| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PDGFRL |
| Uniprot No | Q15198 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22-375aa |
| 氨基酸序列 | QHLPKNKRP KEPGENRIKP TNKKVKPKIP KMKDRDSANS APKTQSIMMQ VLDKGRFQKP AATLSLLAGQ TVELRCKGSR IGWSYPAYLD TFKDSRLSVK QNERYGQLTL VNSTSADTGE FSCWVQLCSG YICRKDEAKT GSTYIFFTEK GELFVPSPSY FDVVYLNPDR QAVVPCRVTV LSAKVTLHRE FPAKEIPANG TDIVYDMKRG FVYLQPHSEH QGVVYCRAEA GGRSQISVKY QLLYVAVPSG PPSTTILASS NKVKSGDDIS VLCTVLGEPD VEVEFTWIFP GQKDERPVTI QDTWRLIHRG LGHTTRISQS VITVEDFETI DAGYYICTAQ NLQGQTTVAT TVEFS |
| 预测分子量 | 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PDGFRL重组蛋白的3篇模拟参考文献示例(注：内容为虚构，仅供参考)：
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1. **文献名称**: *Expression and Functional Characterization of Recombinant PDGFRL Protein in Cancer Cell Lines*
**作者**: Zhang Y, et al.
**摘要**: 本研究通过哺乳动物表达系统成功制备了PDGFRL重组蛋白，并验证其抑制肿瘤细胞增殖和迁移的能力。实验表明，PDGFRL通过调控MAPK信号通路抑制肺癌细胞的侵袭。
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2. **文献名称**: *Structural Insights into PDGFRL and Its Role in Tumor Suppression*
**作者**: Smith JL, et al.
**摘要**: 利用X射线晶体学解析了PDGFRL重组蛋白的三维结构，发现其胞外域与PDGF配体结合能力较弱。功能实验表明，PDGFRL通过竞争性抑制PDGFRα/β的激活发挥抑癌作用。
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3. **文献名称**: *Recombinant PDGFRL Protein Attenuates Fibrosis in a Murine Liver Model*
**作者**: Tanaka K, et al.
**摘要**: 通过大肠杆菌系统表达并纯化PDGFRL重组蛋白，动物实验显示其能显著减少肝纤维化模型小鼠的胶原沉积，提示PDGFRL可能通过抑制TGF-β通路参与纤维化调控。
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**备注**：以上文献信息为示例，实际研究中请通过学术数据库(如PubMed、Web of Science)检索真实发表的论文。
PDGFR-like (PDGFRL) is a protein closely related to the platelet-derived growth factor receptor (PDGFR) family, which plays critical roles in cell proliferation, migration, and tissue development. Unlike canonical PDGFRs (PDGFRα and PDGFRβ), PDGFRL lacks the intracellular tyrosine kinase domain essential for downstream signaling, suggesting distinct regulatory mechanisms. It is primarily expressed in tissues such as the liver, kidney, and vascular endothelium, though its precise biological functions remain under investigation. PDGFRL is hypothesized to act as a decoy receptor or modulator, competing with PDGFRs for ligand binding (e.g., PDGF-AA, PDGF-BB) to fine-tune signaling activity. This interaction may influence pathways involved in angiogenesis, wound healing, and fibrosis.
Recombinant PDGFRL protein is engineered to study its structural and functional properties in vitro or in vivo. Produced using expression systems like mammalian cells or E. coli, the recombinant form typically retains extracellular domains responsible for ligand or receptor interactions. Researchers utilize it to explore PDGFRL's role in diseases, including cancer, where aberrant PDGF signaling is linked to tumor progression and stromal remodeling. For instance, PDGFRL downregulation has been observed in hepatocellular carcinoma, implying potential tumor-suppressive effects. Conversely, its overexpression in certain contexts may contribute to pathological fibrosis by disrupting normal PDGFR-mediated repair processes.
The protein also serves as a tool for developing therapeutic antibodies or small-molecule inhibitors targeting PDGF/PDGFR pathways. Challenges include clarifying PDGFRL's binding partners, signaling crosstalk, and tissue-specific effects. Current studies leverage recombinant PDGFRL to map interaction networks and validate its diagnostic or prognostic value in disease models. Despite unresolved questions, PDGFRL represents a promising yet underexplored node in growth factor biology, with implications for precision medicine and regenerative therapies.
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