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Recombinant Human DMP1 protein

  • 中文名: 牙本质基质酸性磷蛋白1(DMP1)重组蛋白
  • 别    名: DMP1;Dentin matrix acidic phosphoprotein 1
货号: PA1000-3665
Price: ¥询价
数量:
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产品详情

纯度>85%SDS-PAGE.
种属Human
靶点DMP1
Uniprot No Q13316
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间 17-513aa
氨基酸序列LPVTRYQNNESEDSEEWKGHLAQAPTPPLESSESSEGSKVSSEEQANEDPSDSTQSEEGLGSDDHQYIYRLAGGFSRSTGKGGDDKDDDEDDSGDDTFGDDDSGPGPKDRQEGGNSRLGSDEDSDDTIQASEESAPQGQDSAQDTTSESRELDNEDRVDSKPEGGDSTQESESEEHWVGGGSDGESSHGDGSELDDEGMQSDDPESIRSERGNSRMNSAGMKSKESGENSEQANTQDSGGSQLLEHPSRKIFRKSRISEEDDRSELDDNNTMEEVKSDSTENSNSRDTGLSQPRRDSKGDSQEDSKENLSQEESQNVDGPSSESSQEANLSSQENSSESQEEVVSESRGDNPDPTTSYVEDQEDSDSSEEDSSHTLSHSKSESREEQADSESSESLNFSEESPESPEDENSSSQEGLQSHSSSAESQSEESHSEEDDSDSQDSSRSKEDSNSTESKSSSEEDGQLKNIEIESRKLTVDAYHNKPIGDQDDNDCQDGY
预测分子量 56.0 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.

参考文献

以下是关于DMP1重组蛋白的文献示例(注:以下内容为简化示例,实际文献需根据具体研究查询):

1. **文献名称**: "Recombinant DMP1 enhances osteogenic differentiation of mesenchymal stem cells in vitro"

**作者**: Smith A, et al.

**摘要**: 研究证明重组DMP1蛋白可通过激活MAPK信号通路促进间充质干细胞的成骨分化,为骨组织再生提供潜在治疗策略。

2. **文献名称**: "Expression and purification of dentin matrix protein 1 in Escherichia coli for biomedical applications"

**作者**: Chen L, et al.

**摘要**: 报道了一种在大肠杆菌中高效表达并纯化重组DMP1蛋白的方法,验证其生物活性可用于牙本质修复材料的开发。

3. **文献名称**: "DMP1 recombinant protein regulates phosphate metabolism in chronic kidney disease models"

**作者**: Gupta R, et al.

**摘要**: 发现重组DMP1通过调节FGF23通路改善慢性肾病模型中的磷酸盐代谢紊乱,提示其治疗代谢性骨病的潜力。

4. **文献名称**: "Structural characterization of recombinant DMP1 and its role in biomineralization"

**作者**: Park JH, et al.

**摘要**: 通过X射线晶体学解析重组DMP1蛋白结构,揭示其酸性结构域在羟基磷灰石晶体形成中的关键作用。

(提示:以上文献信息为示例性质,实际引用需查询PubMed、Google Scholar等平台获取具体研究。)

背景信息

Dentin matrix protein 1 (DMP1) is an acidic, non-collagenous extracellular matrix protein predominantly expressed in mineralized tissues, including dentin, bone, and cementum. As a member of the SIBLING (Small Integrin-Binding Ligand N-linked Glycoprotein) family, it plays crucial roles in biomineralization processes through its calcium-binding phosphoprotein domains. The full-length DMP1 protein (~486 amino acids in humans) undergoes post-translational cleavage into N-terminal (37 kDa) and C-terminal (57 kDa) fragments, both functionally active in regulating hydroxyapatite crystal formation and growth.

Recombinant DMP1 production typically employs bacterial (e.g., E. coli) or mammalian expression systems to obtain properly folded protein with post-translational modifications. Studies reveal its dual functionality: as a signaling molecule influencing osteocyte maturation via MAP kinase pathways, and as a structural template guiding mineral deposition through its acidic clusters and phosphorylation sites. Its interaction with collagen fibrils and other SIBLING proteins (e.g., DSPP) enables precise spatial control over mineralization.

Current applications span dental/bone tissue engineering, where DMP1-functionalized scaffolds enhance biomimetic mineralization. Researchers also explore its therapeutic potential in dentin regeneration and osteoporosis management. Notably, DMP1 mutations are linked to autosomal recessive hypophosphatemic rickets, driving interest in recombinant protein for disease modeling. Recent advances include its use as a bioactive component in 3D-printed bioceramics and hydrogel-based delivery systems for localized tissue repair. Emerging evidence suggests broader implications in ectopic calcification regulation and stem cell differentiation modulation, positioning recombinant DMP1 as a versatile tool in both basic research and translational mineralized tissue engineering.

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