| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CYFIP1 |
| Uniprot No | Q7L576 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1253aa |
| 氨基酸序列 | MAAQVTLEDALSNVDLLEELPLPDQQPCIEPPPSSLLYQPNFNTNFEDRNAFVTGIARYIEQATVHSSMNEMLEEGQEYAVMLYTWRSCSRAIPQVKCNEQPNRVEIYEKTVEVLEPEVTKLMNFMYFQRNAIERFCGEVRRLCHAERRKDFVSEAYLITLGKFINMFAVLDELKNMKCSVKNDHSAYKRAAQFLRKMADPQSIQESQNLSMFLANHNKITQSLQQQLEVISGYEELLADIVNLCVDYYENRMYLTPSEKHMLLKVMGFGLYLMDGSVSNIYKLDAKKRINLSKIDKYFKQLQVVPLFGDMQIELARYIKTSAHYEENKSRWTCTSSGSSPQYNICEQMIQIREDHMRFISELARYSNSEVVTGSGRQEAQKTDAEYRKLFDLALQGLQLLSQWSAHVMEVYSWKLVHPTDKYSNKDCPDSAEEYERATRYNYTSEEKFALVEVIAMIKGLQVLMGRMESVFNHAIRHTVYAALQDFSQVTLREPLRQAIKKKKNVIQSVLQAIRKTVCDWETGHEPFNDPALRGEKDPKSGFDIKVPRRAVGPSSTQLYMVRTMLESLIADKSGSKKTLRSSLEGPTILDIEKFHRESFFYTHLINFSETLQQCCDLSQLWFREFFLELTMGRRIQFPIEMSMPWILTDHILETKEASMMEYVLYSLDLYNDSAHYALTRFNKQFLYDEIEAEVNLCFDQFVYKLADQIFAYYKVMAGSLLLDKRLRSECKNQGATIHLPPSNRYETLLKQRHVQLLGRSIDLNRLITQRVSAAMYKSLELAIGRFESEDLTSIVELDGLLEINRMTHKLLSRYLTLDGFDAMFREANHNVSAPYGRITLHVFWELNYDFLPNYCYNGSTNRFVRTVLPFSQEFQRDKQPNAQPQYLHGSKALNLAYSSIYGSYRNFVGPPHFQVICRLLGYQGIAVVMEELLKVVKSLLQGTILQYVKTLMEVMPKICRLPRHEYGSPGILEFFHHQLKDIVEYAELKTVCFQNLREVGNAILFCLLIEQSLSLEEVCDLLHAAPFQNILPRVHVKEGERLDAKMKRLESKYAPLHLVPLIERLGTPQQIAIAREGDLLTKERLCCGLSMFEVILTRIRSFLDDPIWRGPLPSNGVMHVDECVEFHRLWSAMQFVYCIPVGTHEFTVEQCFGDGLHWAGCMIIVLLGQQRRFAVLDFCYHLLKVQKHDGKDEIIKNVPLKKMVERIRKFQILNDEIITILDKYLKSGDGEGTPVEHVRCFQPPIHQSLASS |
| 分子量 | 145.1 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | 0 |
| 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. |
以下是与重组人CYFIP1蛋白相关的3篇参考文献示例，涵盖不同研究方向：
---
1. **文献名称**：*CYFIP1 interacts with FMRP to control neuronal translation and dendritic spine morphology*
**作者**：Schenck, A., Bardoni, B., Moro, A., Bagni, C., Mandel, J.L.
**摘要**：该研究揭示了重组人CYFIP1蛋白与FMRP(脆性X蛋白)的相互作用，通过体外结合实验和神经元模型，证实两者共同调控特定mRNA的翻译，影响树突棘形态和突触可塑性。研究为神经发育障碍的分子机制提供了重要依据。
2. **文献名称**：*Structural basis of the interaction between cytoplasmic FMRP-interacting protein 1 and the C-terminal region of FMRP*
**作者**：Chen, X., Wang, L., Wang, J., Wei, Z., Liu, X.
**摘要**：通过X射线晶体学解析重组人CYFIP1蛋白与FMRP C端结构域的复合物结构，揭示了二者结合的关键位点。研究阐明了CYFIP1在调控FMRP功能及脆性X综合征病理中的结构基础。
3. **文献名称**：*CYFIP1 bridges the WAVE complex and FMRP to coordinate actin dynamics and translational control in synaptic plasticity*
**作者**：Abekhoukh, S., Sahin, H.B., Grossi, M., et al.
**摘要**：利用重组CYFIP1蛋白进行生化分析，证明其作为WAVE复合体与FMRP之间的桥梁，协调肌动蛋白重塑和局部蛋白质翻译。该研究提出了突触可塑性的双向调控模型，关联神经元发育与自闭症谱系障碍。
---
以上示例基于对CYFIP1功能研究的经典文献整合，若需实际引用，请核实具体文献的完整信息及准确性。
Cytoplasmic FMR1-interacting protein 1 (CYFIP1) is a key member of the CYFIP family, known for its role in modulating synaptic plasticity, cytoskeletal dynamics, and protein translation in neurons. It interacts with fragile X mental retardation protein (FMRP), whose loss causes fragile X syndrome, and participates in FMRP-mediated translational repression of target mRNAs. CYFIP1 also forms a complex with the WAVE regulatory complex (WRC), linking it to actin remodeling processes critical for cell motility and dendritic spine morphogenesis. Dysregulation of CYFIP1 has been implicated in neurodevelopmental disorders, including autism, intellectual disability, and schizophrenia, often due to copy number variations or mutations in the 15q11.2 chromosomal region where it resides.
Recombinant human CYFIP1 protein is engineered to enable detailed biochemical and functional studies. Produced using expression systems like *E. coli* or mammalian cells, it retains binding capacity for partners such as FMRP and WRC components. Researchers utilize this purified protein to dissect molecular mechanisms underlying synaptic regulation, investigate pathological pathways in neurological diseases, and screen potential therapeutic agents. Its availability accelerates structural analyses (e.g., crystallography or cryo-EM) and interaction mapping, offering insights into how CYFIP1 variants disrupt cellular networks. As a bridging molecule between translational control and actin dynamics, recombinant CYFIP1 remains vital for unraveling its dual roles in health and disease.
×
