FMN1 Antibody, HRP conjugated

What is FMN1 and what are its key biological functions in research models?

FMN1 (Formin 1) is a cytoskeletal protein that plays critical roles in actin filament assembly and organization. It is involved in the formation of adherens junctions and the polymerization of linear actin cables . FMN1 has significant developmental functions, particularly in limb development, which is why it's also known as "Limb deformity protein homolog" .

In neuronal contexts, FMN1 has been identified as a key mediator of dendritogenesis and synaptogenesis. Research has demonstrated that overexpression of the Fmn1-Ib isoform increases the number of primary dendrites by approximately 50% in cultured hippocampal neurons and significantly increases the number of glutamatergic synaptic terminals without affecting GABAergic terminals . FMN1 has been shown to localize to the cytoplasm of neurons, particularly concentrating along microtubules, indicating its role in both actin and microtubule cytoskeletal organization .

Additionally, a circular RNA derived from the FMN1 gene (ciRNA-Fmn1) is specifically enriched in nervous tissue and has been implicated in neuropathic pain regulation through interaction with the ubiquitin ligase UBR5 .

What applications can FMN1 Antibody, HRP conjugated be used for in molecular and cellular research?

FMN1 Antibody, HRP conjugated has been validated for several laboratory applications including:

The HRP (Horseradish Peroxidase) conjugation provides direct enzymatic detection capability, simplifying experimental protocols by eliminating the need for secondary antibody incubation. This conjugation enables direct visualization through chemiluminescent, colorimetric, or fluorescent substrates depending on the detection system used .

How should researchers verify the specificity of FMN1 Antibody, HRP conjugated in experimental systems?

To ensure reliable and reproducible results, researchers should implement multiple validation approaches:

Positive and negative controls:

• Use tissues or cell lines with known FMN1 expression as positive controls (neuronal tissues are particularly relevant)

• Implement FMN1 knockdown models as biological negative controls

siRNA validation approach:
Research has demonstrated that FMN1-specific siRNAs can effectively reduce both FMN1 mRNA and protein levels, providing an excellent validation system. In particular, siRNA2 and siRNA3 have been shown to significantly reduce FMN1 expression without affecting β-actin levels, demonstrating specificity . This approach can be used to:

• Transfect cells with FMN1-specific siRNA

• Confirm knockdown by qPCR

• Validate antibody specificity by Western blot showing reduced signal intensity

Peptide competition assay:

• Pre-incubate the antibody with the immunizing peptide

• A significant reduction in signal indicates specificity for the target epitope

Cross-validation with multiple detection methods:

• Compare results between different antibody-based techniques (WB, IHC, ELISA)

• Correlate protein detection with mRNA expression data

What are the optimal conditions for using FMN1 Antibody, HRP conjugated in Western blot analysis?

For detecting FMN1 (expected MW: ~158 kDa) in Western blot applications, the following optimized protocol is recommended:

Sample preparation:

• Use RIPA or NP-40 lysis buffers containing protease inhibitor cocktails

• Denature proteins at 95°C for 5 minutes in Laemmli buffer with reducing agent

Gel electrophoresis parameters:

• Use 7-8% polyacrylamide gels for optimal resolution of high molecular weight FMN1

• Load 20-50 μg of total protein per lane

• Include molecular weight markers covering 100-250 kDa range

Transfer conditions:

• Transfer to 0.45 μm nitrocellulose or PVDF membranes

• For large proteins like FMN1, use wet transfer at 30V overnight at 4°C or 100V for 2 hours in cold transfer buffer with 10-20% methanol

Blocking and antibody incubation:

• Block with 5% non-fat dry milk or BSA in TBST for 1-2 hours at room temperature

• Dilute FMN1 Antibody, HRP conjugated at 1:500-1:2,000 in blocking buffer

• Incubate overnight at 4°C with gentle rocking

• Wash 5-6 times with TBST, 5-10 minutes each

Detection system:

• Use enhanced chemiluminescent (ECL) substrate optimized for HRP

• Begin with 30-second exposure and adjust as needed

• For densitometric analysis, ensure images are captured within the linear range

When analyzing FMN1 in neuronal samples, researchers should be aware that the protein may display altered mobility patterns due to post-translational modifications or tissue-specific expression of different isoforms .

How can researchers troubleshoot non-specific binding when using FMN1 Antibody, HRP conjugated?

When encountering non-specific bands or high background in experiments with FMN1 Antibody, HRP conjugated, implement these evidence-based troubleshooting strategies:

For Western blot applications:

For immunohistochemistry applications:

• Critical step: Quench endogenous peroxidase activity

  • For paraffin sections: 0.3% H₂O₂ in methanol for 30 minutes

  • For frozen sections: 0.1% H₂O₂ in PBS for 15 minutes

• Optimization matrix approach:
  Test combinations of:

  • Blocking agents (BSA, normal serum, commercial blockers)

  • Antibody dilutions (starting at the higher end of recommended range)

  • Incubation temperatures (4°C vs. room temperature)

• Control experiments:

  • Include no-primary antibody controls

  • Use isotype controls (rabbit IgG at equivalent concentration)

  • When possible, include FMN1 knockdown samples

What is the recommended protocol for studying FMN1-FNBP4 interactions using FMN1 Antibody, HRP conjugated?

Research has established that FNBP4 interacts with the poly-proline-rich formin homology 1 (FH1) domain of FMN1 . This interaction can be studied using FMN1 Antibody, HRP conjugated through the following protocol:

Co-Immunoprecipitation Protocol:

• Lysate preparation:

  • Lyse cells in non-denaturing buffer (e.g., 20 mM Tris-HCl pH 8.0, 137 mM NaCl, 1% NP-40, 2 mM EDTA) with protease inhibitors

  • Clear lysates by centrifugation (14,000 × g, 15 min, 4°C)

• Pre-clearing:

  • Incubate lysate with Protein A/G beads for 1 hour at 4°C

  • Remove beads by centrifugation

• Immunoprecipitation:

  • Add anti-FNBP4 antibody (5 μg) to pre-cleared lysate

  • Incubate overnight at 4°C with gentle rotation

  • Add Protein A/G beads and incubate for 2-4 hours at 4°C

  • Wash beads 4-5 times with lysis buffer

• Detection:

  • Elute proteins by boiling in Laemmli buffer

  • Separate by SDS-PAGE

  • Transfer to membrane

  • Detect FMN1 using FMN1 Antibody, HRP conjugated (1:500 dilution)

• Validation:

  • Perform reciprocal Co-IP using FMN1 antibody for immunoprecipitation and FNBP4 antibody for detection

  • Include appropriate controls (IgG control, input lysate)

Key scientific insights for experimental design:

Surface plasmon resonance studies have revealed the precise binding characteristics of the FMN1-FNBP4 interaction:

• The binding affinity (KD) between FNBP4 and FMN1 is 1.84 nM

• Association rate constant (ka): 3.31*106 M-1s-1

• Dissociation rate constant (kd): 5.705*10-4 s-1

Furthermore, domain-specific analysis has shown that:

• Only the WW1 domain of FNBP4 binds to FMN1, with a KD of 2 nM

• The WW2 domain of FNBP4 does not interact with FMN1

• Only the FH1 domain of FMN1 participates in this interaction; the FH2 domain does not

These insights should guide experimental design when analyzing FMN1-FNBP4 interactions.

How can FMN1 Antibody, HRP conjugated be used to study dendritogenesis in neuronal cultures?

FMN1 has been identified as a critical mediator of dendritogenesis in hippocampal neurons . To study this role using FMN1 Antibody, HRP conjugated, researchers can implement the following methodological approach:

Experimental design for FMN1-mediated dendritogenesis studies:

• Neuronal culture preparation:

  • Prepare primary hippocampal neurons from E18-19 rat or mouse embryos

  • Plate neurons at intermediate density (100-150 cells/mm²) on poly-L-lysine coated coverslips

  • Culture in Neurobasal medium supplemented with B27 and GlutaMAX

• Experimental manipulations:

  • Gain-of-function: Transfect neurons with FMN1-Ib expression vectors

  • Loss-of-function: Transfect neurons with FMN1-specific siRNAs (siRNA2 or siRNA3)

  • Include GFP co-expression for morphological analysis

• Immunocytochemistry protocol:

  • Fix neurons with 4% PFA for 15 minutes at room temperature

  • Permeabilize with 0.1% Triton X-100 for 10 minutes

  • Block with 3% BSA + 5% normal goat serum for 1 hour

  • For dendrite visualization: Co-stain with anti-MAP2 antibody

  • For FMN1 detection: Use FMN1 Antibody, HRP conjugated (1:100-1:200)

  • Develop using DAB substrate or TSA amplification for fluorescent detection

• Quantitative analysis:

  • Capture images at 20-40X magnification

  • Analyze:

    • Number of primary dendrites

    • Dendrite length and branching pattern

    • FMN1 localization along dendrites

Expected outcomes based on published research:

• Overexpression of FMN1-Ib increases primary dendrite number by approximately 50% within 16 hours post-transfection

• FMN1 knockdown reduces neurite number and counteracts the dendrite-promoting effects of Ngn3

• FMN1-Ib localizes to the cytoplasm and is not found in neuronal nuclei

This experimental approach enables detailed investigation of FMN1's role in dendrite initiation and development, with the HRP-conjugated antibody providing sensitive detection of endogenous or overexpressed FMN1.

What is the optimal protocol for analyzing FMN1's role in glutamatergic synapse formation?

Research has revealed that FMN1 specifically increases the number of glutamatergic synaptic terminals without affecting GABAergic synapses . To investigate this phenomenon using FMN1 Antibody, HRP conjugated, implement this specialized protocol:

Materials and methods for synaptic analysis:

• Neuronal culture preparation:

  • Culture hippocampal neurons at high density (250-300 cells/mm²) to ensure proper synaptic network formation

  • Maintain cultures for at least 10-14 days to allow synaptic maturation

• Experimental manipulations:

  • Transfect neurons with FMN1-Ib expression vectors at DIV7-10

  • Include appropriate controls (empty vector or GFP-only expression)

  • For knockdown studies: Transfect FMN1-specific siRNAs

• Immunocytochemistry for synaptic analysis:

  • Fix neurons with 4% PFA + 4% sucrose (to preserve synaptic structures)

  • Permeabilize with 0.2% Triton X-100 for 10 minutes

  • Block with 5% BSA + 5% normal goat serum for 1 hour

  • Triple immunostaining:

    • FMN1 Antibody, HRP conjugated (1:100-1:200)

    • Anti-VGlut1 antibody (marker for glutamatergic presynaptic terminals)

    • Anti-VGAT antibody (marker for GABAergic presynaptic terminals)

  • Use TSA amplification system to convert HRP signal to fluorescence

• Quantitative analysis:

  • Capture high-resolution confocal z-stack images

  • Analyze:

    • Number of VGlut1-positive puncta per unit dendrite length

    • Number of VGAT-positive puncta per unit dendrite length

    • Calculate excitatory/inhibitory (E/I) synapse ratio

    • Co-localization of FMN1 with synaptic markers

Expected outcomes based on published data:

This methodology enables comprehensive analysis of FMN1's differential effects on excitatory versus inhibitory synapse formation, with implications for understanding neuronal circuit development and function.

How can researchers study the relationship between ciRNA-Fmn1 and FMN1 protein in neuropathic pain models?

Recent research has identified ciRNA-Fmn1 (a circular RNA derived from the FMN1 gene) as a key player in neuropathic pain regulation . Investigating the relationship between ciRNA-Fmn1 and FMN1 protein requires an integrated approach:

Comprehensive protocol for ciRNA-Fmn1/FMN1 protein studies:

• Neuropathic pain model preparation:

  • Implement peripheral nerve injury model (e.g., chronic constriction injury or spared nerve injury)

  • Include sham-operated controls

  • Monitor pain behavior (mechanical allodynia, thermal hyperalgesia)

• Tissue collection and processing:

  • Collect ipsilateral and contralateral spinal cord dorsal horn segments

  • Process for both RNA and protein extraction from parallel samples

  • For histological analysis: Prepare spinal cord sections (lumbar enlargement)

• ciRNA-Fmn1 analysis:

  • Extract total RNA using methods optimized for circular RNA preservation

  • Perform RT-qPCR with divergent primers specific for ciRNA-Fmn1

  • RNA in situ hybridization to localize ciRNA-Fmn1 in tissue sections

• FMN1 protein detection:

  • Western blot: Use FMN1 Antibody, HRP conjugated (1:500)

  • Immunohistochemistry:

    • Quench endogenous peroxidase activity

    • Incubate with FMN1 Antibody, HRP conjugated (1:200)

    • Develop with DAB substrate

    • Counterstain with hematoxylin

• Correlation analysis:

  • Analyze temporal relationship between ciRNA-Fmn1 downregulation and FMN1 protein changes

  • Perform co-localization studies to determine cellular distribution

  • Investigate relationships with other key molecules (DHX9, UBR5, albumin)

Functional mechanistic studies:

• Prevent ciRNA-Fmn1 downregulation (using RNA mimics or overexpression)

• Assess effects on FMN1 protein levels

• Analyze impact on UBR5-controlled albumin ubiquitination

• Correlate molecular changes with pain behavior outcomes

Expected outcomes based on published research:

• ciRNA-Fmn1 is significantly downregulated in ipsilateral dorsal horn neurons after peripheral nerve injury

• This downregulation relates to decreased DHX9, which regulates ciRNA-Fmn1 production

• Changes in ciRNA-Fmn1 affect its binding to ubiquitin ligase UBR5

• This alters albumin ubiquitination and expression in the dorsal horn, contributing to pain hypersensitivity

This multifaceted approach allows researchers to elucidate the complex relationships between circular RNA and protein expression in neuropathic pain pathways.

What are the optimal storage and handling conditions for maintaining FMN1 Antibody, HRP conjugated activity?

To preserve the activity and specificity of FMN1 Antibody, HRP conjugated, researchers should adhere to these evidence-based storage and handling guidelines:

Storage conditions:

• Store at -20°C in the dark to prevent HRP degradation

• Aliquot upon receipt to minimize freeze-thaw cycles (each cycle can reduce activity by 10-15%)

• For short-term storage (≤1 week), 4°C is acceptable

Buffer composition:
Most commercial FMN1 Antibody, HRP conjugated products are supplied in stabilizing buffers containing:

• 0.01M TBS (pH 7.4)

• 1% BSA (stabilizes protein)

• 0.03% Proclin300 (antimicrobial preservative)

• 50% Glycerol (prevents freezing damage)

Stability considerations:

• HRP conjugates typically maintain >80% activity for 12 months when properly stored

• Avoid exposure to strong oxidizing agents, which can inactivate HRP

• Protect from prolonged light exposure, particularly UV light

Working solution handling:

• Prepare working dilutions immediately before use

• Do not store diluted antibody for extended periods

• When removing from freezer, thaw at 4°C (never at high temperatures)

• Centrifuge briefly after thawing to collect all material

Quality control testing:

• Periodically verify antibody performance using positive control samples

• Monitor for increased background or decreased signal intensity, which may indicate degradation

• Consider including an HRP activity control in experiments

These practices will ensure maximum sensitivity and specificity of FMN1 Antibody, HRP conjugated throughout your research applications.

How can researchers quantitatively analyze FMN1 expression data across different experimental techniques?

For rigorous quantitative analysis of FMN1 expression using FMN1 Antibody, HRP conjugated, researchers should implement technique-specific approaches:

Western Blot Densitometric Analysis:

• Image acquisition parameters:

  • Capture images with a cooled CCD camera or digital imaging system

  • Ensure exposure time falls within the linear range of detection

  • Include a standard curve of recombinant FMN1 if absolute quantification is needed

• Software-based quantification:

  • Use ImageJ, Image Studio, or similar analysis software

  • Define regions of interest (ROIs) for FMN1 bands (~158 kDa)

  • Subtract local background for each lane

  • Normalize to loading controls (GAPDH or total protein stain)

• Data representation:

  • Express as relative fold change compared to control conditions

  • Present with appropriate statistical analysis (t-test, ANOVA)

  • Include error bars representing standard deviation or SEM

ELISA Quantification:

• Standard curve preparation:

  • Use recombinant human FMN1 at concentrations of 0-1000 ng/ml

  • Commercial assays report a sensitivity of approximately 30 ng/ml

  • Apply appropriate curve fitting (four-parameter logistic regression)

• Sample interpolation:

  • Ensure sample readings fall within the linear portion of the standard curve

  • Dilute samples if readings exceed the upper limit

  • Account for dilution factors in final calculations

• Quality control metrics:

  • Monitor intra-assay CV (<10%) and inter-assay CV (<15%)

  • Include duplicate or triplicate measurements for each sample

  • Record standard curve parameters (R² value should be >0.99)

Immunohistochemical Quantification:

• Image acquisition standardization:

  • Use identical microscope settings across all samples

  • Capture multiple representative fields per sample

  • Include internal control regions within each section

• Quantification approaches:

  • For DAB staining: Measure optical density using calibrated systems

  • Convert to H-score (calculation: [1 × (% cells 1+) + 2 × (% cells 2+) + 3 × (% cells 3+)])

  • For neuronal studies: correlate with morphological parameters

• Advanced analysis for neuronal samples:

  • Measure FMN1 expression along dendrite length

  • Quantify co-localization with synaptic markers (Mander's coefficient)

  • Correlate expression with dendrite number or synaptic density

By implementing these quantification approaches, researchers can generate reliable, reproducible data on FMN1 expression across experimental conditions.

How do the binding characteristics of FMN1 Antibody compare across different species models?

Understanding species cross-reactivity is essential when designing experiments with FMN1 Antibody, HRP conjugated across different model systems:

Species reactivity profile:

Epitope conservation analysis:
Most commercial FMN1 antibodies target epitopes within the region of amino acids 350-750 of the human FMN1 protein . Cross-species reactivity depends on conservation of these regions:

• The immunogen range of 651-750/1419 amino acids in human FMN1 shows high conservation across mammals

• The region corresponding to amino acids 350-495 of human FMN1 (NP_001096654.1) is also highly conserved

Experimental validation recommendations:

When using FMN1 Antibody, HRP conjugated in non-human models:

• Perform preliminary validation with positive control samples from the target species

• Include human samples as positive controls when possible

• For unverified species, conduct pilot experiments with increasing antibody concentrations (1:300, 1:500, 1:1000)

• Verify specificity using knockdown approaches in the species of interest

Species-specific considerations:

• Rodent models (mouse/rat): Particularly useful for neuronal studies given the validated role of FMN1 in rodent hippocampal development

• Human samples: Optimal for studying disease-relevant changes in FMN1 expression

• Non-mammalian models: Limited validation data available; extensive testing recommended before use

Understanding these cross-species reactivity profiles enables appropriate experimental design and interpretation of results when studying FMN1 across different model systems.

How can researchers design experiments to investigate FMN1's role in the actin-microtubule crosstalk?

FMN1 has been shown to interact with both actin and microtubule cytoskeletons through distinct domains . To investigate this dual functionality using FMN1 Antibody, HRP conjugated, researchers can implement this specialized experimental design:

Cytoskeletal co-localization analysis protocol:

• Cell preparation:

  • Culture appropriate cell types (fibroblasts, epithelial cells, or neurons)

  • For neurons: use hippocampal cultures at DIV1-5 for developmental studies

• Cytoskeletal disruption experiments:

  • Actin disruption: Treat cells with Cytochalasin D (1-5 μM, 30 min)

  • Microtubule disruption: Treat with Nocodazole (10 μM, 30 min)

  • Combined disruption: Sequential treatment with both agents

  • Include DMSO-treated controls

• Triple immunostaining approach:

  • Fix cells with 4% PFA (preserves both cytoskeletal networks)

  • Permeabilize with 0.1% Triton X-100

  • Primary antibodies:

    • FMN1 Antibody, HRP conjugated (1:200) with TSA amplification

    • Anti-α-tubulin (microtubule marker)

    • Fluorescent phalloidin (F-actin marker)

• Advanced imaging analysis:

  • Capture images using confocal microscopy with Z-stacks

  • Perform deconvolution to enhance resolution

  • Quantify co-localization using Pearson's or Mander's coefficients

  • Analyze FMN1 distribution following cytoskeletal disruption

Domain-specific analysis:
Research has shown that:

• The peptide encoded by exon 2 of the Fmn1-Ib gene regulates localization to interphase microtubules

• This localization is independent of the FH2 domain

• Different regions of FMN1-Ib are responsible for associations with actin versus microtubule cytoskeletons

To investigate domain-specific functions:

• Express wild-type FMN1-Ib or domain-specific mutants

• Analyze differential localization to cytoskeletal structures

• Evaluate effects on cytoskeletal organization and dynamics

This experimental approach enables detailed investigation of FMN1's dual role in coordinating actin and microtubule cytoskeletal networks.

What experimental approaches can detect the interaction between ciRNA-Fmn1, UBR5, and albumin in neuropathic pain models?

Recent research has uncovered a novel pathway involving ciRNA-Fmn1, the ubiquitin ligase UBR5, and albumin in neuropathic pain . To investigate this complex interaction using FMN1 Antibody, HRP conjugated alongside other molecular tools, researchers can implement this comprehensive protocol:

Integrated experimental approach:

• Neuropathic pain model:

  • Establish peripheral nerve injury model in rodents

  • Confirm pain phenotype (mechanical allodynia, thermal hyperalgesia)

  • Collect ipsilateral and contralateral spinal cord dorsal horn samples

• Molecular expression analysis:

  • ciRNA-Fmn1: RT-qPCR with divergent primers

  • FMN1 protein: Western blot with FMN1 Antibody, HRP conjugated (1:500)

  • UBR5 and albumin (ALB): Western blot with respective antibodies

• Protein-RNA interaction studies:

  • RNA immunoprecipitation (RIP):

    • Immunoprecipitate UBR5 protein

    • Extract bound RNA and detect ciRNA-Fmn1 by RT-qPCR

    • Compare binding efficiency between injured and control conditions

• Protein-protein interaction analysis:

  • Co-immunoprecipitation:

    • Immunoprecipitate UBR5

    • Detect albumin by Western blot

    • Assess how ciRNA-Fmn1 levels affect this interaction

• Ubiquitination assay:

  • Immunoprecipitate albumin

  • Detect ubiquitination using anti-ubiquitin antibodies

  • Compare ubiquitination levels across experimental conditions

  • Correlate with ciRNA-Fmn1 expression levels

• Functional manipulation experiments:

  • Prevent ciRNA-Fmn1 downregulation (using viral vectors)

  • Knockdown UBR5 expression using siRNA

  • Assess effects on:

    • Albumin ubiquitination

    • Albumin protein levels

    • Pain behaviors

Expected molecular pathway based on published research:

• Peripheral nerve injury leads to decreased DHX9, reducing ciRNA-Fmn1 levels

• Reduced ciRNA-Fmn1 decreases its binding to UBR5

• This reduces UBR5-mediated albumin ubiquitination

• Decreased ubiquitination increases albumin levels in the dorsal horn

• Elevated albumin contributes to neuropathic pain hypersensitivity

This integrated approach enables comprehensive investigation of the novel ciRNA-Fmn1/UBR5/albumin pathway in neuropathic pain, with potential therapeutic implications.

How can researchers simultaneously analyze FMN1 binding to both FNBP4 and cytoskeletal components?

To investigate the complex interplay between FMN1, its binding partner FNBP4, and cytoskeletal structures, researchers can implement this advanced multidimensional analysis protocol:

Integrated experimental workflow:

• Domain-specific binding characterization:

  • Express tagged constructs of FMN1 domains:

    • Full-length FMN1-Ib

    • FH1 domain only (amino acids 870-970)

    • FH2 domain only (amino acids 983-1466)

    • FH1-FH2 combined (amino acids 870-1466)

  • Express tagged constructs of FNBP4 domains:

    • Full-length FNBP4

    • WW1 domain only (amino acids 214-248)

    • WW2 domain only (amino acids 595-629)

• Protein-protein interaction mapping:

  • Co-immunoprecipitation assays with domain-specific constructs

  • Surface plasmon resonance (SPR) analysis:

    • Immobilize FNBP4 domains on CM5 sensor chips

    • Flow FMN1 domain constructs as analytes

    • Determine binding kinetics (ka, kd, KD)

    • Published data shows WW1-FNBP4 binds FH1-FH2 FMN1 with KD of 2 nM (ka: 0.6372106 M-1s-1, kd: 1.27310-3 s-1)

• Cytoskeletal co-localization analysis:

  • Triple immunofluorescence staining:

    • FMN1 Antibody, HRP conjugated with TSA amplification

    • Anti-FNBP4 antibody

    • Cytoskeletal markers (tubulin and/or actin)

  • Super-resolution microscopy (STED or STORM) to visualize:

    • Spatial relationships between FMN1, FNBP4, and cytoskeletal elements

    • Domain-specific localization patterns

• Functional perturbation experiments:

  • siRNA knockdown of FMN1 or FNBP4

  • Expression of dominant-negative domain constructs

  • Analysis of effects on:

    • Protein-protein interactions

    • Cytoskeletal organization

    • Cellular morphology (particularly in neurons)

Data integration and analysis:

• Correlate binding affinities with cellular co-localization patterns

• Map domain-specific interactions to cytoskeletal structures

• Generate comprehensive interaction models