ZNF260 Antibody

What is ZNF260 and what role does it play in cellular processes?

ZNF260 is a nuclear transcription factor that functions as a cardiac regulator and an effector of alpha1-adrenergic signaling pathways. The protein binds to PE response elements (PERE) present in the promoter regions of genes such as ANF/NPPA and acts as a direct transcriptional activator of NPPA. Additionally, ZNF260 serves as a cofactor with GATA4, a key cardiac regulator, suggesting its important role in cardiac development and function . The protein is primarily localized in the nucleus, which aligns with its function as a transcription factor . Immunocytochemistry studies have demonstrated nucleoplasmic localization, although some cytosolic presence has also been observed in certain cell types, indicating potential non-nuclear functions or trafficking mechanisms that warrant further investigation .

What applications are ZNF260 antibodies commonly used for in research?

ZNF260 antibodies are employed across multiple research applications with varying degrees of optimization. The primary applications include:

These applications enable researchers to investigate ZNF260 expression, localization, and function across different experimental contexts, from protein lysates to tissue sections and cellular preparations .

How should researchers select the appropriate ZNF260 antibody for specific experimental needs?

Selection of the optimal ZNF260 antibody requires careful consideration of several key factors:

• Epitope recognition region: Different antibodies target distinct regions of ZNF260. For instance, available antibodies recognize epitopes in the N-terminal region (AA 1-200, 64-114, or 89-115) or other specific regions (AA 101-200/412) . Select antibodies recognizing regions relevant to your research question, particularly if studying protein domains, variants, or potential cleavage products.

• Host species compatibility: Most ZNF260 antibodies are raised in rabbit, which must be considered when designing multi-labeling experiments to avoid cross-reactivity with other primary or secondary antibodies .

• Species reactivity: Verify the antibody's validated reactivity with your experimental model. Some antibodies react with human ZNF260 only, while others cross-react with mouse and/or rat orthologs .

• Conjugation requirements: ZNF260 antibodies are available in unconjugated forms or with various conjugates (FITC, PE, HRP, Biotin) depending on the intended application .

• Validation documentation: Review available validation data, including Western blot images, IHC staining patterns, or ICC/IF results provided by manufacturers to ensure the antibody demonstrates appropriate specificity and sensitivity .

The experimental context should ultimately guide your selection, with consideration for technical compatibility with existing protocols and reagents .

What are the recommended storage and handling guidelines for ZNF260 antibodies?

Proper storage and handling of ZNF260 antibodies are critical for maintaining reactivity and specificity. Based on manufacturer recommendations:

• Storage temperature: Store ZNF260 antibodies at -20°C for long-term preservation, with some products stable for up to one year from receipt when properly stored .

• Aliquoting practice: Divide antibodies into multiple small-volume aliquots upon receipt to avoid repeated freeze-thaw cycles, which can significantly degrade antibody quality and performance .

• Formulation considerations: ZNF260 antibodies are typically supplied in stabilizing buffers containing components such as:

  • Glycerol (typically 40-50%) for cryoprotection

  • PBS or TBS (pH 7.2-7.4) for maintaining physiological pH

  • BSA (0.5-1%) for protein stabilization

  • Preservatives like sodium azide (0.02-0.03%) or Proclin300 to prevent microbial growth

• Working solution handling: For diluted working solutions, maintain at 4°C for short-term use (typically 1-2 weeks), and avoid extended storage of diluted antibody to prevent performance degradation.

• Transportation requirements: ZNF260 antibodies are typically shipped with polar packs and should be stored according to manufacturer recommendations immediately upon receipt .

Adhering to these storage practices ensures optimal antibody performance and extends the functional lifespan of these valuable research reagents .

What are the optimal protocols for using ZNF260 antibodies in Western blot applications?

For optimal Western blot results with ZNF260 antibodies, researchers should follow these methodological guidelines:

• Sample preparation:

  • Prepare cell or tissue lysates in RIPA or NP-40 buffer containing protease inhibitors

  • Include phosphatase inhibitors if investigating phosphorylation status

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

• Gel electrophoresis:

  • Use 10-12% SDS-PAGE gels for optimal resolution of ZNF260 (expected MW approximately 40-50 kDa)

  • Load 20-50 μg total protein per lane depending on expression level

• Transfer conditions:

  • Transfer to PVDF membrane (preferred over nitrocellulose for zinc finger proteins)

  • Use wet transfer at 100V for 1 hour or 30V overnight at 4°C

• Blocking:

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

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

• Antibody incubation:

  • Dilute primary ZNF260 antibody in blocking buffer at 1:500-2000 as recommended

  • Incubate overnight at 4°C with gentle agitation

  • Wash 3-5 times with TBST, 5 minutes each

  • Incubate with appropriate HRP-conjugated secondary antibody (typically anti-rabbit IgG at 1:5000-10000) for 1 hour at room temperature

  • Wash 3-5 times with TBST, 5 minutes each

• Detection:

  • Use ECL reagents appropriate for the expected signal intensity

  • For low expression levels, consider enhanced chemiluminescence substrates

• Controls:

  • Include positive control lysates from cells known to express ZNF260

  • Consider including a blocking peptide control to confirm specificity

These methodology recommendations incorporate principles from standard Western blot protocols optimized for zinc finger proteins while integrating the specific dilution ranges and conditions recommended for ZNF260 antibodies .

How can researchers validate the specificity of ZNF260 antibodies in their experimental systems?

Thorough validation of ZNF260 antibody specificity is essential for generating reliable research data. A comprehensive validation approach should include:

• Positive and negative control samples:

  • Test antibody on tissues or cell lines with known high (cardiac tissues) and low/absent ZNF260 expression

  • Compare staining/signal patterns with expected subcellular localization (primarily nuclear according to literature)

• Peptide competition assays:

  • Pre-incubate the antibody with excess immunizing peptide (when available)

  • Perform parallel experiments with blocked and unblocked antibody

  • Specific signals should be significantly reduced or eliminated with peptide blocking

• Genetic validation approaches:

  • Test antibody on ZNF260 knockout or knockdown models

  • The specific signal should be absent or significantly reduced

  • Alternatively, test on ZNF260 overexpression systems, which should show increased signal

• Multiple antibody concordance:

  • Compare results using antibodies targeting different epitopes of ZNF260 (e.g., N-terminal regions AA 64-114 vs. AA 89-115)

  • Consistent results across antibodies increase confidence in specificity

• Cross-reactivity assessment:

  • Evaluate potential cross-reactivity with related zinc finger proteins

  • Consider sequence homology in the immunogen region when selecting antibodies

• Molecular weight verification:

  • Confirm that the detected band in Western blot corresponds to the expected molecular weight

  • Watch for potential post-translationally modified forms or splice variants

• Immunoprecipitation followed by mass spectrometry:

  • For highest confidence validation, perform IP with the antibody followed by mass spectrometric identification

These validation steps collectively provide strong evidence for antibody specificity and should be documented in publications to enhance reproducibility .

What procedures should be followed for effective immunohistochemical detection of ZNF260?

Successful immunohistochemical (IHC) detection of ZNF260 requires attention to several critical parameters:

• Tissue preparation:

  • Fix tissues in 10% neutral buffered formalin for 24-48 hours

  • Process and embed in paraffin following standard histological procedures

  • Section at 4-5 μm thickness onto charged slides

• Antigen retrieval (critical step):

  • Heat-induced epitope retrieval (HIER) at pH 6.0 is specifically recommended for ZNF260 detection

  • Use citrate buffer and heat treatment (pressure cooker, microwave, or water bath at 95-98°C for 20 minutes)

  • Allow slides to cool in retrieval solution for 20 minutes before proceeding

• Blocking and permeabilization:

  • Block endogenous peroxidase with 3% hydrogen peroxide for 10 minutes

  • Block non-specific binding with 5-10% normal serum from the same species as the secondary antibody

  • For nuclear antigens like ZNF260, ensure adequate permeabilization using 0.2-0.5% Triton X-100 in PBS for 10 minutes

• Antibody incubation:

  • Apply primary ZNF260 antibody at dilutions of 1:50-1:200 as recommended

  • Incubate overnight at 4°C in a humidified chamber

  • Wash thoroughly with PBS or TBS (3 × 5 minutes)

  • Apply appropriate detection system (typically HRP-polymer or ABC method)

• Detection and counterstaining:

  • Develop with DAB or other chromogen

  • Counterstain with hematoxylin for nuclear visualization

  • Dehydrate, clear, and mount with permanent mounting medium

• Controls and interpretation:

  • Include positive control tissues (cardiac tissue shows strong nuclear positivity)

  • Note that while ZNF260 is primarily nuclear, some cytoplasmic staining may be observed in certain cell types, particularly glandular cells in stomach tissue

  • Evaluate staining intensity and distribution pattern rather than simple presence/absence

This protocol maximizes the likelihood of specific ZNF260 detection while minimizing background and non-specific staining .

How can ZNF260 antibodies be employed in studying cardiac development and disease mechanisms?

ZNF260 antibodies offer powerful tools for investigating cardiac development and pathology due to the protein's role as a cardiac regulator and effector of alpha1-adrenergic signaling . Advanced research applications include:

• Developmental expression profiling:

  • Employ immunohistochemistry with ZNF260 antibodies on embryonic heart sections at different developmental stages

  • Correlate ZNF260 expression patterns with cardiac chamber formation and maturation

  • Use dual immunofluorescence with cardiac progenitor markers to identify ZNF260's role in lineage commitment

• Pathological alterations in cardiac disease models:

  • Compare ZNF260 expression and localization in normal versus diseased heart tissues (hypertrophy, failure, ischemia)

  • Quantify expression changes using Western blot with normalization to appropriate loading controls

  • Assess potential alterations in post-translational modifications that may affect function

• Mechanistic investigations of alpha1-adrenergic signaling:

  • Use ZNF260 antibodies in chromatin immunoprecipitation (ChIP) assays to identify genomic binding sites

  • Combine with RNA-seq after alpha1-adrenergic stimulation to correlate binding with transcriptional changes

  • Perform co-immunoprecipitation to detect dynamic interactions with GATA4 and other cardiac transcription factors

• Cellular response to stress:

  • Monitor ZNF260 expression, localization, and post-translational modifications during hypoxia, oxidative stress, or mechanical strain

  • Correlate changes with activation of fetal gene programs characteristic of cardiac remodeling

• Therapeutic target validation:

  • Use immunoblotting to assess ZNF260 modulation in response to cardioprotective compounds

  • Evaluate ZNF260 as a potential biomarker for cardiac pathologies or treatment response

These approaches leverage ZNF260 antibodies to elucidate fundamental mechanisms in cardiac biology and pathophysiology, potentially identifying new therapeutic targets or diagnostic biomarkers .

What strategies can be employed to study ZNF260 interactions with GATA4 and other cardiac transcription factors?

ZNF260's function as a cofactor with GATA4 and other cardiac transcription factors provides a rich area for advanced investigation . Researchers can employ several sophisticated approaches:

• Co-immunoprecipitation (Co-IP) strategies:

  • Perform reciprocal Co-IPs using antibodies against ZNF260 and GATA4

  • Optimize lysis conditions to preserve nuclear protein complexes (typically using non-denaturing buffers)

  • Consider crosslinking approaches for transient interactions

  • Analyze precipitated complexes by Western blot or mass spectrometry to identify additional interaction partners

• Proximity ligation assays (PLA):

  • Utilize ZNF260 antibodies in combination with GATA4 antibodies for in situ PLA

  • This approach provides spatial resolution of interactions within specific subcellular compartments

  • Quantify interaction events in different cardiac cell types or under various physiological conditions

• Chromatin immunoprecipitation sequencing (ChIP-seq):

  • Perform parallel ChIP-seq with ZNF260 and GATA4 antibodies

  • Identify genomic regions co-occupied by both factors

  • Correlate binding with gene expression data to determine functional significance

  • Consider sequential ChIP (Re-ChIP) to definitively identify co-occupied regions

• Bimolecular fluorescence complementation (BiFC):

  • Generate fusion constructs of ZNF260 and potential partners with split fluorescent protein fragments

  • Visualize interactions through reconstitution of fluorescence when proteins interact

  • This approach allows visualization of interactions in living cells

• Domain mapping of interactions:

  • Use antibodies recognizing different epitopes of ZNF260 (e.g., AA 64-114, AA 89-115)

  • Perform Co-IP with truncated versions of ZNF260 to identify interaction domains

  • Design blocking peptides based on interaction surfaces to disrupt specific protein-protein interactions

• Functional assays of transcriptional synergy:

  • Employ reporter gene assays with promoters containing PERE elements and GATA binding sites

  • Assess transcriptional output with individual factors versus combinations

  • Use ZNF260 antibodies in chromatin immunoprecipitation to correlate occupancy with transcriptional activity

These methodologies provide complementary approaches to comprehensively characterize the functional interactions between ZNF260 and cardiac transcription factors at molecular, cellular, and genomic levels .

How do post-translational modifications affect ZNF260 antibody recognition and what techniques can detect these modifications?

Post-translational modifications (PTMs) of ZNF260 represent an important regulatory layer that can significantly impact antibody recognition and protein function. Advanced researchers should consider:

• Common PTMs affecting zinc finger proteins:

  • Phosphorylation: Often regulates DNA binding affinity and protein-protein interactions

  • SUMOylation: Frequently modifies nuclear transcription factors

  • Ubiquitination: Controls protein turnover and potentially signaling functions

  • Acetylation: May regulate DNA binding specificity and transcriptional activity

• Impact on antibody recognition:

  • Epitope masking: PTMs can sterically block antibody binding sites

  • Conformational changes: Modifications may alter protein folding, affecting antibody accessibility

  • Enhanced recognition: Some antibodies may preferentially recognize modified forms

• Detection strategies for ZNF260 PTMs:

  Modification	Detection Method	Technical Considerations
  Phosphorylation	Phospho-specific antibodies, Phos-tag gels	Phosphatase inhibitors essential during lysis; consider lambda phosphatase treatment as control
  SUMOylation	Co-IP under denaturing conditions with SUMO antibodies	NEM in lysis buffer to inhibit SUMO proteases
  Ubiquitination	IP under denaturing conditions followed by ubiquitin detection	Proteasome inhibitors (MG132) pre-treatment
  Acetylation	IP followed by acetyl-lysine antibody detection	Deacetylase inhibitors during sample preparation

• Modification-specific experimental approaches:

  • Use different ZNF260 antibodies recognizing distinct epitopes (e.g., AA 1-200, AA 64-114, AA 89-115)

  • Compare recognition patterns across different conditions known to induce specific PTMs

  • Employ mass spectrometry following immunoprecipitation to identify and map modifications

  • Create site-specific mutants to validate the identity and function of modified residues

• Functional implications assessment:

  • Correlate PTM status with DNA binding activity using ChIP

  • Assess protein-protein interactions in relation to modification state

  • Evaluate subcellular localization changes dependent on modification

Understanding the PTM landscape of ZNF260 provides insights into its regulation in different physiological and pathological contexts, potentially revealing new intervention points for cardiac conditions .

What considerations are important when designing multiplexed detection systems involving ZNF260 antibodies?

Multiplexed detection systems offer powerful insights into complex biological processes by simultaneously visualizing multiple targets. When incorporating ZNF260 antibodies into such systems, researchers should consider:

• Antibody compatibility factors:

  • Host species selection: Most ZNF260 antibodies are rabbit-derived, requiring careful planning when combining with other primary antibodies

  • Isotype considerations: ZNF260 antibodies are typically IgG, which influences secondary antibody selection

  • Available conjugates: ZNF260 antibodies come in various forms including unconjugated, FITC-conjugated, PE-conjugated, and HRP-conjugated versions

• Spectral separation strategies:

  • When using fluorescently-labeled ZNF260 antibodies (FITC, PE), ensure adequate spectral separation from other fluorophores

  • Consider brightness hierarchy, placing brightest fluorophores on least abundant targets

  • Use linear unmixing for closely overlapping spectra in advanced imaging systems

• Multiplexed immunohistochemistry approaches:

  • Sequential immunostaining with ZNF260 antibodies:

    • Perform complete staining with first antibody, including detection

    • Strip or inactivate first round reagents

    • Proceed with second antibody staining

  • Tyramide signal amplification (TSA) for sequential multi-color IHC using antibodies from the same host species

• Spatial considerations:

  • ZNF260's primarily nuclear localization facilitates co-staining with cytoplasmic or membrane markers

  • When combining with other nuclear transcription factors, high-resolution imaging may be necessary for colocalization analysis

  • Consider super-resolution microscopy for detailed nuclear colocalization studies

• Quantitative analysis planning:

  • Design appropriate controls for spectral bleed-through

  • Include single-stained controls for each fluorophore

  • Plan for quantitative colocalization analysis using appropriate software tools

  • Consider automated image analysis workflows for consistent quantification

• Cross-platform validation:

  • Validate multiplexed findings using complementary techniques (e.g., confirm imaging results with biochemical approaches)

  • Consider multi-omic approaches combining antibody-based detection with transcriptomic or proteomic analyses

These considerations ensure robust, artifact-free multiplexed detection involving ZNF260, enabling reliable investigation of its interactions, modifications, and functional relationships in complex biological systems .

What are common challenges when using ZNF260 antibodies in Western blot applications and how can they be addressed?

Researchers may encounter several challenges when using ZNF260 antibodies for Western blotting. Here are the common issues and their solutions:

• Weak or absent signal:

  • Increase antibody concentration within recommended ranges (1:500-1:2000)

  • Extend primary antibody incubation time to overnight at 4°C

  • Increase protein loading (50-100 μg total protein)

  • Enhance sensitivity with stronger detection reagents (e.g., femto-level ECL substrates)

  • Verify sample preparation - ensure adequate lysis of nuclear proteins using appropriate buffers

• High background or non-specific bands:

  • Decrease antibody concentration

  • Increase blocking time or concentration (5-10% milk or BSA)

  • Add 0.1-0.5% Tween-20 to antibody dilution buffer

  • Increase washing stringency (more washes, longer duration)

  • Consider alternative blocking agents (casein, commercial blockers)

  • Prepare fresh buffers to eliminate contamination

• Multiple bands:

  • Determine if bands represent splice variants, degradation products, or post-translational modifications

  • Run positive control samples with known expression

  • Consider peptide competition assays to identify specific bands

  • Use gradient gels for better resolution of closely migrating species

  • Verify with antibodies targeting different epitopes of ZNF260

• Inconsistent results between experiments:

  • Standardize lysate preparation protocols

  • Aliquot antibodies to avoid freeze-thaw cycles

  • Use consistent exposure times for acquisition

  • Include loading controls appropriate for nuclear proteins (e.g., Lamin B)

  • Develop standard curves with positive control lysates

• Antibody performance degradation over time:

  • Store antibodies in recommended conditions (-20°C)

  • Avoid repeated freeze-thaw cycles by preparing small working aliquots

  • Note lot-to-lot variations from manufacturers

  • Check expiration dates and storage conditions

By implementing these technical adjustments and quality control measures, researchers can optimize Western blot protocols for reliable and reproducible detection of ZNF260 protein .

How can researchers optimize immunofluorescence protocols for detecting ZNF260 in different cell types?

Optimizing immunofluorescence (IF) protocols for ZNF260 detection requires careful attention to fixation, permeabilization, and detection parameters:

• Fixation optimization:

  • Test multiple fixation methods:

    • 4% paraformaldehyde (10-15 minutes) - preserves structure but may mask some epitopes

    • Methanol (-20°C, 10 minutes) - better for some nuclear antigens but can distort membranes

    • Combined PFA/methanol - PFA followed by methanol permeabilization

  • Manufacturer recommends PFA fixation with Triton X-100 permeabilization

• Permeabilization strategies:

  • For nuclear transcription factors like ZNF260, permeabilization is critical

  • Test various permeabilization agents and concentrations:

    • 0.1-0.5% Triton X-100 (10 minutes)

    • 0.1-0.5% NP-40 (5-10 minutes)

    • 0.1-0.3% Saponin (15 minutes) - gentler but may require inclusion in all buffers

  • Optimize time and temperature for each cell type

• Cell type-specific considerations:

  • Adherent vs. suspension cells: Suspension cells may require cytospin or attachment to charged slides

  • Primary vs. immortalized cells: Primary cells often have lower expression, requiring signal amplification

  • Cardiac vs. non-cardiac cells: Expression levels vary significantly, requiring different antibody dilutions

• Antibody dilution and incubation optimization:

  • Test range of concentrations (0.25-2 μg/ml as recommended)

  • Optimize incubation time and temperature (1 hour at room temperature vs. overnight at 4°C)

  • Consider signal amplification methods for low expression:

    • Tyramide signal amplification

    • Biotin-streptavidin amplification

    • Sequential antibody layering

• Background reduction strategies:

  • Extended blocking (1-2 hours with 5-10% normal serum)

  • Add 0.1-0.3% Triton X-100 to antibody dilution buffer

  • Include 1% BSA in all antibody dilutions

  • Consider autofluorescence quenching for certain tissues:

    • Sodium borohydride treatment

    • Sudan Black B treatment

    • Commercial autofluorescence quenchers

• Counterstaining and mounting considerations:

  • DAPI or Hoechst for nuclear counterstaining

  • Phalloidin for F-actin visualization if studying cytoskeletal relationships

  • Use mounting media with anti-fade properties to prevent photobleaching

  • Consider hardset mounting media for long-term preservation

• Verification approaches:

  • Perform Z-stack imaging to confirm nuclear localization

  • Include positive controls (cardiac cell lines) and negative controls (primary antibody omission)

  • Consider co-staining with markers of nuclear compartments to precisely localize ZNF260

These optimizations allow detection of both the predominant nuclear ZNF260 population and any cytosolic fraction that may be present in certain cell types or conditions .

How can ZNF260 antibodies contribute to understanding transcriptional networks in cardiac development and disease?

ZNF260 antibodies offer valuable tools for dissecting complex transcriptional networks in cardiac biology:

• Genome-wide binding site identification:

  • ChIP-seq using validated ZNF260 antibodies can map all genomic binding sites

  • Integration with histone modification data reveals the epigenetic context of binding

  • Motif analysis of binding regions identifies potential co-regulatory factors

  • This approach has revealed ZNF260 binding to PE response elements (PERE) in promoters of cardiac genes like ANF/NPPA

• Dynamic regulatory complex assembly:

  • Sequential ChIP (Re-ChIP) with ZNF260 and GATA4 antibodies identifies co-occupied genomic regions

  • Temporal analysis during development or disease progression reveals dynamic assembly of regulatory complexes

  • Investigation of alpha1-adrenergic signaling pathways and their impact on ZNF260-mediated transcription

• Single-cell approaches:

  • Single-cell immunofluorescence with ZNF260 antibodies reveals heterogeneity in cardiac progenitor populations

  • Correlation with single-cell transcriptomics identifies cell state-specific functions

  • Spatial transcriptomics combined with ZNF260 immunostaining connects protein localization with local gene expression

• Protein interaction networks:

  • Proximity labeling approaches (BioID, APEX) combined with ZNF260 antibodies for validation

  • Construction of ZNF260-centered protein interaction networks in normal and diseased hearts

  • Integration with transcriptomic data to build comprehensive gene regulatory networks

• Clinical correlations and biomarker potential:

  • Quantitative analysis of ZNF260 expression in patient samples using validated antibodies

  • Correlation with cardiac disease progression and treatment response

  • Evaluation as a potential diagnostic or prognostic biomarker

These approaches collectively enable construction of comprehensive models of cardiac transcriptional regulation, with ZNF260 functioning as both an effector of alpha1-adrenergic signaling and a cofactor with key cardiac regulators like GATA4 .

What role might ZNF260 play in cardiac regeneration research and how can antibodies facilitate these investigations?

Cardiac regeneration represents a frontier in cardiovascular medicine, and ZNF260's function as a cardiac transcription factor positions it as a potential player in regenerative processes. ZNF260 antibodies can facilitate several innovative research approaches:

• Developmental cardiomyocyte proliferation studies:

  • Immunostaining for ZNF260 in combination with proliferation markers (Ki67, pH3, EdU) during cardiac development

  • Analysis of ZNF260 expression dynamics during the transition from proliferative to post-mitotic cardiomyocytes

  • Correlation with cell cycle regulators to identify potential regulatory relationships

• Reprogramming factor screening:

  • Assessment of ZNF260 expression during direct cardiac reprogramming of fibroblasts

  • Testing ZNF260 as a potential reprogramming factor alone or in combination with established factors

  • Antibody-based validation of successful reprogramming through monitoring nuclear localization patterns

• Injury response monitoring:

  • Temporal and spatial analysis of ZNF260 expression following cardiac injury in animal models

  • Co-localization studies with markers of activated cardiac progenitors

  • Correlation with regenerative capacity across species with different regenerative potentials

• Stem cell differentiation tracking:

  • Monitoring ZNF260 expression during cardiac differentiation of pluripotent stem cells

  • Identification of ZNF260-expressing subpopulations with enhanced cardiogenic potential

  • Assessment of ZNF260's role in cardiac subtype specification (ventricular, atrial, nodal)

• Therapeutic manipulation assessment:

  • Evaluation of ZNF260 modulation following administration of pro-regenerative compounds

  • Correlation of ZNF260 activity with functional recovery in cardiac injury models

  • Antibody-based screening assays for compounds that modulate ZNF260 expression or activity

• Mechanistic investigations:

  • ChIP-seq in regenerating cardiac tissue to identify regeneration-specific ZNF260 target genes

  • Analysis of ZNF260 post-translational modifications during regenerative processes

  • Investigation of ZNF260's interaction with the Hippo pathway and other known regulators of cardiac regeneration

These research directions leverage ZNF260 antibodies to explore the protein's potential roles in cardiac regeneration, potentially identifying new therapeutic targets or approaches for heart disease .