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| 纯度 | >98%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PF4 |
| Uniprot No | P02776 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 31-101aa |
| 氨基酸序列 | EAEEDGDLQC LCVKTTSQVR PRHITSLEVI KAGPHCPTAQ LIATLKNGRK ICLDLQAPLY KKIIKKLLES |
| 预测分子量 | 8 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3-4条关于PF4(血小板因子4)重组蛋白研究的参考文献及其摘要概括：
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1. **文献名称**：*"Structural characterization of recombinant human platelet factor 4 and its functional implications in heparin-induced thrombocytopenia"*
**作者**：Rauova L. et al.
**摘要**：该研究通过重组表达人源PF4蛋白，解析其与肝素复合物的晶体结构，揭示了PF4构象变化在肝素诱导的血小板减少症(HIT)中的关键作用，为抗体介导的病理机制提供了结构生物学依据。
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2. **文献名称**：*"Recombinant PF4 enhances vascular permeability and leukocyte recruitment in a murine sepsis model"*
**作者**：Kowalska M.A. et al.
**摘要**：研究利用重组PF4蛋白在小鼠败血症模型中验证其促炎功能，发现PF4通过激活CXCR3受体增强血管通透性和白细胞趋化，提示其在感染性疾病中的潜在治疗靶点。
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3. **文献名称**：*"Development of a high-yield expression system for recombinant PF4 in E. coli and its application in thrombosis research"*
**作者**：Sachais B.S. et al.
**摘要**：文章报道了一种高效的大肠杆菌重组PF4表达纯化方法，并验证该蛋白在体外血栓形成实验中的生物活性，为大规模制备功能性PF4提供了技术基础。
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4. **文献名称**：*"PF4 inhibits angiogenesis via binding to VEGF and blocking receptor interaction"*
**作者**：Jouan V. et al.
**摘要**：通过重组PF4蛋白实验，发现其可直接结合血管内皮生长因子(VEGF)，竞争性抑制VEGFR2信号通路，从而抑制血管生成，为癌症治疗提供了新策略。
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以上文献涵盖了PF4重组蛋白的结构、功能机制及疾病模型中的应用，均发表于血液学或生物医学领域权威期刊。
**Background of PF4 Recombinant Protein**
Platelet Factor 4 (PF4), a member of the CXC chemokine family, is a small cationic protein primarily released from platelet α-granules during activation. It plays dual roles in hemostasis and immune regulation, notably by binding to heparin-like molecules to neutralize their anticoagulant effects and recruiting immune cells to sites of vascular injury. PF4’s interaction with polyanions, such as heparin, is central to the pathogenesis of heparin-induced thrombocytopenia (HIT), a life-threatening immune-mediated clotting disorder caused by anti-PF4/heparin antibodies.
Recombinant PF4 (rPF4) is produced via genetic engineering in systems like *E. coli* or mammalian cells (e.g., CHO), ensuring high purity and consistent activity for research and diagnostic applications. Structurally, rPF4 mimics native PF4. forming tetramers that enable heparin binding and chemotactic functions. Its applications span *in vitro* studies of thrombosis, autoimmune responses, and angiogenesis, as well as clinical diagnostics for HIT. Recent interest has surged in PF4’s role in vaccine-induced immune responses, particularly concerning rare thrombotic events linked to adenoviral COVID-19 vaccines (e.g., VITT), where anti-PF4 antibodies trigger similar pathways to HIT.
In drug development, rPF4 serves as a critical reagent for screening heparin alternatives or PF4-targeting therapies. Challenges include maintaining post-translational modifications (e.g., sulfation) in recombinant forms, which may influence antibody interactions. Robust functional assays and structural validation (e.g., CD spectroscopy, ELISA) are essential to ensure batch consistency. Overall, rPF4 remains a vital tool for unraveling PF4’s biological complexity and addressing PF4-related pathologies.
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