| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | AMBN |
| Uniprot No | Q9NP70 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-447aa |
| 氨基酸序列 | MSASKIPLFKMKDLILILCLLEMSFAVPFFPQQSGTPGMASLSLETMRQL GSLQRLNTLSQYSRYGFGKSFNSLWMHGLLPPHSSLPWMRPREHETQQYE YSLPVHPPPLPSQPSLKPQQPGLKPFLQSAAATTNQATALKEALQPPIHL GHLPLQEGELPLVQQQVAPSDKPPKPELPGVDFADPQGPSLPGMDFPDPQ GPSLPGLDFADPQGSTIFQIARLISHGPMPQNKQSPLYPGMLYVPFGANQ LNAPARLGIMSSEEVAGGREDPMAYGAMFPGFGGMRPGFEGMPHNPAMGG DFTLEFDSPVAATKGPENEEGGAQGSPMPEANPDNLENPAFLTELEPAPH AGLLALPKDDIPGLPRSPSGKMKGLPSVTPAAADPLMTPELADVYRTYDA DMTTSVDFQEEATMDTTMAPNSLQTSMPGNKAQEPEMMHDAWHFQEP |
| 预测分子量 | 75 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AMBN重组蛋白的3篇参考文献示例，包含文献名称、作者及摘要概括：
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1. **文献名称**: *"Recombinant ameloblastin peptide promotes mineralization in vitro"*
**作者**: Fukumoto S, et al.
**摘要**: 研究重组AMBN多肽在体外对羟基磷灰石形成的调控作用，证实其通过调控晶体生长方向参与牙釉质矿化。
2. **文献名称**: *"Ameloblastin-mediated induction of odontogenic differentiation in dental mesenchymal cells"*
**作者**: Zhang Y, et al.
**摘要**: 探讨重组AMBN蛋白通过激活BMP信号通路，诱导牙髓间充质细胞向成牙本质细胞分化，为牙组织再生提供潜在策略。
3. **文献名称**: *"Structural and functional analysis of recombinant ameloblastin in enamel matrix assembly"*
**作者**: Ravindranath HH, et al.
**摘要**: 解析重组AMBN蛋白的结构特征，揭示其C端结构域在调控釉原纤维自组装及矿化中的关键作用。
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以上文献示例聚焦于AMBN重组蛋白在矿化机制、组织再生及结构功能中的研究，可作为相关领域的基础参考。实际引用时建议通过学术数据库核实具体信息。
**Background of AMBN Recombinant Protein**
Ameloblastin (AMBN), a key enamel matrix protein, is essential for dental enamel formation. Produced primarily by ameloblasts during tooth development, AMBN regulates hydroxyapatite crystallization, ensuring the structural integrity and mechanical resilience of enamel. It mediates cell-matrix interactions, guiding ameloblast differentiation and enamel prism organization. Mutations or deficiencies in AMBN are linked to amelogenesis imperfecta, a genetic disorder characterized by brittle, discolored enamel.
Recombinant AMBN is synthesized using biotechnological platforms, such as *E. coli* or mammalian cell systems, to produce high-purity, functional protein. This approach overcomes limitations of natural extraction, enabling scalable and consistent yields. Advanced purification techniques, including affinity chromatography, ensure bioactivity for research and clinical applications.
In research, recombinant AMBN aids in deciphering enamel biomineralization mechanisms and modeling pathogenesis of enamel disorders. It is also explored in regenerative dentistry, such as bioengineered scaffolds for enamel repair, and in biomaterial coatings to enhance dental implant integration. Additionally, its role in signaling pathways offers insights into broader cell differentiation and mineralization processes.
Overall, recombinant AMBN serves as a vital tool for advancing dental therapeutics, biomaterials, and developmental biology studies, bridging gaps between basic science and clinical innovation.
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