CYFIP1 Antibody

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Description

Introduction to CYFIP1 Antibody

CYFIP1 antibodies are polyclonal or monoclonal immunoglobulins designed to bind specifically to the CYFIP1 protein. These antibodies are essential for:

  • Western blotting (WB): Quantifying CYFIP1 protein levels in cell lysates or tissues .

  • Immunoprecipitation (IP): Identifying protein-protein interactions (e.g., CYFIP1-FMRP complexes) .

  • Immunofluorescence (IF): Localizing CYFIP1 at synapses or subcellular compartments .

  • ELISA: Measuring CYFIP1 concentrations in biological fluids .

CYFIP1 antibodies are typically raised against synthetic peptides corresponding to specific regions of the protein, such as AA 1159–1208 or AA 320–449, ensuring epitope specificity .

Applications in Research

CYFIP1 antibodies enable diverse experimental approaches:

Western Blotting

  • Detection specificity: Validates CYFIP1 expression in neurons, blood cells, or lymphoblastoid lines .

  • Example: In Cyfip1 +/− mice, WB confirmed reduced CYFIP1 levels in hippocampal lysates .

Immunoprecipitation

  • Interaction studies: Co-immunoprecipitation (Co-IP) identified CYFIP1 binding partners, including FMRP and eIF4E .

  • mRNA profiling: RIP-qPCR with anti-CYFIP1 antibodies revealed interactions with Grin2a, Grin2b, and Gabbr2 mRNAs, linking CYFIP1 to NMDAR and GABA receptor regulation .

Immunofluorescence

  • Synaptic localization: Demonstrated CYFIP1 enrichment at inhibitory synapses and its role in regulating GABA receptor β-subunits .

  • Dendritic spine dynamics: Showed CYFIP1 overexpression increases immature spine density in hippocampal neurons .

Specificity and Reactivity Profile

CYFIP1 antibodies exhibit broad cross-reactivity:

AntibodyTarget RegionReactivityApplicationsSource
ABIN6749221AA 1159–1208Human, Mouse, Rat, Zebrafish, etc.WB, ELISA, IF
Cell Signaling #44353Not specifiedHuman, MouseWB
Abcam ab108220Not specifiedHuman, MouseWB, IP
Sigma-Aldrich HPA068106Not specifiedHumanIHC, IF

Note: Cross-reactivity with CYFIP2 is minimal due to divergent epitopes .

Synaptic Regulation

  • Inhibitory synapses: CYFIP1 overexpression reduces miniature inhibitory postsynaptic current (mIPSC) amplitude, while loss increases mIPSC amplitude and GABA receptor clustering .

  • Excitatory/inhibitory balance: CYFIP1 haploinsufficiency enhances AMPA receptor mobility, disrupting synaptic plasticity .

Neurodevelopmental Disorders

  • 15q11.2 CNV: Copy number variations in CYFIP1 are linked to autism and schizophrenia. Antibody studies revealed CYFIP1’s role in regulating neuroligin 3 and NMDAR subunits .

  • White matter changes: Cyfip1 +/− rats showed reduced fractional anisotropy in corpus callosum, correlating with myelin deficits .

Molecular Interactions

  • FMRP antagonism: CYFIP1 and FMRP counteract each other’s effects on mTOR signaling and synaptic growth .

  • mRNA translation: CYFIP1 represses eIF4E-eIF4G interaction, inhibiting translation of target mRNAs .

Product Specs

Buffer
Preservative: 0.03% ProClin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Form
Liquid
Lead Time
Order fulfillment typically takes 1-3 business days. Delivery times may vary depending on the order fulfillment method and destination. Please contact your local distributor for precise delivery estimates.
Synonyms
CY antibody; CYFIP 1 antibody; CYFIP1 antibody; CYFP1_HUMAN antibody; Cytoplasmic FMR1 interacting protein 1 antibody; Cytoplasmic FMR1-interacting protein 1 antibody; FLJ45151 antibody; KIAA0068 antibody; p140sra 1 antibody; p140sra-1 antibody; P140SRA1 antibody; Selective hybridizing clone antibody; SHYC antibody; Specifically Rac1 associated protein 1 antibody; Specifically Rac1-associated protein 1 antibody; SRA 1 antibody; Sra-1 antibody; SRA1 antibody
Target Names
Uniprot No.

Target Background

Function

CYFIP1 antibody targets CYFIP1, a component of the CYFIP1-EIF4E-FMR1 complex. This complex binds to the mRNA cap and mediates translational repression. Within the complex, CYFIP1 acts as an adapter protein between EIF4E and FMR1, enhancing FMR1's translational repression activity in the brain, likely by facilitating its interaction with EIF4E and mRNA. Furthermore, CYFIP1 plays a role in regulating the formation of membrane ruffles and lamellipodia, axon outgrowth, and is involved in the WAVE complex, regulating actin filament reorganization via interaction with the Arp2/3 complex. Its actin remodeling activity is modulated by RAC1. CYFIP1 also functions as a regulator of epithelial morphogenesis and, as part of the WAVE1 complex, is essential for BDNF-NTRK2 endocytic trafficking and signaling from early endosomes. Some studies suggest it may function as a tumor suppressor in certain cancers.

Gene References Into Functions

CYFIP1's Role in Various Biological Processes: The following studies highlight CYFIP1's involvement in several key biological processes and disease states:

  • Upregulation of CYFIP1 gene expression in the blood of epileptic patients. PMID: 29992499
  • The MNK-eiF4E axis regulates translation of specific mRNAs involved in cancer metastasis and neuronal synaptic plasticity through a novel mechanism involving CYFIP1, a translational repressor (Review). PMID: 27527252
  • Association of the rs4778298 variant in CYFIP1 with inter-individual variation in the surface area of the left supramarginal gyrus. PMID: 27351196
  • Significantly lower mRNA and protein expression levels of Cyfip1 observed in Acute Lymphoblastic Leukemia (ALL) patients. PMID: 26779626
  • Dysregulation of schizophrenia and epilepsy gene networks resulting from reduced CYFIP1 in human neural progenitors. PMID: 26824476
  • Hippocampal synapses with reduced Cyfip1 exhibit increased size and faster neurotransmitter release. PMID: 26843638
  • CYFIP1 upregulation observed in transformed lymphoblastoid cell lines and, for the first time, in post-mortem brain tissue from patients with 15q11-13 duplication. PMID: 25311365
  • Alterations in CYFIP2 levels in the postsynaptic density of schizophrenia patients. PMID: 25048004
  • CYFIP1 haploinsufficiency causes cell polarity defects through WAVE complex destabilization; genetic polymorphism is associated with schizophrenia. PMID: 24996170
  • Imbalance in specific CYFIP1 isoforms (an FMRP interaction partner) and CAMK4 (an FMRP gene transcriptional regulator) modulates autism spectrum disorder risk. PMID: 24442360
  • CYFIP/Sra/PIR121-containing protein complexes coordinate Arf1 and Rac1 signaling during clathrin-AP-1-coated carrier biogenesis at the trans-Golgi network. PMID: 20228810
  • CYFIP1 located in the genomic region between breakpoints 1 and 2 on chromosome 15, implicated in Prader-Willi/Angelman syndromes. PMID: 14508708
  • CRMP-2 transports the Sra-1/WAVE1 complex to axons in a kinesin-1-dependent manner, regulating axon outgrowth and formation. PMID: 16260607
  • Correlation between quantified mRNA levels of NIPA2, NIPA2, CYFIP1, and GCP5 in Prader-Willi syndrome and psychological/behavioral scales. PMID: 16982806
  • Frequent deletion of Cyfip1, a subunit of the WAVE complex regulating cytoskeletal dynamics, in human epithelial cancers. PMID: 19524508
Database Links

HGNC: 13759

OMIM: 606322

KEGG: hsa:23191

STRING: 9606.ENSP00000324549

UniGene: Hs.26704

Protein Families
CYFIP family
Subcellular Location
Cytoplasm. Cytoplasm, perinuclear region. Cell projection, lamellipodium. Cell projection, ruffle. Cell junction, synapse, synaptosome.

Q&A

What is CYFIP1 and why is it significant in neurodevelopmental research?

CYFIP1 is a highly conserved protein that interacts with Fragile X mental retardation protein (FMRP) and serves as a member of the WAVE regulatory complex (WRC). It represents a critical link between translational regulation and the actin cytoskeleton . CYFIP1 has gained significant attention in neurodevelopmental research as a candidate gene for intellectual disability, autism spectrum disorders, schizophrenia, and epilepsy . Its importance stems from its dual functionality: as a co-repressor of translation through interaction with FMRP and eIF4E, and as a regulator of actin cytoskeleton remodeling through the WRC . Research indicates that altered CYFIP1 expression leads to abnormal neuronal morphology and function, making it a valuable target for understanding the molecular basis of several neurological conditions .

What are the key characteristics of commercially available CYFIP1 antibodies?

Commercial CYFIP1 antibodies are available in several formats, with rabbit monoclonal antibodies showing high specificity and sensitivity for endogenous detection . Most CYFIP1 antibodies detect a protein of approximately 140-145 kDa molecular weight . Species reactivity typically includes human, mouse, and rat samples, making these antibodies versatile for comparative studies across model organisms . The antibodies are generally suitable for multiple applications including Western blotting (recommended dilution 1:500-1:1000), immunoprecipitation, immunohistochemistry (recommended dilution 1:300-1:1200), and flow cytometry . Some antibodies may cross-react with CYFIP2 due to sequence homology, so validation experiments are essential when specificity between family members is required .

How do CYFIP1 expression patterns differ across tissue types and developmental stages?

CYFIP1 expression is predominantly observed in neural tissues, with particularly high expression in the brain . Within the brain, CYFIP1 shows differential expression across regions, with notable presence in cortical neurons and the olfactory bulb . During development, CYFIP1 plays crucial roles in neuronal growth and differentiation, with its expression being tightly regulated throughout neurodevelopment . The protein is also detectable in non-neural tissues including blood cells, where altered expression has been documented in patients with the BP1-BP2 deletion of chromosome 15q11.2 . When designing studies to assess CYFIP1 expression, researchers should consider these tissue-specific and developmental variations, selecting appropriate positive controls such as brain tissue for Western blotting or immunohistochemistry applications .

What are the optimal conditions for using CYFIP1 antibodies in Western blotting?

For optimal Western blotting results with CYFIP1 antibodies, researchers should prepare lysates from tissues or cells with adequate expression levels, with brain tissue from human, mouse, or rat being ideal positive controls . The high molecular weight of CYFIP1 (approximately 145 kDa) requires careful consideration of gel percentage and transfer conditions; use of 8% SDS-PAGE gels and extended transfer times (overnight at lower voltage) often yields better results for large proteins . Recommended antibody dilutions range from 1:500 to 1:1000 for most commercial CYFIP1 antibodies . For blocking and antibody dilution, 5% non-fat dry milk or BSA in TBST is typically effective . Detection can be performed using standard chemiluminescence methods, with exposure times adjusted based on expression levels. When troubleshooting weak signals, consider increasing protein load, extending primary antibody incubation time (overnight at 4°C), or using signal enhancement systems.

How should immunoprecipitation protocols be optimized for CYFIP1 studies?

For successful CYFIP1 immunoprecipitation, begin with fresh tissue or cell lysates prepared in a non-denaturing lysis buffer containing protease inhibitors . Brain tissue lysates provide reliable positive controls due to high endogenous CYFIP1 expression . The recommended antibody amount is 0.5-4.0 μg for 1.0-3.0 mg of total protein lysate . Pre-clearing lysates with protein A/G beads can reduce non-specific binding . Incubate lysates with CYFIP1 antibody overnight at 4°C with gentle rotation, followed by addition of protein A/G beads for 2-4 hours . After thorough washing with lysis buffer, elute proteins by boiling in SDS sample buffer . For verification of successful immunoprecipitation, perform Western blotting with a second CYFIP1 antibody that recognizes a different epitope or with antibodies against known CYFIP1 interaction partners such as FMRP or eIF4E . This approach will help confirm the specificity of the immunoprecipitated complex.

What controls are essential when using CYFIP1 antibodies for immunohistochemistry?

When performing immunohistochemistry with CYFIP1 antibodies, several controls are critical for result validation. Include positive control tissues with known CYFIP1 expression such as mouse or human brain tissue, specifically cortical neurons where CYFIP1 is abundantly expressed . Negative controls should include tissues from CYFIP1 knockdown models or sections processed identically but with primary antibody omitted . For antigen retrieval, both TE buffer (pH 9.0) and citrate buffer (pH 6.0) have been reported effective, though comparative testing may be necessary to determine optimal conditions for specific tissue preparations . A dilution series (e.g., 1:300, 1:600, 1:1200) should be tested to establish the optimal antibody concentration that maximizes specific signal while minimizing background . When interpreting results, consider that CYFIP1 typically shows cytoplasmic localization with enrichment in neuronal processes . Cross-validation using multiple detection methods (e.g., in situ hybridization for mRNA expression alongside protein detection) provides stronger evidence for expression patterns.

How can researchers effectively distinguish between CYFIP1 and CYFIP2 in experimental systems?

Distinguishing between CYFIP1 and CYFIP2 presents a significant challenge due to their structural similarity and sequence homology . For antibody-based differentiation, carefully select antibodies raised against unique regions of each protein and thoroughly validate specificity using positive controls (overexpression systems) and negative controls (knockdown/knockout systems) . Western blotting may reveal subtle differences in molecular weight (CYFIP1 at approximately 145 kDa and CYFIP2 at approximately 130 kDa) . RNA-based methods offer an alternative approach, with RT-qPCR using gene-specific primers providing quantitative distinction between transcripts . For functional studies, siRNA or shRNA knockdown with validated target specificity allows selective depletion of either protein, though off-target effects should be carefully controlled . When interpreting published literature, researchers should critically assess which CYFIP family member was actually studied, as some earlier publications may not have clearly distinguished between them.

What mechanisms underlie the antagonistic relationship between CYFIP1 and FMRP in neuronal development?

The antagonistic relationship between CYFIP1 and FMRP represents a complex regulatory mechanism in neuronal development. Research reveals that these proteins have opposing effects on neuromuscular junction growth in Drosophila and neuronal differentiation in the mouse olfactory bulb . Mechanistically, this antagonism operates through differential modulation of the mTor signaling pathway . While CYFIP1 positively correlates with mTor expression (with CYFIP1 reduction leading to 40-60% decrease in mTor protein levels), FMRP negatively regulates this pathway through distinct mechanisms . FMRP's effect appears to operate through PI3K pathway overactivation via the catalytic subunit p110β, rather than through direct alteration of mTor expression . Importantly, CYFIP1 does not influence p110β expression, suggesting these proteins regulate mTor through independent pathways that ultimately have opposing functional outcomes . This antagonism extends beyond mTor signaling, as CYFIP1 and FMRP also differentially regulate G-quadruplex-dependent translation, with FMRP but not CYFIP1 acting as a repressor in this context .

How does altered CYFIP1 expression correlate with the pathophysiology of neurodevelopmental disorders?

Altered CYFIP1 expression significantly impacts neurodevelopmental pathways, with both reduced and increased expression linked to pathological conditions . In patients carrying the BP1-BP2 deletion of chromosome 15q11.2 (which includes CYFIP1), reduced CYFIP1 mRNA levels are accompanied by decreased expression of other WRC members (CYFIP2, NAP1, ABI1, WAVE2, and HSPC300) . This suggests coordinated regulation of the entire complex rather than independent regulation of individual components. Conversely, in rare cases of BP1-BP2 duplication, mRNA levels of WRC members tend to increase . At the cellular level, CYFIP1 knockdown in neurons results in reduced dendritic arborization, with more profound effects in mature neurons (21 DIV) compared to younger neurons (14 DIV) . The phenotypic consequences of altered CYFIP1 expression appear to be mediated through multiple mechanisms, including changes in mTor signaling, cytoskeletal reorganization, and potentially altered translation of specific mRNAs . These findings suggest that precise CYFIP1 dosage is critical for normal neurodevelopment, with both haploinsufficiency and overexpression potentially contributing to disorder pathophysiology.

Why might CYFIP1 antibodies show inconsistent results across different experimental platforms?

Inconsistent results with CYFIP1 antibodies across experimental platforms can stem from multiple factors. Antibody epitope accessibility may vary depending on sample preparation methods, with certain fixatives or extraction buffers potentially masking recognition sites . Post-translational modifications of CYFIP1 in different cellular contexts might alter antibody binding, as CYFIP1 undergoes regulatory modifications that could affect epitope recognition . Splice variants or isoforms of CYFIP1 may be differentially detected by antibodies targeting distinct regions of the protein . Cross-reactivity with CYFIP2 can occur due to sequence homology, creating false positive signals in tissues where both proteins are expressed . Researchers should validate antibody specificity using multiple approaches: 1) comparing results with different antibodies targeting distinct CYFIP1 epitopes, 2) including positive and negative controls (particularly CYFIP1 knockdown/knockout samples), and 3) confirming results with complementary techniques such as mass spectrometry or RNA-level analysis .

How can researchers overcome challenges in detecting CYFIP1 protein-protein interactions?

Detecting CYFIP1 protein-protein interactions presents several challenges due to its involvement in multiple complexes. To overcome these challenges, researchers can employ a multi-faceted approach. Crosslinking proteins prior to lysis can stabilize transient interactions that might otherwise be lost during extraction . Optimizing lysis conditions is crucial, as harsh detergents may disrupt interactions while insufficient extraction may limit protein accessibility; testing multiple buffers with varying detergent strengths is advisable . For co-immunoprecipitation, using antibodies directed against different epitopes of CYFIP1 can help avoid interference with binding sites involved in protein interactions . Proximity ligation assays provide an alternative for detecting interactions in situ, offering spatial information about where interactions occur within cells . For comprehensive interaction mapping, mass spectrometry following immunoprecipitation (IP-MS) can identify both known and novel interaction partners . Control experiments should include testing interactions under different cellular conditions (e.g., stimulation with BDNF, which has been shown to regulate CYFIP1 interactions with eIF4E) .

What strategies can address discrepancies in CYFIP1 expression data between transcript and protein levels?

Discrepancies between CYFIP1 transcript and protein levels represent a common challenge in molecular research. Several strategies can help address this issue. Perform time-course experiments to account for temporal delays between transcription and translation, as regulatory mechanisms may operate with different kinetics at each level . Consider post-transcriptional regulation through microRNAs or RNA-binding proteins that might affect translation efficiency of CYFIP1 mRNA without altering transcript levels . Assess protein stability and turnover using pulse-chase experiments or proteasome inhibitors to determine if differences stem from altered protein degradation rather than synthesis . Examine subcellular localization, as changes in protein distribution rather than total expression may underlie observed discrepancies . For comprehensive analysis, combine absolute quantification methods for both mRNA (digital PCR) and protein (selected reaction monitoring mass spectrometry) to obtain comparable measurements across levels . When interpreting published literature, consider method sensitivity limitations—Western blotting may not detect subtle changes that are statistically significant at the mRNA level, and vice versa .

How might single-cell analysis techniques advance our understanding of CYFIP1 function in heterogeneous neural populations?

Single-cell analysis techniques offer unprecedented opportunities to resolve cell-type specific roles of CYFIP1 in heterogeneous neural populations. Single-cell RNA sequencing can reveal cell populations with differential CYFIP1 expression patterns and identify co-regulated gene networks across diverse neural cell types . Spatial transcriptomics provides additional context by mapping CYFIP1 expression to specific brain regions while maintaining information about cellular relationships and microenvironments . For protein-level analysis, mass cytometry (CyTOF) with metal-conjugated CYFIP1 antibodies enables quantitative assessment across numerous cells while simultaneously measuring dozens of other proteins . Single-cell western blotting and proximity ligation assays can detect CYFIP1 protein interactions at the individual cell level . These approaches will help resolve conflicting findings from bulk tissue analyses by determining whether observed effects represent global changes across all cells or dramatic alterations in specific cell subpopulations . This cell-type resolution is particularly relevant given CYFIP1's involvement in disorders affecting specific neural circuits and its differential expression across brain regions .

What novel approaches can better elucidate the dynamic regulation of CYFIP1 in response to neuronal activity?

Understanding the dynamic regulation of CYFIP1 in response to neuronal activity requires innovative approaches beyond static measurements. Live imaging using genetically encoded CYFIP1 fusion proteins (e.g., CYFIP1-GFP) enables real-time monitoring of protein localization and trafficking in response to neuronal stimulation . For temporal regulation of protein interactions, optogenetic tools can be adapted to manipulate CYFIP1 associations with binding partners like FMRP or components of the WRC in specific subcellular compartments with precise timing . Fluorescence resonance energy transfer (FRET) sensors designed to detect CYFIP1 conformational changes could reveal how activity-dependent signaling modifies protein function . Time-resolved proteomics using CYFIP1 immunoprecipitation at defined intervals following neuronal stimulation can map dynamic changes in interacting protein networks . To link these molecular dynamics to functional outcomes, researchers can combine these approaches with simultaneous monitoring of local protein synthesis (using techniques like FUNCAT) and cytoskeletal dynamics (using LifeAct or SiR-Actin) . These multi-modal analyses will provide mechanistic insights into how activity-dependent CYFIP1 regulation contributes to synapse-specific modifications underlying learning and memory.

How can integrative multi-omics approaches resolve contradictory findings in CYFIP1 research?

Integrative multi-omics approaches offer powerful strategies to resolve contradictory findings in CYFIP1 research by providing comprehensive, systems-level perspectives. Combining transcriptomics, proteomics, and phosphoproteomics from the same samples can identify discrepancies between RNA and protein expression while revealing regulatory post-translational modifications of CYFIP1 and its interaction partners . Network analysis integrating protein-protein interaction data with transcriptional co-expression patterns can contextualize CYFIP1 function within broader cellular pathways and identify potential compensatory mechanisms that might explain contradictory experimental outcomes . Comparative analyses across model systems (from cell lines to different animal models) using standardized methodologies can distinguish species-specific effects from conserved CYFIP1 functions . For translational relevance, parallel studies in patient-derived samples (such as induced pluripotent stem cell-derived neurons from individuals with CYFIP1 mutations) alongside animal models can validate findings across systems . Data integration platforms and machine learning approaches can help identify patterns across heterogeneous datasets, potentially revealing conditional factors that determine when CYFIP1 exhibits specific functional properties . This systems-level understanding will help resolve seemingly contradictory roles of CYFIP1 in different experimental contexts.

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