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Recombinant Human AMELX protein

  • 中文名: 牙釉蛋白X连锁(AMELX)重组蛋白
  • 别    名: AMELX;AMG;AMGX;Amelogenin, X isoform
货号: PA1000-145DB
Price: ¥询价
数量:
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产品详情

纯度> 90 % SDS-PAGE.
种属Human
靶点AMELX
Uniprot NoQ99217
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.

参考文献

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)。

背景信息

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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