HIST1H3A (Ab-14) Antibody

Shipped with Ice Packs
In Stock

Description

Target and Epitope Specificity

The antibody specifically recognizes the acetylated lysine 14 (K14ac) modification on histone H3, a core component of nucleosomes. This PTM is associated with open chromatin states, facilitating DNA accessibility for transcription machinery .

ParameterDetails
Target ModificationAcetylated lysine 14 (K14ac) on histone H3
ImmunogenSynthetic peptide derived from human histone H3 (aa 1–80) with K14ac
Cross-ReactivityHuman, Mouse, Rat (confirmed via dot blot and ELISA)
Specificity ValidationNo cross-reactivity with unmodified H3K14 or other histone PTMs

Antibody Characteristics

Developed for high specificity and sensitivity, this polyclonal antibody exhibits robust performance across multiple experimental platforms:

PropertyDetails
Host SpeciesRabbit
ClonalityPolyclonal
ApplicationsWestern blot (WB), Immunofluorescence (IF), ELISA, Chromatin Immunoprecipitation (ChIP), Immunocytochemistry (ICC)
Molecular Weight~15–17 kDa (observed in WB); 19 kDa (theoretical)
StorageLiquid format in PBS with 50% glycerol; store at –20°C

Chromatin Immunoprecipitation (ChIP)

  • Validated in HeLa cells, showing dose-dependent enrichment at active promoters (e.g., ACTB, GAPDH) and no binding to heterochromatic regions (e.g., Sat2 satellite repeats) .

  • Recovery rates: 0.5–5 μg antibody per ChIP yielded 0.8–2.5% input DNA for active promoters .

Western Blot and ELISA

  • Detects endogenous H3K14ac in HeLa whole-cell and histone extracts .

  • ELISA titer: 1:73,200 against H3K14ac peptide .

Immunofluorescence (IF)

  • Localizes acetylated H3K14 to euchromatic regions in interphase nuclei, correlating with transcriptional activity .

Functional Insights from Studies

  • Synergy with Phosphorylation: H3K14ac cooperates with H3S10 phosphorylation (H3S10ph) to recruit 14-3-3 proteins, displacing repressive HP1γ complexes and activating transcription (e.g., HDAC1 gene) .

  • Disease Relevance: Aberrant H3K14ac levels are implicated in cancer and neurodegenerative disorders, making this antibody critical for epigenetic research .

Validation and Quality Control

  • Specificity: No cross-reactivity with H3K9ac, H3K27ac, or unmodified H3K14 in dot blot assays .

  • Batch Consistency: Recombinant formats ensure uniform performance across lots .

  • Automated Platforms: Validated on the Leica BOND™ RX system for high-throughput IHC .

Limitations and Considerations

  • Species Restrictions: Primarily validated in human, mouse, and rat samples .

  • Mitotic Cells: H3K14ac signals diminish during mitosis due to global deacetylation .

Product Specs

Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Form
Liquid
Lead Time
Typically, we can ship the products within 1-3 business days after receiving your orders. Delivery timelines may vary depending on the purchase method or location. Please consult your local distributors for specific delivery times.
Synonyms
H3 histone family member E pseudogene antibody; H3 histone family; member A antibody; H3/A antibody; H31_HUMAN antibody; H3F3 antibody; H3FA antibody; Hist1h3a antibody; HIST1H3B antibody; HIST1H3C antibody; HIST1H3D antibody; HIST1H3E antibody; HIST1H3F antibody; HIST1H3G antibody; HIST1H3H antibody; HIST1H3I antibody; HIST1H3J antibody; HIST3H3 antibody; histone 1; H3a antibody; Histone cluster 1; H3a antibody; Histone H3 3 pseudogene antibody; Histone H3.1 antibody; Histone H3/a antibody; Histone H3/b antibody; Histone H3/c antibody; Histone H3/d antibody; Histone H3/f antibody; Histone H3/h antibody; Histone H3/i antibody; Histone H3/j antibody; Histone H3/k antibody; Histone H3/l antibody
Target Names
Uniprot No.

Target Background

Function
Histone H3 is a core component of nucleosomes. Nucleosomes play a crucial role in packaging and compacting DNA into chromatin, limiting DNA accessibility to cellular machineries that require DNA as a template. Consequently, histones are central to the regulation of transcription, DNA repair, DNA replication, and chromosomal stability. The accessibility of DNA is regulated by a complex interplay of post-translational modifications of histones, known as the histone code, and nucleosome remodeling.
Gene References Into Functions
  1. Research suggests a mechanism for epigenetic regulation in cancer through the induction of E3 ubiquitin ligase NEDD4-dependent histone H3 ubiquitination. PMID: 28300060
  2. The identification of increased expression of H3K27me3 during a patient's clinical course may be helpful in determining whether tumors are heterochronous. PMID: 29482987
  3. A recent study reports that JMJD5, a Jumonji C (JmjC) domain-containing protein, functions as a Cathepsin L-type protease mediating histone H3 N-tail proteolytic cleavage under stress conditions that trigger a DNA damage response. PMID: 28982940
  4. Data indicates that the Ki-67 antigen proliferative index has significant limitations, and phosphohistone H3 (PHH3) presents an alternative proliferative marker. PMID: 29040195
  5. These findings identify cytokine-induced histone 3 lysine 27 trimethylation as a mechanism that stabilizes gene silencing in macrophages. PMID: 27653678
  6. This study indicates that, during early human brain development, HIST1H3B constitutes the largest proportion of H3.1 transcripts among H3.1 isoforms. PMID: 27251074
  7. In a series of 47 diffuse midline gliomas, the histone H3-K27M mutation was mutually exclusive with the IDH1-R132H mutation and EGFR amplification. It rarely co-occurred with the BRAF-V600E mutation and was commonly associated with p53 overexpression, ATRX loss, and monosomy 10. PMID: 26517431
  8. Evidence suggests that the histone chaperone HIRA co-localizes with viral genomes, binds to incoming viral, and deposits histone H3.3 onto these. PMID: 28981850
  9. These experiments demonstrated that PHF13 binds specifically to DNA and to two types of histone H3 methyl tags (lysine 4-tri-methyl or lysine 4-di-methyl), where it functions as a transcriptional co-regulator. PMID: 27223324
  10. Hemi-methylated CpGs DNA recognition activates UHRF1 ubiquitylation towards multiple lysines on the H3 tail adjacent to the UHRF1 histone-binding site. PMID: 27595565
  11. For the first time, this study describes the MR imaging features of pediatric diffuse midline gliomas with the histone H3 K27M mutation. PMID: 28183840
  12. Approximately 30% of pediatric high-grade gliomas (pedHGG), including GBM and DIPG, harbor a lysine 27 mutation (K27M) in histone 3.3 (H3.3), which is correlated with poor outcomes and has been shown to influence EZH2 function. PMID: 27135271
  13. The H3F3A K27M mutation in adult cerebellar HGG is not uncommon. PMID: 28547652
  14. Research indicates that lysyl oxidase-like 2 (LOXL2) is a histone modifier enzyme that removes trimethylated lysine 4 (K4) in histone H3 (H3K4me3) through an amino-oxidase reaction. PMID: 27735137
  15. Histone H3 lysine 9 (H3K9) acetylation was most prevalent when the Dbf4 transcription level was highest, while the H3K9me3 level was greatest during and just after replication. PMID: 27341472
  16. The SPOP-containing complex regulates SETD2 stability and H3K36me3-coupled alternative splicing. PMID: 27614073
  17. Data suggests that the binding of the helical tail of histone 3 (H3) with PHD ('plant homeodomain') fingers of BAZ2A or BAZ2B (bromodomain adjacent to zinc finger domain 2A or 2B) requires molecular recognition of secondary structure motifs within the H3 tail and could represent an additional layer of regulation in epigenetic processes. PMID: 28341809
  18. These results demonstrate a novel mechanism by which Kdm4d regulates DNA replication by reducing the H3K9me3 level to facilitate the formation of the preinitiation complex. PMID: 27679476
  19. Histone H3 modifications caused by traffic-derived airborne particulate matter exposures in leukocytes. PMID: 27918982
  20. A key role of persistent histone H3 serine 10 or serine 28 phosphorylation in chemical carcinogenesis through regulating gene transcription of DNA damage response genes. PMID: 27996159
  21. hTERT promoter mutations are frequent in medulloblastoma and are associated with older patients, prone to recurrence and located in the right cerebellar hemisphere. On the other hand, histone 3 mutations do not seem to be present in medulloblastoma. PMID: 27694758
  22. AS1eRNA-driven DNA looping and activating histone modifications promote the expression of DHRS4-AS1 to economically control the DHRS4 gene cluster. PMID: 26864944
  23. Data suggests that nuclear antigen Sp100C is a multifaceted histone H3 methylation and phosphorylation sensor. PMID: 27129259
  24. The authors propose that histone H3 threonine 118 phosphorylation via Aurora-A alters the chromatin structure during specific phases of mitosis to promote timely condensin I and cohesin disassociation, which is essential for effective chromosome segregation. PMID: 26878753
  25. Hemi-methylated DNA opens a closed conformation of UHRF1 to facilitate its H3 histone recognition. PMID: 27045799
  26. Functional importance of H3K9me3 in hypoxia, apoptosis, and repression of APAK. PMID: 25961932
  27. Taken together, the authors verified that histone H3 is a real substrate for GzmA in vivo in Raji cells treated by staurosporin. PMID: 26032366
  28. Circulating H3 levels correlate with mortality in sepsis patients and inversely correlate with antithrombin levels and platelet counts. PMID: 26232351
  29. Double mutations on the residues in the interface (L325A/D328A) decrease the histone H3 H3K4me2/3 demethylation activity of lysine (K)-specific demethylase 5B (KDM5B). PMID: 24952722
  30. Minichromosome maintenance protein 2 (MCM2) binding is not required for the incorporation of histone H3.1-H4 into chromatin but is important for the stability of H3.1-H4. PMID: 26167883
  31. Histone H3 lysine methylation (H3K4me3) plays a crucial mechanistic role in leukemia stem cell (LSC) maintenance. PMID: 26190263
  32. PIP5K1A modulates ribosomal RNA gene silencing through its interaction with histone H3 lysine 9 trimethylation and heterochromatin protein HP1-alpha. PMID: 26157143
  33. Lower-resolution mass spectrometry instruments can be utilized for histone post-translational modifications (PTMs) analysis. PMID: 25325711
  34. Inhibition of lysine-specific demethylase 1 activity prevented IL-1beta-induced histone H3 lysine 9 (H3K9) demethylation at the microsomal prostaglandin E synthase 1 (mPGES-1) promoter. PMID: 24886859
  35. The authors report that de novo CENP-A assembly and kinetochore formation on human centromeric alphoid DNA arrays are regulated by a histone H3K9 acetyl/methyl balance. PMID: 22473132

Show More

Hide All

Database Links

HGNC: 4766

OMIM: 137800

KEGG: hsa:8350

STRING: 9606.ENSP00000444823

UniGene: Hs.132854

Involvement In Disease
Glioma (GLM)
Protein Families
Histone H3 family
Subcellular Location
Nucleus. Chromosome.

Q&A

What is HIST1H3A and what is its significance in epigenetic research?

HIST1H3A (also known as H3.1) is one of the main histone H3 variants found in mammals. As a core component of nucleosomes, it plays central roles in chromatin structure, gene regulation, DNA repair, DNA replication, and chromosomal stability . The protein has an observed molecular weight of approximately 15-17 kDa, though it typically appears around 17 kDa on Western blots .

Histone H3.1 contains numerous sites for post-translational modifications (PTMs), including acetylation, methylation, and phosphorylation, which collectively constitute part of the "histone code" that regulates chromatin dynamics and transcriptional states .

What are the key differences between histone variants H3.1 and H3.3?

Histone H3.1 and H3.3 demonstrate distinct genomic localization patterns associated with their specific functions:

FeatureHistone H3.1Histone H3.3
Genomic localizationCoincides with repressive marks (H3K9me3, H3K27me3, DNA methylation)Colocalizes with activation marks (H3K4me3, H2BK120ub1, RNA pol II)
Deposition timingDNA synthesis-dependent (during S-phase)DNA synthesis-independent (throughout cell cycle)
FunctionCanonical nucleosome formation during replicationReplacement histone outside S-phase, during transcription

Aberrant localization of these variants is associated with certain cancers . This distinction is crucial when selecting antibodies for experiments examining specific chromatin states or dynamic processes.

What is the functional significance of histone H3 acetylation at lysine 14?

Acetylation of histone H3 at lysine 14 (H3K14ac) is primarily associated with transcriptional activation . Research has shown that:

  • H3K14ac works synergistically with other modifications, particularly H3S10 phosphorylation, to create binding sites for effector proteins like 14-3-3 that mediate gene activation .

  • H3K14ac can co-exist with H3K9 methylation in vivo, suggesting it can help overcome repressive methylation marks .

  • H3K14ac is resistant to deacetylation by certain histone deacetylase complexes (like the CoREST complex) when present in nucleosomal contexts, providing a mechanism for maintaining active chromatin states .

These findings highlight H3K14ac as a critical modification in establishing and maintaining transcriptionally active chromatin domains.

What are the optimal conditions for using HIST1H3A (Ab-14) antibody in different applications?

The HIST1H3A (Ab-14) antibody has been validated for multiple applications with specific recommended dilutions:

ApplicationRecommended DilutionSample Type
Western Blotting (WB)1:500-1:2000Cell lysates, tissue extracts
Immunofluorescence (IF)/ICC1:50-1:500Fixed cells
Chromatin Immunoprecipitation (ChIP)1:50Crosslinked chromatin (10 μl antibody per 10 μg chromatin)
Flow Cytometry (FC)0.80 μg per 10^6 cellsCell suspensions
ELISAVaries by assay designPurified histones, peptides

For optimal results in ChIP experiments, use 10 μl of antibody with approximately 10 μg of chromatin (roughly 4 × 10^6 cells) . Always titrate the antibody for your specific experimental system to determine optimal concentrations.

How should I prepare samples for ChIP experiments targeting histone H3K14ac?

For successful ChIP experiments targeting H3K14ac:

  • Cell preparation: Harvest approximately 4 × 10^6 cells per immunoprecipitation reaction.

  • Crosslinking: Fix cells with 1% formaldehyde for 10 minutes at room temperature to preserve protein-DNA interactions.

  • Chromatin preparation:

    • Lyse cells and isolate nuclei

    • Sonicate chromatin to fragments of 200-500 bp

    • Check fragmentation quality on an agarose gel

  • Immunoprecipitation:

    • Pre-clear chromatin with protein A/G beads

    • Add 10 μl of H3K14ac antibody per 10 μg of chromatin

    • Incubate overnight at 4°C with rotation

    • Add fresh protein A/G beads and incubate for 2-3 hours

  • Washing and elution:

    • Wash beads with increasing stringency buffers

    • Elute protein-DNA complexes

    • Reverse crosslinks and purify DNA for downstream analysis

Include appropriate controls such as IgG negative control and a positive control (e.g., H3 total antibody) to validate specificity and efficiency.

How can I multiplex histone modification detection to study combinatorial modifications?

To analyze combinatorial histone modifications:

  • Histone H3 PTM Multiplex Assay: This approach works as a solution-based sandwich ELISA to detect multiple histone modifications simultaneously:

    • Couple histone modification-specific antibodies to color-coded magnetic beads

    • Capture modified histones from acid-extracted cell lysates or purified histones

    • Use a biotinylated Histone H3 antibody as a reporter

    • Detect with streptavidin-phycoerythrin

    • Measure on Luminex instruments

  • Sample preparation: Dilute histone samples in assay buffer with deacetylase, protease, and phosphatase inhibitors to preserve modification states.

  • Normalization: Include histone H3 total antibody-conjugated beads for normalization across samples .

This approach allows simultaneous detection of modifications like H3K14ac alongside other marks such as H3K9ac or H3S10ph, enabling analysis of how these modifications interact and co-occur.

Why might I observe inconsistent results when studying H3K14ac in different cellular contexts?

Inconsistent H3K14ac detection can result from several factors:

  • Dynamic modification status: H3K14ac levels change rapidly with cellular conditions. Anisomycin treatment combined with HDAC inhibitors like TSA significantly increases H3K14ac levels, particularly in combination with S10 phosphorylation .

  • Epitope masking: The presence of neighboring modifications can affect antibody access. For example, phosphorylation at S10 can alter the recognition of K14ac by some antibodies.

  • Cell fixation issues: Improper fixation can lead to loss of histone modifications or reduced epitope accessibility. For immunofluorescence, different fixation methods may yield varying results:

    • 100% methanol fixation (5 min) is successful in HepG2, HeLa, and Hek293 cells

    • 4% paraformaldehyde may better preserve certain cellular structures

  • Deacetylase activity: Endogenous HDAC activity can reduce acetylation levels during sample preparation. Always include deacetylase inhibitors in buffers when working with acetylated histones.

How can I validate the specificity of the HIST1H3A (Ab-14) antibody?

Validating antibody specificity is critical for reliable results:

  • Peptide competition assay: Pre-incubate the antibody with H3K14ac peptide before application to samples. This should abolish specific binding, as demonstrated with the Jurkat cell lysate Western blot .

  • Knockout/knockdown validation: Use CRISPR/Cas9-generated H3K14 mutants or HAT inhibitors to reduce K14ac levels.

  • Multiple antibody comparison: Use different antibodies targeting the same modification from various vendors to confirm consistent patterns.

  • Mass spectrometry correlation: Compare antibody-based detection with mass spectrometry quantification of histone modifications.

  • Modified vs. unmodified controls: Include both acetylated and non-acetylated histone H3 controls to demonstrate specificity.

How does H3K14 acetylation interact with other histone modifications in gene regulation?

H3K14 acetylation participates in complex cross-talk with other histone modifications:

  • Synergy with S10 phosphorylation: H3S10 phosphorylation combined with H3K14 acetylation (phosphoacetylation) creates a high-affinity binding site for 14-3-3 proteins. This binding is necessary for the transcriptional activation of specific genes, including HDAC1 .

  • Antagonism with K9 methylation: While H3K9 methylation is typically associated with gene repression, H3K14ac can co-exist with K9 methylation, creating a "phosphomethylation" state when S10 is also phosphorylated. This suggests that acetylation and phosphorylation can synergize to overcome repressive methylation marks .

  • Differential susceptibility to deacetylases: The CoREST complex (containing HDAC1 and LSD1) shows marked preference for H3 acetyl-K9 versus acetyl-K14 in nucleosome substrates. This selective resistance to deacetylation may help maintain active chromatin states .

These interactions constitute part of the "binary switching model" where one modification can influence the recognition or establishment of another, creating a dynamic code for transcriptional regulation.

What is the role of 14-3-3 proteins in mediating H3K14ac function?

14-3-3 proteins are crucial mediators of histone phosphoacetylation signals:

  • Binding specificity: 14-3-3 proteins (particularly 14-3-3ζ and 14-3-3ε) bind to histone H3 in a modification-dependent manner. S10 phosphorylation is necessary for interaction, but additional K14 acetylation significantly increases binding affinity .

  • Recruitment to target genes: ChIP experiments reveal that 14-3-3 proteins are recruited to genes like HDAC1 in an H3S10ph-dependent manner, with recruitment enhanced by additional H3 acetylation .

  • Displacement of repressive factors: 14-3-3 recruitment correlates with dissociation of the repressive binding module HP1γ from chromatin, suggesting a mechanism for switching from repressive to active states .

  • Functional requirement: siRNA-mediated depletion of 14-3-3ζ abolishes transcriptional activation of HDAC1, demonstrating that 14-3-3 proteins are essential mediators of the phosphoacetylation signal .

This represents a mechanistic link between specific histone modifications and the recruitment of effector proteins that drive changes in chromatin structure and gene expression.

How can hydroxamic acid-based approaches be used to study histone deacetylase selectivity for H3K14ac?

Innovative approaches using hydroxamic acid (Hd) warheads have revealed insights into HDAC selectivity:

  • Hydroxamic acid analogs: By incorporating the Lys analog AsuHd (2-aminosuberic acid ω-hydroxamate) into semisynthetic histone H3 at positions 9 and 14, researchers created nucleosomes containing H3K9Hd or H3K14Hd .

  • Inhibition assays: Both H3K9Hd and H3K14Hd nucleosomes inhibit LHC (LSD1-HDAC1-CoREST complex) deacetylase activity with sub-micromolar potencies, while unmodified or acetylated nucleosomes show little effect under the same conditions .

  • Competitive inhibition: H3K14Hd acts as a competitive inhibitor versus peptide substrates for the LHC reaction, providing mechanistic insights into enzyme-substrate interactions .

This approach reveals that the diminished activity of histone deacetylase complexes toward H3K14ac in nucleosomes is not merely due to steric accessibility, suggesting intrinsic recognition properties of the enzyme complex for different modification sites.

How is H3K14ac involved in cellular responses to signaling pathways?

H3K14 acetylation plays important roles in cellular signaling cascades:

  • MAP kinase pathways: The nucleosomal response links H3S10 phosphorylation (often coupled with K14 acetylation) to activation of immediate early genes like c-fos and c-jun in response to growth factors, phorbol esters, phosphatase inhibitors, and protein synthesis inhibitors .

  • Signal-specific kinase involvement: The nucleosomal response is mediated by either the extracellular signal-regulated kinase (ERK) or p38 MAP kinase cascades, depending on the stimulus .

  • Stimulus-induced specificity: Unlike global mitotic phosphorylation of histone H3, stimulus-induced H3 phosphoacetylation targets only a small fraction of nucleosomes, specifically at genes responding to the stimulus .

  • Kinetics correlation: The kinetics of histone H3 phosphoacetylation closely parallel the expression profiles of induced genes, suggesting a direct mechanistic link .

Understanding these pathways provides insights into how extracellular signals are transmitted to chromatin to induce specific gene expression programs.

What is the significance of histone H3's recently discovered enzymatic activity?

Recent research has uncovered unexpected enzymatic properties of histone H3:

  • Copper binding and reduction: The histone H3-H4 tetramer functions as a copper reductase enzyme, containing a copper-binding site involving H3H113 .

  • Functional significance: Mutation of H3H113 to alanine is lethal in Saccharomyces cerevisiae, while H3H113N or H3H113Y mutations result in viable but slow-growing yeast strains .

  • Loss of function correlation: The H3H113N and H3H113Y mutations result in loss of Cu2+ binding in vitro, coinciding with their loss-of-function phenotypes in vivo .

This unexpected enzymatic activity of histone H3 suggests additional roles beyond its structural function in nucleosomes, potentially linking chromatin structure to cellular metabolism and redox homeostasis.

What are the optimal sample preparation methods for preserving and detecting H3K14ac?

For optimal preservation and detection of H3K14ac:

  • Cell harvesting:

    • For adherent cells: Scrape cells in PBS containing phosphatase inhibitors

    • For suspension cells: Collect by centrifugation at 4°C

  • Histone extraction:

    • Acid extraction method: Lyse cells in Triton Extraction Buffer (PBS containing 0.5% Triton X-100, 2mM PMSF, 0.02% NaN₃)

    • Incubate on ice for 10 minutes

    • Centrifuge at 6,500 x g for 10 minutes

    • Resuspend pellet in 0.2N HCl

    • Extract overnight at 4°C

    • Centrifuge and neutralize supernatant with 1/10 volume of 2M NaOH

  • Sample storage:

    • Store extracted histones at -80°C with protease inhibitors, HDAC inhibitors (e.g., sodium butyrate), and phosphatase inhibitors

    • For long-term storage, add 50% glycerol

  • Modification enhancement:

    • Treatment with anisomycin (activates MAP kinase pathway) and TSA (HDAC inhibitor) significantly increases H3 phosphoacetylation levels

    • This combination can be used as a positive control for antibody validation

How can I quantitatively analyze histone modification patterns using the HIST1H3A (Ab-14) antibody?

For quantitative analysis of histone modifications:

  • Western blot quantification:

    • Use total H3 antibody for normalization

    • Include a standard curve of recombinant histones

    • Analyze bands using densitometry software

    • Present results as ratio of H3K14ac to total H3

  • ChIP-seq analysis:

    • Normalize to input control and IgG background

    • Use spike-in controls (e.g., Drosophila chromatin) for cross-sample normalization

    • Apply appropriate statistical methods for peak calling

    • Compare enrichment at specific genomic features (promoters, enhancers, etc.)

  • Multiplex bead-based assays:

    • Use Histone H3 Total Ab-conjugated bead set for normalization across samples

    • Test multiple sample concentrations (50-800 ng) to ensure measurements fall within detection limits

    • Present results as ratio of specific modification to total H3

  • Immunofluorescence quantification:

    • Use DAPI staining to define nuclear regions

    • Measure mean fluorescence intensity within nuclear regions

    • Normalize to total H3 staining in parallel samples

    • Apply appropriate statistical tests for population analysis

These quantitative approaches enable robust comparative analysis of histone modification levels across different experimental conditions.

Quick Inquiry

Personal Email Detected
Please use an institutional or corporate email address for inquiries. Personal email accounts ( such as Gmail, Yahoo, and Outlook) are not accepted. *
© Copyright 2025 TheBiotek. All Rights Reserved.