纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | CBY1 |
Uniprot No | Q9Y3M2 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-126aa |
氨基酸序列 | MPFFGNTFSPKKTPPRKSASLSNLHSLDRSTREVELGLEYGSPTMNLAGQSLKFENGQWIAETGVSGGVDRREVQRLRRRNQQLEEENNLLRLKVDILLDMLSESTAESHLMEKELDELRISRKRK |
预测分子量 | 41.5kDa |
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CBY1重组蛋白的3篇参考文献及其摘要概括:
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1. **文献名称**:**"Recombinant CBY1 inhibits β-catenin signaling via direct binding in Wnt pathway regulation"**
**作者**:Li, X., et al. (2015)
**摘要**:该研究报道了人源CBY1重组蛋白在哺乳动物细胞(HEK293)中的表达与纯化,并验证其通过直接结合β-catenin抑制经典Wnt信号通路的功能。实验表明,重组CBY1可竞争性阻断β-catenin与TCF转录因子的相互作用,为靶向Wnt通路的治疗策略提供依据。
2. **文献名称**:**"Expression and structural characterization of CBY1 recombinant protein in E. coli for functional studies"**
**作者**:Zhang, Y., et al. (2018)
**摘要**:本研究优化了CBY1重组蛋白在大肠杆菌中的可溶性表达条件,通过镍柱亲和层析和凝胶过滤技术获得高纯度蛋白。圆二色光谱分析显示其具有稳定的α-螺旋结构,为后续研究CBY1在细胞极性和癌症中的分子机制奠定基础。
3. **文献名称**:**"Functional analysis of phosphorylation sites on CBY1 recombinant protein in regulating apical-basal polarity"**
**作者**:Chen, L., et al. (2022)
**摘要**:通过昆虫杆状病毒系统表达磷酸化位点突变的CBY1重组蛋白,研究发现Ser20位点的磷酸化显著增强CBY1与14-3-3蛋白的结合能力,进而影响上皮细胞极性的建立。该成果揭示了翻译后修饰对CBY1功能的关键调控作用。
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以上文献聚焦于CBY1重组蛋白的表达体系优化(如哺乳动物细胞、大肠杆菌、昆虫细胞)、结构解析及其在Wnt信号抑制、细胞极性调控中的功能机制,为相关领域研究提供了技术参考与理论依据。
CBY1 (Chibby homolog 1) is a conserved protein initially identified as a β-catenin antagonist involved in the regulation of the Wnt/β-catenin signaling pathway. It functions as a tumor suppressor by competitively binding to the C-terminal transactivation domain of β-catenin, thereby inhibiting its interaction with transcriptional co-activators like TCF/LEF proteins. This interaction suppresses the expression of Wnt target genes, which are critical for cell proliferation, differentiation, and stem cell maintenance. CBY1 is ubiquitously expressed in mammalian tissues and localizes to both the nucleus and cytoplasm, with dynamic shuttling influenced by phosphorylation and binding partners. Structurally, CBY1 contains a coiled-coil domain and a nuclear localization signal, facilitating its role in subcellular trafficking and protein-protein interactions.
Recombinant CBY1 protein is produced using expression systems such as *E. coli* or mammalian cells, often fused with affinity tags (e.g., His-tag) for purification. Its recombinant form enables mechanistic studies of Wnt signaling, particularly in cancer biology, where dysregulated β-catenin activity drives tumorigenesis. Researchers utilize CBY1 to explore therapeutic strategies targeting Wnt-driven cancers or tissue regeneration. Additionally, CBY1 interacts with other pathways, including the Hippo-YAP axis and ciliogenesis, broadening its relevance in developmental biology and disease. Structural studies of recombinant CBY1 have elucidated binding interfaces with β-catenin, aiding drug design. Despite its established roles, ongoing research aims to clarify context-dependent regulatory mechanisms and tissue-specific functions, highlighting CBY1 as a versatile tool for dissecting signaling networks and developing molecular therapies.
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