IVNS1ABP Antibody

What is IVNS1ABP and why is it significant in research?

IVNS1ABP (Influenza Virus NS1A Binding Protein) is a 642 amino acid protein that interacts with the influenza A virus nonstructural NS1 protein and plays crucial roles in cellular integrity. The protein localizes to both the nucleus and cytoplasm and contains specialized domains—including one BACK domain, one BTB (POZ) domain, and six Kelch repeats—that contribute to its structural stability and functional versatility . IVNS1ABP's significance stems from its multifunctional role in:

• Maintaining dynamic organization of the actin cytoskeleton by stabilizing actin filaments through association with F-actin via its Kelch repeats

• Functioning as a homodimer linked through its BTB domain

• Regulating cell division and pre-mRNA splicing processes

• Activating ERK signaling pathways and providing neuroprotective effects by safeguarding dendritic spines

• Influencing inflammatory responses in macrophages

• Association with cardiovascular diseases such as acute myocardial infarction

These diverse functions make IVNS1ABP antibodies valuable tools for investigating cytoskeletal dynamics, viral-host interactions, and disease mechanisms.

What types of IVNS1ABP antibodies are available for research and how do they differ?

IVNS1ABP antibodies are available in several configurations to suit different experimental needs:

The choice between monoclonal and polyclonal antibodies depends on your experimental goals: monoclonal antibodies offer high specificity to a single epitope with consistent performance across batches, while polyclonal antibodies recognize multiple epitopes, potentially providing stronger signals but with higher batch-to-batch variation.

How should IVNS1ABP antibodies be validated before use in critical experiments?

Methodological validation of IVNS1ABP antibodies should follow a multi-step approach:

• Positive and negative controls: Use tissues or cell lines with known IVNS1ABP expression levels. HEK293 cells typically express IVNS1ABP and can serve as positive controls.

• Knockdown/knockout verification: Compare antibody signals between wild-type samples and those with IVNS1ABP knockdown (using siRNA) or knockout to confirm specificity.

• Cross-reactivity assessment: Test antibody against purified recombinant IVNS1ABP protein alongside other structural homologs with Kelch repeat domains.

• Application-specific validation:

  • For Western blot: Verify the molecular weight (approximately 70-72 kDa for human IVNS1ABP)

  • For immunofluorescence: Compare with known subcellular localization patterns (both nuclear and cytoplasmic)

  • For immunoprecipitation: Confirm using mass spectrometry of pulled-down proteins

• Lot-to-lot consistency testing: When obtaining new lots of the same antibody, perform parallel experiments with previous lots to ensure consistent performance.

This systematic validation approach reduces the risk of experimental artifacts and improves reproducibility in IVNS1ABP research.

What are the optimal conditions for Western blotting with IVNS1ABP antibodies?

Western blotting with IVNS1ABP antibodies requires specific optimization:

Recommended Protocol:

• Sample preparation:

  • Use RIPA buffer with protease inhibitors

  • Include phosphatase inhibitors if studying phosphorylation status

  • Denature samples at 95°C for 5 minutes in Laemmli buffer

• Gel electrophoresis:

  • 8-10% SDS-PAGE gels work best for resolving IVNS1ABP (~70-72 kDa)

  • Load 20-40 μg of total protein per lane

• Transfer conditions:

  • Semi-dry transfer: 15V for 45 minutes

  • Wet transfer: 100V for 60 minutes at 4°C

• Blocking:

  • 5% non-fat dry milk in TBST for 1 hour at room temperature

  • For phospho-specific detection, use 5% BSA in TBST

• Primary antibody incubation:

  • For ABIN1680538: 1:500 - 1:1000 dilution overnight at 4°C

  • For G-9 (sc-373909): 1:200 - 1:500 dilution overnight at 4°C

• Signal detection troubleshooting:

  • If signal is weak: Increase antibody concentration or extend incubation time

  • If background is high: Increase washing steps or reduce antibody concentration

The expected band should appear at approximately 70-72 kDa, with possible additional bands if detecting specific isoforms or post-translational modifications.

How can IVNS1ABP antibodies be effectively used in immunofluorescence studies?

For optimal immunofluorescence (IF) results with IVNS1ABP antibodies:

Methodological Approach:

• Cell preparation:

  • Fix cells with 4% paraformaldehyde for 15 minutes at room temperature

  • For nuclear epitopes, permeabilize with 0.2% Triton X-100 for 10 minutes

• Blocking:

  • 5% normal serum (matching secondary antibody host) with 0.3% Triton X-100 for 1 hour

• Antibody dilutions:

  • G-9 monoclonal antibody: 1:50 - 1:200 in 1% BSA/PBST

  • Incubate overnight at 4°C in a humidified chamber

• Controls and co-staining recommendations:

  • Include F-actin staining (phalloidin) to examine colocalization with actin cytoskeleton

  • Use nuclear counterstain (DAPI/Hoechst) to verify nuclear localization

  • For viral studies, co-stain with influenza NS1 protein antibodies

• Expected pattern:

  • Normal cells: Both nuclear and cytoplasmic localization

  • Influenza-infected cells: Often shows redistribution with NS1 protein

• Advanced application: For live-cell imaging, consider using the fluorescently conjugated versions of G-9 antibody (FITC or Alexa Fluor® conjugates)

Being aware that IVNS1ABP's localization may change under different cellular conditions, particularly during viral infection or stress responses, is crucial for proper interpretation of results.

What considerations are important when using IVNS1ABP antibodies for co-immunoprecipitation experiments?

Co-immunoprecipitation (Co-IP) with IVNS1ABP antibodies requires careful optimization:

Methodological Considerations:

• Lysis buffer selection:

  • For cytoskeletal interactions: Use mild NP-40 buffer (1% NP-40, 150mM NaCl, 50mM Tris pH 8.0)

  • For nuclear interactions: Include 0.1% SDS or 0.5% sodium deoxycholate

  • Always include protease/phosphatase inhibitors

• Antibody selection:

  • Monoclonal G-9 antibody is preferred for Co-IP due to its high specificity

  • For agarose-conjugated versions, use 2-5 μg antibody per 500 μg protein lysate

• Pre-clearing step:

  • Pre-clear lysates with Protein A/G beads for 1 hour at 4°C to reduce non-specific binding

• Controls:

  • IgG control of the same isotype as the IP antibody

  • Input sample (5-10% of protein used for IP)

  • When studying virus interactions, include both infected and uninfected controls

• Washing conditions:

  • Use at least 4-5 washes with decreasing salt concentrations

  • Final wash should be in PBS to remove detergents

• Elution and detection:

  • For gentle elution: Use competing peptide if available

  • For denaturing elution: 0.1M glycine (pH 2.5) or SDS sample buffer

• Expected interaction partners:

  • F-actin and cytoskeletal components

  • Influenza NS1 protein (in infected samples)

  • Components of the pre-mRNA splicing machinery

The success of Co-IP experiments depends significantly on preserving the native protein-protein interactions while minimizing non-specific binding.

How can IVNS1ABP antibodies be used to study its role in viral infection mechanisms?

IVNS1ABP antibodies can provide valuable insights into viral infection mechanisms:

Methodological Approach:

• Time-course infection studies:

  • Infect cells with influenza virus (MOI 1-5)

  • Collect samples at 0, 2, 4, 8, 12, and 24 hours post-infection

  • Use IVNS1ABP antibodies in immunoblotting and immunofluorescence to track localization changes

• Co-localization analysis:

  • Perform dual staining with IVNS1ABP and influenza NS1 antibodies

  • Quantify co-localization using Pearson's correlation coefficient or Mander's overlap coefficient

  • Compare these metrics between different viral strains or mutants

• Functional inhibition experiments:

  • Transfect cells with IVNS1ABP-targeting siRNA (verify knockdown with IVNS1ABP antibodies)

  • Measure viral replication efficiency using plaque assays or qPCR

  • Compare viral protein expression patterns using Western blot

• Protein complex identification:

  • Use IVNS1ABP antibodies for immunoprecipitation followed by mass spectrometry

  • Compare protein interaction networks between mock and infected conditions

  • Validate key interactions with reciprocal co-IP experiments

• Post-translational modification analysis:

  • Examine changes in IVNS1ABP phosphorylation status during infection

  • Use phospho-specific antibodies or phospho-enrichment followed by IVNS1ABP immunoblotting

These approaches help elucidate the dynamic interplay between viral components and IVNS1ABP during infection, potentially revealing targets for antiviral intervention.

What are the optimal approaches for studying IVNS1ABP in inflammation and cardiovascular disease models?

Recent research has identified IVNS1ABP as relevant in inflammation and cardiovascular disease :

Research Methodology:

• Animal models:

  • For cardiovascular studies: Use ischemia/reperfusion (I/R) models (45 min bilateral ischemia followed by 24h reperfusion)

  • For inflammation: Consider LPS-induced inflammation models in macrophages

• Gene modulation approaches:

  • Adenoviral vectors for Ivns1abp overexpression (MOI 250)

  • shRNA for knockdown (MOI 100)

  • Validate expression changes using IVNS1ABP antibodies via Western blot

• Macrophage-specific studies:

  • Isolate macrophages and modify Ivns1abp expression ex vivo

  • Perform adoptive transfer into animal models

  • Monitor inflammatory markers and tissue damage

• Cardiovascular assessment:

  • For AMI models: Measure PLAUR, QKI, and IVNS1ABP expression using RT-qPCR

  • Perform diagnostic efficacy analysis (AUC values were reported as 0.773, 0.933, and 0.807 for PLAUR, QKI, and IVNS1ABP respectively)

• Pathway analysis:

  • Examine platelet activation pathways using IVNS1ABP antibodies

  • Focus on connections between hyperlipidemia, lipophagy and AMI risk

  • Consider Mendelian randomization approaches for causal relationship studies

The combined odds ratio data from recent studies suggests IVNS1ABP is a risk factor for AMI (OR = 1.047, 95% CI: 1.000–1.096, P = 0.048) , highlighting its potential value as a biomarker in cardiovascular research.

How can contradictory IVNS1ABP antibody results be reconciled across different experimental systems?

When faced with contradictory IVNS1ABP antibody results:

Systematic Troubleshooting Approach:

• Antibody epitope mapping:

  • Different antibodies target different regions of IVNS1ABP:

    • ABIN1680538 targets AA 1-300

    • Other antibodies may target N-terminal or C-terminal regions

  • Map epitopes to functional domains (BTB domain, Kelch repeats) to understand potential masking effects

• Expression level variations:

  • Quantify baseline IVNS1ABP expression across cell lines/tissues using qPCR

  • Normalize Western blot signals to total protein rather than housekeeping genes

  • Consider creating standard curves with recombinant IVNS1ABP

• Isoform-specific detection:

  • Verify which isoforms your antibody detects

  • Use RT-PCR to determine which isoforms are expressed in your model system

• Post-translational modifications:

  • Test whether phosphorylation affects antibody recognition

  • Consider phosphatase treatment of samples prior to immunoblotting

  • Verify if ubiquitination or other modifications alter detection

• Protocol harmonization:

  • Standardize fixation conditions for immunostaining (methanol vs. paraformaldehyde)

  • Use consistent lysis buffers and denaturation conditions for Western blotting

  • Document detailed protocols to facilitate comparison between experiments

• Meta-analysis approach:

  • Create a systematic table of experimental conditions, antibody used, and results

  • Identify patterns in contradictory results to generate testable hypotheses

  • Consider collaborative validation across different laboratories

This methodical approach helps distinguish genuine biological variation from technical artifacts in IVNS1ABP research.

How might IVNS1ABP antibodies contribute to understanding novel therapeutic targets for viral infections?

IVNS1ABP antibodies can drive research into therapeutic targets:

Research Strategies:

• Structure-function relationship studies:

  • Use domain-specific IVNS1ABP antibodies to identify critical regions for NS1-binding

  • Develop competitive peptides that disrupt IVNS1ABP-NS1 interaction

  • Screen for small molecules that mimic these interactions

• Signaling pathway elucidation:

  • Map IVNS1ABP's role in ERK signaling pathway using phospho-specific antibodies

  • Identify druggable nodes in these pathways using IVNS1ABP antibodies for verification

  • Study cross-talk between IVNS1ABP and interferon response pathways

• Biomarker development:

  • Quantify IVNS1ABP levels during infection progression using standardized immunoassays

  • Correlate with disease severity and treatment response

  • Develop point-of-care diagnostic tools based on these findings

• Therapeutic modulation strategies:

  • Target IVNS1ABP expression using antisense oligonucleotides

  • Evaluate effect on viral replication using IVNS1ABP antibodies to monitor knockdown

  • Combine with existing antivirals to assess synergistic effects

• Broad-spectrum antiviral potential:

  • Investigate IVNS1ABP interaction with other viral proteins beyond influenza

  • Use antibodies to compare binding patterns across virus families

  • Identify conserved interaction motifs as targets for broad-spectrum antivirals

By systematically exploring these areas, researchers can develop novel therapeutic strategies that target host-pathogen interactions rather than viral components alone, potentially reducing the risk of resistance development.

What techniques can be used to study IVNS1ABP's role in cytoskeletal dynamics and cell migration?

Advanced methodologies for studying IVNS1ABP's cytoskeletal functions:

Technical Approaches:

• Live-cell imaging:

  • Generate IVNS1ABP-GFP fusion constructs (validate with antibodies)

  • Perform FRAP (Fluorescence Recovery After Photobleaching) to measure dynamics

  • Use TIRF microscopy to visualize interactions with cortical actin

• Super-resolution microscopy:

  • Employ STORM or STED imaging with IVNS1ABP antibodies

  • Co-stain with actin markers to visualize nanoscale organization

  • Quantify colocalization at single-molecule resolution

• Proximity ligation assays (PLA):

  • Use IVNS1ABP antibodies paired with actin or other cytoskeletal protein antibodies

  • Visualize direct interactions in situ

  • Quantify interaction changes during cell migration or division

• Functional migration assays:

  • Perform wound healing assays with IVNS1ABP knockdown/overexpression

  • Use Transwell or microfluidic migration assays

  • Quantify migration parameters while monitoring IVNS1ABP localization

• Mechanical force measurements:

  • Use traction force microscopy while modulating IVNS1ABP levels

  • Measure cellular stiffness using atomic force microscopy

  • Correlate mechanical properties with IVNS1ABP distribution (verified by antibodies)

• Biomechanical modeling:

  • Develop mathematical models of IVNS1ABP-actin interactions

  • Validate predictions using quantitative immunofluorescence

  • Simulate effects of IVNS1ABP mutations on cytoskeletal dynamics

These techniques together provide a comprehensive understanding of IVNS1ABP's role in cytoskeletal organization and cell motility, with implications for both normal cellular function and disease states.

How can quantitative proteomics be integrated with IVNS1ABP antibody-based techniques?

Integrating quantitative proteomics with antibody-based techniques:

Methodological Framework:

• Immunoprecipitation-Mass Spectrometry (IP-MS):

  • Use IVNS1ABP antibodies to pull down protein complexes

  • Perform label-free quantification of interacting partners

  • Compare interactomes under different conditions (e.g., viral infection, stress)

• Proximity-dependent labeling:

  • Create IVNS1ABP-BioID or APEX2 fusion proteins

  • Validate fusion protein localization using IVNS1ABP antibodies

  • Identify proximal proteins through streptavidin pulldown and mass spectrometry

• Cross-linking Mass Spectrometry (XL-MS):

  • Cross-link protein complexes containing IVNS1ABP

  • Enrich using IVNS1ABP antibodies

  • Identify direct binding interfaces through cross-linked peptide analysis

• Absolute quantification:

  • Develop AQUA peptides for IVNS1ABP

  • Use targeted proteomics (PRM/MRM) to quantify IVNS1ABP across samples

  • Correlate with antibody-based quantification methods

• Post-translational modification mapping:

  • Enrich IVNS1ABP using antibodies

  • Perform phosphoproteomics, ubiquitylomics, or acetylomics

  • Create modification-specific antibodies based on identified sites

• Spatial proteomics integration:

  • Combine IVNS1ABP immunofluorescence with laser capture microdissection

  • Perform proteomics on specific subcellular regions

  • Create spatial maps of IVNS1ABP-associated protein networks

This integrated approach provides deeper insights into IVNS1ABP function than either technique alone, offering both candidate discovery through proteomics and targeted validation using antibodies.

What are common pitfalls in IVNS1ABP antibody usage and how can they be avoided?

Common challenges and solutions in IVNS1ABP antibody applications:

Systematic Troubleshooting Guide:

• Non-specific binding issues:

  • Problem: Multiple unexpected bands in Western blot

  • Solution: Increase blocking time (2 hours), use gradient gel to better resolve bands, validate with IVNS1ABP knockdown controls

• Poor signal-to-noise ratio:

  • Problem: High background in immunofluorescence

  • Solution: Optimize antibody concentration through titration, increase washing steps, use phosphate-free buffer for G-9 antibody

• Epitope masking:

  • Problem: Inconsistent detection in different sample preparations

  • Solution: Compare multiple fixation methods, try antigen retrieval techniques, test different antibodies targeting distinct epitopes

• Batch-to-batch variation:

  • Problem: Performance differences between antibody lots

  • Solution: Maintain reference samples for validation, normalize to positive controls, consider monoclonal antibodies for critical applications

• Cross-reactivity concerns:

  • Problem: Signal in presumed negative samples

  • Solution: Validate with recombinant protein panels, perform peptide competition assays, confirm with orthogonal detection methods

• Protocol optimization decision tree:

  • For weak signal: Increase antibody concentration → Extend incubation time → Try different detection system

  • For high background: Increase blocking time → Use more stringent washing → Reduce antibody concentration

Maintaining detailed laboratory records of antibody performance across different applications helps identify optimal conditions and troubleshoot emerging issues consistently.

How should researchers evaluate and compare different IVNS1ABP antibodies for specific applications?

Comprehensive evaluation framework for IVNS1ABP antibodies:

Systematic Comparison Methodology:

• Performance metrics table:

  Metric	Evaluation Method	Acceptance Criteria
  Specificity	Western blot of KO/KD samples	Single band at 70-72 kDa; >80% signal reduction in KD
  Sensitivity	Limit of detection analysis	Detect <10ng recombinant protein
  Reproducibility	CV% across technical replicates	CV <15%
  Application versatility	Testing in multiple applications	Successful in ≥3 applications
  Species cross-reactivity	Testing on multi-species samples	Consistent detection across claimed species

• Validation experimental design:

  • Side-by-side testing of multiple antibodies on identical samples

  • Include positive and negative controls for each application

  • Randomize and blind sample analysis to prevent bias

  • Perform at least three independent replicates

• Documentation standards:

  • Record complete antibody information (catalog number, lot, dilution)

  • Document detailed protocols including all buffer compositions

  • Maintain unedited original images alongside analyzed data

  • Report both successful and failed experiments

• Collaborative validation strategies:

  • Implement multi-laboratory testing of the same antibody

  • Use standardized samples distributed across sites

  • Analyze results with consistent statistical methods

• Decision-making framework:

  • For research continuity: Prioritize reproducibility over absolute sensitivity

  • For novel applications: Select antibodies with most relevant epitope

  • For quantitative analysis: Choose antibodies with linear response range

This methodical evaluation approach ensures selection of optimal IVNS1ABP antibodies for specific research applications while promoting transparency and reproducibility.

What advanced protocols exist for detecting low-abundance IVNS1ABP in complex samples?

Advanced detection strategies for challenging samples:

Technical Approaches:

• Sample enrichment methods:

  • Subcellular fractionation to concentrate IVNS1ABP-rich compartments

  • Immunoprecipitation followed by Western blotting (IP-WB)

  • Phospho-protein enrichment if targeting phosphorylated IVNS1ABP forms

• Signal amplification techniques:

  • Tyramide signal amplification (TSA) for immunohistochemistry

  • Proximity ligation assay (PLA) for detecting IVNS1ABP interactions

  • Polymer-based detection systems for enhanced sensitivity

• Alternative detection platforms:

  • Single-molecule immunofluorescence

  • Capillary Western immunoassay (Wes/Jess systems)

  • Flow cytometry with intracellular staining

• Protocol modifications for challenging samples:

  • For fixed tissues: Extended antigen retrieval (citrate buffer pH 6.0, 20 min)

  • For blood samples: Red blood cell lysis followed by white blood cell enrichment

  • For brain tissues: Special fixation protocols to preserve cytoskeletal elements

• Quantification approaches:

  • Digital pathology with automated image analysis

  • Droplet digital PCR (ddPCR) paired with antibody validation

  • Mass cytometry (CyTOF) for single-cell protein quantification

• Standardization methods:

  • Include recombinant IVNS1ABP standard curve in each experiment

  • Use validated reference samples with known IVNS1ABP levels

  • Normalize to total protein rather than single housekeeping proteins

These approaches significantly enhance detection sensitivity and specificity for IVNS1ABP in tissues with naturally low expression or in conditions where protein levels are pathologically reduced.

How are IVNS1ABP antibodies being used to investigate its role as a potential biomarker for acute myocardial infarction?

Current research methodologies for IVNS1ABP as an AMI biomarker:

Research Approaches:

• Clinical validation studies:

  • Recent studies identified IVNS1ABP as a risk factor for AMI (OR = 1.047, 95% CI: 1.000–1.096, P = 0.048)

  • Demonstrated robust diagnostic efficacy with AUC value of 0.807

  • Combined with PLAUR and QKI in nomogram models achieving AUC of 0.924

• Mechanistic investigation techniques:

  • Use IVNS1ABP antibodies to study expression in cardiac tissue samples

  • Examine relationship to platelet activation pathways

  • Investigate connections to hyperlipidemia and lipophagy processes

• Mendelian randomization approaches:

  • Apply two-sample MR analysis with IVNS1ABP as exposure factor

  • Use genetic instruments (SNPs) significantly associated with IVNS1ABP expression

  • Establish causal relationships with AMI outcomes

• Biomarker panel development:

  • Develop standardized immunoassays for clinical settings

  • Create reference intervals across different populations

  • Validate in prospective studies with diverse AMI presentations

• Therapeutic target assessment:

  • Screen compounds that modulate IVNS1ABP expression or function

  • Evaluate effects on experimental AMI models

  • Monitor IVNS1ABP levels as pharmacodynamic markers

The emergence of IVNS1ABP as a biomarker represents a promising avenue for improving AMI diagnosis and prognostication, particularly when integrated with other established and novel biomarkers.

What insights can IVNS1ABP antibodies provide about its potential role in regulating inflammation and immune responses?

Research strategies for investigating IVNS1ABP in inflammation:

Methodological Framework:

• Macrophage-specific studies:

  • Recent research shows modulation of Ivns1abp gene in macrophages can modify resistance against inflammation

  • Use ex vivo–modified macrophages overexpressing Ivns1abp to study adoptive transfer effects in inflammatory models

  • Apply IVNS1ABP antibodies to track protein expression and localization during inflammatory responses

• Signal transduction analysis:

  • Examine IVNS1ABP's role in inflammatory signaling cascades

  • Investigate interaction with NF-κB pathway components

  • Study phosphorylation status during activation of immune cells

• Transcriptomic integration:

  • Correlate IVNS1ABP protein levels (detected by antibodies) with:

    • Inflammatory gene expression profiles

    • Cytokine production patterns

    • Response to anti-inflammatory treatments

• Tissue-specific inflammation models:

  • Ischemia/reperfusion injury models in kidney (45 min bilateral ischemia, 24h reperfusion)

  • Monitor tissue damage markers alongside IVNS1ABP expression

  • Evaluate therapeutic potential of IVNS1ABP modulation

• Cross-disciplinary approaches:

  • Integrate findings with research on IVNS1ABP's viral interaction functions

  • Explore potential overlap between antiviral and anti-inflammatory roles

  • Develop unified mechanistic models of IVNS1ABP function

These investigations may reveal IVNS1ABP as a critical regulatory node connecting viral infection responses with broader inflammatory pathways, potentially offering novel therapeutic targets for inflammatory conditions.

How might new antibody technologies advance our understanding of IVNS1ABP's structure-function relationships?

Emerging antibody technologies for IVNS1ABP research:

Advanced Technological Approaches:

• Single-domain antibodies (nanobodies):

  • Develop camelid-derived nanobodies against specific IVNS1ABP domains

  • Use for intracellular tracking in living cells

  • Apply in structural studies due to small size and stability

• Conformation-specific antibodies:

  • Generate antibodies that recognize specific IVNS1ABP conformational states

  • Distinguish between monomeric and dimeric forms

  • Map dynamic structural changes during protein-protein interactions

• Antibody-fragment crystallography:

  • Use Fab fragments to facilitate IVNS1ABP crystallization

  • Determine high-resolution structures of specific domains

  • Identify critical binding interfaces with viral proteins

• CRISPR-based antibody validation:

  • Generate precise IVNS1ABP domain deletions or mutations

  • Test antibody specificity against modified protein variants

  • Create comprehensive epitope maps for available antibodies

• Intrabodies for functional perturbation:

  • Express antibody fragments intracellularly to block specific domains

  • Target BTB dimerization domain or Kelch repeats separately

  • Dissect domain-specific functions without altering expression levels

• Cutting-edge applications:

  • IVNS1ABP interactome mapping using proximity-dependent biotinylation

  • Single-molecule tracking of IVNS1ABP dynamics during viral infection

  • Optogenetic control of IVNS1ABP cellular localization

These new antibody technologies provide unprecedented opportunities to understand the complex structural dynamics of IVNS1ABP and their functional implications in both normal cellular processes and disease states.