Crotonyl-HIST1H2AG (K118) Antibody

What is Crotonyl-HIST1H2AG (K118) Antibody and what does it detect?

Crotonyl-HIST1H2AG (K118) Antibody is a polyclonal antibody raised in rabbits that specifically recognizes the crotonylation modification at lysine 118 (K118) of the histone H2A type 1 protein (HIST1H2AG). This antibody detects a specific post-translational modification that involves the addition of a crotonyl group to the ε-amino group of lysine 118 in histone H2A .

Histone H2A functions as a core component of nucleosomes, which wrap and compact DNA into chromatin. This compaction limits DNA accessibility to cellular machineries that require DNA as a template for various processes. Histone modifications like crotonylation play central roles in regulating transcription, DNA repair, DNA replication, and maintaining chromosomal stability .

The specificity of this antibody is crucial as it allows researchers to distinguish crotonylation from other acyl modifications that may occur at the same lysine residue, such as acetylation or other short-chain acylations. The antibody is generated using a peptide sequence surrounding the crotonylated lysine 118 site derived from human histone H2A type 1 .

How does histone crotonylation differ from histone acetylation?

Histone crotonylation and acetylation are both acyl modifications of lysine residues in histone proteins, but they differ in several important aspects:

• Chemical Structure: Crotonylation involves the addition of a crotonyl group (C₄H₅O), which contains an α,β-unsaturated bond, making it larger and more hydrophobic than the acetyl group (C₂H₃O) involved in acetylation.

• Transcriptional Impact: Research has demonstrated that p300-catalyzed histone crotonylation directly stimulates transcription to a greater degree than histone acetylation . This suggests that crotonylation may have more potent effects on gene expression regulation.

• Metabolic Regulation: Levels of histone crotonylation are regulated by the cellular concentration of crotonyl-CoA, which can fluctuate based on genetic and environmental factors. This creates a direct link between cellular metabolism and gene expression that may be distinct from acetylation pathways .

• Enzyme Specificity: While many enzymes that catalyze acetylation (such as p300/CBP) can also catalyze crotonylation, the efficiency and regulation of these activities may differ. Similarly, deacetylases like SIRT1 can also remove crotonyl groups, though potentially with different kinetics .

• Functional Consequences: Crotonylation appears to have specific roles in cellular processes like replication stress response that may be distinct from acetylation. For example, the dynamic switching between crotonylation and ubiquitination at H2A lysine 119 has been implicated in managing transcription-replication conflicts .

What are the primary applications for Crotonyl-HIST1H2AG (K118) Antibody in epigenetic research?

The Crotonyl-HIST1H2AG (K118) Antibody serves multiple critical applications in epigenetic research:

• Western Blotting (WB): This antibody can be used at dilutions of 1:200-1:2000 to detect crotonylated H2A in protein extracts, allowing researchers to quantify global changes in H2A K118 crotonylation across different experimental conditions .

• Immunocytochemistry (ICC): At dilutions of 1:20-1:200, this antibody enables visualization of the subcellular localization of crotonylated H2A K118 within fixed cells .

• Immunofluorescence (IF): Using dilutions of 1:50-1:200, researchers can examine the spatial distribution of crotonylated H2A K118 within cells or tissues, often in combination with other markers .

• Chromatin Immunoprecipitation (ChIP): This application allows researchers to identify genomic regions associated with crotonylated H2A K118, providing insights into how this modification influences gene expression and chromatin structure. When combined with sequencing (ChIP-seq), it enables genome-wide profiling of crotonylation patterns .

• ELISA: At dilutions of 1:2000-1:10000, the antibody can be employed in enzyme-linked immunosorbent assays to quantitatively measure crotonylation levels in extracted histones .

These applications collectively enable researchers to investigate how crotonylation at H2A K118 responds to various stimuli, correlates with transcriptional states, and interacts with other epigenetic modifications in different biological contexts.

How do histone crotonylation patterns change in response to cellular stress?

Histone crotonylation patterns undergo dynamic changes in response to various forms of cellular stress, particularly replication stress. Research findings indicate several important aspects of this relationship:

• Replication Stress Response: Crotonylation of histone H2A at lysine residues (such as K119, which is adjacent to the K118 site recognized by this antibody) is reversibly regulated by replication stress. This suggests that crotonylation marks serve as responsive elements within the cellular stress management system .

• Metabolic Fluctuations: Since histone crotonylation levels are regulated by the cellular concentration of crotonyl-CoA, metabolic stress that affects the availability of this metabolite can directly impact crotonylation patterns. This creates a direct coupling between cellular metabolism and the epigenetic landscape .

• Transcription-Replication Conflicts: During replication stress, the dynamic switching between crotonylation and other modifications (particularly ubiquitination) helps resolve conflicts between transcription and replication machineries. For instance, decrotonylation of H2AK119 by SIRT1 is a prerequisite for subsequent ubiquitination by BMI1, which then helps attenuate transcription-replication conflicts .

• DNA Damage Response: Research suggests that histone crotonylation is involved in the DNA damage response pathway. HDAC-regulated histone crotonylation is reduced after DNA damage, indicating that changes in crotonylation may be part of the cellular response to genomic insults .

Understanding these stress-responsive patterns has significant implications for research into cancer, aging, and other conditions characterized by disrupted epigenetic regulation.

What experimental design considerations are crucial when using Crotonyl-HIST1H2AG (K118) Antibody for ChIP experiments?

When designing ChIP experiments using the Crotonyl-HIST1H2AG (K118) Antibody, researchers should consider these critical factors:

• Cross-linking Optimization: The standard 1% formaldehyde cross-linking protocol may need adjustment for optimal detection of crotonylation marks. Researchers should consider testing different cross-linking times (typically 5-15 minutes) to balance between sufficient cross-linking and preservation of epitope accessibility.

• Sonication Parameters: Chromatin shearing conditions should be carefully optimized to generate fragments of 200-500 bp for high-resolution mapping of crotonylation sites. Oversonication can damage epitopes, while insufficient sonication may reduce immunoprecipitation efficiency.

• Antibody Validation: Prior to full ChIP experiments, validation of the antibody's specificity is essential. This can be achieved through peptide competition assays using crotonylated and non-crotonylated peptides, or by testing the antibody on samples with genetically or chemically manipulated crotonylation levels .

• Controls: Several controls are essential:

  • Input chromatin (pre-immunoprecipitation sample)

  • IgG negative control (non-specific antibody of the same isotype)

  • Positive control using antibodies against well-characterized histone marks

  • Spike-in normalization controls for quantitative comparisons between conditions

• Sequential ChIP Considerations: For investigating the co-occurrence of H2A K118 crotonylation with other histone modifications, sequential ChIP (re-ChIP) protocols need careful optimization to ensure epitope preservation throughout multiple immunoprecipitation steps.

• Enzymatic Modulation: Consider including experimental conditions that modify crotonylation levels, such as SIRT1 inhibition or activation, to provide functional validation of the ChIP results .

These considerations help ensure that ChIP experiments yield reliable, reproducible data on the genomic distribution of H2A K118 crotonylation and its relationship to transcriptional regulation.

How can researchers distinguish between crotonylation-specific effects and other histone modifications?

Distinguishing between crotonylation-specific effects and those caused by other histone modifications requires a multi-faceted approach:

• Antibody Specificity Validation: Conducting peptide competition assays with various modified peptides (acetylated, crotonylated, etc.) can confirm that the Crotonyl-HIST1H2AG (K118) Antibody specifically recognizes the crotonyl modification without cross-reactivity to acetylation or other acyl modifications .

• Mass Spectrometry Analysis: High-resolution mass spectrometry can definitively identify and quantify different acyl modifications at specific lysine residues. This technique can distinguish crotonylation from acetylation, butyrylation, and other modifications based on their unique mass signatures and fragmentation patterns.

• Metabolic Manipulation: Altering cellular levels of crotonyl-CoA (the donor for crotonylation) without affecting acetyl-CoA can help isolate crotonylation-specific effects. This can be achieved through the addition of crotonate to cell culture medium or manipulation of enzymes like CDYL, which acts as a crotonyl-CoA hydratase .

• Enzyme Specificity Experiments: Using deacetylases/decrotonylases with different specificities (e.g., SIRT1 has decrotonylase activity) can help separate the effects of different modifications. Selective inhibition or genetic manipulation of these enzymes can reveal modification-specific phenotypes .

• Site-Specific Mutagenesis: Generating histone mutants where specific lysine residues are replaced with arginine (K→R) can eliminate the possibility of any acyl modification at that site. Comparing these mutants with wild-type histones can isolate the effects of modifications at specific residues.

• Temporal Dynamics Analysis: Monitoring the timing of changes in different modifications following stimuli can help distinguish their specific roles. For example, the dynamic switching between crotonylation and ubiquitination at H2AK119 during replication stress suggests distinct temporal functions .

By combining these approaches, researchers can effectively differentiate between the biological effects specifically attributable to crotonylation versus other histone modifications.

What strategies can optimize signal-to-noise ratio in Crotonyl-HIST1H2AG (K118) Antibody experiments?

Optimizing signal-to-noise ratio when working with Crotonyl-HIST1H2AG (K118) Antibody requires careful attention to several experimental parameters:

• Antibody Titration: Determining the optimal antibody concentration is crucial. While the manufacturer recommends dilutions of 1:50-1:200 for IF applications and 1:200-1:2000 for WB , researchers should perform titration experiments to find the concentration that maximizes specific signal while minimizing background for their particular experimental system.

• Blocking Optimization: Testing different blocking agents (BSA, non-fat dry milk, normal serum) at various concentrations can significantly improve signal-to-noise ratio. For crotonylation detection, BSA is often preferred as milk can contain enzymes that might affect acyl modifications.

• Antigen Retrieval Methods: For immunohistochemistry or immunofluorescence applications, optimizing antigen retrieval conditions (buffer composition, pH, temperature, and duration) can dramatically improve epitope accessibility while preserving tissue morphology.

• Washing Stringency: Adjusting the stringency of washing steps by modifying salt concentration or detergent levels in wash buffers can help reduce non-specific binding. For the Crotonyl-HIST1H2AG (K118) Antibody, incremental increases in washing stringency should be tested to determine optimal conditions.

• Signal Amplification: For weak signals, consider using signal amplification systems such as tyramide signal amplification (TSA) or polymer-based detection methods, particularly for tissues with naturally low levels of crotonylation.

• Cross-Adsorption: If background issues persist, consider pre-adsorbing the antibody with non-specific proteins or tissue homogenates to remove antibodies that might contribute to background.

• Fixation Optimization: The choice and duration of fixation can significantly impact epitope preservation. For crotonylation marks, overfixation can mask epitopes, while underfixation may lead to poor morphology. Researchers should test multiple fixation protocols to optimize for their specific sample type.

By systematically optimizing these parameters, researchers can significantly improve the signal-to-noise ratio in experiments using the Crotonyl-HIST1H2AG (K118) Antibody, leading to more reliable and interpretable results.

How should ChIP-seq data for H2A K118 crotonylation be analyzed in relation to transcriptional activity?

Analysis of ChIP-seq data for H2A K118 crotonylation in relation to transcriptional activity requires a comprehensive analytical framework:

• Peak Calling and Annotation: After standard quality control and alignment of sequencing reads, peaks representing enrichment of H2A K118 crotonylation should be identified using appropriate peak-calling algorithms. These peaks should then be annotated relative to genomic features (promoters, enhancers, gene bodies, etc.) to determine their distribution pattern.

• Integration with Transcriptome Data: Crotonylation ChIP-seq data should be integrated with RNA-seq or other transcriptome data to correlate crotonylation patterns with gene expression levels. Research indicates that p300-catalyzed histone crotonylation stimulates transcription to a greater degree than histone acetylation , suggesting that genes with high K118 crotonylation might show particularly robust expression.

• Motif Analysis: Analyzing DNA sequence motifs enriched within crotonylation peaks can identify potential transcription factors that might be associated with crotonylation-dependent transcriptional regulation.

• Comparison with Other Histone Modifications: Comparing H2A K118 crotonylation patterns with datasets for other histone modifications (acetylation, methylation, ubiquitination) can reveal relationships between these marks. Of particular interest is the relationship between crotonylation and ubiquitination, as research has shown dynamic switching between these modifications at specific lysine residues like K119 .

• Differential Binding Analysis: For experiments comparing different conditions (e.g., normal vs. replication stress), differential binding analysis should be performed to identify regions with significant changes in crotonylation. These regions can then be analyzed for common features or enriched pathways.

• Correlation with Chromatin States: Integrating crotonylation data with chromatin accessibility data (ATAC-seq, DNase-seq) and histone modification patterns can help classify chromatin states and determine how crotonylation contributes to different functional chromatin domains.

• Visualization and Interpretation: Creating composite plots showing crotonylation enrichment around transcription start sites, stratified by gene expression levels, can reveal relationships between crotonylation positioning and transcriptional output.

This analytical framework enables researchers to comprehensively understand how H2A K118 crotonylation relates to transcriptional regulation and influences genome function.

What is the relationship between histone crotonylation and cellular metabolism?

The relationship between histone crotonylation and cellular metabolism represents a critical intersection of epigenetics and metabolic regulation:

• Crotonyl-CoA as a Metabolic Sensor: Levels of histone crotonylation are directly regulated by the cellular concentration of crotonyl-CoA, which serves as the donor for the crotonyl group. This creates a direct link whereby changes in cellular metabolism that affect crotonyl-CoA levels can impact the epigenome .

• Transcriptional Amplification: Research has demonstrated that increasing or decreasing the cellular concentration of crotonyl-CoA leads to enhanced or diminished gene expression, respectively. These changes correlate with the levels of histone crotonylation flanking the regulatory elements of activated genes, suggesting that crotonylation serves as a metabolic-epigenetic amplifier of transcription .

• Enzymatic Regulation: The enzymes that regulate crotonylation levels respond to metabolic cues. For instance, sirtuin deacetylases like SIRT1, which can remove crotonyl groups, are NAD⁺-dependent enzymes whose activity is influenced by the cellular redox state and energy levels .

• Metabolic Pathway Integration: Crotonyl-CoA is an intermediate in various metabolic pathways, including fatty acid oxidation and certain amino acid metabolism pathways. Changes in these metabolic routes due to nutritional status, stress, or disease can alter crotonyl-CoA availability and subsequently affect histone crotonylation patterns.

• Stress Response Mechanism: The dynamic regulation of histone crotonylation in response to cellular stresses, particularly replication stress, suggests that this modification serves as a responsive element within the cellular stress management system that integrates metabolic status with chromatin regulation .

This metabolic-epigenetic connection through crotonylation provides a mechanism by which cells can adjust gene expression patterns in response to changing metabolic conditions, potentially influencing diverse processes from development to disease progression.

How does crotonylation at K118 interact with other histone modifications in response to replication stress?

The interaction between crotonylation at K118 and other histone modifications during replication stress reveals complex regulatory dynamics:

• Crotonylation-Ubiquitination Switching: Research on the adjacent K119 residue has shown that crotonylation and ubiquitination at this site are reversibly regulated during replication stress. This finding suggests that K118 crotonylation may participate in similar regulatory dynamics, as these residues are in close proximity and their modifications would likely influence each other .

• SIRT1-Mediated Regulation: Decrotonylation by SIRT1 has been identified as a prerequisite for subsequent ubiquitination in the case of K119. This suggests a sequential modification process where removal of the crotonyl group by SIRT1 is necessary before other modifications can be added. Similar processes may occur at K118 .

• Chromatin Compaction Effects: The presence or absence of crotonylation at K118 likely affects chromatin structure and accessibility. During replication stress, changes in crotonylation patterns may contribute to local chromatin remodeling that facilitates DNA repair processes or prevents further damage.

• Transcriptional Regulation: The accumulation of ubiquitinated H2A at K119 near stalled replication forks leads to the release of RNA Polymerase II and transcription repression in these regions. This helps attenuate transcription-replication conflicts. Crotonylation at K118 may play a complementary or opposing role in this regulatory process .

• R-loop Regulation: Replication stress-induced changes in histone modifications, including crotonylation, affect R-loop formation. The crotonylation status at K118 may influence how the cell manages R-loops, which are important structures in both normal cellular processes and pathological conditions .

• Recruitment of Specific Factors: Different histone modifications recruit specific proteins or complexes. Changes in the crotonylation status at K118 during replication stress likely alter the protein interaction landscape at these chromatin regions, facilitating the recruitment of factors involved in resolving replication stress.

Understanding these complex interactions between K118 crotonylation and other modifications provides insights into how cells coordinate chromatin-based responses to replication stress and maintain genome stability.

What are common pitfalls when using Crotonyl-HIST1H2AG (K118) Antibody and how can they be addressed?

Researchers using Crotonyl-HIST1H2AG (K118) Antibody may encounter several common challenges that can be addressed with specific strategies:

• High Background Signal:

  • Cause: Insufficient blocking or non-specific antibody binding.

  • Solution: Increase blocking time and concentration (recommended: 5% BSA for 1-2 hours), optimize antibody dilution (starting with manufacturer's recommendation of 1:200-1:2000 for WB) , and increase washing duration and stringency.

• Weak or No Signal:

  • Cause: Low abundance of the modification, epitope masking during fixation, or antibody degradation.

  • Solution: Enrich for histones using acid extraction methods, optimize fixation protocols to preserve epitopes, and ensure proper antibody storage at -20°C or -80°C as recommended .

• Non-specific Bands in Western Blot:

  • Cause: Cross-reactivity with other crotonylated proteins or partially degraded histones.

  • Solution: Perform peptide competition assays to confirm specificity, use higher antibody dilutions, and optimize protein extraction and electrophoresis conditions to minimize histone degradation.

• Variability Between Experiments:

  • Cause: Inconsistent sample preparation or differences in crotonylation levels due to metabolic fluctuations.

  • Solution: Standardize sample collection and processing protocols, consider normalizing results to total H2A levels, and maintain consistent cell culture conditions to minimize metabolic variations that affect crotonyl-CoA levels .

• Poor ChIP Efficiency:

  • Cause: Suboptimal cross-linking, inefficient chromatin shearing, or epitope inaccessibility.

  • Solution: Optimize cross-linking time for histone modifications (typically 10-15 minutes), adjust sonication parameters to achieve 200-500 bp fragments, and consider using epitope retrieval steps before immunoprecipitation.

• Inconsistent Results in Cells Under Stress:

  • Cause: Dynamic nature of crotonylation in response to cellular stress, particularly replication stress .

  • Solution: Carefully control and synchronize stress induction, consider time-course experiments to capture dynamic changes, and use SIRT1 inhibitors to stabilize crotonylation marks when needed .

• Difficulty Distinguishing from Other Acyl Modifications:

  • Cause: Structural similarities between different acyl modifications.

  • Solution: Include appropriate controls with known acetylation or other acylation patterns, consider parallel experiments with acetylation-specific antibodies, and validate key findings with mass spectrometry.

By anticipating these potential issues and implementing the suggested solutions, researchers can significantly improve the reliability and interpretability of experiments using the Crotonyl-HIST1H2AG (K118) Antibody.

How can researchers validate the specificity of Crotonyl-HIST1H2AG (K118) Antibody?

Validating the specificity of Crotonyl-HIST1H2AG (K118) Antibody is crucial for ensuring reliable experimental results. Researchers should consider implementing the following comprehensive validation strategies:

• Peptide Competition Assays: Perform pre-absorption experiments using the immunizing crotonylated peptide versus non-crotonylated peptide and peptides with other acyl modifications (acetylation, butyrylation) at the same site. A specific antibody will show signal elimination only with the crotonylated peptide.

• Modification Enzyme Manipulation: Test the antibody on samples from cells where enzymes affecting crotonylation have been manipulated:

  • SIRT1 knockdown or inhibition should increase crotonylation signals due to its decrotonylase activity

  • p300/CBP knockdown should decrease crotonylation signals as these are major crotonyltransferases

  • These changes should be detectable with the antibody if it is truly specific for crotonylation

• Metabolic Manipulation: Treat cells with crotonate to increase cellular crotonyl-CoA levels and enhance crotonylation, or manipulate pathways that affect crotonyl-CoA availability. The antibody should detect corresponding changes in crotonylation levels .

• Western Blot Analysis: Perform western blots on acid-extracted histones from various cell types or tissues. A specific crotonylation antibody should detect a single band at the expected molecular weight of H2A (~14 kDa), which changes in intensity under conditions known to affect crotonylation.

• Mass Spectrometry Correlation: Correlate antibody-based detection results with mass spectrometry analysis of histone post-translational modifications. This gold-standard approach can confirm the presence and abundance of crotonylation specifically at K118.

• Knockout/Knockin Validation: Test the antibody on samples from cells expressing a K118R mutant of H2A, which cannot be crotonylated at position 118. The antibody should show no signal in these samples if it is specific for K118 crotonylation.

• Cross-Reactivity Assessment: Test the antibody against related histone variants and modifications, particularly K118 crotonylation on other H2A variants and crotonylation at different lysine residues (such as K119), to determine its selectivity.

These validation steps provide complementary evidence for antibody specificity and should ideally be performed before using the Crotonyl-HIST1H2AG (K118) Antibody in major experimental projects.

What emerging applications of Crotonyl-HIST1H2AG (K118) Antibody show promise for epigenetic research?

Several emerging applications of Crotonyl-HIST1H2AG (K118) Antibody show significant promise for advancing epigenetic research:

• Single-Cell Epigenomics: Adapting ChIP protocols for use with the Crotonyl-HIST1H2AG (K118) Antibody in single-cell technologies could reveal cell-to-cell variation in crotonylation patterns, providing insights into epigenetic heterogeneity within tissues and during development.

• Live-Cell Imaging: Developing cell-permeable antibody derivatives or nanobodies specific for H2A K118 crotonylation could enable real-time visualization of crotonylation dynamics in living cells, particularly during stress responses or cell cycle progression.

• Combination with Genome Editing Technologies: Using CRISPR-Cas9 systems in conjunction with the antibody could help establish causal relationships between site-specific crotonylation and gene expression. For example, recruiting crotonyltransferases to specific loci and then using the antibody to confirm successful modification.

• Therapeutic Target Identification: The antibody could be used to screen for compounds that modulate crotonylation levels, potentially identifying novel epigenetic drugs for conditions where crotonylation is dysregulated.

• Replication Stress Response Mechanisms: Building on findings about the role of crotonylation in managing transcription-replication conflicts , the antibody could be used to map genome-wide changes in crotonylation patterns during replication stress, potentially revealing mechanisms of genome protection.

• Metabolic-Epigenetic Interface Studies: The antibody could be used to investigate how various metabolic perturbations affect the distribution of H2A K118 crotonylation, furthering our understanding of how metabolism influences gene expression through epigenetic mechanisms .

• Multi-Omics Integration: Combining ChIP-seq using the Crotonyl-HIST1H2AG (K118) Antibody with other omics approaches (RNA-seq, metabolomics, proteomics) could provide comprehensive views of how crotonylation connects to broader cellular regulatory networks.

These emerging applications highlight the potential of the Crotonyl-HIST1H2AG (K118) Antibody to contribute to our understanding of fundamental biological processes and potentially inform therapeutic strategies for diseases involving epigenetic dysregulation.

How might the study of H2A K118 crotonylation contribute to understanding disease mechanisms?

The study of H2A K118 crotonylation using specific antibodies may contribute significantly to understanding disease mechanisms through several pathways:

• Cancer Epigenetics: Altered histone crotonylation patterns may contribute to oncogenesis through dysregulated gene expression. Studies have shown that p300-catalyzed histone crotonylation stimulates transcription to a greater degree than acetylation , suggesting that aberrant crotonylation could lead to inappropriate activation of oncogenes. The Crotonyl-HIST1H2AG (K118) Antibody could help map these changes in various cancer types.

• Genomic Instability Disorders: Given the role of histone crotonylation in managing transcription-replication conflicts and protecting genome stability , abnormal crotonylation patterns may contribute to conditions characterized by genomic instability. These include cancer predisposition syndromes, neurodegenerative disorders, and premature aging syndromes.

• Metabolic Disorders: Since crotonylation levels are regulated by crotonyl-CoA availability , metabolic conditions that affect fatty acid metabolism or related pathways may influence histone crotonylation patterns, potentially contributing to disease phenotypes through altered gene expression.

• Inflammatory and Stress-Related Conditions: Cellular stress responses, including inflammation, oxidative stress, and replication stress, involve changes in histone modifications. Dysregulation of the dynamic switching between crotonylation and other modifications like ubiquitination may contribute to inflammatory diseases and stress-related pathologies.

• Developmental Disorders: If crotonylation plays critical roles during development through regulation of gene expression programs, abnormal crotonylation patterns could contribute to developmental disorders. The antibody could help investigate this connection by mapping crotonylation changes during normal and abnormal development.

• Neurodegenerative Diseases: Neurons are particularly sensitive to transcription-replication conflicts and genomic instability. Since crotonylation helps manage these conflicts , dysregulated crotonylation might contribute to neurodegenerative processes.

• Drug Resistance Mechanisms: Changes in histone crotonylation may contribute to adaptive responses in cancer cells that lead to therapy resistance. Studying these changes with the antibody could reveal epigenetic mechanisms of resistance and suggest combination therapy approaches.

By enabling detailed studies of H2A K118 crotonylation in diverse disease contexts, the Crotonyl-HIST1H2AG (K118) Antibody may contribute to identifying novel therapeutic targets and biomarkers for conditions involving epigenetic dysregulation.