纯度 | >85%SDS-PAGE. |
种属 | Human |
靶点 | FRK |
Uniprot No | P42685 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-505aa |
氨基酸序列 | MSNICQRLWE YLEPYLPCLS TEADKSTVIE NPGALCSPQS QRHGHYFVAL FDYQARTAED LSFRAGDKLQ VLDTLHEGWW FARHLEKRRD GSSQQLQGYI PSNYVAEDRS LQAEPWFFGA IGRSDAEKQL LYSENKTGSF LIRESESQKG EFSLSVLDGA VVKHYRIKRL DEGGFFLTRR RIFSTLNEFV SHYTKTSDGL CVKLGKPCLK IQVPAPFDLS YKTVDQWEID RNSIQLLKRL GSGQFGEVWE GLWNNTTPVA VKTLKPGSMD PNDFLREAQI MKNLRHPKLI QLYAVCTLED PIYIITELMR HGSLQEYLQN DTGSKIHLTQ QVDMAAQVAS GMAYLESRNY IHRDLAARNV LVGEHNIYKV ADFGLARVFK VDNEDIYESR HEIKLPVKWT APEAIRSNKF SIKSDVWSFG ILLYEIITYG KMPYSGMTGA QVIQMLAQNY RLPQPSNCPQ QFYNIMLECW NAEPKERPTF ETLRWKLEDY FETDSSYSDA NNFIR |
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. |
由于我无法访问实时数据库或提供真实文献,以下是模拟的参考文献结构示例,供您参考如何描述相关研究。建议您通过PubMed或Google Scholar搜索关键词(如“FRK recombinant protein”、“FRK kinase expression”)获取真实文献。
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1. **标题**: *"High-yield production of recombinant FRK in E. coli and its functional characterization in cancer signaling"*
**作者**: Zhang Y, et al.
**摘要**: 研究报道了在大肠杆菌中优化FRK重组蛋白表达的条件,纯化后的蛋白在体外激酶实验中显示对EGFR信号通路的抑制作用,提示其作为肿瘤治疗靶点的潜力。
2. **标题**: *"Crystal structure of the FRK kinase domain reveals autoinhibitory mechanisms"*
**作者**: Thompson R, et al.
**摘要**: 通过昆虫细胞系统表达并解析了FRK重组蛋白的晶体结构,揭示了其自抑制构象,为开发选择性激酶抑制剂提供结构依据。
3. **标题**: *"Recombinant FRK modulates T-cell activation via phosphorylation of LAT adaptor protein"*
**作者**: Martinez L, et al.
**摘要**: 利用哺乳动物细胞表达的重组FRK蛋白,证实其通过磷酸化LAT蛋白调控T细胞活化,为免疫调节机制研究提供新视角。
4. **标题**: *"Development of a FRK recombinant protein-based assay for drug screening in hepatocellular carcinoma"*
**作者**: Chen X, et al.
**摘要**: 构建了基于FRK重组蛋白的高通量药物筛选平台,筛选出多个小分子化合物可抑制肝癌细胞中FRK的异常激活。
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**建议**:
- 使用上述结构在学术数据库中搜索,结合关键词“FRK recombinant protein” + “expression”、“kinase activity”或“cancer”。
- 关注近年文献(如2020年后),以获取最新进展。
- 检查文献的引用次数,优先选择高影响力期刊的研究。
希望这些示例对您整理文献有所帮助!
**Background of FRK Recombinant Protein**
FRK (Fyn-related kinase), a member of the Src family tyrosine kinases (SFKs), plays a critical role in regulating cellular signaling pathways involved in proliferation, differentiation, and apoptosis. Unlike other SFKs, FRK exhibits unique tissue-specific expression, with high levels observed in epithelial cells and certain cancer types. It functions as a tumor suppressor in some contexts, such as breast cancer, by inhibiting oncogenic signaling through pathways like Ras-MAPK and PI3K-AKT. FRK achieves this by phosphorylating key regulatory proteins or sequestering signaling molecules, thereby modulating downstream effects.
Recombinant FRK protein is engineered using genetic cloning techniques, where the *FRK* gene is inserted into expression vectors (e.g., bacterial, mammalian, or insect systems) to produce purified, functional protein. This recombinant form retains the kinase activity and structural domains (SH2 and SH3) essential for substrate recognition and protein interactions. Its production enables precise study of FRK's biochemical properties, substrate specificity, and interaction networks in vitro.
Research applications include elucidating FRK's role in cancer progression, immune regulation, and metabolic disorders. For instance, FRK recombinant protein is utilized in kinase assays, drug screening for tyrosine kinase inhibitors, and structural studies to design targeted therapies. Additionally, it serves as a tool to investigate cross-talk between FRK and receptors like EGFR or integrins, offering insights into cell adhesion and migration mechanisms. The development of FRK recombinant protein thus bridges molecular biology and translational research, providing a foundation for therapeutic innovations in oncology and beyond.
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