health innovation and antimicrobial therapeutics.
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