纯度 | > 90 % SDS-PAGE. |
种属 | Human |
靶点 | AMELX |
Uniprot No | Q99217 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 17-191aa |
氨基酸序列 | MPLPPHPGHPGYINFSYEVLTPLKWYQSIRPPYPSYGYEPMGGWLHHQIIPVLSQQHPPTHTLQPHHHIPVVPAQQPVIPQQPMMPVPGQHSMTPIQHHQPNLPPPAQQPYQPQPVQPQPHQPMQPQPPVHPMQPLPPQPPLPPMFPMQPLPPMLPDLTLEAWPSTDKTKREEVD |
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AMELX重组蛋白的模拟参考文献示例(内容为虚构,仅供参考):
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1. **文献名称**: *Recombinant Human AMELX Promotes Enamel Crystallization in vitro*
**作者**: Smith J, et al.
**摘要**: 研究利用重组表达的AMELX蛋白在体外模拟牙釉质矿化过程,证明其能够调控羟基磷灰石晶体的有序生长,为牙釉质修复材料开发提供理论支持。
2. **文献名称**: *Structural and Functional Analysis of AMELX Self-Assembly Properties*
**作者**: Chen L, Fincham AG.
**摘要**: 通过重组AMELX蛋白的自组装实验,揭示其纳米级结构动态变化及在生物矿化中的关键作用,阐明特定结构域对蛋白功能的调控机制。
3. **文献名称**: *AMELX Recombinant Protein Enhances Dental Pulp Stem Cell Differentiation*
**作者**: Wang Y, et al.
**摘要**: 发现重组AMELX蛋白可激活Wnt/β-catenin信号通路,促进牙髓干细胞向成釉细胞分化,为基于蛋白疗法的牙齿再生策略提供新思路。
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**注**: 以上文献信息为示例,实际研究中请通过PubMed、Web of Science等平台检索真实文献(关键词:recombinant amelogenin/AMELX)。
AMELX, or amelogenin X-linked, is a gene encoding the amelogenin protein, a critical component in enamel formation during tooth development. As the predominant matrix protein in developing enamel, amelogenin plays a vital role in organizing hydroxyapatite crystals, guiding their growth into the highly ordered structure responsible for enamel's exceptional hardness and resilience. The AMELX gene is located on the X chromosome, and mutations in this gene are associated with X-linked amelogenesis imperfecta (AI), a disorder characterized by defective enamel formation.
Recombinant AMELX protein is produced using genetic engineering techniques, typically through expression in bacterial (e.g., *E. coli*) or eukaryotic systems. This involves cloning the AMELX gene into expression vectors, followed by protein purification using chromatographic methods such as affinity or ion-exchange chromatography. Recombinant technology allows for the production of amelogenin variants, including splice isoforms and post-translationally modified forms, which are essential for studying structure-function relationships.
Research on recombinant AMELX has provided insights into its self-assembly properties, interaction with mineral phases, and role in biomineralization. Beyond dental research, it has applications in biomaterial development, particularly in designing enamel-mimetic composites or scaffolds for regenerative dentistry. Studies also explore its potential in promoting hydroxyapatite nucleation for bone tissue engineering. However, challenges remain in replicating the protein's native post-translational modifications and hierarchical assembly processes observed *in vivo*. Ongoing work aims to optimize recombinant production methods to better mimic natural amelogenin behavior for therapeutic and material science applications.
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