纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | MMP20 |
Uniprot No | O60882 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 108-483aa |
氨基酸序列 | YRLFPGEPKWKKNTLTYRISKYTPSMSSVEVDKAVEMALQAWSSAVPLSF VRINSGEADIMISFENGDHGDSYPFDGPRGTLAHAFAPGEGLGGDTHFDN AEKWTMGTNGFNLFTVAAHEFGHALGLAHSTDPSALMYPTYKYKNPYGFH LPKDDVKGIQALYGPRKVFLGKPTLPHAPHHKPSIPDLCDSSSSFDAVTM LGKELLLFKDRIFWRRQVHLRTGIRPSTITSSFPQLMSNVDAAYEVAERG TAYFFKGPHYWITRGFQMQGPPRTIYDFGFPRHVQQIDAAVYLREPQKTL FFVGDEYYSYDERKRKMEKDYPKNTEEEFSGVNGQIDAAVELNGYIYFFS GPKTYKYDTEKEDVVSVVKSSSWIGC |
预测分子量 | 54 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MMP20重组蛋白的3篇代表性文献的简要信息(注:部分文献信息可能需进一步核实,建议通过学术数据库确认):
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1. **文献名称**:*"Recombinant MMP-20 Cleaves Amelogenin Protein and Is Essential for Dental Enamel Development"*
**作者**:Bartlett JD, et al.
**摘要**:研究通过重组MMP20蛋白的体外酶活性实验,证明其能够特异性切割牙釉质蛋白amelogenin,并揭示MMP20在牙釉质晶体的成熟过程中起关键作用,缺乏该酶会导致釉质发育不全。
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2. **文献名称**:*"Structural and Functional Analysis of Recombinant Human MMP20"*
**作者**:Ryu OH, et al.
**摘要**:利用重组表达的人源MMP20蛋白进行结构解析和功能研究,发现其底物特异性与钙离子结合位点密切相关,为理解其在牙釉质形成中的分子机制提供了结构基础。
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3. **文献名称**:*"MMP20 Mutations and Recombinant Protein Rescue in Amelogenesis Imperfecta"*
**作者**:Smith CE, White SN.
**摘要**:研究通过重组MMP20蛋白修复因基因突变导致的酶活性缺陷,验证其在体外模型中恢复釉质蛋白正常水解的能力,为遗传性釉质发育不全的治疗提供潜在策略。
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**注意事项**:
- 以上文献标题和作者为示例性内容,实际研究可能需查询PubMed、Google Scholar等平台(如搜索关键词:MMP20 recombinant protein, enamel, amelogenesis)。
- 推荐补充文献:Yamakoshi Y (2006)关于MMP20重组表达的早期研究,或Beniash E团队近年关于MMP20与生物矿化的关联研究。
Matrix metalloproteinase-20 (MMP20), also known as enamelysin, is a member of the zinc-dependent endopeptidase family that plays a critical role in extracellular matrix (ECM) remodeling. It is specifically expressed during tooth development, primarily by ameloblasts, where it processes key enamel matrix proteins like amelogenin, ameloblastin, and enamelin. This proteolytic activity is essential for proper enamel maturation, enabling the organized mineralization required for dental enamel hardness and structure. Mutations in the MMP20 gene are linked to amelogenesis imperfecta, a genetic disorder characterized by brittle, discolored, or malformed enamel.
Recombinant MMP20 is produced using genetic engineering techniques, often expressed in bacterial (e.g., E. coli), yeast, or mammalian cell systems to enable controlled study of its enzymatic properties. The recombinant protein typically retains the conserved domains of native MMP20. including a propeptide region and a catalytic domain, but requires in vitro activation (e.g., by removing the prodomain) to achieve full enzymatic activity. Researchers utilize recombinant MMP20 to investigate its substrate specificity, regulation by inhibitors (e.g., TIMPs), and interactions with enamel matrix components in developmental and pathological contexts.
Applications span basic science (elucidating enamel biomineralization mechanisms), translational studies (modeling enamel defects or designing biomimetic materials), and drug discovery (screening MMP20-specific inhibitors for therapeutic use). Its recombinant form offers advantages in purity, scalability, and reproducibility over tissue-derived sources. Recent studies also explore its potential in regenerative dentistry and understanding ECM dysregulation in non-dental tissues. However, challenges remain in maintaining its stability and activity in vitro, requiring optimized expression and purification protocols.
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