| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ENAM |
| Uniprot No | Q9NRM1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1043-1142aa |
| 氨基酸序列 | ERQQQRPSNILHLPCFGSKLAKHHSSTTGTPSSDGRQSPFDGDSITPTENPNTLVELATEEQFKSINVDPLDADEHSPFEFLQRGTNVQDQVQDCLLLQA |
| 预测分子量 | 18.0 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ENAM(牙釉蛋白)重组蛋白的3篇参考文献示例，供参考：
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1. **文献名称**：*Recombinant human enamelin promotes in vitro hydroxyapatite nucleation*
**作者**：Fan Y. et al.
**摘要**：研究利用重组技术表达人ENAM蛋白片段，验证其与羟基磷灰石的结合能力，发现ENAM重组蛋白可促进体外矿化，为牙釉质再生提供理论基础。
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2. **文献名称**：*Expression and purification of recombinant porcine enamelin in Escherichia coli*
**作者**：Li R. et al.
**摘要**：通过大肠杆菌系统成功表达猪ENAM重组蛋白，优化纯化工艺并验证其结构完整性，为后续研究ENAM在釉质发育中的功能提供实验材料。
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3. **文献名称**：*Functional analysis of a recombinant murine enamelin polypeptide*
**作者**：Smith C.E. et al.
**摘要**：构建小鼠ENAM重组蛋白，发现其可调控釉质晶体生长方向，并通过基因敲除实验证明ENAM对釉质硬度及结构的关键作用。
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**备注**：以上文献信息为示例性质，具体文献需通过PubMed、Google Scholar等平台检索关键词“recombinant ENAM protein”或“enamelin expression”获取。近年研究可能涉及ENAM在生物材料或再生医学中的应用拓展。
**Background of ENAM Recombinant Protein**
Enamelin (ENAM) is a critical extracellular matrix protein predominantly involved in enamel formation during tooth development. As one of the key structural components of the enamel matrix, ENAM plays a vital role in regulating the nucleation, growth, and organization of hydroxyapatite crystals, which are essential for the mechanical strength and durability of dental enamel. Mutations in the *ENAM* gene have been linked to amelogenesis imperfecta, a genetic disorder characterized by defective enamel structure and increased susceptibility to dental decay.
The production of recombinant ENAM protein has emerged as a valuable tool for studying enamel biomineralization mechanisms and developing therapeutic strategies for enamel-related pathologies. Recombinant ENAM is typically generated using heterologous expression systems, such as bacterial (e.g., *E. coli*), mammalian, or insect cell lines. These systems enable the production of purified, bioactive ENAM fragments that retain functional domains necessary for interactions with other enamel proteins (e.g., amelogenin) and mineral phases.
Research utilizing recombinant ENAM has provided insights into its structural-functional relationships, including pH-dependent conformational changes and calcium-binding properties. Additionally, it facilitates the exploration of enamel biomimetics for dental tissue engineering and regenerative dentistry. Recent studies also leverage ENAM recombinant proteins to design bioactive coatings for dental implants or to model pathological enamel defects in vitro.
Despite progress, challenges remain in replicating post-translational modifications (e.g., phosphorylation) critical for ENAM's native function, necessitating optimization of expression systems. Overall, recombinant ENAM serves as a cornerstone for both basic research in biomineralization and translational applications in dental medicine.
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