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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PDGFC |
| Uniprot No | Q9NRA1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-345aa |
| 氨基酸序列 | MSLFGLLLLTSALAGQRQGTQAESNLSSKFQFSSNKEQNGVQDPQHERII TVSTNGSIHSPRFPHTYPRNTVLVWRLVAVEENVWIQLTFDERFGLEDPE DDICKYDFVEVEEPSDGTILGRWCGSGTVPGKQISKGNQIRIRFVSDEYF PSEPGFCIHYNIVMPQFTEAVSPSVLPPSALPLDLLNNAITAFSTLEDLI RYLEPERWQLDLEDLYRPTWQLLGKAFVFGRKSRVVDLNLLTEEVRLYSC TPRNFSVSIREELKRTDTIFWPGCLLVKRCGGNCACCLHNCNECQCVPSK VTKKYHEVLQLRPKTGVRGLHKSLTDVALEHHEECDCVCRGSTGG |
| 预测分子量 | 65 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篇关于PDGFC重组蛋白的参考文献概要：
1. **《Recombinant PDGF-C promotes wound healing through activation of PDGFRα and α-smooth muscle actin upregulation》**
- **作者**: Smith et al.
- **摘要**: 研究通过大肠杆菌系统表达重组PDGFC蛋白，验证其通过激活PDGFRα受体促进成纤维细胞迁移和皮肤伤口修复的作用，并揭示其调控α-SMA表达的机制。
2. **《Structural and functional characterization of platelet-derived growth factor C (PDGF-C)》**
- **作者**: Reigstad et al.
- **摘要**: 首次报道PDGFC重组蛋白的哺乳动物细胞表达与纯化，解析其蛋白结构域特征，证明其与PDGFRα结合的特异性及促血管生成活性。
3. **《PDGFC signaling in glioblastoma proliferation and invasion》**
- **作者**: Cao et al.
- **摘要**: 利用重组PDGFC蛋白处理胶质母细胞瘤细胞，发现其通过激活ERK和PI3K/AKT通路增强肿瘤细胞增殖和侵袭能力，提示PDGFC作为治疗靶点的潜力。
4. **《Recombinant PDGF-C enhances cardiac repair after myocardial infarction》**
- **作者**: Li et al.
- **摘要**: 在小鼠心梗模型中注射重组PDGFC蛋白，结果显示其通过促进心肌细胞再生和血管新生改善心脏功能，为心血管疾病治疗提供新策略。
(注：上述文献为示例，实际引用时需根据具体研究核实真实文献信息。)
Platelet-derived growth factor C (PDGFC) is a member of the PDGF family, a group of secreted signaling proteins critical for cell proliferation, migration, and tissue development. Identified in the early 2000s, PDGFC distinguishes itself from classical PDGFs (PDGFA and PDGFB) through its unique structure, featuring a conserved growth factor domain and two N-terminal CUB domains. These domains require proteolytic cleavage (e.g., by plasmin or tPA) to release the active ligand, enabling binding to PDGF receptors (primarily PDGFR-αα and αβ heterodimers). PDGFC plays roles in embryonic development, angiogenesis, and wound healing, but dysregulation is linked to fibrosis, atherosclerosis, and cancers, where it promotes tumor growth, metastasis, and stromal interactions.
Recombinant PDGFC is produced using expression systems like mammalian cells (e.g., HEK293) or *E. coli*, ensuring proper folding and post-translational modifications. Purification via affinity chromatography yields high-purity proteins validated by SDS-PAGE and functional assays. Its applications span basic research—studying PDGF/RTK signaling pathways—and preclinical models of disease, including organ fibrosis and tumor xenografts. In biotechnology, recombinant PDGFC serves as a culture additive to maintain stem cell pluripotency or drive mesenchymal cell expansion in tissue engineering. Therapeutic exploration focuses on neutralizing antibodies or receptor inhibitors in PDGFC-driven pathologies. However, challenges remain in understanding context-dependent signaling and optimizing delivery strategies for clinical translation. Overall, recombinant PDGFC is a versatile tool bridging mechanistic studies and translational innovation in regenerative medicine and oncology.
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