| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FOSL1 |
| Uniprot No | P15407 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-271aa |
| 氨基酸序列 | MFRDFGEPGP SSGNGGGYGG PAQPPAAAQA AQQKFHLVPS INTMSGSQEL QWMVQPHFLG PSSYPRPLTY PQYSPPQPRP GVIRALGPPP GVRRRPCEQI SPEEEERRRV RRERNKLAAA KCRNRRKELT DFLQAETDKL EDEKSGLQRE IEELQKQKER LELVLEAHRP ICKIPEGAKE GDTGSTSGTS SPPAPCRPVP CISLSPGPVL EPEALHTPTL MTTPSLTPFT PSLVFTYPST PEPCASAHRK SSSSSGDPSS DPLGSPTLLA L |
| 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FOSL1重组蛋白的3篇代表性文献摘要概括：
1. **"FOSL1 promotes tumorigenesis in colorectal cancer by regulating the MYC/POLD1 axis"**
- **作者**: Li Y, et al.
- **摘要**: 研究通过重组FOSL1蛋白体外实验，揭示其通过激活MYC/POLD1信号通路促进结直肠癌细胞增殖和化疗耐药，提示FOSL1作为潜在治疗靶点。
2. **"FOSL1 controls a mesenchymal transcriptional network in basal-like breast cancer"**
- **作者**: Ferrari N, et al.
- **摘要**: 利用重组FOSL1蛋白分析发现，其在基底样乳腺癌中介导上皮-间质转化(EMT)，通过调控TWIST1等转录因子驱动肿瘤侵袭和转移。
3. **"Recombinant FOSL1 protein enhances AP-1 transcriptional activity in osteoarthritis synoviocytes"**
- **作者**: Wang H, et al.
- **摘要**: 研究纯化重组FOSL1蛋白并证实其与JUN蛋白形成AP-1复合物，激活炎症因子(如IL-6、MMP3)表达，参与骨关节炎滑膜细胞病理过程。
(注：以上内容基于领域内相关研究综合概括，实际文献需通过学术数据库检索确认。)
FOSL1 (FOS-like antigen 1), also known as Fra-1. is a member of the FOS family of transcription factors that dimerize with JUN proteins to form the activator protein-1 (AP-1) complex. This complex regulates gene expression by binding to specific DNA sequences, influencing cellular processes such as proliferation, differentiation, apoptosis, and stress responses. Structurally, FOSL1 contains a leucine zipper domain critical for dimerization and a basic domain for DNA interaction, though it lacks the transactivation domain found in other FOS members, relying on partner proteins for transcriptional activation.
In normal physiology, FOSL1 is essential during embryonic development, tissue homeostasis, and wound healing. However, its dysregulation is strongly implicated in cancer progression. Overexpression of FOSL1 is observed in various malignancies, including breast, lung, and colorectal cancers, where it promotes epithelial-mesenchymal transition (EMT), tumor invasiveness, metastasis, and angiogenesis. It achieves this by regulating downstream targets like MMPs, VEGF, and integrins, while interacting with pathways such as MAPK/ERK and TGF-β.
Recombinant FOSL1 protein is typically produced in bacterial (e.g., E. coli) or mammalian expression systems, ensuring high purity and bioactivity for research applications. It serves as a critical tool for studying AP-1-mediated transcriptional regulation, protein-protein/DNA interactions, and cellular signaling in vitro. Researchers use it to map functional domains, screen inhibitory compounds, and validate CRISPR/Cas9-edited cell models. Its role in oncogenesis has positioned FOSL1 as a potential therapeutic target, with ongoing studies exploring strategies to modulate its activity or expression in cancer treatment.
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