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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FGF5 |
| Uniprot No | P12034 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 18-268aa |
| 氨基酸序列 | MAWAHGEKRLAPKGQPGPAATDRNPIGSSSRQSSSSAMSSSSASSSPAAS LGSQGSGLEQSSFQWSPSGRRTGSLYCRVGIGFHLQIYPDGKVNGSHEAN MLSVLEIFAVSQGIVGIRGVFSNKFLAMSKKGKLHASAKFTDDCKFRERF QENSYNTYASAIHRTEKTGREWYVALNKRGKAKRGCSPRVKPQHISTHFL PRFKQSEQPELSFTVTVPEKKNPPSPIKSKIPLSAPRKNTNSVKYRLKFR FG |
| 预测分子量 | 28 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FGF5重组蛋白的3篇代表性文献示例(注：文献信息为示例性质，实际引用需核实)：
1. **文献名称**: "Recombinant human FGF5 accelerates hair follicle regression in murine models"
**作者**: Suzuki K, et al.
**摘要**: 研究利用重组人FGF5蛋白处理小鼠皮肤，发现其通过调控毛囊从生长期向退行期转化，证实FGF5在毛发周期中的关键作用。
2. **文献名称**: "Expression and purification of bioactive FGF5 in Escherichia coli for functional studies"
**作者**: Wang Y, et al.
**摘要**: 报道了一种利用大肠杆菌表达系统高效生产可溶性重组FGF5蛋白的方法，并通过细胞增殖实验验证其生物活性。
3. **文献名称**: "FGF5-mediated epithelial-mesenchymal transition in cancer: Role of recombinant protein delivery"
**作者**: Chen L, et al.
**摘要**: 发现重组FGF5蛋白可通过激活MAPK/ERK通路促进肿瘤细胞上皮间质转化(EMT)，提示其在癌症转移中的潜在机制。
4. **文献名称**: "Therapeutic potential of FGF5 inhibition in alopecia: In vivo evidence from recombinant protein-based approaches"
**作者**: Higgins CA, et al.
**摘要**: 使用重组FGF5中和抗体阻断其活性，显著延长小鼠毛发生长期，为脱发治疗提供新策略。
**注意**：以上文献标题及内容为领域相关方向示例，实际文献需通过PubMed、Web of Science等数据库检索最新研究。建议结合具体研究方向(如分子机制、疾病模型、生产工艺)进一步筛选。
**Background on Recombinant FGF5 Protein**
Fibroblast Growth Factor 5 (FGF5), a member of the FGF family, is a signaling protein involved in regulating cellular processes such as proliferation, differentiation, and survival. Initially identified for its role in hair growth cycle regulation, FGF5 is notably expressed during the catagen phase, where it signals hair follicles to transition from active growth (anagen) to regression. Beyond its dermatological relevance, FGF5 participates in broader physiological and pathological contexts, including embryonic development, tissue repair, and cancer progression. Its biological activity is mediated through binding to fibroblast growth factor receptors (FGFRs), triggering downstream signaling cascades like MAPK and PI3K-AKT pathways.
Recombinant FGF5 protein is engineered using biotechnological platforms, such as *E. coli* or mammalian expression systems, to produce bioactive forms with high purity and consistency. This engineered protein retains the native structure and function, enabling researchers to study FGF5’s mechanisms *in vitro* and *in vivo*. Applications span basic research—elucidating its role in hair follicle biology, angiogenesis, or neural development—to therapeutic exploration. For instance, inhibiting FGF5 activity (via antibodies or small molecules) has emerged as a strategy to delay hair loss by prolonging the anagen phase, a concept explored in androgenetic alopecia treatments. Conversely, in cancers where FGF5 overexpression correlates with tumor growth and metastasis, recombinant FGF5 serves as a tool to model pathways or screen targeted therapies.
The development of recombinant FGF5 also underscores its dual role as both a potential therapeutic target and a disease biomarker. Its versatility in research and drug development highlights the growing interest in modulating FGF signaling for precision medicine, particularly in oncology and regenerative therapies. However, challenges remain in optimizing delivery methods and minimizing off-target effects, underscoring the need for continued mechanistic studies. Overall, recombinant FGF5 represents a critical reagent for advancing our understanding of FGF biology and translating these insights into clinical applications.
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