纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | OMD |
Uniprot No | Q99983 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 21-421aa |
氨基酸序列 | QYETYQWDED YDQEPDDDYQ TGFPFRQNVD YGVPFHQYTL GCVSECFCPT NFPSSMYCDN RKLKTIPNIP MHIQQLYLQF NEIEAVTANS FINATHLKEI NLSHNKIKSQ KIDYGVFAKL PNLLQLHLEH NNLEEFPFPL PKSLERLLLG YNEISKLQTN AMDGLVNLTM LDLCYNYLHD SLLKDKIFAK MEKLMQLNLC SNRLESMPPG LPSSLMYLSL ENNSISSIPE KYFDKLPKLH TLRMSHNKLQ DIPYNIFNLP NIVELSVGHN KLKQAFYIPR NLEHLYLQNN EIEKMNLTVM CPSIDPLHYH HLTYIRVDQN KLKEPISSYI FFCFPHIHTI YYGEQRSTNG QTIQLKTQVF RRFPDDDDES EDHDDPDNAH ESPEQEGAEG HFDLHYYENQ E |
预测分子量 | 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OMD(Osteomodulin)重组蛋白研究的模拟参考文献示例(注:内容为假设性概括,实际文献需通过学术数据库核实):
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1. **标题**: *"Recombinant Osteomodulin Promotes Osteogenic Differentiation of Mesenchymal Stem Cells In Vitro"*
**作者**: Zhang L, et al.
**摘要**: 研究通过大肠杆菌表达系统制备重组OMD蛋白,并证明其可显著增强骨髓间充质干细胞的成骨分化,提示其在骨组织工程中的应用潜力。
2. **标题**: *"Structural Characterization of Recombinant Human Osteomodulin and Its Role in Collagen Mineralization"*
**作者**: Tanaka K, et al.
**摘要**: 利用哺乳动物细胞表达重组人源OMD,解析其与胶原蛋白的相互作用机制,揭示OMD通过调控胶原纤维排列促进羟基磷灰石沉积的功能。
3. **标题**: *"High-Yield Production of Recombinant OMD in Pichia pastoris and Its Anti-Inflammatory Effects in Periodontal Ligament Cells"*
**作者**: Chen R, et al.
**摘要**: 开发毕赤酵母表达系统高效生产重组OMD,并发现其能抑制牙周膜细胞的炎症反应,为牙周疾病治疗提供新思路。
4. **标题**: *"Engineering Thermostable OMD Variants for Bone Regeneration Applications"*
**作者**: Gupta S, et al.
**摘要**: 通过蛋白质工程改造获得热稳定性增强的OMD突变体,动物实验表明其可显著加速临界尺寸骨缺损的修复过程。
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**建议**:以上内容为模拟示例,实际文献需通过PubMed、Web of Science等平台检索关键词(如"recombinant osteomodulin"、"OMD protein engineering")获取。部分研究可能聚焦于OMD在牙齿、骨骼疾病或生物材料中的功能机制。
Osteomodulin (OMD), also known as osteoadherin, is a small leucine-rich proteoglycan (SLRP) primarily associated with mineralized tissues, including bone and dentin. It plays a critical role in extracellular matrix (ECM) organization and biomineralization by interacting with collagen fibrils and regulating hydroxyapatite crystal growth. OMD is expressed by osteoblasts and odontoblasts, where it contributes to tissue remodeling, cell adhesion, and mechanotransduction. Its structure includes a central leucine-rich repeat domain, which facilitates collagen binding, and a C-terminal domain involved in mineralization modulation.
Recombinant OMD protein is engineered using biotechnological platforms, such as bacterial or mammalian expression systems, to produce purified, functional OMD for research and therapeutic applications. This involves cloning the OMD gene into expression vectors, optimizing conditions for protein folding, and employing chromatography-based purification. Recombinant OMD retains bioactivity, enabling studies on its mechanisms in skeletal development, osteoporosis, or dental regeneration. It also serves as a potential therapeutic agent for bone defect repair or biomaterial coatings to enhance osseointegration of implants.
Recent research highlights OMD’s dual role: promoting mineralization while inhibiting ectopic calcification in soft tissues. Dysregulation of OMD is linked to pathological conditions, including osteoarthritis and cardiovascular calcification, making it a biomarker or target for intervention. The development of recombinant OMD has accelerated structural and functional analyses, overcoming challenges in isolating the protein from native tissues. Its applications extend to tissue engineering, where OMD-functionalized scaffolds improve bone regeneration by mimicking natural ECM signaling. Overall, recombinant OMD bridges fundamental understanding of biomineralization with translational innovations in regenerative medicine.
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