MAPRE1 Antibody

What is MAPRE1 and why is it significant in cellular research?

MAPRE1, also known as EB1 (End-binding protein 1), is a key regulator of microtubule dynamics that localizes at the growing plus ends of microtubules and the centrosome. It plays critical roles in cell division, cell migration, and the regulation of cell polarity and chromosome stability . The human MAPRE1 protein is 268 amino acids in length with a mass of approximately 30 kDa and is ubiquitously expressed across many tissue types . Its significance stems from its interactions with the adenomatous polyposis coli (APC) tumor suppressor protein, targeting APC to microtubule plus ends . This interaction has implications for understanding cytoskeletal dynamics, cellular division mechanisms, and potentially cancer development pathways. MAPRE1 is essential for anchoring cytoplasmic microtubule minus ends to the subdistal appendages of the mother centriole, making it a vital component in studies of cellular architecture and function .

What epitopes are most commonly targeted in MAPRE1 antibodies and why?

MAPRE1 antibodies target various epitopes across the protein structure, with several common regions being particularly important for research applications. Based on the search results, common epitope regions include:

The C-terminal region (AA 134-268) contains the sequence "ETAVAPSLVAPALNKPKKPLTSSSAAPQRPISTQRTAAAPKAGPGVVRKNPGVGNGDDEAAELMQQVNVLKLTVEDLEKERFYFGKLRNIELICQENEGENDPVLQRIVDILYATDEGFVIP" which is targeted by several antibodies . This region is significant as it contains domains necessary for protein-protein interactions, including those with APC. N-terminal domains (approximately AA 1-110) are often targeted because they contain microtubule-binding regions essential for MAPRE1's localization and function .

How should researchers distinguish between MAPRE1 isoforms when selecting antibodies?

When studying MAPRE1, researchers must carefully consider potential isoforms and ensure their selected antibody recognizes the specific variant of interest. The canonical human MAPRE1 protein has 268 amino acid residues, but alternative splicing may produce variant isoforms . To properly distinguish between these:

• Epitope mapping: Verify which amino acid sequence the antibody recognizes and whether this sequence is present in all isoforms or specific to certain variants .

• Western blot validation: Perform preliminary Western blots with positive controls to confirm the antibody detects bands at the expected molecular weights for your target isoform. The canonical form appears at approximately 30 kDa .

• Literature cross-referencing: Compare your experimental needs with published studies that have successfully used specific antibodies for particular MAPRE1 isoforms.

• Recombinant protein controls: Use recombinant proteins representing different MAPRE1 isoforms to validate antibody specificity before conducting your main experiments .

• Cross-reactivity assessment: Review the antibody's documented cross-reactivity with isoforms in different species if performing comparative studies .

What are the optimal applications for different formats of MAPRE1 antibodies?

MAPRE1 antibodies are available in various formats that are optimized for specific experimental applications. Based on the search results, the following applications are most commonly supported:

For cellular localization studies, fluorophore-conjugated antibodies like the MAPRE1 Antibody [Janelia Fluor® 525] provide direct visualization of MAPRE1 at microtubule plus ends and centrosomes . For protein interaction studies using immunoprecipitation, unconjugated antibodies raised against the C-terminal domain (AA 134-268) are particularly effective as this region contains binding sites for partner proteins . When selecting an antibody format, researchers should consider the subcellular localization of interest (Golgi, cytoplasm, microtubule plus ends) and the need for co-localization with other proteins .

How should researchers optimize MAPRE1 antibody dilutions for immunostaining applications?

Optimizing antibody dilutions is critical for achieving specific staining with minimal background. For MAPRE1 antibodies, a systematic approach is recommended:

• Starting point determination: For most MAPRE1 antibodies, manufacturers recommend that "optimal dilutions should be experimentally determined" . This typically begins with a dilution series (e.g., 1:100, 1:250, 1:500, 1:1000).

• Tissue-specific optimization: MAPRE1 is ubiquitously expressed but at varying levels across tissues. Higher expressing tissues may require more dilute antibody solutions, while lower expressing tissues might need more concentrated antibody preparations .

• Fixation consideration: Different fixation methods can affect epitope accessibility. For formalin-fixed paraffin-embedded (FFPE) tissues, antigen retrieval methods should be optimized alongside antibody dilution .

• Signal-to-noise assessment matrix:

  Dilution	Signal Strength	Background	Signal-to-Noise Ratio
  1:100	Strong	High	Low to Moderate
  1:250	Strong to Moderate	Moderate	Moderate
  1:500	Moderate	Low to Moderate	Moderate to High
  1:1000	Weak to Moderate	Low	Variable

• Block optimization: Since MAPRE1 is found in both Golgi and cytoplasm , effective blocking is crucial. A combination of serum (5-10%) matched to the secondary antibody species and BSA (1-3%) is typically effective.

• Incubation conditions: Overnight incubation at 4°C often yields better results than shorter incubations at room temperature, particularly for dilute antibody solutions.

The optimal dilution will balance specific staining of MAPRE1's characteristic patterns (microtubule plus ends, centrosomes) while minimizing non-specific background .

What controls are essential when validating MAPRE1 antibody specificity?

Proper validation of MAPRE1 antibody specificity requires several critical controls:

• Positive tissue/cell controls: Include samples known to express MAPRE1 (e.g., dividing cells where MAPRE1 localizes to plus ends of microtubules and centrosomes) .

• Negative controls:

  • Primary antibody omission: Apply only secondary antibody to detect non-specific binding

  • Isotype control: Use non-specific IgG from the same host species (rabbit or mouse, depending on the antibody)

  • Peptide competition/blocking: Pre-incubate antibody with immunizing peptide to confirm binding specificity

• Genetic controls:

  • MAPRE1 knockdown/knockout: Compare staining between wild-type cells and those with reduced/absent MAPRE1 expression

  • Overexpression system: Cells transfected with MAPRE1 expression constructs should show enhanced signal

• Cross-validation with multiple antibodies: Use antibodies targeting different epitopes of MAPRE1 (e.g., N-terminal AA 1-110 versus C-terminal AA 134-268) . Agreement between antibodies increases confidence in specificity.

• Application-specific controls:

  • For Western blotting: Molecular weight markers to confirm the 30 kDa band expected for MAPRE1

  • For immunostaining: Co-staining with tubulin to confirm localization at microtubule plus ends

  • For immunoprecipitation: Input, flow-through, and non-specific binding controls

• Cross-species reactivity: If using antibodies across species, include positive controls from each species to confirm cross-reactivity as documented (e.g., Human, Mouse, Rat) .

What are common technical challenges when using MAPRE1 antibodies in Western blotting?

Researchers often encounter specific challenges when using MAPRE1 antibodies in Western blotting. Here are common issues and their methodological solutions:

• Multiple bands or unexpected molecular weights: MAPRE1 has a canonical molecular weight of 30 kDa . If detecting bands at unexpected sizes:

  • Verify sample preparation methods (proper lysis buffers that preserve protein integrity)

  • Check for post-translational modifications (MAPRE1 undergoes acetylation)

  • Consider splice variants or degradation products

  • Use phosphatase inhibitors as MAPRE1 can be phosphorylated

• Weak signal strength: When signal is faint despite adequate protein loading:

  • Increase primary antibody concentration or incubation time (overnight at 4°C)

  • Enhance detection sensitivity with higher-sensitivity ECL substrates

  • For epitopes in the AA 134-268 region, ensure your antibody specifically targets this region

  • Use polyclonal antibodies for signal amplification due to their recognition of multiple epitopes

• High background signal:

  • Increase washing duration and frequency (5-6 washes of 10 minutes each)

  • Optimize blocking (5% BSA often performs better than milk for phosphoprotein detection)

  • Dilute antibody in fresh blocking buffer

  • Use more stringent antibody diluent (add 0.1-0.2% Tween-20)

• Inconsistent results across experiments:

  • Standardize lysate preparation methods

  • Use freshly prepared samples (MAPRE1 is subject to degradation)

  • Consider using purified recombinant MAPRE1 as a positive control

  • Document lot numbers of antibodies as different lots may have slight variations in performance

• Cross-reactivity issues:

  • Choose antibodies validated for your species of interest (Human, Mouse, Rat)

  • Check homology between species for the specific epitope targeted by your antibody

  • Increase washing stringency to remove weak cross-reactive binding

How can researchers optimize immunofluorescence protocols for visualizing MAPRE1 at microtubule plus ends?

Visualizing MAPRE1 at microtubule plus ends requires special considerations for immunofluorescence protocols:

• Fixation optimization:

  • Cold methanol fixation (5-10 minutes at -20°C) often preserves microtubule structures better than formaldehyde

  • If using formaldehyde, a brief permeabilization with 0.1% Triton X-100 is essential for antibody access

  • Avoid harsh detergents that may disrupt microtubule architecture

• Cell culture considerations:

  • Plate cells at subconfluent density to observe individual cells clearly

  • Use cell lines with well-defined microtubule networks (e.g., U2OS, RPE1)

  • Consider treating cells with microtubule-stabilizing agents (e.g., low-dose taxol) to enhance visualization of plus ends

• Antibody selection and application:

  • For direct visualization, fluorophore-conjugated antibodies like MAPRE1 Antibody [Janelia Fluor® 525] provide high sensitivity without secondary antibody amplification

  • For co-localization studies, carefully select primary antibodies from different host species to avoid cross-reactivity

  • Apply antibodies in sequence with thorough washing between steps

• Imaging parameters optimization:

  • Use high-NA objectives (1.3-1.4) for optimal resolution

  • Consider deconvolution or super-resolution techniques for detailed plus-end visualization

  • Confocal microscopy with appropriate pinhole settings improves signal-to-noise ratio

  • Z-stack acquisition is recommended as microtubules occupy different focal planes

• Signal enhancement strategies:

  • Implement tyramide signal amplification for weak signals

  • Use image acquisition settings that maximize dynamic range without saturation

  • Consider quantum dots or other bright, photostable fluorophores for long-term imaging

• Co-staining recommendation matrix:

  Co-staining Partner	Information Provided	Technical Considerations
  α-tubulin	Localization relative to microtubule lattice	Use different host species antibodies
  EB3 (MAPRE3)	Distinction between EB family members	May require careful titration due to homology
  APC	Interaction between MAPRE1 and APC tumor suppressor	Often requires gentler fixation
  CLIP-170	+TIP complex visualization	Consider sequential rather than simultaneous staining
  Phospho-specific markers	Cell cycle status correlation	May require phosphatase inhibitors

Successful visualization typically shows MAPRE1 as distinct "comet-like" structures at growing microtubule plus ends, particularly evident in cells undergoing division or migration .

How can MAPRE1 antibodies be used to investigate microtubule dynamics in different disease models?

MAPRE1 antibodies provide valuable tools for investigating microtubule dynamics in disease contexts, particularly in cancer, neurodegeneration, and developmental disorders:

• Cancer research applications:

  • MAPRE1 interacts with the APC tumor suppressor protein, making it relevant for colorectal cancer studies

  • Use immunohistochemistry with paraffin-embedded tissue samples to compare MAPRE1 localization patterns between normal and tumor tissues

  • Quantify MAPRE1 levels by Western blotting to correlate with tumor invasion or metastasis potential

  • Co-immunoprecipitation experiments can identify altered protein interactions in cancer cells

• Neurodegenerative disease investigations:

  • In Alzheimer's and Parkinson's models, microtubule dynamics are frequently disrupted

  • Analyze MAPRE1 localization in primary neuronal cultures using fluorophore-conjugated antibodies

  • Compare MAPRE1-decorated microtubule plus-end density between control and disease-state samples

  • Correlate MAPRE1 binding patterns with tau aggregation or α-synuclein accumulation

• Developmental disorder research:

  • MAPRE1's role in cell division makes it relevant for studying disorders of neuronal migration and positioning

  • Examine MAPRE1 immunoreactivity patterns in developmental time course experiments

  • Combine with cell cycle markers to assess potential mitotic defects

• Methodological approach by disease context:

  Disease Context	Recommended Antibody Application	Key Parameters to Assess
  Cancer	IHC-P, WB, IP	Expression levels, protein interactions, subcellular localization
  Neurodegeneration	IF, WB, Live imaging	Comet density, microtubule growth rates, correlation with aggregates
  Developmental disorders	IHC, IF time course	Temporal expression patterns, localization during cell division
  Inflammation	FACS, WB	Expression levels in immune cell populations

• Specialized techniques:

  • Proximity ligation assay (PLA) to visualize MAPRE1 interactions with disease-relevant proteins

  • FRAP (Fluorescence Recovery After Photobleaching) using fluorophore-conjugated antibodies to assess dynamic protein turnover

  • Correlative light-electron microscopy to connect MAPRE1 localization with ultrastructural features

When interpreting results, researchers should note that alterations in MAPRE1 patterns may be either causal factors or consequences of disease processes, requiring careful experimental design to distinguish between these possibilities .

What approaches are recommended for studying post-translational modifications of MAPRE1 using antibodies?

Post-translational modifications (PTMs) of MAPRE1, particularly acetylation and phosphorylation, play crucial roles in regulating its function and interactions . Studying these modifications requires specialized approaches:

• PTM-specific antibody selection:

  • Use antibodies specifically raised against acetylated or phosphorylated forms of MAPRE1

  • For phosphorylation studies, consider site-specific phospho-antibodies targeting known regulatory residues

  • Validate PTM-specific antibodies using appropriate controls (e.g., phosphatase-treated samples)

• Enrichment strategies before detection:

  • For acetylation studies: Immunoprecipitate total MAPRE1 first, then probe with anti-acetyl lysine antibodies

  • For phosphorylation: Use phospho-enrichment techniques (phospho-protein enrichment kits, TiO₂ enrichment)

  • Include phosphatase inhibitors in all buffers when studying phosphorylation

• Validation approaches:

  • Compare PTM detection before and after treatment with modifying enzymes (phosphatases, deacetylases)

  • Use recombinant MAPRE1 with site-directed mutations at modification sites as negative controls

  • Employ mass spectrometry to independently confirm antibody-detected modifications

• PTM dynamics investigation:

  • Analyze modifications across cell cycle phases (G1, S, G2/M)

  • Examine PTM patterns after treatment with microtubule-targeting drugs

  • Study modification changes in response to cellular stress or signaling events

• Technical recommendations by modification type:

  Modification Type	Recommended Technique	Critical Controls	Common Pitfalls
  Phosphorylation	Phos-tag SDS-PAGE with WB	Lambda phosphatase treatment	Multiple phosphorylation sites causing band shifts
  Acetylation	IP followed by acetyl-lysine WB	Deacetylase treatment	Weaker signals requiring enhanced detection
  Ubiquitination	IP under denaturing conditions	Proteasome inhibitor treatment	Short half-life of ubiquitinated species
  Sumoylation	IP with SUMO-specific antibodies	SUMO-protease inhibitors	Low abundance requiring enrichment

• Functional correlation methods:

  • Combine PTM detection with functional assays (microtubule binding, protein interaction)

  • Use live-cell imaging to correlate PTM status with MAPRE1 dynamics at microtubule plus ends

  • Employ super-resolution microscopy to analyze spatial distribution of modified MAPRE1

When interpreting results, consider that different antibodies may have different sensitivities to various PTM combinations, and that modifications can influence each other hierarchically .

How should researchers interpret different MAPRE1 localization patterns throughout the cell cycle?

MAPRE1 exhibits distinct localization patterns during different cell cycle phases, and proper interpretation of these patterns provides insights into both normal cell cycle progression and potential abnormalities:

• Interphase patterns:

  • Normal pattern: MAPRE1 appears as distinct "comet-like" structures at growing microtubule plus ends, with additional localization at the centrosome

  • Interpretation: Represents active microtubule growth and normal cytoskeletal organization

  • Quantification approach: Measure comet density, length, and intensity to assess microtubule growth dynamics

• Mitotic patterns:

  • Prophase/Prometaphase: MAPRE1 localizes to astral microtubules and kinetochore fibers

  • Metaphase: Enrichment at spindle poles and along spindle microtubules

  • Anaphase/Telophase: Concentration at the central spindle and midbody

  • Interpretation: Changes in localization reflect MAPRE1's roles in spindle assembly, chromosome alignment, and cytokinesis

  • Quantification approach: Measure fluorescence intensity ratios between spindle regions

• Pattern analysis by cell cycle phase:

  Cell Cycle Phase	Expected MAPRE1 Pattern	Potential Abnormal Patterns	Implications
  G1	Distinct comets throughout cytoplasm	Diffuse cytoplasmic staining	Defective microtubule dynamics
  S	Comets plus centrosomal enrichment	Aggregation or loss of centrosomal signal	Replication stress or centrosome abnormalities
  G2	Increased comet density	Premature spindle-like patterns	Cell cycle checkpoint issues
  Mitosis	Dynamic redistribution to mitotic structures	Asymmetric distribution or persistent interphase pattern	Chromosome segregation defects

• Co-localization interpretation:

  • MAPRE1 and APC co-localization: Normal at microtubule plus ends, with implications for Wnt signaling

  • MAPRE1 and tubulin: Should show comets at the ends of microtubules rather than along the entire length

  • MAPRE1 and centrosomal markers: Partial overlap expected during interphase and mitosis

• Quantitative assessment approaches:

  • Fluorescence intensity profiling along microtubules to confirm plus-end enrichment

  • Co-localization coefficients (Pearson's, Manders') to quantify spatial relationships with other proteins

  • Tracking analysis to measure growth rates of MAPRE1-decorated microtubule ends

When interpreting MAPRE1 patterns, consider that antibody selection can influence results, particularly when comparing monoclonal antibodies (which recognize specific epitopes) versus polyclonal antibodies (which recognize multiple epitopes) . Standardized imaging conditions and analysis parameters are essential for reliable interpretation across experiments.

What statistical approaches are recommended for quantifying MAPRE1 expression differences between experimental conditions?

Quantitative analysis of MAPRE1 expression requires rigorous statistical approaches tailored to the specific experimental technique. Here are recommended methods based on common research applications:

• Western blot quantification:

  • Normalization strategy: Use housekeeping proteins (β-actin, GAPDH) or total protein stains (Ponceau S)

  • Relative quantification: Calculate MAPRE1/loading control ratio across samples

  • Statistical analysis: Apply paired t-tests for direct comparisons or ANOVA for multiple conditions

  • Data visualization: Box plots showing median, quartiles, and outliers rather than simple bar graphs

• Immunofluorescence intensity analysis:

  • Cellular compartment analysis: Separately quantify MAPRE1 signals in cytoplasm, Golgi, centrosome, and microtubule plus ends

  • Background correction: Subtract local background using cell-free regions

  • Cell population analysis: Analyze sufficient cells (≥50-100 per condition) to account for natural variation

  • Statistical approach: Hierarchical analysis accounting for cell-to-cell variation within experiments

• Flow cytometry quantification:

  • Population gating: Isolate specific cell populations based on cell cycle phase or other parameters

  • Fluorescence calibration: Use calibration beads to convert arbitrary units to molecules of equivalent soluble fluorochrome (MESF)

  • Analysis: Compare median fluorescence intensity (MFI) rather than mean values

  • Statistics: Non-parametric tests (Mann-Whitney U) if distributions are non-normal

• Recommended statistical approaches by experimental design:

  Experimental Design	Recommended Statistical Test	Sample Size Recommendations	Power Considerations
  Two condition comparison	Paired t-test or Wilcoxon	Minimum n=3-5 biological replicates	Effect size >1.5 for n=3
  Multiple conditions	One-way ANOVA with post-hoc	Minimum n=4-6 per condition	Adjust for multiple comparisons
  Time course experiments	Repeated measures ANOVA	Consistent sampling intervals	Consider autocorrelation
  Correlation with clinical outcomes	Cox regression or Kaplan-Meier	Power analysis based on expected HR	Account for covariates

• Advanced quantitative approaches:

  • Machine learning classification of MAPRE1 localization patterns

  • Bayesian hierarchical modeling to account for technical and biological variability

  • Meta-analysis approaches when combining data across multiple experiments

• Reporting recommendations:

  • Always include exact p-values rather than threshold statements (p<0.05)

  • Report confidence intervals alongside point estimates

  • Clearly state normalization methods and statistical tests used

  • Consider the clinical or biological significance beyond statistical significance

What emerging techniques are advancing MAPRE1 antibody applications in research?

The field of MAPRE1 research is evolving with several emerging technologies that enhance antibody-based studies:

• Super-resolution microscopy applications:

  • STORM/PALM techniques allow visualization of individual MAPRE1 molecules at microtubule plus ends

  • Structured illumination microscopy (SIM) enables dynamic tracking of MAPRE1 comets in live cells

  • Expansion microscopy physically enlarges samples to visualize MAPRE1-microtubule interactions at nanoscale resolution

  • These approaches overcome the diffraction limit of conventional microscopy, revealing previously undetectable details of MAPRE1 organization

• Proximity-based protein interaction detection:

  • BioID/TurboID fusion with MAPRE1 to identify transient interaction partners in living cells

  • APEX2-based proximity labeling to map the MAPRE1 interactome at specific subcellular locations

  • Split-protein complementation assays to visualize MAPRE1 interactions with APC and other partners in real-time

  • These methods capture interactions that may be lost during traditional immunoprecipitation

• Antibody engineering advancements:

  • Single-domain antibodies (nanobodies) against MAPRE1 for improved penetration in thick tissues

  • Bi-specific antibodies that simultaneously target MAPRE1 and interacting partners

  • Antibody fragments with enhanced tissue penetration for whole-organ imaging

  • Genetically encoded intrabodies for live-cell visualization of MAPRE1 without fixation artifacts

• High-throughput and multiplexed approaches:

  • Imaging mass cytometry to simultaneously measure MAPRE1 and dozens of other proteins

  • Cyclic immunofluorescence (CycIF) to detect MAPRE1 alongside >30 other proteins in the same sample

  • Automated image analysis pipelines for quantifying MAPRE1 localization across thousands of cells

  • These techniques enable systems-level analysis of MAPRE1 in complex cellular contexts

• In vivo applications:

  • Intravital microscopy with fluorophore-conjugated antibodies to track MAPRE1 dynamics in living tissues

  • Antibody-based optical imaging probes for non-invasive visualization of microtubule dynamics

  • Clearing-compatible antibodies for whole-organ MAPRE1 mapping in development and disease

These emerging approaches are expanding our understanding of MAPRE1's roles in cellular processes and disease mechanisms, moving beyond traditional applications like Western blotting, immunohistochemistry, and basic immunofluorescence .

How can researchers integrate MAPRE1 antibody data with other omics approaches?

Integrating MAPRE1 antibody-derived data with multi-omics approaches enables comprehensive understanding of microtubule dynamics in health and disease:

• Integration with transcriptomics:

  • Correlate MAPRE1 protein levels (detected by antibodies) with mRNA expression data

  • Identify potential transcriptional regulators of MAPRE1 expression

  • Examine splice variant expression that might affect antibody recognition sites

  • Approach: Perform Western blotting with antibodies targeting different MAPRE1 epitopes and correlate with RNA-seq data from the same samples

• Integration with proteomics:

  • Use immunoprecipitation with MAPRE1 antibodies followed by mass spectrometry to identify interaction partners

  • Compare MAPRE1 post-translational modifications detected by specific antibodies with global proteomics data

  • Validate proteomics-identified MAPRE1 interactions using co-immunoprecipitation and proximity ligation assays

  • Approach: Combine MAPRE1 immunoprecipitation using antibodies against different epitopes with LC-MS/MS analysis

• Integration with genomics:

  • Correlate genetic variations in MAPRE1 or interacting partners with protein expression or localization

  • Examine effects of cancer-associated mutations on MAPRE1 detection by specific antibodies

  • Investigate epigenetic regulation of MAPRE1 expression

  • Approach: Compare MAPRE1 immunostaining patterns across cell lines with different genetic backgrounds

• Multi-modal data integration framework:

  Omics Layer	MAPRE1 Antibody Application	Integration Approach	Expected Insights
  Transcriptomics	WB quantification	Correlation analysis	Transcriptional regulation mechanisms
  Proteomics	IP-MS, PTM-specific detection	Network analysis	Protein interaction dynamics, regulation
  Genomics	Expression pattern comparison	Genotype-phenotype association	Genetic influences on MAPRE1 function
  Metabolomics	Antibody-based imaging with metabolite detection	Spatial correlation	Metabolic influences on microtubule dynamics
  Single-cell analysis	Antibody-based flow cytometry	Clustering and trajectory analysis	Cell state-dependent MAPRE1 regulation

• Computational integration strategies:

  • Machine learning approaches to identify patterns across multi-omics datasets

  • Causal network inference to establish regulatory relationships

  • Pathway enrichment analysis incorporating MAPRE1 antibody-derived interaction data

  • Temporal modeling of MAPRE1 dynamics in response to perturbations

• Validation and functional assessment:

  • Use CRISPR-based perturbations to validate computationally predicted relationships

  • Employ fluorophore-conjugated MAPRE1 antibodies for live-cell imaging to confirm dynamic predictions

  • Develop mathematical models of microtubule dynamics informed by integrated datasets

This integrated approach moves beyond descriptive characterization of MAPRE1 to mechanistic understanding of its roles in complex cellular processes, potentially revealing new therapeutic targets for diseases involving cytoskeletal dysregulation .