首页 / 产品 / 蛋白 / 细胞因子、趋化因子与生长因子
| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FGFB |
| Uniprot No | P09038 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 143-288aa |
| 氨基酸序列 | PALPEDGGSGAFPPGHFKDPKRLYCKNGGFFLRIHPDGRVDGVREKSDPHIKLQLQAEERGVVSIKGVCANRYLAMKEDGRLLASKCVTDECFFFERLESNNYNTYRSRKYTSWYVALKRTGQYKLGSKTGPGQKAILFLPMSAKS |
| 预测分子量 | 20.4 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. |
以下是关于重组FGF2(碱性成纤维细胞生长因子)蛋白的3篇代表性文献，按规范格式整理：
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1. **标题**：*"High-level expression and purification of recombinant human FGF-2 in Escherichia coli"*
**作者**：Zhang Y. et al.
**摘要**：研究报道了通过大肠杆菌表达系统高效表达人源FGF2重组蛋白的优化策略，采用亲和层析和离子交换层析纯化，获得高纯度活性蛋白，适用于细胞增殖实验。
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2. **标题**：*"Recombinant FGF-2 promotes diabetic wound healing by enhancing angiogenesis and collagen deposition"*
**作者**：Li H. et al.
**摘要**：通过动物模型证明重组FGF2蛋白通过激活FGFR/MAPK信号通路，促进糖尿病创面血管新生和胶原重塑，加速伤口愈合，具有临床转化潜力。
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3. **标题**：*"Stabilization of recombinant FGF-2 by heparin-mimicking polymers for tissue engineering applications"*
**作者**：Wang X. et al.
**摘要**：开发了一种肝素模拟聚合物载体，显著提高了重组FGF2的稳定性及生物活性，在3D打印支架中成功应用于软骨组织再生。
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**备注**：以上文献为示例性内容，实际引用时需以真实发表的论文为准(建议通过PubMed/Web of Science检索关键词：recombinant FGF2. bFGF, fibroblast growth factor expression)。如需具体文献DOI或补充领域，可进一步说明。
Fibroblast Growth Factor Basic (FGFB), also known as FGF2. is a multifunctional signaling protein belonging to the fibroblast growth factor family. Initially identified in the 1970s for its mitogenic activity on fibroblasts, FGFB regulates diverse biological processes, including cell proliferation, differentiation, angiogenesis, wound healing, and tissue repair. It binds to fibroblast growth factor receptors (FGFRs) on target cells, activating downstream signaling pathways such as MAPK and PI3K-AKT, which mediate its physiological effects.
Recombinant FGFB is produced using biotechnological platforms like *E. coli* or mammalian expression systems, ensuring high purity and bioactivity. Its recombinant form overcomes limitations of natural FGFB extraction, such as low yield and contamination risks. This engineered protein retains the ability to interact with heparin sulfate proteoglycans, a critical feature for stabilizing FGFB-FGFR interactions and enhancing signaling efficiency.
In research and therapeutics, recombinant FGFB has shown promise in regenerative medicine. It accelerates tissue repair in burns, chronic ulcers, and ischemic injuries by promoting vascularization and epithelialization. Additionally, it supports stem cell expansion in vitro, aiding tissue engineering applications. However, its dual role in both tissue regeneration and tumor progression necessitates careful therapeutic evaluation. Overexpression of FGFB is linked to cancer angiogenesis and metastasis, prompting studies into context-specific delivery systems or engineered variants with reduced oncogenic potential.
Despite challenges in stability and targeted delivery, recombinant FGFB remains a pivotal tool in developmental biology and translational research, bridging fundamental science with clinical innovation in regenerative therapies. Ongoing studies focus on optimizing its pharmacokinetics and exploring combinatorial approaches with biomaterials to enhance therapeutic precision.
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