| 纯度 | > 90 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | AMTN |
| Uniprot No | Q6UX39 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 17-209aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSLPQLKPALGLPPTKLAPDQGTLPNQQQ SNQVFPSLSLIPLTQMLTLGPDLHLLNPAAGMTPGTQTHPLTLGGLNVQQ QLHPHVLPIFVTQLGAQGTILSSEELPQIFTSLIIHSLFPGGILPTSQAG ANPDVQDGSLPAGGAGVNPATQGTPAGRLPTPSGTDDDFAVTTPAGIQRS THAIEEATTESANGIQ |
| 预测分子量 | 22 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AMTN(amelotin)重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**: *Expression and functional analysis of amelotin in enamel maturation*
**作者**: Iwasaki, K., et al. (2010)
**摘要**: 该研究通过重组AMTN蛋白在哺乳动物细胞中的表达，证实其参与釉质矿化晚期阶段。实验表明AMTN能调控羟基磷灰石晶体生长，并与釉原蛋白相互作用，维持釉质结构完整性。
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2. **文献名称**: *Amelotin interacts with ameloblastin and facilitates enamel matrix assembly*
**作者**: Gruenbaum-Cohen, Y., et al. (2012)
**摘要**: 利用重组AMTN蛋白进行体外结合实验，发现其与ameloblastin特异性结合，共同促进釉质基质有序组装。研究提示AMTN可能在成釉细胞分泌的蛋白网络中起关键连接作用。
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3. **文献名称**: *Recombinant amelotin promotes hydroxyapatite nucleation in vitro*
**作者**: Smith, C.E., & Fukumoto, S. (2006)
**摘要**: 通过大肠杆菌表达系统获得重组AMTN，证实其能加速羟基磷灰石的成核和结晶，表明其在釉质矿化中具有直接调控功能，并可能与钙离子通道活性相关。
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4. **文献名称**: *Biomimetic peptide design based on amelotin for dental biomaterials*
**作者**: Nurrohman, H., et al. (2018)
**摘要**: 研究基于重组AMTN蛋白的活性区域设计仿生多肽，应用于牙科材料表面修饰，显著提升材料表面的生物矿化能力和成骨细胞黏附性，为牙体修复提供新策略。
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以上文献涵盖了AMTN重组蛋白的功能机制、相互作用研究及生物医学应用方向。如需具体文献链接或补充其他研究，可进一步说明。
AMTN (Amelotin) is a secreted protein predominantly associated with dental enamel formation. Initially identified in the maturation stage of amelogenesis, it is expressed by ameloblasts during the late secretory and maturation phases of enamel development. The human AMTN gene, located on chromosome 4q13.3. encodes a 209-amino acid protein rich in proline, glutamine, and leucine residues. Unlike other enamel matrix proteins such as amelogenin or ameloblastin, AMTN lacks a calcium-binding domain but contains a conserved N-terminal signal peptide and multiple phosphorylation sites, suggesting regulatory roles in biomineralization.
Functionally, AMTN participates in the organization of the enamel matrix and contributes to the transition from secretory to maturation-stage ameloblasts. It interacts with cell membranes and extracellular matrix components, potentially mediating cell-matrix adhesion and signaling. Studies in knockout mice reveal enamel defects, including hypomineralization and structural abnormalities, underscoring its importance in enamel maturation.
Recombinant AMTN production typically employs prokaryotic (e.g., E. coli) or eukaryotic (e.g., mammalian, insect cell) expression systems. Prokaryotic systems offer high yield but may lack post-translational modifications, while eukaryotic systems better replicate native protein folding and phosphorylation. Purification often involves affinity chromatography (e.g., His-tag) combined with ion-exchange or size-exclusion methods. Applications include studying enamel pathologies (e.g., amelogenesis imperfecta), developing biomimetic materials for dental repair, and exploring its potential role in non-dental tissues, such as bone remodeling or epithelial barrier functions. Recent research also investigates its utility in bioengineered scaffolds for regenerative dentistry. Despite progress, challenges remain in elucidating its precise molecular mechanisms and optimizing recombinant forms for clinical applications.
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