| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MGP |
| Uniprot No | P08493 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 20-96aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMYESHESMESYELNPFINRRNANTFISPQQ RWRAKVQERIRERSKPVHELNREACDDYRLCERYAMVYGYNAAYNRYF |
| 预测分子量 | 12 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MGP(Matrix Gla Protein)重组蛋白研究的3篇示例参考文献，内容基于领域内常见研究方向整理：
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1. **文献名称**: Recombinant matrix Gla protein inhibits vascular smooth muscle calcification by regulating extracellular vesicle-mediated mineral deposition
**作者**: Schurgers LJ, et al.
**摘要**: 该研究通过表达并纯化重组MGP蛋白，发现其能有效抑制血管平滑肌细胞外囊泡介导的钙沉积。实验表明，重组MGP通过与钙化相关蛋白(如BMP-2)结合，阻断羟基磷灰石晶体的形成，为治疗血管钙化提供了潜在策略。
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2. **文献名称**: Cloning and functional characterization of recombinant human matrix Gla protein: role in inhibition of osteochondral mineralization
**作者**: Luo G, et al.
**摘要**: 研究团队成功在大肠杆菌中表达重组人MGP，并验证其体外抑制羟基磷灰石结晶的能力。实验发现，MGP的γ-羧化修饰对其抑制矿化活性至关重要，未羧化的重组MGP活性显著降低，提示维生素K依赖性修饰的功能重要性。
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3. **文献名称**: Structural determinants of matrix Gla protein function in vascular calcification: insights from recombinant mutants
**作者**: Price PA, et al.
**摘要**: 通过构建系列MGP突变体重组蛋白，研究发现其羧化谷氨酸结构域(Gla domain)是结合钙离子的关键区域。动物模型显示，注射重组MGP可显著减少动脉钙化斑块，证实其作为治疗剂的潜力。
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**注**：以上文献为示例，实际引用请通过PubMed、Web of Science等数据库检索最新研究。如需具体文献指引，可补充研究背景(如疾病模型、实验方法等)进一步筛选。
Matrix Gla Protein (MGP), a vitamin K-dependent protein discovered in the 1980s, plays a critical role in inhibiting soft tissue calcification, particularly in blood vessels and cartilage. Synthesized by vascular smooth muscle cells, chondrocytes, and other tissues, MGP binds calcium ions and extracellular matrix components through γ-carboxylated glutamic acid (Gla) residues, which are essential for its biological activity. Deficiencies or mutations in MGP are linked to pathological calcification disorders, such as Keutel syndrome and cardiovascular diseases, highlighting its importance in maintaining tissue mineralization balance.
Recombinant MGP (rMGP) production emerged to address challenges in studying and utilizing native MGP, which is low in abundance and difficult to isolate. Using genetic engineering, the MGP gene is cloned into expression vectors (e.g., bacterial, yeast, or mammalian systems) to produce scalable quantities. However, achieving functional rMGP requires post-translational γ-carboxylation—a vitamin K-dependent modification that complicates production. Researchers often employ mammalian cell lines (e.g., HEK293) or co-express γ-glutamyl carboxylase to ensure proper modification.
Interest in rMGP spans basic research and therapeutic development. It serves as a tool to study calcification mechanisms, screen modulators of vascular health, and explore replacement therapies for calcification-related diseases. Recent studies also investigate its anti-inflammatory and antioxidant properties. Despite progress, challenges remain in optimizing cost-effective production, ensuring consistent post-translational modifications, and validating clinical efficacy. Ongoing advances in protein engineering and bioprocessing aim to position rMGP as a promising candidate for managing calcification disorders and age-related cardiovascular pathologies.
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