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| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PF4V1 |
| Uniprot No | P10720 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 31-104aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSFARAEAE EDGDLQCLCV KTTSQVRPRH ITSLEVIKAG PHCPTAQLIA TLKNGRKICL DLQALLYKKI IKEHLES |
| 预测分子量 | 11 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PF4V1重组蛋白的虚构参考文献示例(注：内容为模拟创作，非真实文献)：
1. **文献名称**：Structural Characterization and Heparin Binding Properties of Recombinant PF4V1 Protein
**作者**：Chen L, et al.
**摘要**：本研究成功在大肠杆菌中表达并纯化了重组PF4V1蛋白，通过圆二色谱和表面等离子共振技术证实其与肝素的高亲和力结合，揭示了PF4V1与经典PF4的结构差异及其潜在病理意义。
2. **文献名称**：Functional Role of PF4V1 in Thrombosis: Insights from Recombinant Protein Models
**作者**：Wang Y, et al.
**摘要**：利用重组PF4V1蛋白进行体外实验，发现其通过增强血小板聚集和抑制血管内皮细胞迁移，显著促进血栓形成，提示PF4V1可能是抗血栓治疗的新靶点。
3. **文献名称**：Optimization of PF4V1 Recombinant Expression in Mammalian Cells for Therapeutic Antibody Development
**作者**：Zhang H, et al.
**摘要**：通过哺乳动物细胞系统优化PF4V1重组蛋白表达，获得高糖基化活性蛋白，并基于此开发出靶向PF4V1的单克隆抗体，为自身免疫性血栓疾病提供了新型诊断工具。
4. **文献名称**：PF4V1 Recombinant Protein Induces Pro-Inflammatory Cytokine Release in Macrophages
**作者**：Kim S, et al.
**摘要**：研究发现重组PF4V1蛋白可激活巨噬细胞NF-κB通路，诱导IL-6和TNF-α大量分泌，揭示了其在炎症性疾病中的潜在作用机制。
(注：以上文献为示例性内容，实际研究中请通过学术数据库检索真实文献。)
**Background on PF4V1 Recombinant Protein**
Platelet Factor 4 Variant 1 (PF4V1), also known as SCYB4V1 or CXCL4L1. is a splice variant of Platelet Factor 4 (PF4/CXCL4), a chemokine primarily released from platelet α-granules during blood clotting and inflammation. Unlike the canonical PF4. which is encoded by the *PF4* gene, PF4V1 arises from alternative splicing of the *PF4* pre-mRNA, resulting in a truncated C-terminal region. This structural difference alters its biochemical properties and functional interactions.
PF4V1 retains the conserved N-terminal domain critical for chemokine activity but lacks 21 amino acids at the C-terminus compared to PF4. This truncation reduces its affinity for heparin and other glycosaminoglycans (GAGs), influencing its localization and signaling. While PF4 promotes thrombosis and inflammation by binding heparin and forming antigenic complexes in conditions like heparin-induced thrombocytopenia (HIT), PF4V1 exhibits distinct roles. It demonstrates stronger angiostatic and anti-tumor effects compared to PF4. potentially due to altered receptor binding or reduced GAG-mediated retention.
Recombinant PF4V1 protein is produced using expression systems like *E. coli* or mammalian cells, enabling studies on its structure-function relationships. Its production allows researchers to explore its unique biological activities, including modulation of immune responses, endothelial cell migration, and interactions with other chemokines like CCL5. Additionally, recombinant PF4V1 serves as a tool to investigate pathological mechanisms in thromboinflammatory diseases and cancer.
Interest in PF4V1 has grown due to its potential therapeutic applications. For example, its anti-angiogenic properties are being explored in cancer therapy, while its reduced heparin-binding capacity may lower risks of HIT-like complications in heparinized therapies. However, its precise physiological role and clinical relevance remain under investigation, highlighting the need for further studies using recombinant protein tools.
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