IAN13 Antibody

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Description

Understanding Interleukin-13 and Its Role in Inflammatory Pathways

Interleukin-13 (IL-13) functions as a key cytokine mediating type 2 inflammation and serves as an important pathogenic factor in various inflammatory conditions. This cytokine has emerged as a significant contributor to the pathophysiology of atopic dermatitis, where it drives inflammatory processes and tissue damage . The biological importance of IL-13 has made it a prime target for therapeutic intervention, particularly in conditions characterized by type 2 inflammatory responses. Understanding the role of IL-13 in these pathways has led to the development of specific monoclonal antibodies designed to neutralize its activity and thereby reduce inflammatory burden in affected tissues. This targeting approach represents a more precise intervention compared to broader immunosuppressive strategies.

Pharmacokinetic Profile of Anrukinzumab

The pharmacokinetic properties of anrukinzumab have been systematically investigated across different patient populations. Studies by Hua et al. (2015) conducted comparative pharmacokinetic analyses among healthy volunteers, asthma patients, and ulcerative colitis patients to characterize how different disease states affect drug disposition . These investigations provide crucial information about how the antibody behaves in different patient populations.

In clinical investigations, anrukinzumab has been administered intravenously at doses of 200 mg to ulcerative colitis patients . Concentration-time profiles show the pharmacokinetic behavior following multiple intravenous administrations of 200 mg doses, with comparisons between ulcerative colitis patients and non-UC subjects . These profiles help determine parameters such as maximum concentration (Cmax), area under the curve (AUC), elimination half-life, and clearance rates, which are essential for establishing appropriate dosing regimens.

Systematic pharmacokinetic modeling has been employed to predict antibody behavior across different doses, as evidenced by visual predictive check analyses for different dosing strategies . This modeling approach allows for optimization of dosing regimens and helps predict antibody behavior in different clinical scenarios.

Clinical Applications and Efficacy Evidence

Anrukinzumab has undergone clinical evaluation for inflammatory conditions, particularly ulcerative colitis. Research by Reinisch et al. (2015) assessed the efficacy and safety profile of anrukinzumab in active ulcerative colitis through a phase IIa randomized multicentre study . This study represents a significant step in establishing the clinical utility of anti-IL-13 therapy for inflammatory bowel conditions.

One important biomarker evaluated was faecal calprotectin, a sensitive indicator of intestinal inflammation. Studies have measured the effect of anrukinzumab compared with placebo on fold changes in this marker, providing objective assessment of anti-inflammatory effects . Reduction in faecal calprotectin levels would suggest decreased neutrophil migration to the intestinal mucosa, indicating reduced inflammatory activity.

Pharmacodynamic effects were monitored through measurement of total IL-13 levels over time, with median IL-13 level versus time profiles compared between treatment groups . These measurements help establish the relationship between antibody administration, target engagement, and subsequent clinical effects. The temporal relationship between antibody administration and changes in IL-13 levels provides insight into the duration of effect and optimal dosing intervals.

Laboratory Applications and Research Utility

Beyond clinical applications, anrukinzumab derivatives serve important functions in laboratory research. The IL-13 Antibody (anrukinzumab) conjugated with FITC (fluorescein isothiocyanate) is utilized in multiple research applications including ELISA, flow cytometry, and functional assays . This laboratory-grade antibody enables investigation of IL-13 biology and potential therapeutic approaches.

The technical specifications for research-grade anrukinzumab include:

PropertySpecification
Species ReactivityHuman
ApplicationsELISA, Flow Cytometry, Functional assays
Fluorescent LabelFITC (Excitation = 495 nm, Emission = 519 nm)
Antibody SourceRecombinant Monoclonal Human IgG
Cloneanrukinzumab
ImmunogenIL-13
ClonalityMonoclonal
HostHuman
IsotypeIgG
Purification MethodProtein A purified
FormulationPBS with 0.05% Sodium Azide
Storage Conditions4°C in the dark

These research tools are specified for laboratory use only and are not approved for human administration or clinical diagnosis . The availability of such research reagents facilitates investigation into IL-13 biology and therapeutic development.

Comparative Analysis with Lebrikizumab

Lebrikizumab represents another important anti-IL-13 monoclonal antibody that has been extensively studied for inflammatory conditions, particularly atopic dermatitis . Comparing anrukinzumab with lebrikizumab provides important insights into the therapeutic potential of IL-13 targeting across different inflammatory conditions.

A phase 2 clinical study evaluated lebrikizumab as an adjunctive therapy to topical corticosteroids (TCS) in patients with moderate-to-severe atopic dermatitis . This study employed a rigorous methodology:

  • Randomized, placebo-controlled, double-blind design

  • Four treatment arms with 1:1:1:1 randomization:

    • Lebrikizumab 125 mg single dose

    • Lebrikizumab 250 mg single dose

    • Lebrikizumab 125 mg every 4 weeks for 12 weeks

    • Placebo every 4 weeks for 12 weeks

  • Initial 2-week TCS run-in period before randomization

  • Primary endpoint: percentage of patients achieving at least 50% improvement in Eczema Area and Severity Index (EASI-50) at week 12

The clinical outcomes demonstrated significant therapeutic benefit:

Treatment GroupEASI-50 AchievementP-value vs Placebo
Lebrikizumab 125 mg Q4W82.4%0.026
Placebo Q4W62.3%-
Single dose lebrikizumab groupsNo statistically significant difference>0.05

Safety analysis revealed comparable adverse event profiles between lebrikizumab and placebo groups (66.7% for all lebrikizumab groups vs. 66.0% for placebo), with most events being mild or moderate in severity . This favorable safety profile, combined with efficacy data, supports further investigation of lebrikizumab for inflammatory skin conditions.

Future Research Directions and Therapeutic Potential

The development of anti-IL-13 antibodies represents an evolving field with significant therapeutic potential. Current research limitations highlight important areas for future investigation :

Understanding efficacy as monotherapy remains a crucial research gap, as most studies have evaluated these antibodies as add-on therapies to treatments like topical corticosteroids. Establishing their effectiveness as standalone treatments would clarify their therapeutic value and potentially expand their clinical applications. The optimal dosing regimens, including dose amount and frequency, continue to be refined through ongoing clinical investigations.

Long-term efficacy and safety evaluations are needed beyond the relatively short duration of existing studies . Given that many inflammatory conditions requiring these therapies are chronic in nature, understanding the sustained benefits and potential long-term risks is essential for clinical decision-making. Extended follow-up studies will help establish the durability of response and identify any delayed adverse effects that might not be apparent in shorter trials.

Additional inflammatory conditions mediated by IL-13 beyond the currently studied indications represent potential therapeutic opportunities. As our understanding of IL-13 biology expands, new applications may emerge for anti-IL-13 antibodies in various inflammatory and allergic conditions where this cytokine plays a pathogenic role.

Product Specs

Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M Phosphate Buffered Saline (PBS), pH 7.4
Form
Liquid
Lead Time
Made-to-order (14-16 weeks)
Synonyms
IAN13 antibody; At4g09950 antibody; T5L19.80 antibody; Immune-associated nucleotide-binding protein 13 antibody; AtIAN13 antibody; AIG1-like protein antibody
Target Names
IAN13
Uniprot No.

Q&A

What is IAN13 and why is it studied in Arabidopsis thaliana?

IAN13 (Immune-Associated Nucleotide-binding protein 13) belongs to the GTPase of immunity-associated proteins (GIMAP) family in Arabidopsis thaliana. This protein family plays crucial roles in plant immune responses, development, and stress signaling pathways. IAN13 (UniProt ID: Q9T0F4) is particularly important in studying plant immunity mechanisms. The IAN13 Antibody enables researchers to investigate protein localization, expression patterns, and protein-protein interactions under various experimental conditions. Studies of IAN13 contribute to our understanding of how plants regulate immune responses at the molecular level, potentially leading to applications in crop improvement and disease resistance .

What are the recommended storage conditions for IAN13 Antibody?

Proper storage of IAN13 Antibody is critical for maintaining its activity and specificity. Based on standard antibody handling protocols:

Storage DurationTemperatureAdditivesNotes
Long-term (>1 month)-20°C50% glycerolAliquot to avoid freeze-thaw cycles
Short-term (<1 month)4°C0.02% sodium azideProtect from light
Working solution4°C1% BSA, 0.02% sodium azideUse within 7 days

Repeated freeze-thaw cycles significantly reduce antibody activity. For optimal results, dividing the stock into small aliquots upon receipt is strongly recommended. When preparing working dilutions, use sterile techniques and high-quality buffers to prevent microbial contamination that could degrade the antibody .

How does IAN13 Antibody specificity compare to other plant immune response antibodies?

IAN13 Antibody (such as CSB-PA154892XA01DOA) is designed with high specificity for the IAN13 protein in Arabidopsis thaliana. When compared to antibodies targeting related immune proteins:

AntibodyTarget ProteinCross-ReactivityApplication Strength
IAN13 AntibodyIAN13 (Q9T0F4)Minimal with IAN familyStrong in Western blot, IHC
IAN12 AntibodyIAN12 (Q9T0F3)May cross-react with IAN13Similar applications
IAN5 AntibodyIAN5 (Q9C8U8)Low cross-reactivityGood for differential studies
IAN9 AntibodyIAN9 (F4HT21)Distinct epitope recognitionComplementary validation

Researchers should validate specificity through appropriate controls, especially when studying multiple IAN family members simultaneously. Using antibodies raised against different epitopes can provide confirmatory evidence for protein identification .

What are the optimal protocols for using IAN13 Antibody in Western blot analysis?

For successful Western blot analysis with IAN13 Antibody:

Sample Preparation:

  • Extract total protein from Arabidopsis tissues using buffer containing 50mM Tris-HCl (pH 7.5), 150mM NaCl, 1% Triton X-100, 0.5% sodium deoxycholate, and protease inhibitor cocktail

  • Homogenize tissue thoroughly while keeping samples cold

  • Centrifuge at 12,000g for 15 minutes at 4°C and collect supernatant

Gel Electrophoresis and Transfer:

  • Separate 20-40μg protein on 10-12% SDS-PAGE

  • Transfer to PVDF membrane (100V for 60 minutes or 30V overnight)

  • Verify transfer efficiency with reversible staining

Antibody Incubation:

  • Block membrane with 5% non-fat milk in TBST for 1 hour at room temperature

  • Incubate with IAN13 Antibody (1:1000 dilution) in blocking buffer overnight at 4°C

  • Wash 3×15 minutes with TBST

  • Incubate with HRP-conjugated secondary antibody (1:5000) for 1 hour

  • Wash 3×15 minutes with TBST

  • Develop using ECL substrate and image

Troubleshooting Guide:

IssuePossible CauseSolution
No signalProtein degradationUse fresh samples, increase protease inhibitors
Multiple bandsCross-reactivityIncrease antibody dilution, extend washing
High backgroundInsufficient blockingOptimize blocking conditions, try 3% BSA alternative
Weak signalLow protein abundanceIncrease protein loading, reduce antibody dilution

Including both wild-type and ian13 mutant samples as controls is essential for confirming signal specificity .

How can I verify the specificity of IAN13 Antibody in my experimental system?

Rigorous validation of IAN13 Antibody specificity is crucial for reliable experimental outcomes. A comprehensive validation approach includes:

  • Genetic Controls Testing:

    • Compare signal between wild-type Arabidopsis and ian13 knockout/knockdown mutants

    • Examine IAN13 overexpression lines for increased signal intensity

    • Use CRISPR-edited plants with epitope modifications

  • Biochemical Validation:

    • Perform peptide competition assays by pre-incubating antibody with immunizing peptide

    • Conduct immunoprecipitation followed by mass spectrometry to confirm target identity

    • Compare results with alternative antibodies targeting different IAN13 epitopes

  • Cross-Reactivity Assessment:

    • Test against recombinant IAN family proteins to evaluate potential cross-reactivity

    • Examine tissues with known differential expression of IAN family members

    • Perform Western blots under high-stringency conditions

The most convincing validation combines multiple approaches, particularly the absence of signal in genetic knockout lines coupled with specific recognition of the target protein at the expected molecular weight in wild-type samples .

What controls are essential when using IAN13 Antibody for immunoprecipitation experiments?

For robust immunoprecipitation (IP) experiments with IAN13 Antibody, implement these essential controls:

Mandatory Controls:

Control TypePurposeImplementation
Input sampleVerify starting materialSet aside 5-10% of pre-IP lysate
Isotype controlDetect non-specific bindingUse same concentration of irrelevant antibody
Negative genetic controlConfirm specificityProcess ian13 mutant samples identically
Beads-only controlIdentify matrix bindingPerform IP without antibody
Pre-immune serum controlEstablish baseline bindingIf using polyclonal antibodies

Additional Controls for Co-IP Experiments:

  • Binding condition controls:

    • Compare native versus denaturing conditions to identify specific interactions

    • Include RNase/DNase treatments to exclude nucleic acid-mediated associations

  • Reciprocal co-IP:

    • Perform reverse experiment using antibodies against suspected interaction partners

    • Validate interactions through orthogonal methods (Y2H, BiFC)

  • Specificity controls:

    • Use competitive elution with excess IAN13 peptide

    • Include predicted non-interacting proteins as negative controls

These controls help distinguish genuine interactions from experimental artifacts and are particularly important when studying novel protein-protein interactions involving IAN13 .

How should I interpret contradictory results between IAN13 Antibody immunostaining and gene expression data?

Discrepancies between antibody-based protein detection and gene expression analysis are common in plant research and may reflect important biological phenomena rather than technical errors:

Post-transcriptional Regulation Assessment:

  • mRNA abundance frequently does not correspond directly to protein levels due to translation efficiency differences

  • Investigate protein stability through cycloheximide chase experiments

  • Examine potential miRNA regulation of IAN13 mRNA

Protein Modification Considerations:

  • Post-translational modifications may mask antibody epitopes

  • Treatment with phosphatases or deubiquitinating enzymes before analysis

  • Test multiple antibodies targeting different regions of IAN13

Methodological Approach to Resolve Discrepancies:

ObservationPossible Biological ExplanationValidation Method
High mRNA, low proteinRapid protein turnoverProteasome inhibitor treatment (MG132)
Inefficient translationPolysome fractionation analysis
Post-translational regulationPhosphorylation or ubiquitination analysis
Low mRNA, high proteinHigh protein stabilityCycloheximide chase with timepoints
Regulated protein degradationCompare stress vs. normal conditions
Antibody cross-reactivityImmunoprecipitation with MS verification

The integration of multiple techniques (RT-qPCR, Western blot, mass spectrometry) provides complementary data for a more complete understanding of IAN13 regulation .

What are the common artifacts when using IAN13 Antibody in immunofluorescence microscopy of plant tissues?

Immunofluorescence microscopy in plant tissues presents unique challenges when using antibodies like IAN13 Antibody:

Common Artifacts and Solutions:

  • Plant-Specific Autofluorescence:

    • Chlorophyll autofluorescence in green tissues (especially problematic in red channels)

    • Cell wall components (lignin, suberin) create background signal

    • Solution: Use appropriate filter sets, spectral unmixing, or chemical treatments to quench autofluorescence

  • Fixation-Related Artifacts:

    • Overfixation can mask epitopes and create false negatives

    • Insufficient fixation compromises cellular architecture

    • Solution: Optimize fixation protocols specifically for IAN13 detection (typically 2-4% paraformaldehyde for 1-2 hours)

  • Cell Wall Penetration Issues:

    • Plant cell walls hinder antibody penetration

    • Solution: Include appropriate permeabilization steps (0.1-0.3% Triton X-100) and consider enzymatic digestion with cell wall-degrading enzymes

  • Non-Specific Binding:

    • Plant tissues often show high background due to hydrophobic interactions

    • Solution: Use specialized blocking reagents containing BSA, normal serum, and plant-specific blockers

Artifact Identification Guide:

Artifact TypeDistinguishing FeaturesCritical Controls
AutofluorescencePresent in untreated samplesImage unlabeled tissue with identical settings
Fixation artifactVariable pattern between fixation methodsCompare multiple fixation protocols
Cell wall bindingUniform signal at cell peripheryInclude pre-immune serum control
Vacuolar trappingSignal accumulation in vacuolesTest shorter incubation times, different detergents

Always include negative controls (pre-immune serum, secondary antibody only) and positive controls (proteins known to co-localize with IAN13) .

How can I use IAN13 Antibody to study protein-protein interactions in plant immune responses?

IAN13 Antibody offers several approaches for investigating protein-protein interactions in plant immunity contexts:

Co-Immunoprecipitation (Co-IP):

  • Use IAN13 Antibody to pull down IAN13 protein complexes from plant lysates

  • Identify interaction partners through mass spectrometry analysis

  • Validate interactions using reciprocal Co-IP with antibodies against putative partners

  • Consider mild crosslinking to capture transient interactions in immune signaling cascades

Proximity Labeling Approaches:

  • Combine with BioID or TurboID systems for proximity-dependent biotinylation

  • Create fusion proteins with IAN13 and proximity labeling enzymes

  • Use IAN13 Antibody to verify expression and localization of fusion proteins

  • Identify proximal proteins through streptavidin pulldown and mass spectrometry

Immunofluorescence Co-Localization:

  • Perform dual labeling with IAN13 Antibody and antibodies against suspected partners

  • Analyze co-localization using quantitative methods (Pearson's correlation, Manders' coefficients)

  • Examine dynamic changes in localization during immune responses

Methodological Workflow:

  • Initial screening via Co-IP/MS to identify potential interaction partners

  • Validation using orthogonal methods (Y2H, BiFC)

  • Functional characterization through mutant analysis

  • Spatiotemporal dynamics using advanced microscopy

These approaches can uncover novel components of plant immune signaling networks and provide mechanistic insights into IAN13 function .

What are the best approaches for quantitative analysis of IAN13 expression using antibody-based methods?

Quantifying IAN13 expression levels requires careful consideration of methodological limitations and appropriate controls:

Western Blot Quantification:

  • Semi-quantitative assessment with densitometry

  • Requires carefully optimized loading controls (ACTIN, TUBULIN, or total protein stains)

  • Standard curve using recombinant protein recommended for absolute quantification

  • Maintain samples within linear dynamic range of detection system

  • Include biological and technical replicates (minimum n=3)

ELISA-Based Quantification:

  • Develop sandwich ELISA using IAN13 Antibody and a second antibody targeting different epitope

  • Create standard curve using purified recombinant IAN13 protein

  • Higher throughput for multiple samples and conditions

  • More suitable for absolute quantification than Western blot

Flow Cytometry (for Protoplasts):

  • Quantify IAN13 expression at single-cell level

  • Require permeabilization for intracellular IAN13 detection

  • Use fluorophore-conjugated secondary antibodies

  • Include calibration beads for standardization

Quantification Method Comparison:

MethodQuantitation PrecisionDynamic RangeSample ThroughputKey Considerations
Western blotModerate~10-foldLowBest for relative comparisons
ELISAHigh~1000-foldHighRequires purified standards
Flow cytometryHigh~10,000-foldMediumRequires protoplast preparation
ImmunohistochemistryLow-ModerateVariableLowProvides spatial information

The choice of method should be guided by experimental requirements for sensitivity, throughput, and whether spatial information is needed .

How can IAN13 Antibody be used to study the dynamics of protein modifications during immune responses?

IAN13 Antibody is a valuable tool for investigating post-translational modifications (PTMs) that regulate IAN13 function during immune responses:

Phosphorylation Analysis:

  • Combine IAN13 Antibody immunoprecipitation with phospho-specific staining

  • Compare phosphorylation status before and after pathogen treatment

  • Use phosphatase treatments to confirm modification

  • Phospho-specific antibodies can be developed if modification sites are known

Ubiquitination Studies:

  • Perform IAN13 immunoprecipitation followed by ubiquitin Western blot

  • Include proteasome inhibitors (MG132) to stabilize ubiquitinated forms

  • Examine changes in ubiquitination patterns during immune activation

  • Consider tandem ubiquitin binding entity (TUBE) pulldowns to enrich ubiquitinated proteins

Other Modifications:

  • SUMOylation can be assessed through similar immunoprecipitation approaches

  • Redox modifications may be investigated using redox-sensitive probes

  • Glycosylation can be examined using glycosidase treatments

Experimental Workflow for PTM Analysis:

  • Immunoprecipitate IAN13 from control and treated samples

  • Divide precipitated material for different analyses:

    • Direct Western blot for total IAN13

    • Modification-specific antibody detection

    • Mass spectrometry analysis for unbiased PTM mapping

  • Validate findings with site-directed mutagenesis of modified residues

  • Assess functional consequences of mutations in plant immunity assays

This approach can reveal regulatory mechanisms controlling IAN13 activity during plant immune responses and stress adaptation .

What are the critical steps to optimize IAN13 Antibody concentration for immunohistochemistry?

Optimizing IAN13 Antibody concentration for plant immunohistochemistry requires systematic titration and protocol refinement:

Antibody Titration Strategy:

  • Initial Concentration Range Testing:

    • Prepare serial dilutions (1:50, 1:100, 1:200, 1:500, 1:1000)

    • Use consistent tissue samples with known IAN13 expression

    • Process all samples identically except for antibody concentration

  • Fixation Method Optimization:

    • Test multiple fixatives (4% paraformaldehyde, 2% glutaraldehyde, acetone)

    • Evaluate different fixation durations (30 min, 1 hour, 2 hours, overnight)

    • Assess requirement for antigen retrieval methods

  • Signal-to-Background Evaluation:

    • Systematically document signal intensity versus background at each concentration

    • Include ian13 mutant tissues as negative controls

    • Test secondary antibody alone to assess non-specific binding

Optimization Results Template:

DilutionFixativeAntigen RetrievalSignal StrengthBackgroundSpecificity
1:504% PFA, 1hNone++++++Medium
1:1004% PFA, 1hNone++++High
1:2004% PFA, 1hNone+++/-Very High
1:100Acetone, 10mNone++++High
1:1002% Glut., 1hCitrate buffer++++Low

The optimal dilution provides clear specific signal with minimal background. For most applications with IAN13 Antibody in Arabidopsis tissues, a 1:100-1:200 dilution with PFA fixation typically yields the best results .

How can I overcome weak signals when using IAN13 Antibody in Western blot analysis?

When facing weak signal issues with IAN13 Antibody in Western blot analysis, consider these targeted optimization approaches:

Sample Preparation Enhancement:

  • Use fresh tissue and maintain cold chain throughout extraction

  • Include additional protease inhibitors (PMSF, aprotinin, leupeptin)

  • Optimize buffer composition for IAN13 solubilization

  • Consider using specialized plant protein extraction kits designed for low-abundance proteins

Protocol Modifications for Signal Amplification:

  • Increase protein loading (40-60μg per lane)

  • Reduce antibody dilution incrementally (1:1000 to 1:500 to 1:250)

  • Extend primary antibody incubation time (overnight at 4°C)

  • Use high-sensitivity detection reagents (enhanced chemiluminescence plus)

  • Consider biotin-streptavidin amplification systems

Technical Optimization:

  • Switch membrane type (PVDF typically better than nitrocellulose for weak signals)

  • Reduce washing stringency slightly (use 0.05% instead of 0.1% Tween-20)

  • Try different blocking agents (BSA vs. milk vs. commercial blockers)

  • Use film exposure for very weak signals (more sensitive than digital imaging)

Systematic Troubleshooting Approach:

IssueDiagnostic TestSolution
Protein degradationRun sample immediately after extraction vs. stored sampleUse fresh samples, add more protease inhibitors
Poor transferStain membrane for total protein after transferOptimize transfer conditions, reduce methanol %
Inactive antibodyDot blot test with recombinant proteinUse new antibody aliquot
Low abundance targetVerify expression with RT-PCREnrich target through immunoprecipitation first
Epitope maskingTest multiple extraction buffersTry denaturing conditions, heat samples longer

If IAN13 is consistently difficult to detect, consider creating transgenic plants expressing epitope-tagged versions (HA, FLAG, GFP) which can be detected with highly optimized commercial antibodies .

How can multiplexed antibody techniques be used to study IAN13 in relation to other immune response proteins?

Advanced multiplexed approaches enable simultaneous analysis of IAN13 and other immune-related proteins:

Multiplex Immunofluorescence Strategies:

  • Use IAN13 Antibody alongside antibodies against defense-related proteins (NPR1, EDS1, PAD4)

  • Combine with subcellular markers to track localization changes during immune responses

  • Employ spectrally distinct fluorophores for each target protein

  • Utilize automated image analysis for colocalization quantification

Sequential Immunoblotting Approaches:

  • Strip and reprobe membranes to detect multiple proteins on the same blot

  • Use differently sized proteins with same-species antibodies

  • Employ fluorescently-labeled secondary antibodies with different emission spectra

  • Conduct quantitative analysis of relative protein levels

Advanced Multiplex Technologies:

  • Mass cytometry (CyTOF) adapted for plant protoplasts with metal-conjugated antibodies

  • Proximity extension assays for protein interaction networks

  • Micro-western arrays for high-throughput, low-volume analysis

These multiplexed approaches are particularly valuable for studying signaling networks, as they preserve the relationships between different immune components within the same sample and eliminate variation that might occur between separate analyses .

What new technologies are being developed for antibody-based spatial profiling of proteins like IAN13?

Emerging spatial biology technologies are revolutionizing our ability to study the distribution and interactions of proteins like IAN13 in plant tissues:

Advanced Microscopy Techniques:

  • Super-resolution microscopy (STORM, PALM, SIM) to visualize IAN13 distribution beyond diffraction limit

  • Expansion microscopy for physical magnification of plant tissues while preserving protein epitopes

  • Light-sheet microscopy for rapid 3D imaging with reduced phototoxicity

Spatial Transcriptomics Integration:

  • Combined antibody detection with in situ RNA analysis

  • Correlation of protein localization with transcriptomic data

  • Multi-modal data integration for comprehensive pathway analysis

Emerging Antibody-Based Spatial Technologies:

  • Imaging mass cytometry for highly multiplexed protein detection in plant tissues

  • Digital spatial profiling platforms adapted for plant tissue architecture

  • Proximity ligation assays for in situ protein interaction detection

Future Directions and Applications:

TechnologyResolutionMultiplexing CapacityApplication to IAN13 Research
Expansion Microscopy~70nm4-5 proteinsSubcellular localization in relation to cellular structures
CODEXCell-level40+ proteinsComprehensive immune protein networks
Imaging Mass Cytometry1μm40+ proteinsTissue-specific expression patterns during infection
Spatial Transcriptomics10-100μmWhole transcriptome + proteinsIntegration of protein and RNA regulation

These technologies promise to provide unprecedented insights into how IAN13 functions within the spatial context of plant tissues during immune responses .

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