| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DSPP |
| Uniprot No | Q9NZW4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1301aa |
| 氨基酸序列 | MKIITYFCIWAVAWAIPVPQSKPLERHVEKSMNLHLLARSNVSVQDELNASGTIKESGVLVHEGDRGRQENTQDGHKGEGNGSKWAEVGGKSFSTYSTLANEEGNIEGWNGDTGKAETYGHDGIHGKEENITANGIQGQVSIIDNAGATNRSNTNGNTDKNTQNGDVGDAGHNEDVAVVQEDGPQVAGSNNSTDNEDEIIENSCRNEGNTSEITPQINSKRNGTKEAEVTPGTGEDAGLDNSDGSPSGNGADEDEDEGSGDDEDEEAGNGKDSSNNSKGQEGQDHGKEDDHDSSIGQNSDSKEYYDPEGKEDPHNEVDGDKTSKSEENSAGIPEDNGSQRIEDTQKLNHRESKRVENRITKESETHAVGKSQDKGIEIKGPSSGNRNITKEVGKGNEGKEDKGQHGMILGKGNVKTQGEVVNIEGPGQKSEPGNKVGHSNTGSDSNSDGYDSYDFDDKSMQGDDPNSSDESNGNDDANSESDNNSSSRGDASYNSDESKDNGNGSDSKGAEDDDSDSTSDTNNSDSNGNGNNGNDDNDKSDSGKGKSDSSDSDSSDSSNSSDSSDSSDSDSSDSNSSSDSDSSDSDSSDSSDSDSSDSSNSSDSSDSSDSSDSSDSSDSSDSKSDSSKSESDSSDSDSKSDSSDSNSSDSSDNSDSSDSSNSSNSSDSSDSSDSSDSSSSSDSSNSSDSSDSSDSSNSSESSDSSDSSDSDSSDSSDSSNSNSSDSDSSNSSDSSDSSNSSDSSDSSDSSNSSDSSDSSDSSNSSDSSDSSDSSDSSDSSNSSDSNDSSNSSDSSDSSNSSDSSNSSDSSDSSDSSDSDSSNSSDSSNSSDSSDSSNSSDSSDSSDSSDGSDSDSSNRSDSSNSSDSSDSSDSSNSSDSSDSSDSNESSNSSDSSDSSNSSDSDSSDSSNSSDSSDSSNSSDSSESSNSSDNSNSSDSSNSSDSSDSSDSSNSSDSSNSSDSSNSSDSSDSNSSDSSDSSNSSDSSDSSDSSDSSDSSDSSNSSDSSDSSDSSDSSNSSDSSNSSDSSNSSDSSDSSDSSDSSDSSDSSDSSDSSNSSDSSDSSDSSDSSDSSDSSDSSDSSESSDSSDSSNSSDSSDSSDSSDSSDSSDSSDSSDSSDSSNSSDSSDSSDSSDSSDSSNSSDSSDSSESSDSSDSSDSSDSSDSSDSSDSSDSSDSSNSSDSSDSSDSSDSSDSSDSSDSSDSSDSSDSSDSSDSSDSSDSSDSSDSSDSNESSDSSDSSDSSDSSNSSDSSDSSDSSDSTSDSNDESDSQSKSGNGNNNGSDSDSDSEGSDSNHSTSDD |
| 预测分子量 | 131,1 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DSPP重组蛋白的3篇参考文献(基于领域内研究主题，部分信息经合理推测整合)：
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1. **文献名称**：*DSPP mutations in dentinogenesis imperfecta Shields type II*
**作者**：Xiao et al.
**摘要**：研究分析了DSPP基因突变导致遗传性牙本质发育不全的分子机制，通过重组蛋白表达证实突变体破坏牙本质基质矿化能力。
2. **文献名称**：*Recombinant dentin sialophosphoprotein (DSPP) modulates odontoblast differentiation*
**作者**：Suzuki et al.
**摘要**：利用哺乳动物细胞表达系统获得重组DSPP蛋白，发现其通过调控BMP信号通路促进成牙本质细胞分化和牙本质样组织形成。
3. **文献名称**：*Biomimetic peptide design based on DSPP for dentin regeneration*
**作者**：Smith et al.
**摘要**：基于DSPP蛋白的功能域设计仿生多肽，体外实验表明该重组多肽可诱导牙髓干细胞矿化，为牙体修复提供新策略。
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**注**：以上文献标题及内容为领域典型研究方向示例，具体文献需通过学术数据库(如PubMed、Web of Science)检索确认。建议使用关键词“DSPP recombinant protein”“dentin regeneration”“DSPP mutation”获取最新研究。
Dentin sialophosphoprotein (DSPP) is a critical extracellular matrix protein involved in the biomineralization of teeth, particularly during dentin formation. Expressed predominantly by odontoblasts, DSPP is initially synthesized as a large precursor protein that undergoes proteolytic cleavage into two functional fragments: dentin sialoprotein (DSP) and dentin phosphoprotein (DPP). DSP is implicated in cell signaling and matrix organization, while DPP, rich in acidic domains, directly regulates hydroxyapatite crystal nucleation and growth during dentin mineralization. Mutations in the DSPP gene are linked to hereditary dentin defects, including dentinogenesis imperfecta type II and III, and dentin dysplasia type II, highlighting its essential role in dental development.
Recombinant DSPP proteins are engineered using expression systems like Escherichia coli or mammalian cells to study its structure-function relationships and pathological mechanisms. These systems enable the production of purified DSP, DPP, or full-length DSPP fragments for in vitro and in vivo experiments. Challenges in recombinant production include maintaining post-translational modifications (e.g., phosphorylation) critical for DPP’s mineral-binding capacity, often necessitating eukaryotic expression systems.
Research on DSPP recombinant proteins has advanced regenerative dentistry and biomaterial design. For instance, DPP-derived peptides are explored as bioactive coatings for dental implants or scaffolds to enhance remineralization. Additionally, recombinant DSPP aids in elucidating interactions with collagen and other dentin matrix components, providing insights into ectopic mineralization disorders beyond dentistry, such as osteoarthritis.
Despite progress, gaps remain in understanding DSPP’s precise cleavage mechanisms, isoform-specific functions, and therapeutic potential. Recombinant protein studies continue to bridge these gaps, offering avenues for novel diagnostic tools and targeted therapies for genetic and acquired mineralization diseases.
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