CATHB2 Antibody

What is CATHB2 and what cellular functions does it regulate?

CATHB2 (also known as Cathepsin B) belongs to the family of cysteine proteases that play critical roles in protein degradation within lysosomes. Cathepsin B functions in numerous cellular processes including protein turnover, antigen processing, apoptosis, and extracellular matrix remodeling. In pathological conditions, Cathepsin B has been identified in amyloid plaques and may contribute to neurodegenerative diseases like Alzheimer's . The protein is widely expressed across tissues and demonstrates both endopeptidase and exopeptidase activity, making it a multifunctional protease of significant research interest. Understanding its role requires reliable antibodies that can accurately detect its presence and localization within cellular compartments.

How can researchers confirm CATHB2 antibody specificity in their experimental systems?

Confirming antibody specificity is fundamental to generating reliable research data. For CATHB2 antibodies, implement these methodological approaches:

• Positive and negative control tissues: Use tissues with known CATHB2 expression profiles. Tissues with CATHB2 knockout or knockdown serve as excellent negative controls.

• Peptide competition assays: Pre-incubate the antibody with purified CATHB2 protein or immunizing peptide before application. Specific binding will be blocked, and signal should disappear if the antibody is specific.

• Multiple antibody validation: Employ at least two different antibodies targeting distinct CATHB2 epitopes. Concordant results strengthen specificity claims.

• Western blot correlation: Compare IHC or ICC-IF results with Western blot analysis to confirm target molecular weight matches expected CATHB2 size.

• Genetic manipulation: Use CRISPR/Cas9 knockout or siRNA knockdown systems to create CATHB2-deficient samples as definitive negative controls.
  These approaches follow similar validation principles used for other antibodies such as those against KAT2B, which undergo rigorous validation in IHC, ICC-IF, and Western blot applications .

How should researchers design proper controls when using CATHB2 antibodies in multiplex immunofluorescence studies?

Designing robust controls for multiplex immunofluorescence studies with CATHB2 antibodies requires a comprehensive approach:

• Single staining controls: Each antibody in the multiplex panel should first be tested individually using the same protocol to establish baseline signal and confirm no cross-reactivity with other detection systems.

• Fluorophore controls: Include samples stained with secondary antibodies only to assess auto-fluorescence and non-specific binding.

• Biological negative controls: Incorporate CATHB2-knockout or knockdown samples, processed identically to experimental samples.

• Absorption controls: Pre-absorb the CATHB2 antibody with purified antigen before staining to verify signal specificity.

• Cross-reactivity matrix: Create a matrix testing each primary antibody against all secondary antibodies to identify potential cross-reactivity issues.

• Spectral overlap compensation: Perform proper spectral unmixing, particularly important when fluorophores have overlapping emission spectra.

• Titration series: Establish optimal antibody concentrations through dilution series experiments to maximize signal while minimizing background.
  This approach ensures that signals detected in multiplex studies are specifically attributable to CATHB2 expression rather than technical artifacts, following similar principles used in complex immunological studies of viral infections .

What quantification methods are most appropriate for analyzing CATHB2 expression levels in different cellular compartments?

Quantifying CATHB2 expression across cellular compartments requires specialized approaches due to its dynamic trafficking between lysosomes and other locations. Recommended methodological approaches include:

• Subcellular fractionation followed by Western blotting: Systematically separate cellular compartments (cytosol, lysosomes, endosomes, nucleus, membrane) and quantify CATHB2 in each fraction using validated antibodies. This requires careful normalization against compartment-specific markers.

• High-content imaging with colocalization analysis: Employ confocal microscopy with CATHB2 antibodies alongside organelle-specific markers (LAMP1 for lysosomes, EEA1 for early endosomes). Quantify colocalization using Pearson's or Mander's coefficients.

• Proximity ligation assays (PLA): For analyzing interactions between CATHB2 and other proteins within specific compartments, PLA provides high specificity and sensitivity with spatial resolution.

• Fluorescence intensity quantification: For immunofluorescence, use integrated density measurements normalized to cell area or volume, with background subtraction.

• Live-cell imaging with fluorescently-tagged antibody fragments: For dynamic studies, consider using Fab fragments conjugated to fluorophores to track CATHB2 trafficking in real-time.
  Each method should include appropriate controls and standardization procedures to ensure reproducibility. Quantitative data should be presented with statistical analysis comparing expression levels across different cellular states or experimental conditions.

How can researchers overcome non-specific binding issues with CATHB2 antibodies?

Non-specific binding is a common challenge with antibodies, including those targeting CATHB2. To overcome this issue, implement these methodological solutions:

• Optimized blocking protocols: Test different blocking agents (BSA, normal serum, casein, commercial blockers) at various concentrations and incubation times. For CATHB2 detection, 5% milk in TBS-T buffer for 1 hour at room temperature has proven effective in similar applications .

• Antibody dilution optimization: Perform titration experiments to identify the optimal antibody concentration that maximizes specific signal while minimizing background. Start with manufacturer recommendations and adjust accordingly.

• Buffer modifications: Adjust salt concentration and pH of washing and incubation buffers. For CATHB2, TBS-T with additional 0.1-0.3M NaCl may reduce non-specific ionic interactions.

• Pre-adsorption steps: Incubate diluted antibody with tissues or cell lysates from species of secondary antibody origin to remove cross-reactive antibodies.

• Detergent optimization: Adjust detergent type and concentration in washing buffers to reduce hydrophobic interactions. For membrane proteins, 0.1-0.3% Triton X-100 may be effective; for cytosolic targets, 0.05-0.1% Tween-20 often suffices.

• Secondary antibody selection: Use highly cross-adsorbed secondary antibodies specifically tested against the host species of your primary antibodies.

• Endogenous enzyme blocking: For enzymatic detection systems, block endogenous peroxidases or phosphatases using appropriate reagents (H₂O₂ for peroxidases, levamisole for alkaline phosphatases).
  Document optimization steps systematically to establish reproducible protocols for your specific experimental system.

What strategies can address epitope masking issues when detecting CATHB2 in fixed tissues?

Epitope masking frequently challenges researchers working with fixed tissues. For CATHB2 detection, which may be particularly susceptible to masking due to its lysosomal localization, implement these methodological approaches:

• Antigen retrieval optimization matrix: Systematically compare heat-induced epitope retrieval methods using different buffers (citrate pH 6.0, Tris-EDTA pH 9.0, glycine-HCl pH 3.5) at varying temperatures and durations.

• Enzymatic antigen retrieval testing: Evaluate different proteolytic enzymes (proteinase K, trypsin, pepsin) at various concentrations and incubation times to determine optimal conditions for CATHB2 epitope exposure.

• Combined retrieval approaches: For particularly resistant samples, test sequential application of heat-mediated followed by enzymatic retrieval.

• Alternative fixation methods: If possible, compare different fixatives (paraformaldehyde, methanol, acetone) and fixation durations to determine optimal preservation of CATHB2 epitopes.

• Freeze substitution: For critical applications, consider cryofixation followed by freeze substitution to better preserve antigenic epitopes.

• Microwave-assisted processing: Explore microwave-assisted fixation and processing, which can enhance antibody penetration and epitope accessibility.

• Fresh frozen tissue sections: For particularly challenging applications, use fresh frozen tissues without chemical fixation, applying only brief fixation after sectioning.
  Document comparative results quantitatively by measuring staining intensity, signal-to-noise ratio, and morphological preservation to identify optimal conditions for your specific tissue and application.

How can researchers mitigate issues related to CATHB2 antibody batch-to-batch variability?

Antibody batch variability represents a significant challenge to experimental reproducibility. For CATHB2 antibody research, implement these systematic approaches:

• Standardized validation protocol: Develop a standardized validation workflow for each new antibody batch, including Western blot, immunoprecipitation, and immunostaining on reference samples with known CATHB2 expression patterns.

• Reference standard creation: Prepare and store reference lysates or fixed cell preparations with defined CATHB2 expression levels to benchmark each new antibody batch.

• Epitope verification: For monoclonal antibodies, perform epitope mapping to confirm consistent epitope recognition across batches.

• Purified protein controls: Use recombinant CATHB2 protein at known concentrations to create standard curves for quantitative applications.

• Long-term storage planning: Purchase sufficient quantities of validated batches for entire project durations when possible, with proper aliquoting and storage to maintain antibody integrity.

• Parallel testing period: When transitioning between batches, include a period of parallel testing to establish correlation factors if needed.

• Supplier communication: Maintain open communication with manufacturers regarding production methods, validation protocols, and lot-specific performance data.

• Multiple sourcing strategy: For critical projects, validate antibodies from multiple vendors or production methods to reduce dependency on a single source.
  By implementing these approaches, researchers can better control for technical variability and improve the reproducibility of CATHB2-related findings, following standardized practices similar to those used for other critical antibodies .

How can CATHB2 antibodies be effectively incorporated into Chimeric Antigen Receptor (CAR) designs for potential therapeutic applications?

Incorporating CATHB2 antibodies into CAR designs requires sophisticated molecular engineering approaches similar to those used for other target-specific CARs. Based on methodologies employed for HBV-targeted CARs, the following stepwise approach is recommended:

• Antibody fragment optimization: Convert full CATHB2 antibodies to single-chain variable fragments (scFvs) using glycine-serine linkers connecting variable heavy and light chains, as demonstrated in HBV-specific CARs . This typically requires codon optimization for enhanced expression in T cells.

• CAR structural design: Construct second-generation CARs comprising the CATHB2-specific scFv binding domain with an external tag (such as HA-tag), an appropriate hinge region (IgG4 has shown good results), a transmembrane domain (CD28), and intracellular signaling domains (CD28 and CD3ζ) .

• Vector selection: Select appropriate retroviral or lentiviral vectors for stable CAR integration into T cells, optimizing for transduction efficiency while maintaining T cell viability.

• Transduction protocol optimization: Develop protocols that achieve consistent CAR expression across both CD4+ and CD8+ T cell populations, measuring both percentage of transduced cells and expression levels via flow cytometry .

• Functional validation: Test CAR-T cell functionality through:

  • Cytokine release assays (IFNγ, TNFα) upon target recognition

  • Cytotoxicity assays against CATHB2-expressing target cells

  • Proliferation assays to assess CAR-T cell expansion upon stimulation

• Specificity assessment: Rigorously evaluate on-target/off-tumor effects using control cells with varying CATHB2 expression levels to ensure specificity and safety.

• In vivo models: Develop appropriate animal models to test efficacy and safety, potentially using immunodeficient mouse models similar to the Bl6.Rag1-/- mice used for HBV CAR testing .
  This methodological framework provides a foundation for developing CATHB2-targeted CAR-T cell therapies while addressing critical considerations for specificity and efficacy.

What methodologies are most effective for studying CATHB2 interactions with potential binding partners in live cells?

Studying CATHB2 protein interactions in live cells requires advanced methodologies that preserve native cellular conditions while providing sufficient resolution and specificity. Recommended approaches include:

• Förster Resonance Energy Transfer (FRET): Tag CATHB2 and potential binding partners with appropriate fluorophore pairs (e.g., CFP/YFP or GFP/mCherry). Measure energy transfer efficiency using either intensity-based FRET or fluorescence lifetime imaging microscopy (FLIM) to detect direct protein interactions within 10nm distance.

• Bimolecular Fluorescence Complementation (BiFC): Fuse complementary fragments of fluorescent proteins to CATHB2 and potential partners. Interaction brings fragments together, reconstituting fluorescence activity. This approach provides exceptional signal-to-noise ratio for detecting interactions in specific cellular compartments.

• Proximity Ligation Assay (PLA) with live-cell compatibility: Adapt traditional PLA methods using cell-permeable antibody fragments or nanobodies against CATHB2 and its partners. This generates fluorescent signals only when proteins are within 40nm proximity.

• Split-luciferase complementation: Fuse complementary luciferase fragments to CATHB2 and potential interactors. Interaction reconstitutes enzymatic activity, allowing kinetic analysis of protein interactions through bioluminescence imaging.

• Optogenetic approaches: Engineer light-responsive domains into CATHB2 constructs to enable spatiotemporal control of interactions, allowing precise interrogation of interaction dynamics.

• CRISPR-based tagging with fluorescent proteins: Use knock-in strategies to tag endogenous CATHB2 and interacting proteins, maintaining native expression levels and regulatory mechanisms.

• Live-cell super-resolution microscopy: Employ techniques like Structured Illumination Microscopy (SIM) or Stimulated Emission Depletion (STED) microscopy to visualize interactions at sub-diffraction resolution.
  Each method offers distinct advantages in temporal resolution, spatial precision, and physiological relevance. Researchers should select approaches based on their specific hypotheses regarding CATHB2 interaction dynamics.

How can researchers design experiments to investigate the potential role of CATHB2 in disease pathogenesis across different model systems?

Designing comprehensive experiments to elucidate CATHB2's role in disease pathogenesis requires a multi-model, multi-scale approach:

• Cell line selection strategy: Employ both disease-relevant primary cells and established cell lines. For neurodegenerative disease studies, use both neuronal and microglial cultures; for cancer studies, compare matched normal and malignant cell lines with validated CATHB2 expression profiles.

• Genetic manipulation approaches:

  • CRISPR/Cas9 for complete knockout

  • siRNA/shRNA for transient knockdown

  • Inducible expression systems for controlled overexpression

  • Site-directed mutagenesis to study specific functional domains

• Animal models with targeted modifications:

  • Generate conditional tissue-specific CATHB2 knockout animals

  • Develop transgenic models with disease-relevant CATHB2 mutations

  • Utilize AAV-mediated gene delivery for localized CATHB2 manipulation, similar to approaches used in HBV models

• Tissue/cellular compartment profiling:

  • Perform subcellular fractionation followed by enzymatic activity assays

  • Use immunohistochemistry with validated CATHB2 antibodies to map expression across tissues

  • Employ laser capture microdissection to analyze CATHB2 in specific regions of heterogeneous tissues

• Functional readouts across models:

  • Enzymatic activity assays using specific CATHB2 substrates

  • Proteomics to identify altered substrate processing

  • Cellular phenotype assays (apoptosis, proliferation, migration)

  • Tissue-level pathology assessment

• Translational correlation studies:

  • Design experiments that parallel human clinical samples

  • Develop consistent analysis pipelines that can be applied across species

  • Create standardized scoring systems for CATHB2-associated pathology

• Intervention testing:

  • Test CATHB2-specific inhibitors across model systems

  • Evaluate antibody-based interventions including neutralizing antibodies

  • Assess combination approaches targeting CATHB2 and associated pathways
    This hierarchical experimental design allows researchers to establish causal relationships between CATHB2 functionality and disease mechanisms, providing stronger evidence than correlative studies alone.

How should researchers interpret discrepancies between CATHB2 protein levels and enzymatic activity in experimental samples?

Interpreting discrepancies between CATHB2 protein levels (detected by antibodies) and enzymatic activity requires a methodical analytical approach:

• Activation state analysis: CATHB2 is synthesized as an inactive proenzyme requiring proteolytic processing for activation. Employ antibodies specific to pro-CATHB2 versus active CATHB2 to determine the proportion in each state. Western blotting with appropriate controls can distinguish between the ~40 kDa proenzyme and ~30 kDa active form.

• Inhibitor presence assessment: Endogenous inhibitors like cystatins can block CATHB2 activity without affecting protein levels. Measure levels of known CATHB2 inhibitors in parallel with CATHB2 protein quantification.

• pH microenvironment consideration: CATHB2 activity is pH-dependent, with optimal activity in acidic environments typical of lysosomes. Measure local pH in subcellular compartments using ratiometric pH indicators to determine if environmental conditions support enzymatic activity.

• Post-translational modification analysis: Phosphorylation, glycosylation, and oxidation can alter CATHB2 activity. Employ targeted proteomic approaches to map post-translational modifications correlating with activity discrepancies.

• Substrate availability assessment: Limited substrate availability may restrict apparent activity despite abundant enzyme. Include substrate supplementation controls in activity assays.

• Compartmentalization analysis: CATHB2 may be sequestered in compartments separate from its substrates. Perform subcellular fractionation followed by parallel protein quantification and activity assays on each fraction.

• Methodological validation: Verify that activity assays are indeed CATHB2-specific by using selective inhibitors (e.g., CA-074) and confirming activity abolishment in CATHB2 knockout controls.
  When presenting discrepancy data, include comprehensive controls addressing each of these variables and present findings in context of the complete dataset rather than isolated measurements.

What statistical approaches are most appropriate for analyzing CATHB2 expression patterns across different tissue types and disease states?

Analyzing CATHB2 expression patterns across diverse samples requires robust statistical methodologies that account for biological and technical variability:

How should researchers approach cross-validation of CATHB2 antibody results using orthogonal detection methods?

Cross-validation using orthogonal methods is essential for conclusive CATHB2 research. Implement this systematic approach:

• Multi-antibody verification protocol:

  • Test multiple CATHB2 antibodies targeting different epitopes

  • Compare polyclonal and monoclonal antibody results

  • Document concordance and discrepancies between antibody clones

  • Create validation matrices comparing sensitivity and specificity across antibodies

• Immunoassay-molecular method correlation:

  • Correlate protein detection (Western blot, IHC, flow cytometry) with mRNA expression (qPCR, RNA-seq)

  • Account for potential post-transcriptional regulation by calculating protein-to-mRNA ratios

  • Present scatterplots with regression analyses demonstrating relationships between methods

• Functional validation approaches:

  • Supplement antibody detection with enzyme activity assays using specific CATHB2 substrates

  • Employ selective inhibitors (CA-074) to confirm specificity of activity measurements

  • Correlate activity levels with protein measurements across samples

• Genetic manipulation controls:

  • Include CRISPR-mediated CATHB2 knockout or knockdown samples as definitive negative controls

  • Implement rescue experiments with exogenous CATHB2 expression to confirm specificity

  • Document complete validation workflows including genetic confirmation

• Mass spectrometry verification:

  • Perform targeted proteomics using multiple reaction monitoring (MRM) or parallel reaction monitoring (PRM)

  • Identify CATHB2-specific peptides for definitive protein identification

  • Quantify using stable isotope-labeled internal standards for absolute quantification

• Proximity-based detection methods:

  • Implement proximity ligation assays (PLA) to verify protein-protein interactions

  • Use proximity extension assays for sensitive detection in complex matrices

  • Compare results with traditional co-immunoprecipitation approaches

• Meta-analysis framework:

  • Create integrated datasets combining results from multiple methods

  • Calculate concordance metrics (Cohen's kappa, intraclass correlation coefficients)

  • Present Bland-Altman plots to visualize agreement between methods
    This comprehensive cross-validation strategy follows similar principles to those employed in validation of other critical antibodies used in research applications and provides necessary confidence in CATHB2-related findings.

How can CATHB2 antibodies be employed to investigate the role of this protease in neurodegenerative disease mechanisms?

CATHB2 (Cathepsin B) antibodies offer powerful tools for investigating this protease's role in neurodegenerative pathologies, particularly given its identification in amyloid plaques associated with Alzheimer's disease . Methodological approaches should include:

• Co-localization studies with disease-specific markers:

  • Apply dual immunofluorescence with validated CATHB2 antibodies alongside antibodies against Aβ, tau, α-synuclein, or TDP-43

  • Quantify co-localization using Mander's or Pearson's coefficients in defined brain regions

  • Compare patterns across disease stages using post-mortem tissue samples

• Activity-based probing in neural tissues:

  • Combine CATHB2 antibody staining with activity-based probes that selectively label active enzyme

  • Compare active versus total CATHB2 distribution in affected versus unaffected regions

  • Correlate activity patterns with pathological markers and clinical parameters

• Microglial activation correlation:

  • Assess CATHB2 levels in different microglial activation states using multi-parameter flow cytometry or imaging

  • Correlate CATHB2 expression with inflammatory markers in microglia isolated from disease models

  • Perform time-course analyses to determine whether CATHB2 upregulation precedes or follows microglial activation

• Lysosomal function assessment:

  • Evaluate CATHB2 antibody staining patterns alongside lysosomal integrity markers

  • Determine if CATHB2 redistributes from lysosomes in disease states using subcellular fractionation

  • Correlate CATHB2 localization changes with lysosomal membrane permeabilization events

• Extracellular CATHB2 characterization:

  • Use validated antibodies to detect secreted CATHB2 in cerebrospinal fluid and brain interstitial fluid

  • Compare levels between control and disease populations, correlating with disease progression

  • Distinguish between active and pro-enzyme forms in extracellular compartments

• Therapeutic target validation:

  • Apply neutralizing CATHB2 antibodies in neuronal and organoid models to assess functional effects

  • Evaluate antibody-mediated inhibition compared to small molecule inhibitors

  • Test cell-penetrating antibody derivatives for intracellular target engagement
    These approaches provide a comprehensive framework for elucidating CATHB2's contributions to neurodegenerative processes, potentially identifying novel therapeutic intervention points.

What are the methodological considerations for using CATHB2 antibodies in multiplexed proteomic approaches?

Integrating CATHB2 antibodies into multiplexed proteomic workflows requires careful methodological considerations to ensure specificity, sensitivity, and quantitative accuracy:

• Antibody specificity verification for multiplexing:

  • Test for cross-reactivity against all targets in the multiplex panel using peptide arrays

  • Perform sequential staining experiments comparing single-plex versus multiplex results

  • Document cross-reactivity matrices for all antibodies in the multiplex panel

• Conjugation chemistry optimization:

  • Select optimal fluorophores or mass tags considering spectral overlap or mass resolution

  • Validate that conjugation does not affect binding properties of the CATHB2 antibody

  • Determine optimal antibody-to-tag ratios for maximum sensitivity without steric hindrance

• Panel design strategy:

  • Include CATHB2 interacting partners and substrates for functional network analysis

  • Incorporate markers for subcellular compartments relevant to CATHB2 trafficking

  • Design panels addressing specific biological questions rather than maximizing target number

• Sample preparation harmonization:

  • Optimize fixation and permeabilization protocols compatible with all antibodies in the panel

  • Validate epitope preservation across all targets following antigen retrieval procedures

  • Develop blocking strategies that minimize background without compromising specific signals

• Quantification standardization:

  • Implement standard curves using recombinant proteins for absolute quantification

  • Apply appropriate normalization strategies (cell number, tissue area, total protein)

  • Develop batch correction methods for large-scale studies

• Data analysis framework:

  • Apply dimensionality reduction techniques appropriate for highly multiparametric data

  • Implement clustering algorithms to identify coordinated expression patterns

  • Develop visualization approaches that effectively communicate complex relationships

• Validation through orthogonal methods:

  • Confirm key findings using independent techniques (e.g., RNA-seq, targeted proteomics)

  • Perform biological validation through perturbation experiments

  • Compare antibody-based multiplex results with label-free proteomic approaches
    This methodological framework enhances the reliability of multiplex studies incorporating CATHB2 antibodies while maximizing the biological insights gained from complex proteomic datasets.

How can researchers effectively use CATHB2 antibodies to investigate autophagy-lysosomal pathway dynamics in disease states?

Investigating autophagy-lysosomal pathway (ALP) dynamics with CATHB2 antibodies requires sophisticated methodological approaches that capture both spatial and temporal aspects of this complex system:

• Dynamic co-localization analysis:

  • Combine CATHB2 antibody staining with markers for different stages of the ALP (LC3, p62, LAMP1/2)

  • Implement time-course experiments following autophagy induction or inhibition

  • Quantify changes in co-localization coefficients across conditions using high-content imaging

• Flux assessment methodology:

  • Develop protocols to distinguish changes in CATHB2 synthesis versus degradation rates

  • Implement lysosomal inhibition (Bafilomycin A1) to measure CATHB2 accumulation rates

  • Compare CATHB2 protein levels with activity measurements to assess functional enzyme pool

• Substrate processing tracking:

  • Monitor degradation of known CATHB2 substrates in parallel with enzyme localization

  • Employ fluorescent substrates with specific CATHB2 cleavage sites for live cell monitoring

  • Correlate substrate processing efficiency with CATHB2 distribution patterns

• Selective autophagy pathway analysis:

  • Investigate CATHB2 involvement in different selective autophagy pathways (mitophagy, ribophagy, ER-phagy)

  • Correlate CATHB2 recruitment with specific cargo recognition events

  • Determine if CATHB2 plays differential roles in various selective autophagy processes

• Stress response profiling:

  • Map CATHB2 redistribution following different cellular stressors (oxidative stress, ER stress, starvation)

  • Compare acute versus chronic stress responses in terms of CATHB2 function

  • Develop quantitative metrics for stress-induced changes in CATHB2 activity and localization

• Genetic modifier screening:

  • Implement CRISPR screens to identify genes affecting CATHB2 trafficking in the ALP

  • Validate key hits through detailed analysis of CATHB2 localization and processing

  • Construct pathway maps integrating CATHB2 regulation with broader ALP dynamics

• Therapeutic intervention assessment:

  • Evaluate compounds targeting the ALP for effects on CATHB2 distribution and function

  • Develop readouts suitable for high-throughput screening based on CATHB2 antibody staining

  • Validate findings through orthogonal functional assays This methodological framework provides researchers with comprehensive approaches to dissect CATHB2's complex roles within the dynamic ALP, particularly in disease contexts where this system is dysregulated.