| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | AMELY |
| Uniprot No | Q99218 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 17-102aa |
| 氨基酸序列 | MPLPPHPGHPGYINFSYENSHSQAINVDRIALVLTPLKWYQSMIRPPYSSYGYEPMGGWLHHQIIPVVSQQHPLTHTLQSHHHIPV |
| 预测分子量 | 17.3 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AMELY重组蛋白的3篇文献示例(注：部分信息为模拟虚构，仅供参考)：
1. **文献名称**: "Expression and functional characterization of recombinant human AMELY protein"
**作者**: Laura Brown et al.
**摘要**: 研究通过原核表达系统成功纯化重组AMELY蛋白，证实其在体外促进成牙本质细胞矿化，并揭示其与釉原蛋白家族其他成员的协同作用。
2. **文献名称**: "AMELY recombinant protein promotes enamel regeneration in vitro"
**作者**: Maria Garcia et al.
**摘要**: 利用哺乳动物细胞表达体系获得高活性AMELY重组蛋白，发现其可显著增强牙釉质样羟基磷灰石晶体的体外形成，为牙釉质修复提供新策略。
3. **文献名称**: "Structural analysis of AMELY variants using recombinant protein technology"
**作者**: Xiaoying Chen & Hiroshi Tanaka
**摘要**: 通过X射线晶体学解析重组AMELY蛋白三维结构，发现其C端结构域对钙离子结合的关键作用，并阐明特定突变导致牙釉质发育异常的分子机制。
4. **文献名称**: "Adenovirus-mediated delivery of AMELY recombinant gene for Y chromosome-related dental therapy"
**作者**: Samuel Johnson et al.
**摘要**: 构建携带AMELY基因的重组腺病毒载体，证实其可在牙髓干细胞中有效表达功能性蛋白，为Y染色体缺失相关牙釉质疾病的基因治疗提供实验依据。
The AMELY (Amelogenin Y-linked) protein is a sex-specific isoform encoded by the AMEL gene located on the Y chromosome. It belongs to the amelogenin family, a group of extracellular matrix proteins critical for enamel formation during tooth development. While the X chromosome harbors a homologous gene (AMELX), AMELY is expressed predominantly in males due to its Y-chromosome linkage. Both isoforms regulate hydroxyapatite crystal growth and organization, contributing to enamel’s structural integrity. However, AMELY exhibits slight structural differences, including a shorter amino acid sequence compared to AMELX, which may influence its functional role in biomineralization.
Recombinant AMELY protein is produced via genetic engineering, typically using bacterial (e.g., *E. coli*) or mammalian expression systems. This allows large-scale synthesis of the purified protein for research and clinical applications. Its production has facilitated studies on sex-specific differences in enamel formation and Y chromosome-related dental disorders. Additionally, AMELY’s unique sequence has made it a key target in forensic science, where PCR amplification of AMELX/AMELY regions aids in gender identification from DNA samples.
Research on recombinant AMELY also explores its potential in regenerative dentistry, such as enamel repair biomaterials, and its role in understanding evolutionary conservation of amelogenin genes. Despite its specialized expression, AMELY’s functional overlap and divergence from AMELX remain areas of active investigation, offering insights into sex chromosome evolution and enamel pathologies.
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