β-hydroxybutyryl-HIST1H2AG (K36) Antibody

What is β-hydroxybutyryl-HIST1H2AG (K36) Antibody and what epitope does it target?

β-hydroxybutyryl-HIST1H2AG (K36) Antibody is a polyclonal antibody that specifically recognizes the β-hydroxybutyrylation post-translational modification at lysine 36 of Histone H2A type 1. This antibody has been generated using a peptide sequence surrounding the β-hydroxybutyryl-Lys (36) derived from Human Histone H2A type 1 as the immunogen . The antibody targets a specific histone mark that is part of the emerging landscape of histone lysine acylations, which play crucial roles in epigenetic regulation.

How does β-hydroxybutyrylation differ from other histone post-translational modifications?

β-hydroxybutyrylation (Kbhb) is a relatively newly identified histone post-translational modification that differs from other acylations like acetylation in both structure and function. Unlike acetylation, β-hydroxybutyrylation is specifically induced by β-hydroxybutyrate (BHB), a ketone body that increases during fasting or diabetic ketoacidosis . While acetylation shows minimal changes during metabolic stress, histone Kbhb levels are dramatically elevated in response to increased β-hydroxybutyrate concentrations . Structurally, β-hydroxybutyrylation adds a larger, hydroxylated acyl group to the lysine residue, which may create distinct protein-protein interaction interfaces compared to acetylation or methylation.

What are the validated applications for β-hydroxybutyryl-HIST1H2AG (K36) Antibody?

The β-hydroxybutyryl-HIST1H2AG (K36) Polyclonal Antibody has been validated for enzyme-linked immunosorbent assay (ELISA) and Western blotting (WB) . These applications enable researchers to detect and quantify the presence of β-hydroxybutyrylated histones in various experimental settings, including cell culture systems and tissue samples from animal models. The antibody specificity allows for the monitoring of this modification under different physiological and pathological conditions.

How should researchers design experiments to study the dynamic changes in histone β-hydroxybutyrylation?

To effectively study dynamic changes in histone β-hydroxybutyrylation, researchers should consider a multi-tiered experimental approach. First, establish baseline levels in your model system, then implement metabolic interventions known to affect β-hydroxybutyrate levels, such as:

• Treating cultured cells with sodium β-hydroxybutyrate at various concentrations (e.g., 1-20 mM) for 24 hours

• Subjecting animal models to fasting protocols (typically 24-48 hours for mice)

• Utilizing diabetic models such as streptozotocin (STZ)-induced Type 1 diabetes in mice

Time-course experiments are crucial for capturing the dynamic nature of these modifications. Additionally, researchers should measure blood β-hydroxybutyrate levels concurrently with histone modifications to establish correlations. For comprehensive analysis, combine Western blotting with site-specific antibodies, mass spectrometry, and ChIP-seq to map genomic distribution patterns of the modification .

What are the optimal sample preparation methods to preserve β-hydroxybutyrylation for antibody detection?

For optimal preservation of histone β-hydroxybutyrylation, implement these critical steps in your sample preparation protocol:

• Harvest cells or tissues rapidly to minimize post-collection enzymatic activities

• Include deacetylase inhibitors (e.g., trichostatin A) and β-hydroxybutyrylation deacylase inhibitors in lysis buffers

• Perform histone extraction using acid extraction methods (typically with 0.2N HCl) followed by TCA precipitation

• Store extracted histones at -80°C and avoid repeated freeze-thaw cycles

For tissue samples, flash-freezing in liquid nitrogen immediately after collection is essential. When preparing samples for Western blotting, use freshly prepared loading buffers and avoid excessive heating, which may affect the stability of the modification. For immunoprecipitation experiments, crosslinking conditions should be optimized to preserve the epitope recognized by the antibody .

How can researchers validate the specificity of β-hydroxybutyryl-HIST1H2AG (K36) Antibody in their experimental system?

To rigorously validate the specificity of β-hydroxybutyryl-HIST1H2AG (K36) Antibody in your experimental system, implement these approaches:

• Peptide competition assay: Pre-incubate the antibody with excess β-hydroxybutyrylated peptide (the immunogen) before immunoblotting to demonstrate signal reduction

• Parallel testing with other site-specific antibodies: Compare detection patterns with antibodies against other modifications at the same residue (e.g., H2A K36 acetylation)

• Metabolic labeling: Treat cells with isotopically labeled β-hydroxybutyrate (e.g., 13C-labeled) followed by mass spectrometry to confirm the modification site corresponds to antibody reactivity

• CRISPR-Cas9 mutagenesis: Generate K36R mutants of HIST1H2AG to create a negative control lacking the modifiable residue

• Dose-dependent induction: Verify that antibody signal increases proportionally with β-hydroxybutyrate treatment concentration

This multi-faceted validation approach ensures confidence in antibody specificity and experimental results interpretation.

How can ChIP-seq be optimized for β-hydroxybutyryl-HIST1H2AG (K36) to map genome-wide distribution patterns?

Optimizing ChIP-seq for β-hydroxybutyryl-HIST1H2AG (K36) requires several specialized considerations:

• Crosslinking optimization: Test multiple formaldehyde concentrations (0.5-2%) and incubation times (5-20 minutes) to preserve the modification while ensuring efficient DNA fragmentation

• Sonication parameters: Use gentler sonication conditions compared to standard ChIP protocols to prevent epitope damage

• Antibody titration: Conduct preliminary ChIP-qPCR using different antibody amounts to determine optimal concentration for specificity and sensitivity

• Include spike-in controls: Use exogenous chromatin (e.g., Drosophila) as normalization controls, particularly when comparing samples with varying global modification levels

• Sequential ChIP: Consider sequential ChIP with other histone mark antibodies to identify genomic regions with co-occurring modifications

Based on previous studies, histone Kbhb marks are enriched at promoters of active genes, particularly those involved in starvation-responsive metabolic pathways . Therefore, focus initial validation on known metabolic genes regulated during fasting or ketosis.

What methodological approaches can be used to study the interplay between β-hydroxybutyrylation and other histone modifications?

To investigate the complex interplay between β-hydroxybutyrylation and other histone modifications, implement these methodological approaches:

• Mass spectrometry-based proteomics:

  • Use middle-down MS approaches to analyze co-occurring modifications on the same histone tail

  • Apply top-down proteomics to analyze intact histone proteoforms with multiple modifications

  • Implement crosslinking mass spectrometry to identify protein complexes associated with multiply-modified histones

• Advanced microscopy techniques:

  • Apply proximity ligation assays to detect co-occurrence of different modifications at the single-cell level

  • Use super-resolution microscopy to visualize spatial relationships between different modifications

• Combinatorial biochemical approaches:

  • Perform sequential ChIP (re-ChIP) to identify genomic regions with co-occurring modifications

  • Use synthetic histone peptides with defined modification patterns in protein binding assays

• Genetic and chemical manipulation:

  • Employ CRISPR-based approaches to mutate specific lysine residues

  • Use selective inhibitors of histone-modifying enzymes to perturb specific modifications

These approaches will help decipher whether β-hydroxybutyrylation works cooperatively or competitively with other modifications in regulating gene expression.

How can researchers distinguish between the effects of different acylation types (acetylation vs. β-hydroxybutyrylation) at the same lysine residue?

Distinguishing between different acylation types at the same lysine residue requires sophisticated analytical approaches:

• Modification-specific antibodies: Use highly specific antibodies that can differentiate between acetylation and β-hydroxybutyrylation at the same residue, validating with peptide competition assays

• Mass spectrometry approaches:

  • Employ diagnostic fragment ions in MS/MS spectra that differentiate between acyl modifications

  • Use chemical derivatization strategies that selectively react with specific acyl groups

  • Apply targeted multiple reaction monitoring (MRM) to quantify specific modified peptides

• Metabolic manipulation experiments:

  • Compare cells treated with β-hydroxybutyrate versus acetate to promote specific modifications

  • Use isotopically labeled acyl-CoA precursors to trace the incorporation of specific modifications

• Enzyme selectivity assays:

  • Test the substrate specificity of writers (acetyltransferases vs. β-hydroxybutyryltransferases)

  • Examine deacylase specificity using in vitro enzymatic assays with synthetic peptides

  • Compare the activities of HDAC1-3 and SIRT1-3, which have been identified as enzymes capable of removing β-hydroxybutyryl groups

This systematic approach helps delineate the distinct functional consequences of different acylation types at the same residue.

How does metabolic state influence histone β-hydroxybutyrylation patterns and what are the implications for experimental design?

Metabolic state profoundly influences histone β-hydroxybutyrylation patterns, which has significant implications for experimental design:

• Fasting-induced changes:

  • Prolonged fasting (24-48 hours) in mice increases blood β-hydroxybutyrate levels by approximately 10-fold compared to fed states

  • This leads to dramatically elevated histone Kbhb levels in tissues, particularly liver, while histone acetylation shows minimal changes

• Diabetic ketoacidosis effects:

  • Streptozotocin (STZ)-induced Type 1 diabetes models show approximately 10-fold elevation in blood β-hydroxybutyrate and 2.4-fold elevation in blood glucose

  • This metabolic state is associated with significant increases in histone Kbhb levels

• Experimental design considerations:

  • Control for feeding/fasting status and time of day when collecting samples

  • Monitor blood β-hydroxybutyrate levels concurrently with histone modification analysis

  • Consider the tissue-specific responses to metabolic changes (liver shows pronounced effects)

  • Include both short-term and long-term metabolic interventions to distinguish acute versus chronic effects

• Functional implications:

  • Histone Kbhb marks are enriched at promoters of genes involved in starvation-responsive metabolic pathways

  • The modification may serve as a direct link between metabolic state and transcriptional adaptation

Understanding these metabolic influences is essential for designing physiologically relevant experiments and correctly interpreting results.

What is known about the enzymes that regulate β-hydroxybutyrylation and de-β-hydroxybutyrylation?

Current knowledge about enzymes regulating β-hydroxybutyrylation dynamics includes:

• "Writers" (adding the modification):

  • Unlike histone acetyltransferases (HATs), specific enzymes dedicated to β-hydroxybutyrylation have not been definitively identified

  • Some p300/CBP enzymes may catalyze β-hydroxybutyrylation non-specifically, but this requires further validation

  • Non-enzymatic β-hydroxybutyrylation may occur under conditions of elevated β-hydroxybutyryl-CoA

• "Erasers" (removing the modification):

  • HDAC1-3 and SIRT1-3 have demonstrated significant de-β-hydroxybutyrylation activity against core histones in vitro

  • Interestingly, only HDAC1 and HDAC2 appear to function as histone Kbhb deacetylases in cellular contexts

  • Deacylases may show preferences for specific chiral forms of β-hydroxybutyrylation, suggesting stereochemical regulation

• "Readers" (proteins recognizing the modification):

  • Specific reader proteins for β-hydroxybutyrylation are still being characterized

  • Bromodomain-containing proteins that typically bind acetylated lysines may have different affinities for β-hydroxybutyrylated residues

• Regulatory considerations:

  • The abundance of β-hydroxybutyryl-CoA, which serves as the acyl donor, is a key determinant of modification levels

  • Metabolic pathways that regulate β-hydroxybutyryl-CoA levels (such as ketogenesis) indirectly control histone modification status

This evolving understanding provides targets for experimental manipulation to study β-hydroxybutyrylation dynamics.

How can researchers quantitatively analyze Western blot data from β-hydroxybutyryl-HIST1H2AG (K36) Antibody experiments?

For rigorous quantitative analysis of Western blot data using β-hydroxybutyryl-HIST1H2AG (K36) Antibody, implement this methodological framework:

• Technical optimization:

  • Use a dynamic range of protein loading (5-30 μg of histone extracts) to ensure signal linearity

  • Include a standard curve of recombinant β-hydroxybutyrylated peptides for absolute quantification

  • Process all experimental conditions on the same blot to minimize inter-blot variability

• Normalization strategies:

  • Normalize to total histone H2A (using pan-H2A antibodies) rather than housekeeping proteins

  • Consider dual normalization to both total histone and loading controls

  • For samples with potentially altered histone levels, use spike-in controls of exogenous proteins

• Quantification approaches:

  • Use digital imaging systems with wide dynamic range rather than film

  • Apply background subtraction methods consistently across all samples

  • Quantify integrated density values rather than peak intensity

  • Average technical replicates (minimum of three) before statistical analysis

• Statistical analysis:

  • Apply appropriate statistical tests based on data distribution (parametric or non-parametric)

  • Consider hierarchical analysis for nested experimental designs

  • Report effect sizes and confidence intervals in addition to p-values

• Validation considerations:

  • Confirm key findings with orthogonal methods like mass spectrometry

  • Verify antibody specificity with peptide competition controls

This comprehensive approach ensures reliable quantification and interpretation of β-hydroxybutyrylation dynamics.

What are the common pitfalls in interpreting ChIP-seq data for histone β-hydroxybutyrylation and how can they be avoided?

When interpreting ChIP-seq data for histone β-hydroxybutyrylation, researchers should be aware of these common pitfalls and their solutions:

Previous studies have shown that histone Kbhb is enriched in active gene promoters and associated with starvation-responsive metabolic pathways . When analyzing your own data, consider whether your findings align with or differ from these established patterns.

What are the most common technical issues when using β-hydroxybutyryl-HIST1H2AG (K36) Antibody and how can they be resolved?

When working with β-hydroxybutyryl-HIST1H2AG (K36) Antibody, researchers may encounter these common technical issues and solutions:

• Weak or absent signal:

  • Potential causes: Insufficient modification levels, antibody degradation, epitope masking

  • Solutions:

    • Treat cells with higher concentrations of β-hydroxybutyrate (10-20 mM) to increase modification levels

    • Use fresh antibody aliquots and avoid repeated freeze-thaw cycles

    • Optimize extraction methods to preserve the modification

• High background or non-specific binding:

  • Potential causes: Insufficient blocking, cross-reactivity with other acylations

  • Solutions:

    • Increase blocking time or concentration (5% BSA often works better than milk for PTM antibodies)

    • Include additional washing steps with higher stringency buffers

    • Pre-absorb antibody with unmodified histone peptides

• Inconsistent results between experiments:

  • Potential causes: Variations in metabolic state of cells, lot-to-lot antibody variability

  • Solutions:

    • Standardize culture conditions and harvest times

    • Test each antibody lot against a standard sample

    • Include positive controls in each experiment (e.g., β-hydroxybutyrate-treated cells)

• Discrepancies between antibody-based detection and mass spectrometry:

  • Potential causes: Antibody cross-reactivity, context-dependent epitope recognition

  • Solutions:

    • Validate key findings with orthogonal methods

    • Use peptide competition assays to confirm specificity

    • Consider the effects of neighboring modifications on antibody binding

Implementing these troubleshooting approaches will improve the reliability and reproducibility of your β-hydroxybutyryl-HIST1H2AG (K36) Antibody experiments.

How can researchers optimize immunofluorescence protocols for β-hydroxybutyryl-HIST1H2AG (K36) detection in tissue sections?

Optimizing immunofluorescence protocols for β-hydroxybutyryl-HIST1H2AG (K36) detection in tissue sections requires specific methodological considerations:

• Fixation optimization:

  • Test various fixatives beyond standard PFA (e.g., methanol, ethanol, or dual fixation protocols)

  • Limit fixation time to preserve epitope accessibility (typically 10-15 minutes for PFA)

  • Consider performing antigen retrieval using citrate buffer (pH 6.0) or Tris-EDTA (pH 9.0)

• Permeabilization considerations:

  • Use gentle permeabilization methods (0.1-0.2% Triton X-100) to maintain nuclear architecture

  • Extend permeabilization time (15-30 minutes) to ensure antibody access to nuclear antigens

  • Consider alternative permeabilization agents like saponin for sensitive tissues

• Blocking and antibody incubation:

  • Use 5% BSA or 10% normal serum from the secondary antibody host species

  • Extend primary antibody incubation to overnight at 4°C with optimized dilution (typically 1:50-1:200)

  • Include 0.1% Triton X-100 in antibody dilution buffers to maintain permeabilization

• Signal amplification:

  • Consider tyramide signal amplification for low abundance modifications

  • Use high-sensitivity detection systems (e.g., quantum dots or Alexa Fluor 647)

  • Optimize exposure settings to capture the full dynamic range without saturation

• Controls and validation:

  • Include tissue from fasted animals as positive controls (enhanced modification)

  • Use peptide competition controls to verify antibody specificity

  • Perform parallel staining with antibodies to other histone modifications for comparison

These optimizations will help achieve specific and sensitive detection of β-hydroxybutyrylation in tissue sections.

What are promising research areas for exploring the functional significance of histone β-hydroxybutyrylation in disease models?

Several promising research areas for exploring the functional significance of histone β-hydroxybutyrylation in disease models include:

• Metabolic disorders:

  • Investigate how altered β-hydroxybutyrylation patterns contribute to transcriptional dysregulation in obesity and diabetes

  • Explore whether β-hydroxybutyrylation changes precede or follow insulin resistance development

  • Analyze tissue-specific differences in modification patterns across metabolic disease progression

• Neurodegenerative diseases:

  • Examine β-hydroxybutyrylation in ketogenic diet treatments for epilepsy and neurodegenerative conditions

  • Investigate whether β-hydroxybutyrylation mediates neuroprotective effects of ketone bodies

  • Study how age-related changes in histone β-hydroxybutyrylation affect neuronal gene expression

• Cancer metabolism:

  • Explore how metabolic reprogramming in cancer cells affects histone β-hydroxybutyrylation

  • Investigate whether targeting β-hydroxybutyrylation pathways can sensitize cancer cells to therapy

  • Analyze tumor microenvironment effects on cancer cell β-hydroxybutyrylation patterns

• Inflammatory conditions:

  • Study how β-hydroxybutyrate's anti-inflammatory effects may be mediated through histone β-hydroxybutyrylation

  • Examine modification patterns in macrophages during polarization and inflammatory responses

  • Investigate potential targeting of β-hydroxybutyrylation pathways for inflammatory disease treatment

• Developmental programming:

  • Explore how maternal metabolic state affects offspring histone β-hydroxybutyrylation patterns

  • Investigate transgenerational effects of altered β-hydroxybutyrylation

  • Study the role of this modification in cellular differentiation and developmental transitions

These research directions could reveal how this metabolically-responsive histone modification contributes to disease pathogenesis and identify potential therapeutic targets.

How can computational approaches and systems biology be integrated into the study of histone β-hydroxybutyrylation?

Integrating computational approaches and systems biology into histone β-hydroxybutyrylation research offers powerful methodological frameworks:

• Multi-omics data integration:

  • Develop computational pipelines that integrate ChIP-seq, RNA-seq, and metabolomics data

  • Apply machine learning algorithms to identify patterns linking metabolic state, histone modifications, and gene expression

  • Implement network analysis to map the relationships between modified histones and transcriptional programs

• Predictive modeling:

  • Develop algorithms to predict β-hydroxybutyrylation sites based on sequence context and chromatin features

  • Create mathematical models of the dynamics between β-hydroxybutyrate metabolism and histone modification

  • Simulate the effects of metabolic perturbations on global modification patterns

• Comparative epigenomics:

  • Apply phylogenetic analysis to understand the evolutionary conservation of β-hydroxybutyrylation sites

  • Compare modification patterns across species under similar metabolic states

  • Identify species-specific regulatory mechanisms through comparative genomics

• Structure-function relationships:

  • Use molecular dynamics simulations to predict how β-hydroxybutyrylation affects chromatin fiber structure

  • Model reader protein interactions with modified histones through docking simulations

  • Predict the effects of β-hydroxybutyrylation on nucleosome stability and dynamics

• Clinical data mining:

  • Analyze patient electronic health records to correlate ketosis states with disease outcomes

  • Develop biomarker panels based on histone modification patterns

  • Apply systems pharmacology approaches to identify drugs that might modulate β-hydroxybutyrylation

These computational approaches will accelerate discovery and provide mechanistic insights into this emerging epigenetic regulatory mechanism.

How do the properties and applications of β-hydroxybutyryl-HIST1H2AG (K36) Antibody compare with antibodies targeting other sites such as K95?

A comparative analysis of antibodies targeting different β-hydroxybutyrylation sites reveals important distinctions:

Key considerations when selecting between these antibodies:

• The biological question (specific modification site relevance)

• Required applications (WB vs. IF/ICC capabilities)

• Chromatin context of interest (promoters vs. other regions)

• Experimental system (metabolic state sensitivity)

Understanding these differences enables researchers to select the most appropriate antibody for their specific experimental needs.

What methodological differences should be considered when working with β-hydroxybutyryl versus 2-hydroxyisobutyryl antibodies?

When working with β-hydroxybutyryl versus 2-hydroxyisobutyryl antibodies, researchers should consider these methodological differences:

• Structural recognition differences:

  • β-hydroxybutyryl modifications contain a straight-chain structure with a β-hydroxyl group

  • 2-hydroxyisobutyryl modifications contain a branched structure with a 2-hydroxyl group

  • These structural differences affect antibody specificity and may require different blocking strategies

• Application-specific considerations:

  • β-hydroxybutyryl-HIST1H2AG (K36) is validated for Western blotting, while 2-hydroxyisobutyryl-HIST1H2AG (K95) is optimized for immunofluorescence

  • Different dilution ranges may be required (typically 1:50-1:200 for IF applications with 2-hydroxyisobutyryl antibodies)

• Metabolic induction protocols:

  • β-hydroxybutyrylation is specifically induced by β-hydroxybutyrate treatment

  • 2-hydroxyisobutyrylation may respond differently to metabolic stimuli

  • Researchers should validate the appropriate metabolite treatment for each modification

• Cross-reactivity concerns:

  • Due to structural similarities, validation of specificity between these closely related modifications is essential

  • Include appropriate competition controls with modified and unmodified peptides

• Enzymatic regulation:

  • Different deacylases may show preferences for β-hydroxybutyryl versus 2-hydroxyisobutyryl modifications

  • HDAC inhibitor treatments may affect these modifications differently

Understanding these methodological differences will help researchers design experiments that accurately distinguish between these related but distinct histone modifications.

What are the most significant recent advances in understanding histone β-hydroxybutyrylation and what key questions remain unanswered?

Recent significant advances in histone β-hydroxybutyrylation research include:

• Comprehensive identification of modification sites:

  • 44 histone Kbhb sites have been identified, comparable to the number of known acetylation sites

  • These sites include functionally important lysine residues such as H4K8, H4K12, H3K4, H3K9, and H3K56

• Metabolic regulation mechanisms:

  • Clear demonstration that histone Kbhb levels respond dramatically to elevated β-hydroxybutyrate in fasting and diabetic conditions

  • Evidence that this modification specifically marks genes involved in starvation-responsive metabolic pathways

• Enzymatic regulation:

  • Identification of HDAC1-3 and SIRT1-3 as enzymes with de-β-hydroxybutyrylation activity

  • Discovery that only HDAC1 and HDAC2 function as histone Kbhb deacetylases in cellular contexts

• Functional genomics insights:

  • ChIP-seq studies showing Kbhb enrichment at active gene promoters

  • Association with starvation-responsive gene regulation

Key questions that remain unanswered:

• Dedicated "writers" - Are there specific enzymes that preferentially catalyze β-hydroxybutyrylation, or is it primarily non-enzymatic?

• Selective "readers" - Which proteins specifically recognize β-hydroxybutyrylated histones, and how does this recognition differ from other acylations?

• Tissue specificity - How do β-hydroxybutyrylation patterns differ across tissues, and what are the functional consequences?

• Disease relevance - How are β-hydroxybutyrylation patterns altered in specific diseases, and could targeting these pathways offer therapeutic benefits?

• Evolutionary conservation - How conserved are the functions of β-hydroxybutyrylation across species, and what does this reveal about its fundamental importance?

Addressing these questions represents a significant opportunity for researchers to advance our understanding of this metabolically-responsive epigenetic mechanism.

What emerging technologies might enhance the study of histone β-hydroxybutyrylation in the near future?

Emerging technologies poised to transform histone β-hydroxybutyrylation research include:

• Advanced mass spectrometry approaches:

  • Ion mobility MS for improved separation of modified peptides

  • Targeted SWATH-MS for comprehensive quantification across multiple samples

  • Single-cell proteomics to reveal cell-to-cell variation in modification patterns

• Genome editing technologies:

  • Base editing to precisely modify lysine residues without disrupting histone genes

  • CRISPR activation/interference systems to modulate enzymes involved in β-hydroxybutyrylation

  • Prime editing for introducing specific mutations in histone genes

• Live-cell imaging innovations:

  • FRET-based sensors for real-time monitoring of β-hydroxybutyrylation dynamics

  • Engineered antibody fragments for live-cell modification tracking

  • Super-resolution microscopy combined with specific probes for spatial organization

• Synthetic biology approaches:

  • Engineered histone reader domains with specificity for β-hydroxybutyrylation

  • Orthogonal synthetic systems to control modification levels independently of metabolism

  • Designer nucleosomes with defined modification patterns for biochemical studies

• Microfluidic and organ-on-chip technologies:

  • Microfluidic devices for precise metabolic manipulation and real-time analysis

  • Multi-tissue organ-on-chip models to study modification patterns in physiological context

  • Integrated sensors for concurrent monitoring of metabolites and histone modifications