myf6 Antibody

What is MYF6 and what cellular functions does it regulate?

MYF6 (myogenic factor 6), also known as herculin, is one of the four myogenic regulatory factors (MRFs). It is primarily expressed in fully differentiated muscle fibers, unlike the other three MRFs (Myf5, MyoD, and Myogenin) which are transiently expressed during muscle stem cell activation, commitment, and terminal differentiation . MYF6 is a transcription factor that regulates a broad spectrum of myokines and muscle-secreted proteins in skeletal myofibers, including EGF . It plays a crucial role in establishing ligand/receptor interaction between muscle stem cells and their associated muscle fibers, thereby contributing to the maintenance of the muscle stem cell niche environment . The protein has a calculated molecular weight of 27 kDa (242 amino acids) and is encoded by the gene with ID 4618 in the NCBI database .

What applications are validated for MYF6 antibody use?

The MYF6 antibody (11754-1-AP) has been extensively validated for multiple applications in research settings. According to technical documentation, this antibody can be reliably used in:

• Western Blot (WB) at dilutions of 1:500-1:1000

• Immunohistochemistry (IHC) at dilutions of 1:500-1:2000

• Immunofluorescence (IF)/Immunocytochemistry (ICC) at dilutions of 1:50-1:500

• Chromatin Immunoprecipitation (ChIP)

• Enzyme-Linked Immunosorbent Assay (ELISA)

The antibody has been cited in multiple publications, particularly for Western Blot and ChIP applications . Researchers should note that optimal dilutions may be sample-dependent, and it is recommended to titrate the reagent in each testing system to obtain optimal results .

What sample types are compatible with MYF6 antibody?

The MYF6 antibody (11754-1-AP) has demonstrated reactivity with human, mouse, and rat samples . In published research, it has been predominantly used with mouse and human samples . Positive Western Blot detection has been confirmed in mouse skeletal muscle tissue . For immunohistochemistry, positive detection has been demonstrated in mouse skeletal muscle tissue with recommended antigen retrieval using TE buffer pH 9.0 (alternatively, citrate buffer pH 6.0 may be used) . Positive IF/ICC detection has been documented in C2C12 cells, a mouse myoblast cell line commonly used in muscle differentiation studies .

What are the recommended storage conditions for MYF6 antibody?

For optimal preservation of antibody activity, the MYF6 antibody should be stored at -20°C . Under these conditions, the antibody remains stable for one year after shipment . The antibody is supplied in PBS with 0.02% sodium azide and 50% glycerol at pH 7.3 . Importantly, aliquoting is not necessary for -20°C storage of this particular antibody preparation . Some preparations (20μl sizes) contain 0.1% BSA, which helps stabilize the antibody . When handling the antibody, standard laboratory safety precautions should be followed, particularly due to the presence of sodium azide in the storage buffer.

How can MYF6 antibody be used to investigate transcriptional regulation in muscle cells?

MYF6 antibody can be employed in Chromatin Immunoprecipitation followed by sequencing (ChIP-seq) to identify genome-wide binding sites of MYF6 in myogenic cells. Research has demonstrated that MYF6 occupies regulatory domains of cytokine genes in differentiated muscle cells . When ChIP-seq data is unavailable due to lack of commercial ChIP-grade antibodies, researchers have successfully used Chromatin Tandem Affinity Purification Sequencing (ChTAP-Seq) with MYF6-CTAP constructs .

Analysis of such data has revealed that MYF6 binds to 12,885 sites in primary myotubes, with the top scoring motif being the canonical E-box, centrally located and closely juxtaposed by the MEF2A binding motif . This pattern suggests cooperation between MYF6 and MEF2A transcription factors. The density of E-box motifs is significantly higher under MYF6 peaks compared to random genomic regions, mirroring patterns observed for other myogenic factors such as MyoD and Myf5 .

To implement this methodology:

• Generate primary myoblast cell lines expressing tagged MYF6 or use antibodies for direct ChIP

• Perform chromatin immunoprecipitation following standard protocols

• Sequence precipitated DNA and analyze using tools like MACS2 for peak calling

• Use motif analysis tools such as MEME suite to identify binding motifs

• Compare with controls (e.g., empty vector or IgG) to establish specificity

What role does MYF6 play in muscle stem cell maintenance and how can this be studied?

MYF6 establishes a ligand/receptor interaction between muscle stem cells (MuSCs) and their associated muscle fibers, creating a regulatory niche environment . Research indicates that homozygous deletion of Myf6 causes a progressive reduction in the stem cell pool during postnatal life due to spontaneous exit from quiescence, despite normal muscle stem cell compartments at birth .

To investigate this role, researchers can employ several experimental approaches using MYF6 antibody:

• Immunofluorescence staining of muscle sections to evaluate MuSC numbers and myofiber architecture in wildtype versus Myf6-knockout models

• Western blot analysis to quantify MYF6 expression levels during different stages of muscle regeneration

• Co-immunoprecipitation to identify protein interaction partners in the MuSC niche

• ELISA assays of serum or myotube secretome to measure levels of MYF6-regulated myokines like EGF and VEGFA

Studies have shown that serum from Myf6-knockout mice contains significantly reduced levels of key myokines compared to controls . Moreover, secretome from Myf6-KO myotubes exhibits lower levels of EGF and VEGFA, which can be rescued by reintroduction of Myf6 through retroviral infection . These findings suggest that MYF6 antibody-based assays can help elucidate the molecular mechanisms by which MYF6 maintains muscle stem cell homeostasis.

How can experimental artifacts be minimized when using MYF6 antibody in immunohistochemistry?

When using MYF6 antibody for immunohistochemistry, several technical considerations must be addressed to minimize artifacts:

Following the manufacturer's recommended protocols while incorporating these considerations can significantly improve the specificity and reproducibility of MYF6 immunohistochemistry results.

What is the significance of MYF6 expression in hematological malignancies?

While MYF6 is primarily associated with skeletal muscle, unexpected expression patterns have been observed in certain hematological malignancies, particularly hairy cell leukemia (HCL) . Expression microarrays comparing HCL with its variant form (HCLv) revealed that MYF6 showed the greatest differential expression among 24,694 genes analyzed, with 18.5-fold and 10.8-fold higher expression in HCL than HCLv (p<0.0001) .

Real-time quantitative PCR (RQ-PCR) confirmed MYF6 expression in:

• 100% of 152 classic HCL samples

• 35% of 51 HCLv samples

• 92% of 12 HCL samples expressing unmutated IGHV4-34

• 73% of 48 chronic lymphocytic leukemia (CLL) samples

• 8% of 12 mantle cell lymphoma samples

• Only 6% of 90 blood donors

The mechanism behind this aberrant expression appears to involve epigenetic regulation, as hypomethylation status of MYF6 supported expression in HCL more than in HCLv . This suggests that MYF6 could serve as a potential biomarker for monitoring minimal residual disease in HCL, as 48% of post-treatment blood samples that were negative by flow cytometry remained MYF6-positive by RQ-PCR .

Researchers studying hematological malignancies can employ MYF6 antibody in combination with other markers to improve diagnostic accuracy and monitor treatment efficacy. Western blot or immunofluorescence analysis using MYF6 antibody could complement molecular approaches for detecting aberrant MYF6 expression in leukemic cells.

What methodological approaches can be used to study MYF6's role in regulating myokine production?

Investigating MYF6's regulatory role in myokine production requires a multi-faceted approach:

• ChIP-seq analysis: Using MYF6 antibody for chromatin immunoprecipitation followed by sequencing can identify direct binding of MYF6 to regulatory regions of myokine genes. Research has shown enrichment of MYF6 ChIP-seq reads around the transcription start sites (TSS) of genes like VEGFA and EGF .

• Transcriptome analysis: RNA-Seq comparing wildtype and Myf6-knockout muscle samples can reveal differential expression of myokine genes. This approach has demonstrated that loss of Myf6 leads to downregulation of key myokine genes such as VEGFA and EGF in vivo .

• Protein quantification: ELISA assays of:

  • Serum from wildtype versus Myf6-knockout mice

  • Conditioned media (secretome) from cultured myotubes

  ELISA results have shown significant reduction in key myokines like EGF and VEGFA in both serum and secretome from Myf6-knockout models .

• Rescue experiments: Reintroduction of Myf6 by retroviral infection into Myf6-KO myotubes and subsequent measurement of myokine levels by ELISA and RT-qPCR can confirm the specificity of MYF6's regulatory role. Such experiments have demonstrated restoration of EGF and VEGFA levels following Myf6 reintroduction .

• Correlation with methylation status: Analysis of MYF6 promoter methylation alongside expression data can reveal epigenetic mechanisms of regulation. Hypomethylation status has been shown to support MYF6 expression .

By integrating these methodological approaches, researchers can comprehensively characterize the mechanistic basis of MYF6's function in regulating myokine production and secretion.

What are the optimal conditions for Western blot detection of MYF6?

For optimal Western blot detection of MYF6, the following protocol parameters should be considered:

• Sample preparation:

  • Skeletal muscle tissue is the preferred positive control sample

  • Protein extraction should use buffers compatible with nuclear proteins (as MYF6 is a transcription factor)

  • Include protease inhibitors to prevent degradation

• Gel electrophoresis:

  • Use 10-12% SDS-PAGE gels appropriate for the 27 kDa size of MYF6

  • Load sufficient protein (typically 20-50 μg of total protein)

• Transfer conditions:

  • Semi-dry or wet transfer systems are both appropriate

  • Use PVDF membranes for better protein retention and signal quality

• Blocking:

  • 5% non-fat dry milk or BSA in TBST is typically effective

  • Block for 1 hour at room temperature

• Antibody incubation:

  • Primary antibody (MYF6, 11754-1-AP): Use at 1:500-1:1000 dilution

  • Incubate overnight at 4°C for optimal specificity

  • Secondary antibody: HRP-conjugated anti-rabbit IgG at manufacturer's recommended dilution

  • Incubate for 1 hour at room temperature

• Detection:

  • Enhanced chemiluminescence (ECL) detection systems are suitable

  • Expected molecular weight is 27 kDa

  • Multiple exposure times should be tested to optimize signal-to-noise ratio

• Controls:

  • Positive control: mouse skeletal muscle tissue

  • Loading control: housekeeping protein such as GAPDH or β-actin

  • Negative control: tissue known not to express MYF6

Following the manufacturer's protocol for Western blot using the MYF6 antibody will provide a solid starting point, with optimization based on specific laboratory conditions and equipment .

How should experiments be designed to investigate MYF6's role in muscle stem cell quiescence?

To investigate MYF6's role in muscle stem cell quiescence, a comprehensive experimental design should include:

• Animal models:

  • Myf6-knockout mice (e.g., Myf6 CE mice with Cre-ERT2 cassette knocked into the first exon of the Myf6 gene)

  • Age-matched wildtype controls

  • Consider time course analyses at different postnatal stages to track progressive changes

• Muscle stem cell isolation:

  • Fluorescent-activated cell sorting (FACS) of muscle stem cells using standard markers (e.g., Pax7+/CD34+/α7-integrin+)

  • Compare isolation yields between Myf6-knockout and wildtype mice across different ages

• Quiescence assessments:

  • Immunostaining for quiescence markers (e.g., Pax7, Calcein, Ki67-, PyroninY-, H3K4me3)

  • Cell cycle analysis using EdU incorporation or propidium iodide staining

  • RNA-seq for quiescence gene signature analysis

• Niche factor analysis:

  • ELISA quantification of key myokines (EGF, VEGFA) in serum and muscle secretome

  • Immunostaining of muscle sections for spatial relationships between MYF6+ myofibers and quiescent stem cells

  • Western blot and RT-qPCR analysis of myokine receptor expression on muscle stem cells

• Signaling pathway investigation:

  • Western blot for phosphorylated versus total p38 MAPK (known to be regulated by EGF signaling)

  • Inhibitor studies to block specific pathways (e.g., EGFR inhibitors)

  • Rescue experiments with recombinant myokines or Myf6 overexpression

• In vitro validation:

  • Primary myoblast cultures from Myf6-knockout and wildtype mice

  • Quiescence induction assays (e.g., suspension culture or specific media conditions)

  • Co-culture experiments with myotubes expressing or lacking MYF6

This experimental design allows for comprehensive characterization of how MYF6 influences muscle stem cell quiescence through direct and indirect mechanisms, particularly through regulation of myokine production.

What quality control measures should be implemented when using MYF6 antibody in multiplex immunofluorescence?

When implementing multiplex immunofluorescence with MYF6 antibody, several quality control measures are essential:

• Antibody validation:

  • Verify single-band specificity in Western blot using positive control tissue (skeletal muscle)

  • Compare staining pattern with literature-reported localization

  • Include Myf6-knockout tissue as negative control where available

• Fluorophore selection and spectral separation:

  • Select fluorophores with minimal spectral overlap

  • Include single-stained controls for spectral unmixing if using multispectral imaging

  • Ensure secondary antibody compatibility with rabbit IgG host species of MYF6 antibody

• Panel design considerations:

  • Optimize antibody dilution (1:50-1:500 recommended for IF/ICC)

  • Test antibody combinations for potential steric hindrance or epitope blocking

  • Consider the cellular localization of targets (MYF6 is nuclear) when selecting other markers

• Technical controls:

  • No primary antibody controls

  • Isotype controls (rabbit IgG)

  • Fluorescence-minus-one (FMO) controls

  • Positive control samples (C2C12 cells for MYF6)

• Image acquisition standardization:

  • Maintain consistent exposure settings across samples

  • Use automated microscopy platforms when possible

  • Include fluorescent intensity calibration beads

• Analysis quality control:

  • Apply consistent thresholding methods

  • Include cell segmentation accuracy assessments

  • Perform statistical validation of co-localization measurements

  • Implement batch correction if necessary

• Reproducibility measures:

  • Process biological replicates simultaneously

  • Include technical replicates

  • Document all protocol details for reproducibility

These quality control measures will ensure reliable and interpretable results when using MYF6 antibody in multiplex immunofluorescence applications, particularly important when investigating complex cellular relationships in muscle tissue or unexpected expression in hematological malignancies .

How should researchers address inconsistent MYF6 antibody staining patterns?

When encountering inconsistent staining patterns with MYF6 antibody, systematically address potential issues:

• Sample preparation variables:

  • Fixation method and duration: Overfixation can mask epitopes

  • Antigen retrieval: Test both recommended methods (TE buffer pH 9.0 and citrate buffer pH 6.0)

  • Section thickness: Optimize for the specific application (typically 5-7 μm for IHC)

• Antibody-related factors:

  • Verify antibody lot consistency with manufacturer

  • Test different antibody concentrations within the recommended range (1:500-1:2000 for IHC)

  • Consider antibody storage conditions and potential degradation

  • Use freshly prepared antibody dilutions

• Technical protocol adjustments:

  • Modify blocking conditions (time, temperature, blocking agent)

  • Adjust incubation times and temperatures

  • Implement additional washing steps

  • Consider background reduction reagents

• Control implementations:

  • Run parallel staining with known positive controls (mouse skeletal muscle)

  • Include negative controls (primary antibody omission, non-muscle tissue)

  • Consider dual-staining with alternative MYF6 antibodies from different epitopes

  • Test MYF6-knockout tissue if available

• Detection system optimization:

  • Compare different visualization methods (fluorescent vs. chromogenic)

  • Adjust signal amplification steps

  • Optimize counterstaining to improve contrast

• Tissue-specific considerations:

  • Be aware that MYF6 expression varies by muscle fiber type

  • Consider developmental stage (expression patterns change during myogenesis)

  • Account for pathological conditions that may alter expression

• Instrument settings:

  • Standardize microscope parameters (exposure, gain, offset)

  • Use image analysis software with appropriate thresholding

Systematically testing these variables while maintaining careful documentation can identify the source of inconsistency and lead to reproducible staining patterns.

What are the potential pitfalls in interpreting MYF6 expression in leukemia samples?

Interpreting MYF6 expression in leukemia samples presents several potential pitfalls that researchers should be aware of:

• Context-dependent expression patterns:

  • MYF6 expression varies significantly between leukemia subtypes (100% in classic HCL vs. 35% in HCLv)

  • Expression in 73% of CLL samples suggests it's not exclusively HCL-specific

  • False positives in healthy donors occur at low frequency (6%)

• Methodological considerations:

  • PCR detection is more sensitive than flow cytometry (48% of flow-negative post-treatment samples remained MYF6+ by RQ-PCR)

  • Different detection methods may yield discordant results

  • Antibody specificity should be validated in leukemic contexts

• Biological interpretation challenges:

  • The biological significance of aberrant MYF6 expression in non-muscle cells remains unclear

  • Expression may reflect dysregulated transcriptional programs rather than functional relevance

  • Correlation with methylation status suggests epigenetic regulation mechanisms

• Clinical interpretation complexities:

  • Persistence of MYF6 expression post-treatment may indicate minimal residual disease or could represent non-malignant expression

  • Expression patterns may evolve during disease progression or treatment

  • Cut-off values for positive vs. negative expression need standardization

• Technical limitations:

  • Sample purity affects interpretation (leukemic cell content)

  • RNA quality and degradation can impact PCR-based detection

  • Antibody-based detection may be influenced by protein modifications

• Comparative analysis requirements:

  • Expression should be evaluated relative to appropriate controls

  • Multi-marker panels provide more reliable classification than single markers

  • Integration with other diagnostic methods is essential

Researchers should approach MYF6 expression in leukemia with these considerations in mind, implementing appropriate controls and complementary techniques to ensure accurate interpretation.

How can researchers validate the specificity of chromatin immunoprecipitation using MYF6 antibody?

Validating the specificity of chromatin immunoprecipitation (ChIP) experiments using MYF6 antibody requires a multi-layered approach:

• Pre-ChIP antibody validation:

  • Confirm antibody specificity by Western blot in muscle tissue

  • Test immunoprecipitation efficiency with nuclear extracts

  • Consider using tagged MYF6 constructs as alternative to antibody-based ChIP

• Experimental controls during ChIP:

  • Input DNA control (pre-immunoprecipitation)

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

  • Biological controls (Myf6-knockout cells/tissues where available)

  • Positive control regions (known MYF6 binding sites)

  • Negative control regions (genomic regions not expected to bind MYF6)

• Quantitative validation by qPCR:

  • Measure enrichment at known target sites (E-box containing regions)

  • Calculate percent input or fold enrichment over IgG

  • Include negative control regions

  • Set threshold enrichment values based on biological relevance

• Motif analysis for ChIP-seq data:

  • Confirm enrichment of canonical E-box motif in peak regions

  • Validate presence of co-factor binding motifs like MEF2A

  • Compare E-box motif density in peaks versus random genomic regions

  • Analyze distribution patterns of motifs within peaks

• Functional validation:

  • Correlate ChIP-seq peaks with expression data from RNA-seq

  • Perform reporter assays with identified binding regions

  • Use CRISPR-based approaches to mutate binding sites

  • Conduct rescue experiments with Myf6 re-expression

• Cross-validation with alternative methods:

  • Compare with published ChIP-seq datasets if available

  • Consider orthogonal methods like ATAC-seq to confirm chromatin accessibility

  • Use DNA affinity precipitation assays as alternative binding assessment

• Replication and reproducibility:

  • Perform biological replicates

  • Validate key findings with alternative antibody clones if available

  • Apply consistent bioinformatic pipelines for analysis

Following these validation steps ensures that ChIP results using MYF6 antibody reflect true biological binding events rather than technical artifacts or non-specific interactions.

How can MYF6 antibody be employed in single-cell analyses of muscle development and disease?

MYF6 antibody can be integrated into cutting-edge single-cell analyses through several innovative approaches:

• Single-cell protein profiling:

  • Mass cytometry (CyTOF) incorporating MYF6 antibody conjugated to metal isotopes

  • Imaging mass cytometry for spatial context in tissue sections

  • Single-cell Western blotting for quantitative protein analysis

  • Proximity extension assays for protein-protein interaction studies

• Spatial transcriptomics integration:

  • Combined immunofluorescence with MYF6 antibody and in situ RNA detection

  • Multiplex immunofluorescence with lineage markers to identify specific cell populations

  • Spatial mapping of MYF6+ cells in relation to muscle stem cell niches

  • Correlation of protein expression with single-cell RNA-seq data

• Lineage tracking applications:

  • Pulse-chase experiments with EdU labeling and MYF6 immunostaining

  • Fate mapping using genetic reporters combined with MYF6 antibody staining

  • Live-cell imaging with fluorescent-tagged MYF6 constructs

  • Clonal analysis of myogenic differentiation

• Disease-specific applications:

  • Single-cell profiling of leukemic cells for MYF6 expression heterogeneity

  • Analysis of muscle biopsies from myopathies for aberrant MYF6 expression

  • Correlation of MYF6 expression with disease progression biomarkers

  • Therapeutic response monitoring at single-cell resolution

• Technical implementations:

  • Optimized fixation and permeabilization protocols for nuclear transcription factors

  • Antibody conjugation strategies for compatibility with multiplexed platforms

  • Signal amplification methods for low-abundance detection

  • Computational approaches for integrating protein and transcriptome data

These advanced applications of MYF6 antibody in single-cell analyses will provide unprecedented insights into the heterogeneity of muscle development, regeneration processes, and disease manifestations, potentially revealing new therapeutic targets and diagnostic biomarkers.

What emerging technologies can enhance the utility of MYF6 antibody in research?

Several emerging technologies can significantly enhance the research utility of MYF6 antibody:

• Advanced imaging technologies:

  • Super-resolution microscopy (STORM, PALM, SIM) for nanoscale visualization of MYF6 localization

  • Light-sheet microscopy for 3D imaging of intact muscle tissues

  • Expansion microscopy for improved spatial resolution of nuclear transcription factors

  • Correlative light and electron microscopy for ultrastructural context

• Microfluidic applications:

  • Droplet-based single-cell protein analysis

  • Organ-on-chip muscle models with real-time immunofluorescence

  • Microfluidic Western blotting for higher throughput analysis

  • Antibody-based microfluidic sorting of specific cell populations

• Proximity labeling approaches:

  • APEX2 or BioID fusion with MYF6 for proximity proteomics

  • Split-protein complementation assays to study interaction dynamics

  • FRET/FLIM-based interaction studies with potential binding partners

  • In situ protein interaction detection using proximity ligation assay

• CRISPR-based technologies:

  • CUT&RUN or CUT&Tag as alternatives to traditional ChIP

  • CRISPR activation/inhibition of MYF6 with antibody-based readouts

  • CRISPR screens with MYF6 antibody-based phenotypic assessment

  • CRISPR base editing to introduce tagged versions of endogenous MYF6

• Computational and AI integration:

  • Machine learning algorithms for automated image analysis of MYF6 staining

  • Integrative multi-omics approaches combining ChIP-seq and RNA-seq data

  • Network analysis of MYF6-regulated genes and proteins

  • Digital pathology tools for quantitative assessment of tissue staining

• Biosensor development:

  • Fluorescent biosensors for real-time monitoring of MYF6 activity

  • FRET-based reporters for MYF6-DNA binding dynamics

  • Optogenetic control of MYF6 function with antibody-based readouts

  • Nanobody-based detection systems for improved tissue penetration

These emerging technologies will expand the breadth and depth of MYF6-focused research, enabling more precise, quantitative, and mechanistic insights into its functions in both normal physiology and disease states.

How might MYF6 be targeted therapeutically and what role could MYF6 antibody play in drug development?

MYF6's roles in muscle development and unexpected expression in certain leukemias suggest potential therapeutic applications, with MYF6 antibody playing several roles in drug development:

• Target validation:

  • MYF6 antibody can confirm target expression in disease tissues

  • Immunohistochemistry profiling across tissue panels to assess specificity

  • Co-localization studies to verify cellular compartmentalization

  • Quantitative analysis of expression levels in patient samples

• Mechanism-of-action studies:

  • Western blot assessment of MYF6 modulation by candidate compounds

  • ChIP assays to measure impact on DNA binding activities

  • Immunofluorescence to track subcellular localization changes

  • Proximity ligation assays to detect altered protein interactions

• Biomarker development:

  • Development of companion diagnostics for hematological malignancies

  • Immunoassays for monitoring MYF6 levels during treatment

  • Minimal residual disease detection in leukemia patients

  • Patient stratification based on MYF6 expression patterns

• Therapeutic approaches for modulation:

  • Small molecule screening using antibody-based readouts

  • Targeted protein degradation (PROTACs) with efficacy measured via Western blot

  • Epigenetic modulators affecting MYF6 methylation status

  • Gene therapy approaches for muscle disorders with MYF6 antibody validation

• Antibody-drug conjugates:

  • Exploratory research in MYF6-expressing leukemias

  • Internalization studies using fluorescently-labeled MYF6 antibodies

  • Toxicity screening in MYF6-positive versus negative cell lines

  • In vivo biodistribution studies with labeled antibodies

• Monitoring therapeutic efficacy:

  • Pharmacodynamic biomarker development

  • Assessment of downstream pathway modulation

  • Correlation of MYF6 levels with clinical outcomes

  • Resistance mechanism investigation

While direct therapeutic targeting of transcription factors like MYF6 presents challenges, the antibody plays crucial roles in target validation, mechanism studies, and biomarker applications, potentially leading to novel treatments for muscle disorders or certain leukemias where MYF6 is aberrantly expressed.