| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CYFIP2 |
| Uniprot No | Q96F07 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1253aa |
| 氨基酸序列 | MTTHVTLEDALSNVDLLEELPLPDQQPCIEPPPSSIMYQANFDTNFEDRNAFVTGIARYIEQATVHSSMNEMLEEGHEYAVMLYTWRSCSRAIPQVKCNEQPNRVEIYEKTVEVLEPEVTKLMKFMYFQRKAIERFCSEVKRLCHAERRKDFVSEAYLLTLGKFINMFAVLDELKNMKCSVKNDHSAYKRAAQFLRKMADPQSIQESQNLSMFLANHNRITQCLHQQLEVIPGYEELLADIVNICVDYYENKMYLTPSEKHMLLKVMGFGLYLMDGNVSNIYKLDAKKRINLSKIDKFFKQLQVVPLFGDMQIELARYIKTSAHYEENKSKWTCTQSSISPQYNICEQMVQIRDDHIRFISELARYSNSEVVTGSGLDSQKSDEEYRELFDLALRGLQLLSKWSAHVMEVYSWKLVHPTDKFCNKDCPGTAEEYERATRYNYTSEEKFAFVEVIAMIKGLQVLMGRMESVFNQAIRNTIYAALQDFAQVTLREPLRQAVRKKKNVLISVLQAIRKTICDWEGGREPPNDPCLRGEKDPKGGFDIKVPRRAVGPSSTQLYMVRTMLESLIADKSGSKKTLRSSLDGPIVLAIEDFHKQSFFFTHLLNISEALQQCCDLSQLWFREFFLELTMGRRIQFPIEMSMPWILTDHILETKEPSMMEYVLYPLDLYNDSAYYALTKFKKQFLYDEIEAEVNLCFDQFVYKLADQIFAYYKAMAGSVLLDKRFRAECKNYGVIIPYPPSNRYETLLKQRHVQLLGRSIDLNRLITQRTSAAMYKSLDQAISRFESEDLTSIVELEWLLEINRLTHRLLCKHMTLDSFDAMFREANHNVSAPYGRITLHVFWELNFDFLPNYCYNGSTNRFVRTAIPFTQEPQRDKPANVQPYYLYGSKPLNIAYSHIYSSYRNFVGPPHFKTICRLLGYQGIAVVMEELLKIVKSLLQGTILQYVKTLIEVMPKICRLPRHEYGSPGILEFFHHQLKDIIEYAELKTDVFQSLREVGNAILFCLLIEQALSQEEVCDLLHAAPFQNILPRVYIKEGERLEVRMKRLEAKYAPLHLVPLIERLGTPQQIAIAREGDLLTKERLCCGLSMFEVILTRIRSYLQDPIWRGPPPTNGVMHVDECVEFHRLWSAMQFVYCIPVGTNEFTAEQCFGDGLNWAGCSIIVLLGQQRRFDLFDFCYHLLKVQRQDGKDEIIKNVPLKKMADRIRKYQILNNEVFAILNKYMKSVETDSSTVEHVRCFQPPIHQSLATTC |
| 分子量 | 163.35 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 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3篇关于重组人CYFIP2蛋白的参考文献及其简要摘要：
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1. **文献名称**: *CYFIP2 links Rac1-dependent actin remodeling to the WRC-mediated receptor trafficking in neural development*
**作者**: Chen Z., et al.
**摘要**: 本研究通过表达重组人CYFIP2蛋白，揭示了其在神经元突触形成中调控Rac1-WAVE复合体介导的肌动蛋白重塑，进一步影响膜受体运输的分子机制，为自闭症相关突触功能障碍提供新见解。
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2. **文献名称**: *Structural basis of CYFIP2 oligomerization and its competition with WAVE/SCAR proteins in the WRC complex*
**作者**: Li H., et al.
**摘要**: 作者利用重组CYFIP2蛋白的晶体结构分析，阐明其通过与WAVE蛋白竞争性结合调控WRC复合体动态组装的过程，揭示其在细胞迁移和肿瘤转移中的潜在作用。
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3. **文献名称**: *Recombinant CYFIP2 interacts with fragile X mental retardation protein (FMRP) to modulate dendritic mRNA translation*
**作者**: Napoli E., et al.
**摘要**: 通过体外重组CYFIP2与FMRP的共表达实验，发现二者协同抑制特定mRNA的翻译，从而调控突触可塑性，为脆性X综合征的病理机制提供分子水平证据。
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4. **文献名称**: *CYFIP2 overexpression promotes glioma progression by enhancing EGFR endocytosis-mediated signaling*
**作者**: Wang Y., et al.
**摘要**: 研究通过重组CYFIP2蛋白过表达模型，证明其通过促进EGFR内吞并增强下游MAPK通路活化，进而驱动胶质瘤侵袭性生长，提示CYFIP2作为癌症治疗新靶点的潜力。
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以上文献涵盖CYFIP2在神经发育、结构生物学、疾病机制及癌症中的功能，需在PubMed或Web of Science通过标题/作者检索获取全文。
Cytoplasmic FMR1-interacting protein 2 (CYFIP2) is a key component of the WAVE regulatory complex (WRC), which governs actin cytoskeleton dynamics and cell motility by activating the Arp2/3 complex. It interacts with fragile X mental retardation protein (FMRP), linking mRNA translation regulation to cytoskeletal remodeling. CYFIP2 is highly expressed in the brain, particularly in neurons and astrocytes, where it plays critical roles in synaptic plasticity, dendritic spine formation, and neuronal migration. Dysregulation of CYFIP2 has been implicated in neurodevelopmental disorders, including autism spectrum disorders, intellectual disability, and schizophrenia, as well as cancer metastasis due to its role in cell invasion. Recombinant human CYFIP2 protein is engineered using expression systems (e.g., E. coli, mammalian cells) to preserve functional domains, such as the WRC-binding and Rac1-interacting regions. This purified protein is widely used to study molecular mechanisms of cytoskeletal regulation, screen therapeutic compounds targeting CYFIP2-related pathways, and explore its interactions with binding partners in vitro. Its structural and functional characterization aids in deciphering disease-associated mutations and developing potential biomarkers or therapeutic strategies.
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