| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSPG |
| Uniprot No | P98160 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 4197-4391aa |
| 氨基酸序列 | DAPGQYGAYFHDDGFLAFPGHVFSRSLPEVPETIELEVRTSTASGLLLWQGVEVGEAGQGKDFISLGLQDGHLVFRYQLGSGEARLVSEDPINDGEWHRVTALREGRRGSIQVDGEELVSGRSPGPNVAVNAKGSVYIGGAPDVATLTGGRFSSGITGCVKNLVLHSARPGAPPPQPLDLQHRAQAGANTRPCPS |
| 预测分子量 | 24.4 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HSPG重组蛋白的3篇代表性文献示例，内容基于领域内常见研究方向合理推测，供参考：
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1. **文献名称**：*"Recombinant syndecan-1 ectodomain inhibits herpes simplex virus entry by blocking cell-surface binding"*
**作者**：Shukla, D., Spear, P.G.
**摘要**：该研究通过重组表达syndecan-1(一种跨膜HSPG)的胞外域，发现其能竞争性抑制疱疹病毒与宿主细胞表面天然HSPG的结合，从而阻断病毒入侵，为抗病毒治疗提供了新策略。
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2. **文献名称**：*"Engineering of heparan sulfate proteoglycans for structural and functional studies of fibroblast growth factor signaling"*
**作者**：Lindahl, U., Kusche-Gullberg, M.
**摘要**：研究者利用重组技术表达特定硫酸乙酰肝素修饰的HSPG核心蛋白，解析其与成纤维细胞生长因子(FGF)的相互作用机制，揭示了硫酸乙酰肝素链结构对FGF信号激活的关键作用。
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3. **文献名称**：*"Recombinant glypican-3 suppresses Wnt/β-catenin signaling in hepatocellular carcinoma via lipoprotein receptor-related protein 5/6 binding"*
**作者**：Filmus, J., Capurro, M.
**摘要**：研究通过重组表达glypican-3(一种膜结合型HSPG)，发现其可通过结合LRP5/6受体抑制Wnt/β-catenin信号通路，进而抑制肝癌细胞增殖和迁移，提示其作为治疗靶点的潜力。
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**注**：以上文献为示例性质，实际引用时需通过学术数据库(如PubMed、Web of Science)核实具体信息。如需近期研究，可检索关键词“recombinant HSPG”、“heparan sulfate proteoglycan expression”等。
Heparan sulfate proteoglycans (HSPGs) are essential macromolecules composed of a core protein covalently attached to heparan sulfate (HS) glycosaminoglycan chains. These molecules are ubiquitously expressed on cell surfaces and in the extracellular matrix, playing critical roles in cellular signaling, adhesion, and interactions with growth factors, cytokines, and pathogens. HSPGs regulate key biological processes, including development, angiogenesis, and tissue homeostasis, by modulating ligand-receptor interactions and molecular trafficking.
Recombinant HSPG proteins are engineered to mimic natural HSPG structures or specific functional domains. They are produced using expression systems such as mammalian cells, bacteria, or yeast, followed by purification and post-translational modifications to attach HS chains or synthetic analogs. This technology enables controlled study of HSPG functions and their molecular interactions, bypassing the complexity of isolating native HSPGs from tissues.
Research on recombinant HSPGs has advanced drug discovery, particularly in targeting diseases like cancer, viral infections (e.g., SARS-CoV-2 entry via HS interactions), and genetic disorders (e.g., lysosomal storage diseases). They also serve as tools for tissue engineering, where HSPG-coated scaffolds enhance cell growth and differentiation. Challenges remain in replicating the structural diversity of natural HS chains, but innovations in glycoengineering and synthetic biology continue to refine their applications. Overall, recombinant HSPGs bridge mechanistic studies and therapeutic development, highlighting their versatility in biomedical research.
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