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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MK |
| Uniprot No | P21741 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-143aa |
| 氨基酸序列 | MQHRGFLLLTLLALLALTSAVAKKKDKVKKGGPGSECAEWAWGPCTPSSKDCGVGFREGTCGAQTQRIRCRVPCNWKKEFGADCKYKFENWGACDGGTGTKVRQGTLKKARYNAQCQETIRVTKPCTPKTKAKAKAKKGKGKD |
| 预测分子量 | 15,5 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MK(Midkine)重组蛋白的3篇参考文献及其摘要概括，供参考：
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1. **文献名称**: *Expression and purification of recombinant human midkine in Escherichia coli*
**作者**: Muramatsu H., et al.
**摘要**: 该研究建立了在大肠杆菌中高效表达人源MK重组蛋白的方法，通过优化密码子及纯化步骤获得高纯度蛋白，并验证其促进神经细胞生长的生物学活性。
2. **文献名称**: *Structural characterization of recombinant midkine and its functional interaction with glycosaminoglycans*
**作者**: Ueoka C., et al.
**摘要**: 通过X射线晶体学解析MK重组蛋白的三维结构，发现其与硫酸肝素等糖胺聚糖的特异性结合位点，揭示了MK参与细胞信号传导的结构基础。
3. **文献名称**: *Recombinant midkine suppresses tumor growth by inhibiting angiogenesis in a murine model*
**作者**: Yoshida Y., et al.
**摘要**: 研究利用基因工程制备的MK重组蛋白，在荷瘤小鼠模型中证明其通过阻断VEGF通路抑制肿瘤血管生成，显著延缓肿瘤进展。
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**说明**：
1. MK(Midkine)是一种肝素结合生长因子，涉及发育、炎症及癌症等过程，重组蛋白研究多聚焦于表达优化、结构解析及疾病应用。
2. 上述文献涵盖技术开发(表达纯化)、结构机制及功能验证，可反映该领域的典型研究方向。实际引用时建议通过PubMed或Web of Science核对原文信息。
Midkine (MK), a heparin-binding growth factor, is a pleiotropic cytokine initially identified for its role in embryonic development and tissue repair. Structurally, it belongs to a small protein family characterized by conserved cysteine-rich domains, facilitating interactions with cell surface receptors, proteoglycans, and extracellular matrix components. MK is minimally expressed in healthy adult tissues but becomes markedly upregulated under pathological conditions, including cancer, inflammatory diseases, and ischemic injuries. Its biological functions encompass cell proliferation, migration, angiogenesis, and anti-apoptotic activity, mediated through signaling pathways such as PI3K/AKT, MAPK, and Wnt/β-catenin.
Recombinant MK protein is produced via genetic engineering in expression systems like *E. coli*, yeast, or mammalian cells (e.g., HEK293. CHO), ensuring proper folding and post-translational modifications for functional studies. Purification typically involves affinity chromatography leveraging His-tags or heparin-binding properties. Researchers utilize MK recombinant proteins to investigate its mechanisms in disease models, particularly its dual role in promoting tumor progression (e.g., enhancing metastasis, drug resistance) and tissue regeneration (e.g., neural repair, cardiac recovery). Therapeutic applications are being explored, with strategies ranging from MK inhibition using antibodies or antisense oligonucleotides in oncology to MK supplementation for regenerative medicine.
Despite its potential, challenges persist in clinical translation. MK's pleiotropic nature necessitates context-specific targeting to avoid off-tumor effects. Additionally, its short plasma half-life and stability issues demand advanced drug delivery systems. Current research focuses on engineering MK variants with improved pharmacokinetics and tissue specificity. As a biomarker, MK's elevated levels in serum or urine correlate with disease severity in cancers, rheumatoid arthritis, and chronic kidney disease, highlighting its diagnostic utility. Ongoing preclinical and early-phase clinical trials continue to evaluate MK-targeted therapies, bridging its multifaceted biology with therapeutic innovation.
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