KMT5C Antibody

What is KMT5C and why is it significant in epigenetic research?

KMT5C (lysine methyltransferase 5C), also known as SUV420H2 or Suv4-20h2, is a histone methyltransferase that specifically trimethylates lysine-20 of histone H4 (H4K20me3). This modification represents a specific epigenetic tag for transcriptional repression. KMT5C primarily functions in pericentric heterochromatin regions, playing a central role in establishing constitutive heterochromatin in these areas. The enzyme is targeted to histone H3 through interactions with the RB1 family proteins (RB1, RBL1, and RBL2) . Understanding KMT5C function is crucial because it has been implicated in both tumor suppression and oncogenic activities, depending on cancer type and context, making it an important target for epigenetic research .

What are the key differences between polyclonal and monoclonal KMT5C antibodies in research applications?

Polyclonal KMT5C antibodies, such as those generated in rabbits against synthetic peptides corresponding to amino acids 100-200 of human KMT5C, recognize multiple epitopes on the KMT5C protein. This provides higher sensitivity but potentially lower specificity compared to monoclonal alternatives . For research applications, polyclonal antibodies are particularly valuable when signal amplification is needed, such as in low-abundance KMT5C detection scenarios.

Methodologically, researchers should consider the following when selecting between polyclonal and monoclonal antibodies:

How should KMT5C antibodies be stored and handled to maintain optimal activity?

Proper storage and handling of KMT5C antibodies is critical for maintaining their specificity and sensitivity. Based on manufacturer recommendations, KMT5C antibodies should be stored at -20°C in their recommended buffer formulations, such as PBS with 0.02% sodium azide and 50% glycerol at pH 7.3 . To preserve antibody integrity, researchers should:

• Aliquot antibodies upon first thawing to minimize freeze-thaw cycles

• Avoid repeated freeze-thaw cycles as this can lead to protein denaturation and decreased activity

• When working with the antibody, keep it on ice and return to storage promptly

• Verify the expiration date before each use

• Follow manufacturer-specific recommendations for each antibody formulation

For long-term storage (>1 year), some researchers recommend -80°C, though this should be validated for specific antibody preparations. When antibody performance decreases, optimization of dilution factors may temporarily compensate for activity loss, but replacement with fresh antibody is ultimately necessary for reliable results .

What are the optimal conditions for using KMT5C antibodies in Western blot applications?

Optimizing Western blot protocols for KMT5C detection requires careful consideration of several parameters. Based on validated protocols, the following methodological approach is recommended:

• Sample preparation: Extract total protein from cells or tissues using standard lysis buffers containing protease inhibitors to prevent degradation of KMT5C.

• Gel electrophoresis: Load 25μg protein per lane on 10-12% SDS-PAGE gels for optimal separation of the 52kDa KMT5C protein.

• Transfer conditions: Use wet transfer (100V, 60-90 minutes) to PVDF membranes for optimal protein retention.

• Blocking: Employ 3% nonfat dry milk in TBST for 1 hour at room temperature to minimize background.

• Primary antibody incubation: Dilute KMT5C antibody at 1:500 to 1:2000 in blocking buffer and incubate overnight at 4°C. The exact dilution should be optimized for each application and antibody lot .

• Secondary antibody: Use HRP-conjugated or IR-labeled (e.g., IR 800CW) secondary antibodies at manufacturer-recommended dilutions (typically 1:10000 for HRP-conjugated or 1:800 for IR-labeled antibodies) .

• Detection: For HRP-conjugated antibodies, use ECL detection systems with 5-second exposure as a starting point. For IR-labeled antibodies, use appropriate imaging systems like Odyssey LI-COR .

• Validation: Always include positive controls such as HeLa, 293T, Jurkat cell lysates, or mouse thymus extracts where KMT5C expression has been confirmed .

This methodology has been validated across multiple studies and provides reliable detection of KMT5C protein while minimizing background and non-specific binding.

How can researchers validate the specificity of KMT5C antibodies in their experimental systems?

Validating KMT5C antibody specificity is crucial for generating reliable data. A comprehensive validation approach should include multiple complementary methods:

• Knockout (KO) validation: Use CRISPR-Cas9 to generate KMT5C knockout cell lines as negative controls. This represents the gold standard for antibody validation and is particularly important for polyclonal antibodies .

• Knockdown experiments: Perform siRNA-mediated knockdown of KMT5C as an alternative validation approach. Decreased signal intensity in Western blot or immunostaining correlating with knockdown efficiency provides evidence of specificity .

• Overexpression systems: Compare signal intensity between wildtype cells and those overexpressing KMT5C. This is particularly useful when working with cell lines that have low endogenous expression.

• Peptide competition assays: Pre-incubate the antibody with the immunizing peptide prior to application. Specific binding should be blocked by the peptide, resulting in signal reduction.

• Cross-validation with multiple antibodies: Use different antibodies targeting distinct epitopes of KMT5C and compare their staining patterns .

• Mass spectrometry correlation: For advanced validation, immunoprecipitate KMT5C and confirm identity by mass spectrometry.

For immunofluorescence applications specifically, co-staining with markers of known KMT5C interaction partners (like RB1 family proteins) can provide additional confidence in antibody specificity .

What are the critical considerations when using KMT5C antibodies for immunofluorescence studies?

Successful immunofluorescence detection of KMT5C requires optimized protocols that preserve both antigenicity and cellular architecture. Based on published methodologies, researchers should consider:

• Cell preparation: Seed 2×10^5 cells on collagen-coated coverslips in multi-well plates for optimal cell adherence and distribution .

• Fixation method: Cold methanol fixation (100%, 20 minutes at 4°C or 10 minutes at -20°C) has been validated for KMT5C detection, preserving nuclear architecture while enabling antibody access to nuclear epitopes .

• Permeabilization: Use 0.2% TritonX in PBS for 15 minutes at room temperature after methanol fixation to ensure antibody access to nuclear KMT5C .

• Blocking: LI-COR blocking buffer (1 hour) or filtered 1% BSA are effective in reducing background signal .

• Primary antibody incubation: Dilute KMT5C antibody 1:50 to 1:100 and incubate overnight at 4°C for optimal signal-to-noise ratio.

• Controls: Include H4K20me3 and H4 antibodies as functional controls, as they relate directly to KMT5C activity .

• Imaging considerations: KMT5C localizes primarily to the nucleus with enrichment in pericentric heterochromatin regions. Confocal microscopy with z-stack imaging is recommended for detailed localization studies .

• Co-localization studies: When investigating KMT5C function, co-staining with H4K20me3 can provide insights into enzymatic activity and correlation with its substrate .

By following these methodological considerations, researchers can effectively visualize KMT5C localization patterns in relation to chromatin organization and nuclear architecture.

How does KMT5C function differ between normal cells and cancer cells?

KMT5C exhibits context-dependent roles in normal versus cancer cells, with significant functional differences emerging during carcinogenesis. In normal cells, KMT5C primarily functions as an epigenetic regulator that maintains heterochromatin structure through H4K20 trimethylation, contributing to genomic stability and proper gene silencing .

In cancer contexts, KMT5C function can be altered in two opposing directions:

• As a tumor suppressor: Loss of KMT5C has been implicated in multiple cancer types, suggesting a tumor-suppressive role. In non-small cell lung cancer (NSCLC), KMT5C loss promotes EGFR inhibitor resistance by upregulating the oncogene MET via increased expression of LINC01510, a long non-coding RNA . This mechanism suggests that normal KMT5C activity suppresses oncogenic pathways.

• As an oncogenic driver: Conversely, recent research has identified KMT5C as an oncogenic protein in NSCLC progression. Upregulation of KMT5C correlates with cancer progression and poor patient prognosis . In this context, KMT5C appears to activate DNA repair responses that inhibit the STING-IRF3 pathway and downstream type I interferon signaling, ultimately facilitating tumor immune evasion.

These apparently contradictory roles may be explained by cancer-specific contexts, the stage of cancer progression, or interactions with other genetic alterations. The molecular mechanisms affected by KMT5C in cancer cells include:

• Alterations in heterochromatin formation

• Changes in DNA damage response

• Modulation of immune surveillance mechanisms

• Regulation of oncogene expression through epigenetic reprogramming

Understanding these contextual differences is crucial for developing targeted therapeutic approaches that exploit KMT5C function in specific cancer types.

What methodologies are most effective for studying KMT5C's role in cancer progression?

Investigating KMT5C's role in cancer progression requires a multi-faceted approach combining genetic manipulation, functional assays, and clinical correlation. Based on recent studies, the following methodological framework is recommended:

• Genetic manipulation techniques:

  • CRISPR-Cas9 knockout: Generate KMT5C knockout cell lines using validated sgRNAs targeting conserved regions of KMT5C, followed by clonal isolation for pure populations .

  • Inducible expression systems: Develop tetracycline-inducible KMT5C expression systems for controlled restoration of KMT5C in knockout backgrounds .

  • siRNA knockdown: For transient suppression, use validated siRNAs at 30nM concentration with lipofectamine-based transfection .

• Functional assays:

  • Proliferation assays: Compare growth rates between KMT5C wildtype, knockout, and rescue cell lines.

  • Migration and invasion assays: Assess metastatic potential using transwell chambers.

  • Drug sensitivity assays: Evaluate response to targeted therapies (e.g., EGFR inhibitors) in the presence or absence of KMT5C .

• Mechanistic investigations:

  • ChIP-seq: Map genome-wide H4K20me3 distribution changes upon KMT5C manipulation.

  • RNA-seq: Identify differentially expressed genes in KMT5C-altered cells.

  • Protein-protein interaction studies: Immunoprecipitation followed by mass spectrometry to identify KMT5C interactors in cancer contexts.

• In vivo models:

  • Xenograft models: Implant KMT5C-manipulated cancer cells in immunodeficient mice.

  • Syngeneic models: Essential for studying immune interactions and response to immunotherapy in KMT5C-altered contexts .

• Clinical correlation:

  • Tissue microarray analysis: Correlate KMT5C expression with patient outcomes.

  • Single-cell RNA-seq of patient samples: Evaluate heterogeneity of KMT5C expression.

  • Response to therapy: Correlate KMT5C levels with treatment outcomes, particularly for immunotherapies .

This comprehensive methodological approach enables researchers to dissect both the molecular mechanisms and clinical implications of KMT5C in cancer progression.

How does KMT5C influence response to immunotherapy in lung cancer models?

Recent research has uncovered a significant role for KMT5C in modulating immunotherapy response, particularly in non-small cell lung cancer (NSCLC). The mechanistic relationship between KMT5C and immunotherapy response involves several interconnected pathways:

• Immune surveillance modulation: KMT5C activates DNA repair responses that inhibit the STING-IRF3 pathway, a critical mediator of innate immune activation following DNA damage. This inhibition leads to decreased type I interferon signaling and reduced production of CCL5, a chemokine essential for T cell recruitment .

• CD8+ T cell infiltration and function: KMT5C overexpression results in downregulation of CD8+ T cell infiltration and function in the tumor microenvironment. This creates an immunosuppressive milieu that facilitates tumor immune evasion and progression .

• Synergy with immune checkpoint blockade: Both pharmacological inhibition (using the compound A196) and genetic inhibition of KMT5C significantly enhance the efficacy of anti-PD-1 immunotherapy in lung cancer mouse models. This synergistic effect likely stems from restoring immune surveillance mechanisms suppressed by KMT5C activity .

• Clinical correlation: In NSCLC patients, high KMT5C expression levels correlate with lower response rates and worse clinical outcomes to immune checkpoint blockade therapy. This suggests that KMT5C expression could serve as a predictive biomarker for immunotherapy response .

The experimental approach to study these relationships typically involves:

• Generating KMT5C knockdown/knockout versus overexpression models

• Treating with anti-PD-1 therapy alone or in combination with KMT5C inhibition

• Assessing tumor growth and metastasis

• Analyzing tumor-infiltrating lymphocytes by flow cytometry

• Measuring cytokine/chemokine production in the tumor microenvironment

• Evaluating downstream signaling pathways by Western blotting and immunohistochemistry

These findings highlight KMT5C as a potential therapeutic target for enhancing immunotherapy efficacy in NSCLC patients, representing an important advance in our understanding of epigenetic regulation of anti-tumor immunity .

How can researchers distinguish between the functions of KMT5C and other related histone methyltransferases?

Distinguishing the specific functions of KMT5C from related histone methyltransferases requires sophisticated experimental approaches that exploit their unique properties. For rigorous differentiation, researchers should implement the following methodological strategy:

• Substrate specificity analysis:

  • KMT5C specifically catalyzes trimethylation of H4K20 (H4K20me3), while related enzymes target different residues or produce different methylation states

  • Use antibodies specific to mono-, di-, and tri-methylated H4K20 to distinguish between KMT5C activity (primarily trimethylation) versus KMT5A/SET8 (monomethylation) and KMT5B/SUV420H1 (di- and trimethylation)

• Chromatin localization patterns:

  • KMT5C primarily functions in pericentric heterochromatin regions

  • Perform ChIP-seq experiments with specific antibodies against KMT5C and related methyltransferases to map their genomic distribution

  • Co-immunofluorescence studies with heterochromatin markers can reveal distinct localization patterns

• Protein interaction networks:

  • KMT5C interacts specifically with RB1 family proteins (RB1, RBL1, RBL2) for targeting to histone H3

  • Perform co-immunoprecipitation followed by mass spectrometry to identify specific interaction partners

  • Proximity ligation assays can confirm interactions in intact cells

• Sequential knockdown experiments:

  • Design rescue experiments where one methyltransferase is knocked down and another is overexpressed

  • Assess whether functional compensation occurs or if distinct phenotypes persist

  • This approach reveals unique versus redundant functions

• Inhibitor specificity profiling:

  • Use selective inhibitors like A196 (which targets KMT5B/C)

  • Monitor changes in global H4K20 methylation states by quantitative immunoblotting

  • Correlate inhibitor effects with changes in gene expression and cellular phenotypes

By systematically implementing these approaches, researchers can delineate the specific contributions of KMT5C to cellular processes distinct from those of related histone methyltransferases, enabling more precise targeting in experimental and therapeutic contexts.

What are the most common technical challenges when working with KMT5C antibodies and how can they be overcome?

Researchers working with KMT5C antibodies frequently encounter several technical challenges that can impact experimental outcomes. Based on published literature and best practices, these challenges can be addressed through specific methodological refinements:

• Cross-reactivity with related proteins:

  • Challenge: KMT5C shares sequence homology with KMT5B/SUV420H1, potentially leading to cross-reactivity

  • Solution: Always validate antibody specificity using knockout controls; perform peptide competition assays; consider using antibodies raised against unique regions of KMT5C rather than conserved domains

• Variable nuclear extraction efficiency:

  • Challenge: KMT5C's nuclear localization and chromatin association make complete extraction difficult

  • Solution: Use optimized nuclear extraction buffers with high salt concentration (0.42M NaCl) and include nuclease treatment; sonicate samples adequately to release chromatin-bound KMT5C; verify extraction efficiency with nuclear markers

• Epitope masking due to protein-protein interactions:

  • Challenge: KMT5C interactions with chromatin and other proteins may mask antibody epitopes

  • Solution: Test multiple antibodies targeting different epitopes; optimize fixation conditions for immunofluorescence (comparing paraformaldehyde vs. methanol fixation); consider native versus denaturing conditions for immunoprecipitation

• Low signal-to-noise ratio in immunofluorescence:

  • Challenge: Detection of endogenous KMT5C by immunofluorescence often yields weak signals

  • Solution: Implement signal amplification methods; optimize blocking with 1% BSA filtered through 0.2μm filters; use confocal microscopy with increased exposure times; consider tyramide signal amplification for low abundance detection

• Batch-to-batch variability in polyclonal antibodies:

  • Challenge: Polyclonal antibodies may show performance differences between lots

  • Solution: Purchase larger lots for long-term studies; validate each new lot against previous lots; consider developing monoclonal antibodies for critical applications requiring high reproducibility

• Degradation during sample preparation:

  • Challenge: KMT5C may be susceptible to proteolytic degradation

  • Solution: Include fresh protease inhibitors in all buffers; keep samples consistently cold; process samples rapidly; avoid repeated freeze-thaw cycles

By systematically addressing these technical challenges through the recommended methodological refinements, researchers can significantly improve the reliability and reproducibility of experiments involving KMT5C antibodies.

How can researchers effectively integrate KMT5C chromatin studies with analysis of gene expression and cellular phenotypes?

Integrating KMT5C chromatin studies with gene expression and phenotypic analyses requires a comprehensive multi-omics approach. The following methodological framework enables researchers to establish mechanistic links between KMT5C-mediated epigenetic modifications and their functional consequences:

• Chromatin landscape characterization:

  • Perform ChIP-seq using validated KMT5C antibodies to map genome-wide binding sites

  • Conduct parallel H4K20me3 ChIP-seq to correlate enzyme localization with its catalytic activity

  • Implement CUT&RUN or CUT&Tag for improved signal-to-noise ratio in mapping KMT5C binding

  • Apply ATAC-seq to identify changes in chromatin accessibility associated with KMT5C activity

• Transcriptome analysis:

  • Conduct RNA-seq following KMT5C modulation (knockout, knockdown, or overexpression)

  • Focus on genes proximal to KMT5C binding sites identified in ChIP-seq

  • Analyze expression of specific targets using qRT-PCR for validation

  • Include analysis of non-coding RNAs such as LINC01510, which has been linked to KMT5C function

• Integrative bioinformatics:

  • Perform integrated analysis of ChIP-seq and RNA-seq data to identify direct target genes

  • Apply motif enrichment analysis to identify potential co-regulatory factors

  • Use Gene Ontology and pathway analysis to categorize affected genes functionally

  • Develop correlation networks between H4K20me3 marks and gene expression changes

• Functional validation:

  • Select key target genes identified through multi-omics for functional validation

  • Employ CRISPR activation/inhibition at specific KMT5C target loci to confirm direct regulation

  • Assess rescue phenotypes by modulating downstream targets in KMT5C-altered backgrounds

  • Evaluate cellular phenotypes including proliferation, migration, and drug response

• Clinical correlation:

  • Analyze KMT5C, H4K20me3, and target gene expression in patient samples

  • Correlate expression patterns with clinical outcomes and therapy responses

  • Implement single-cell approaches to address heterogeneity in primary tumors

• Mechanistic investigation of context-dependent functions:

  • Study KMT5C interactions with the DNA repair machinery and the STING-IRF3 pathway

  • Measure type I interferon responses and CCL5 secretion in different contexts

  • Analyze CD8+ T cell infiltration and function in relation to KMT5C expression

This integrated approach enables researchers to establish direct links between KMT5C-mediated epigenetic modifications and their functional consequences in both normal physiology and disease states, particularly in cancer progression and therapy response.

What are the most promising approaches for targeting KMT5C in cancer therapy?

Emerging research has identified KMT5C as a promising therapeutic target in cancer, particularly NSCLC. Based on recent findings, several approaches show significant potential for clinical translation:

• Small molecule inhibitors:

  • The compound A196, which inhibits both KMT5B and KMT5C, has demonstrated efficacy in preclinical lung cancer models

  • When combined with anti-PD-1 immunotherapy, A196 shows synergistic effects in suppressing tumor growth

  • Future development should focus on increasing KMT5C specificity and optimizing pharmacokinetic properties

• Combination with immunotherapy:

  • KMT5C inhibition synergizes with immune checkpoint blockade by enhancing T cell infiltration and function

  • This combination addresses the immune evasion mechanisms promoted by KMT5C overexpression

  • Patient stratification based on KMT5C expression levels could identify those most likely to benefit from this combination approach

• Synthetic lethality approaches:

  • Identifying genes that become essential in KMT5C-overexpressing tumors could reveal synthetic lethal interactions

  • High-throughput CRISPR screens in KMT5C-high versus KMT5C-low contexts can identify such vulnerabilities

  • This approach may enable selective targeting of cancer cells while sparing normal tissues

• RNA-based therapeutics:

  • siRNA or antisense oligonucleotides targeting KMT5C could provide an alternative to small molecule inhibitors

  • These modalities might achieve greater specificity than catalytic inhibitors

  • Advances in RNA delivery technologies make this approach increasingly feasible

• Targeting downstream effectors:

  • In contexts where direct KMT5C inhibition proves challenging, targeting key downstream pathways may be effective

  • The STING-IRF3 pathway, which is inhibited by KMT5C, represents one such opportunity

  • Similarly, targeting the LINC01510-MET axis in EGFR inhibitor-resistant contexts could prove beneficial

The clinical potential of these approaches is supported by observations that high KMT5C expression correlates with poor prognosis and reduced immunotherapy response in NSCLC patients. Developing these targeting strategies could significantly improve outcomes for patients with KMT5C-driven malignancies .

How can researchers effectively integrate KMT5C studies with emerging technologies in epigenetics research?

Integrating KMT5C studies with cutting-edge epigenetic technologies offers unprecedented opportunities to understand its function at multiple scales. A strategic approach to this integration includes:

• Single-cell epigenomics:

  • Apply single-cell ChIP-seq or CUT&Tag to map KMT5C binding and H4K20me3 distribution at single-cell resolution

  • Combine with single-cell RNA-seq to correlate KMT5C activity with transcriptional heterogeneity

  • This approach reveals cell-to-cell variability in KMT5C function within complex tissues or tumors

• Spatial epigenomics:

  • Implement imaging-based approaches like multiplexed immunofluorescence to visualize KMT5C and H4K20me3 in intact tissues

  • Combine with spatial transcriptomics to map KMT5C activity to specific microenvironmental niches

  • Particularly valuable when studying KMT5C's role in tumor-immune interactions

• CRISPR epigenome editing:

  • Use catalytically inactive Cas9 (dCas9) fused to KMT5C or its catalytic domain to target H4K20 trimethylation to specific genomic loci

  • Create synthetic KMT5C binding sites to assess direct effects on chromatin organization and gene expression

  • This approach distinguishes primary from secondary effects of KMT5C activity

• Proteomics integration:

  • Apply proximity labeling methods (BioID, APEX) to identify context-specific KMT5C interaction partners

  • Use mass spectrometry to profile global histone modification changes beyond H4K20me3

  • Investigate post-translational modifications on KMT5C itself that might regulate its activity

• Live-cell dynamics:

  • Develop fluorescently-tagged KMT5C variants compatible with live-cell imaging

  • Study KMT5C recruitment to chromatin in real-time following DNA damage or cell cycle progression

  • Measure enzyme kinetics using FRAP (Fluorescence Recovery After Photobleaching)

• Multi-omics data integration:

  • Apply machine learning approaches to integrate KMT5C ChIP-seq, RNA-seq, and proteomics data

  • Build predictive models of KMT5C function in different cellular contexts

  • Use these models to generate testable hypotheses about KMT5C's role in specific diseases

By systematically implementing these integrative approaches, researchers can develop a comprehensive understanding of KMT5C function across biological scales—from molecular interactions to cellular phenotypes to tissue-level effects—ultimately informing more effective therapeutic strategies targeting this important epigenetic regulator.

What are the outstanding questions about KMT5C biology that require further investigation?

Despite significant advances in understanding KMT5C function, several critical questions remain unanswered. These knowledge gaps represent important opportunities for future research:

• Context-dependent functions:

  • How does KMT5C function as both tumor suppressor and oncogene in different cancer contexts?

  • What molecular switches determine whether KMT5C promotes or inhibits tumorigenesis?

  • Are there tissue-specific cofactors that modify KMT5C activity or target specificity?

• Regulation of KMT5C activity:

  • What post-translational modifications regulate KMT5C enzymatic activity?

  • How is KMT5C expression and localization regulated during cell cycle progression?

  • What signaling pathways modulate KMT5C function in response to cellular stress?

• Non-histone substrates:

  • Does KMT5C methylate non-histone proteins beyond its canonical role in H4K20 trimethylation?

  • If so, how do these alternative activities contribute to its biological functions?

  • Can these non-canonical activities explain some of its context-dependent effects?

• Crosstalk with other epigenetic mechanisms:

  • How does KMT5C-mediated H4K20me3 interact with other histone modifications?

  • What is the relationship between KMT5C activity and DNA methylation patterns?

  • How does KMT5C influence higher-order chromatin organization and nuclear architecture?

• Therapeutic resistance mechanisms:

  • What mechanisms might lead to resistance against KMT5C-targeted therapies?

  • Are there compensatory pathways that activate upon KMT5C inhibition?

  • How might cancer cells adapt to maintain heterochromatin integrity in the absence of KMT5C function?

• Developmental roles:

  • What are the functions of KMT5C during embryonic development and cellular differentiation?

  • How do KMT5C knockout models inform our understanding of its essential functions?

  • Are there specific developmental stages or cell types particularly dependent on KMT5C activity?

• Immune system interactions:

  • How does KMT5C regulate immune cell function beyond the known effects on the STING-IRF3 pathway?

  • Are there direct effects of KMT5C on immune cell development or activation?

  • What is the evolutionary significance of KMT5C's role in immune regulation?

Addressing these questions will require integrated approaches combining genetic, biochemical, and computational methods. The answers will not only advance our fundamental understanding of epigenetic regulation but also inform more effective therapeutic strategies targeting KMT5C in various disease contexts.