# Histone Antibody: Definition, Applications, and Key Considerations

## Introduction to Histone Antibodies

### What Are Histone Antibodies?

A histone antibody is an immunoglobulin molecule that specifically recognizes and binds to one or more histone proteins, or to a specific post-translational modification (PTM) on a histone protein. In molecular biology, these antibodies are indispensable tools for studying [chromatin structure](/knowledge/molecular-biology/chromatin-structure), gene regulation, and [epigenetic mechanisms](/knowledge/molecular-biology/epigenetic-mechanisms). They allow researchers to ask precise questions: Is a particular gene promoter enriched for acetylated histone H3? Does a repressive methylation mark spread across a silenced locus? Is a histone variant incorporated at an active enhancer?

Histone antibodies differ from most other protein-targeting antibodies in a critical way: their epitopes are often small chemical groups—a methyl group, an acetyl group, a phosphate group—attached to specific lysine, arginine, or serine residues. This means the antibody must distinguish not only between different histone proteins but also between different modification states at the same residue. A well-validated histone antibody can discriminate between histone H3 dimethylated at lysine 4 (H3K4me2) and trimethylated at the same residue (H3K4me3), despite the two marks differing by only a single methyl group.

The targets of histone antibodies fall into two broad categories. The first category includes antibodies raised against unmodified histone proteins or their variants, such as pan-H3 antibodies that recognize total histone H3 regardless of modification state. The second, and far more common, category includes modification-specific antibodies that recognize a particular PTM at a defined residue. These antibodies are the workhorses of epigenetics research, enabling the mapping of [Histone Code](/knowledge/molecular-biology/histone-code) marks across genomes.

### Why Study Histone Modifications?

Histone modifications are not merely passive structural features of chromatin; they are dynamic regulatory signals that control DNA-templated processes including transcription, replication, repair, and recombination. Acetylation of lysine residues neutralizes the positive charge on histone tails, weakening histone-DNA contacts and promoting a more open chromatin conformation. Methylation can signal either activation or repression depending on which residue is modified and to what degree. Phosphorylation of serine and threonine residues on histone tails is tightly linked to cell cycle progression and [DNA damage response](/knowledge/molecular-biology/dna-damage-response).

Understanding these modifications is central to modern biology. Misregulation of histone-modifying enzymes—such as [Histone Acetyltransferase](/knowledge/molecular-biology/histone-acetyltransferase) (HAT) enzymes or histone deacetylases (HDACs)—is implicated in cancer, developmental disorders, and neurological disease. Histone antibodies provide the means to track these modifications in space and time, whether across the genome, within a single nucleus, or in patient samples. Without high-quality histone antibodies, the field of epigenetics as we know it would not exist.

## Histone Structure and Modification Landscape

### Core Histones and Linker Histones

The fundamental repeating unit of chromatin is the nucleosome, which consists of approximately 147 base pairs of DNA wrapped around a [Histone Octamer](/knowledge/molecular-biology/histone-octamer) composed of two copies each of the core histones H2A, H2B, H3, and H4. Each core histone has a globular domain that forms the octamer core and a flexible N-terminal tail that protrudes from the nucleosome. These tails, typically 20–35 amino acids long, are the primary sites of post-translational modification, although modifications also occur within the globular domains. The [Histone Structure](/knowledge/molecular-biology/histone-structure) is highly conserved across eukaryotes, reflecting its fundamental role in genome packaging.

A fifth histone, linker histone H1, binds to the DNA between nucleosomes and facilitates higher-order chromatin folding. H1 is also subject to post-translational modifications, though these are less extensively studied than those on core histones. Histone variants—such as H3.3, H2A.Z, and CENP-A—replace canonical histones at specific genomic locations and carry their own modification patterns. Antibodies have been generated against many of these variants, allowing researchers to track their deposition and function.

The N-terminal tails of histones are rich in basic residues, particularly lysine and arginine, which are the primary targets for modification. The modification landscape is complex: lysine residues can be acetylated, mono-, di-, or trimethylated, or ubiquitinated; arginine residues can be mono- or dimethylated (symmetrically or asymmetrically); and serine/threonine residues can be phosphorylated. Each modification is deposited by a specific writer enzyme, removed by a specific eraser enzyme, and recognized by specific reader proteins that translate the modification into a biological outcome.

### Common Histone Modifications

The most extensively studied histone modifications include the following:

**Acetylation.** Lysine acetylation neutralizes the positive charge on the histone tail, reducing its affinity for negatively charged DNA. Acetylation of H3K27 (H3K27ac) and H3K9 (H3K9ac) is associated with active promoters and enhancers. Histone acetyltransferases such as p300/CBP and GCN5 deposit acetyl groups, while HDACs remove them.

**Methylation.** Lysine methylation does not alter the charge of the residue but changes its hydrophobicity and hydrogen-bonding capacity. The methylation state—mono-, di-, or trimethyl—is functionally significant. H3K4me3 marks active promoters, H3K36me3 marks the bodies of actively transcribed genes, H3K9me3 marks constitutive heterochromatin, and H3K27me3 marks facultative heterochromatin at Polycomb-repressed loci. [Histone Methylation](/knowledge/molecular-biology/histone-methylation) is deposited by histone methyltransferases (e.g., SUV39H1 for H3K9, EZH2 for H3K27) and removed by demethylases (e.g., LSD1, JmjC-domain proteins).

**Phosphorylation.** Serine and threonine phosphorylation on histone tails is dynamic and often marks active processes. H3S10 phosphorylation is associated with mitotic chromosome condensation and immediate-early gene activation. H2AX phosphorylation at Ser139 (γH2AX) is a well-established marker of DNA double-strand breaks.

**Ubiquitination.** Monoubiquitination of H2BK120 (in mammals) and H2AK119 are linked to transcription elongation and Polycomb repression, respectively.

**Citrullination.** Deimination of arginine to citrulline by PAD4 enzymes antagonizes arginine methylation and is implicated in gene regulation and neutrophil extracellular trap formation.

The sheer diversity of modifications, combined with the combinatorial possibilities on a single histone tail, forms the basis of the [Histone Code](/knowledge/molecular-biology/histone-code) hypothesis. This hypothesis proposes that specific combinations of modifications are read by effector proteins to produce distinct biological outputs. Histone antibodies are the primary tools for testing this hypothesis experimentally.

## How Histone Antibodies Are Generated

### Monoclonal vs. Polyclonal Antibodies

Histone antibodies are produced using two general strategies, each with distinct advantages and limitations.

**Polyclonal antibodies** are generated by immunizing an animal—typically a rabbit, goat, or chicken—with a histone peptide or protein. The animal's immune system mounts a response against multiple epitopes on the immunogen, and the resulting antiserum contains a heterogeneous mixture of antibodies recognizing different epitopes. Polyclonal antibodies are often highly sensitive because they can bind multiple sites on the target, but they are limited by finite supply and batch-to-batch variability. Once the animal is exhausted, the antibody is gone forever unless a new animal is immunized.

**Monoclonal antibodies** are produced by fusing antibody-producing B cells from an immunized animal (usually a mouse or rat) with immortal myeloma cells to create hybridomas. Each hybridoma clone secretes a single antibody species recognizing a single epitope. Monoclonal antibodies offer unlimited supply, consistent quality, and defined specificity. However, they can be more sensitive to epitope masking in certain applications and may fail to recognize the target in some species due to sequence divergence at the epitope.

For [histone modification](/knowledge/molecular-biology/histone-modification)-specific antibodies, both strategies face a common challenge: the immune system tends to respond more strongly to the peptide backbone than to the small chemical modification. This necessitates careful antigen design and rigorous screening.

### Designing Immunogens for Modified Histones

The design of the immunogen is the single most important factor determining the quality of a modification-specific histone antibody. The standard approach uses synthetic peptides corresponding to the histone tail sequence surrounding the modified residue. The peptide is typically 15–25 amino acids long, with the modified residue placed centrally to maximize exposure.

Several design parameters are critical:

**Peptide length and sequence.** The peptide must include sufficient flanking sequence to present the modification in its native context. For example, an antibody against H3K4me3 might use a peptide spanning residues 1–15 of histone H3: ARTKQTARKSTGGKA, with trimethylated lysine at position 4. Flanking residues contribute to the epitope, and antibodies raised against short peptides may fail to recognize the full-length protein.

**Modification type and carrier conjugation.** The modified lysine analog must be chemically stable and structurally similar to the natural modification. For methylation, this is straightforward: methylated lysine analogs are commercially available. For acetylation, the acetyl group is introduced during peptide synthesis. The peptide is conjugated to a carrier protein—keyhole limpet hemocyanin (KLH) or bovine serum albumin (BSA)—to enhance immunogenicity. The conjugation chemistry must not alter the modified residue.

**Affinity purification.** After immunization, the antiserum is affinity-purified against the modified peptide to enrich for modification-specific antibodies. Critically, the purified antibody must also be negatively selected against the unmodified peptide to remove antibodies that recognize the peptide backbone regardless of modification state. This double-selection strategy is essential for producing antibodies that genuinely discriminate between modified and unmodified histones.

**Validation against related modifications.** A high-quality antibody must be tested for cross-reactivity against closely related modifications. An antibody raised against H3K4me3 must be tested against H3K4me1, H3K4me2, H3K9me3, and H3K27me3, among others. This validation is typically performed using peptide arrays or dot blots containing panels of modified and unmodified peptides.

## Mechanism of Antigen Recognition

### Epitope Specificity

The binding of a histone antibody to its target is governed by the same principles that govern all antibody-antigen interactions: shape complementarity, hydrogen bonding, van der Waals forces, and electrostatic interactions. The antibody's paratope (the antigen-binding site) recognizes a specific epitope on the histone—typically 5–10 amino acids in length, with the modified residue playing a dominant role in binding energy.

For modification-specific antibodies, the modified residue is usually the central contact point. The methyl groups on a trimethylated lysine fit into a hydrophobic pocket in the antibody's binding site, and the surrounding amino acids make additional contacts that confer sequence specificity. This explains why an antibody raised against H3K4me3 generally does not recognize H3K9me3: although both are trimethylated lysines, the flanking sequences differ, and the antibody's binding site is shaped to accommodate the H3K4 context.

The affinity of histone antibodies varies widely. High-quality antibodies typically have dissociation constants (Kd) in the low nanomolar to picomolar range. This high affinity is necessary for applications like chromatin immunoprecipitation (ChIP), where the antibody must capture its target from a complex mixture of chromatin fragments.

### Cross-Reactivity and Its Causes

Cross-reactivity—the binding of an antibody to an unintended target—is a persistent problem with histone antibodies. Several factors contribute:

**Sequence homology.** Histone proteins are highly conserved across species, and even across histone variants within a species. An antibody raised against human H3 may cross-react with H3 from mouse, yeast, or plants. This is often desirable, but it can be problematic if the antibody also recognizes a histone variant with a different function.

**Shared modification motifs.** Antibodies raised against one modification may recognize the same modification in a different sequence context. For example, an antibody against H3K27me3 might cross-react with H3K9me3 if the flanking sequences are sufficiently similar. This is a particular risk for antibodies raised against short peptides.

**Modification state cross-reactivity.** An antibody raised against H3K4me3 may also recognize H3K4me2, albeit with lower affinity. This is because the trimethylated lysine presents a surface that partially overlaps with the dimethylated form. The extent of this cross-reactivity depends on the antibody clone and must be empirically determined.

**Off-target proteins.** Some histone antibodies cross-react with non-histone proteins that contain similar sequence motifs. This is more common with polyclonal antibodies, which contain multiple antibody species.

The practical consequence of cross-reactivity is that histone antibodies must be validated in every application and every cell type in which they are used. An antibody that works perfectly in Western blot may fail in ChIP, and an antibody that is specific in HeLa cells may cross-react in mouse embryonic stem cells.

## Applications in Research and Diagnostics

### Chromatin Immunoprecipitation (ChIP)

Chromatin immunoprecipitation is the most important application of histone antibodies. ChIP allows researchers to determine the genomic location of a specific [histone modification](/knowledge/molecular-biology/histone-modification) or histone variant. The procedure involves several steps:

1. **Cross-linking.** Cells are treated with formaldehyde (typically 1% for 10 minutes at room temperature) to covalently cross-link proteins to DNA. This preserves the in vivo [chromatin structure](/knowledge/molecular-biology/chromatin-structure).

2. **Cell lysis and chromatin fragmentation.** Cells are lysed, and chromatin is sheared into fragments of 200–600 base pairs, typically by sonication or enzymatic digestion with micrococcal nuclease.

3. **Immunoprecipitation.** The fragmented chromatin is incubated with the histone antibody bound to protein A/G beads. The antibody captures chromatin fragments containing its target modification.

4. **Washing.** Beads are washed extensively to remove non-specifically bound chromatin. Typical washes include low-salt buffer (0.1% SDS, 1% Triton X-100, 2 mM EDTA, 150 mM NaCl, 20 mM Tris-HCl pH 8.0), high-salt buffer (same but with 500 mM NaCl), and LiCl buffer.

5. **Elution and reverse cross-linking.** Bound chromatin is eluted, and the cross-links are reversed by heating at 65°C for 4–6 hours in the presence of proteinase K.

6. **DNA purification and analysis.** The purified DNA is analyzed by quantitative PCR (ChIP-qPCR), microarray (ChIP-chip), or high-throughput sequencing (ChIP-seq).

The success of ChIP depends critically on antibody quality. A non-specific antibody will pull down background chromatin, obscuring the true enrichment signal. The amount of antibody required varies by application: ChIP typically uses 1–5 µg of antibody per immunoprecipitation, while ChIP-seq may require more.

### Western Blot and Immunofluorescence

Histone antibodies are also used for protein-level detection. In Western blotting, histones are extracted from cells using acid extraction (0.2 M HCl) or a commercial [histone extraction](/knowledge/molecular-biology/histone-extraction) kit, separated by SDS-PAGE, transferred to a membrane, and probed with the antibody. Histones are small proteins (11–15 kDa for core histones), so they require high-percentage gels (15% or gradient gels) and appropriate molecular weight markers. A loading control—typically total histone H3 or H4—should always be included to normalize for loading differences.

In immunofluorescence, histone antibodies are used to visualize the spatial distribution of modifications within the nucleus. Cells are fixed, permeabilized, and incubated with the primary antibody, followed by a fluorescently labeled secondary antibody. Confocal microscopy can reveal whether a modification is uniformly distributed or concentrated in specific nuclear domains, such as heterochromatin foci or active transcription factories. This application requires antibodies that recognize their target in the context of fixed chromatin, which is not always the case.

### Clinical Diagnostics

Histone antibodies have an important clinical application: the detection of anti-histone autoantibodies in patient serum. These autoantibodies are a hallmark of drug-induced lupus erythematosus and are also found in a subset of patients with systemic lupus erythematosus (SLE). The presence of anti-histone antibodies, particularly against the H2A-H2B dimer, is a diagnostic criterion for drug-induced lupus.

Detection is typically performed using ELISA. Microtiter plates are coated with purified histones or histone peptides, patient serum is added, and bound antibodies are detected with an enzyme-linked anti-human IgG secondary antibody. The assay is quantitative, and results are reported as ELISA units or optical density values. Positive results must be interpreted in the clinical context, as anti-histone antibodies can also appear in other autoimmune diseases.

## Methods to Validate Histone Antibodies

### Peptide Competition Assays

The gold standard for validating modification-specific histone antibodies is the peptide competition assay. In this assay, the antibody is pre-incubated with a molar excess of a competing peptide before being used in the application of interest. If the antibody is specific, the modified peptide will block binding, while the unmodified peptide or a peptide with a different modification will not.

For example, to validate an H3K27ac antibody, the antibody would be pre-incubated with:
- The H3K27ac peptide (should block binding)
- The unmodified H3K27 peptide (should not block binding)
- The H3K9ac peptide (should not block binding)
- The H3K27me3 peptide (should not block binding)

The competition can be performed in Western blot, dot blot, or ChIP. A typical competition uses 10–100-fold molar excess of peptide relative to the antibody. This assay is essential for confirming that the antibody recognizes the intended modification and not a related one.

### Use of Modified Cell Lines

Genetic validation provides an independent check on antibody specificity. Several strategies are available:

**Knockout cells.** Cells lacking a specific histone methyltransferase or acetyltransferase will have reduced levels of the corresponding modification. For example, cells lacking the EZH2 methyltransferase (the catalytic subunit of Polycomb repressive complex 2) have dramatically reduced H3K27me3 levels. If an H3K27me3 antibody shows reduced signal in EZH2-knockout cells compared to wild-type cells, this confirms that the antibody recognizes H3K27me3.

**Knock-in mutations.** Cells with mutations in the histone genes themselves can be used. For example, a cell line expressing only H3 with a K27M mutation (as found in diffuse intrinsic pontine glioma) will have globally reduced H3K27me3. Antibodies against H3K27me3 should show reduced binding in these cells.

**Overexpression of erasers.** Overexpressing a demethylase such as KDM6A/UTX will reduce H3K27me3 levels. Conversely, overexpressing a methyltransferase will increase modification levels. These perturbations provide additional validation.

**Dot blots with recombinant histones.** Recombinant histones with defined modifications, produced by native chemical ligation or expressed in systems that install specific modifications, can be spotted onto membranes and probed with the antibody. This provides a direct test of specificity.

## Common Pitfalls and Troubleshooting

### Dilution and Storage Issues

One of the most common mistakes students make is using the wrong antibody dilution. Histone antibodies are supplied with a recommended dilution range, but the optimal dilution must be determined empirically for each application. A dilution that works for Western blot (e.g., 1:1000) may be too dilute for ChIP (which typically requires 1–5 µg per reaction) or too concentrated for immunofluorescence (which may require 1:200 or lower).

Storage is equally critical. Most histone antibodies should be stored at –20°C in aliquots to avoid repeated freeze-thaw cycles, which degrade antibody activity. Some antibodies are supplied in glycerol and can be stored at –20°C without freezing. Always check the manufacturer's instructions. Antibodies that have been improperly stored may show reduced signal or increased background.

### Interpreting ChIP-qPCR Data

ChIP-qPCR results are often misinterpreted by students. The key metric is enrichment relative to a negative control region, not the raw Ct value. A common mistake is to compare the Ct value of the target region to that of an input sample without accounting for the dilution factor of the input.

The standard analysis method is the percent input method:

1. Calculate the input dilution factor. If the input is 1% of the total chromatin, the dilution factor is 100.
2. For each sample, calculate the percent input using the formula: Percent input = 100 × 2^(Ct_input_adjusted – Ct_ChIP), where Ct_input_adjusted = Ct_input – log2(dilution factor).
3. Compare the percent input at the target region to that at a negative control region (e.g., a gene desert or an unmodified region).

A positive result shows significantly higher percent input at the target region than at the negative control. Students often forget to include a negative control antibody (e.g., normal IgG) to assess non-specific background.

### Crosstalk Between Modifications

Histone modifications do not occur in isolation; they influence each other. This crosstalk can confound antibody-based experiments. For example, H3K4me3 and H3K27ac often co-occur at active promoters. If an H3K4me3 antibody pulls down chromatin, it may indirectly enrich for H3K27ac because the two modifications are on the same nucleosome. This does not mean the H3K27ac antibody is cross-reactive; it reflects the biological co-occurrence of the modifications.

Conversely, some modifications are mutually exclusive. H3K27me3 and H3K27ac cannot coexist on the same histone tail because they modify the same residue. However, they can coexist on different H3 copies within the same nucleosome. This "bivalent" state is important in embryonic stem cells.

Students should also be aware that antibody binding can be affected by neighboring modifications. A modification adjacent to the epitope can sterically hinder antibody binding, leading to false-negative results. This is known as "epitope masking" and is a particular problem in ChIP, where chromatin is cross-linked and fragmented.

## Summary and Best Practices

### Key Takeaways

Histone antibodies are powerful but demanding tools. Their quality determines the reliability of your data, and their validation is non-negotiable. The following principles should guide your work:

1. **Always validate your antibody.** Test it by peptide competition, dot blot, or Western blot before using it in ChIP or immunofluorescence. A new lot number requires re-validation.

2. **Use appropriate controls.** Include a negative control antibody (normal IgG), a positive control antibody (e.g., anti-H3 for total histone), and an input sample in every ChIP experiment.

3. **Optimize conditions for each application.** The optimal antibody concentration, wash stringency, and blocking conditions differ between Western blot, ChIP, and immunofluorescence.

4. **Be aware of cross-reactivity.** Know the modification states and sequence contexts your antibody might recognize. Check the manufacturer's validation data, but verify independently.

5. **Consider the biological context.** Histone modifications are dynamic and cell-type-specific. A modification that is abundant in one cell type may be nearly absent in another.

6. **Document everything.** Record lot numbers, dilutions, and validation results. Reproducibility depends on meticulous record-keeping.

### Checklist for Successful Experiments

Before starting any histone antibody experiment, work through this checklist:

- [ ] Have you confirmed the antibody's specificity by peptide competition or dot blot?
- [ ] Have you checked the antibody's cross-reactivity against related modifications?
- [ ] Is the antibody validated for your application (ChIP, Western blot, IF)?
- [ ] Have you included appropriate [positive and negative controls](/blog/guides/positive-and-negative-controls-how-to-choose-and-use-them)?
- [ ] Have you optimized the antibody concentration for your application?
- [ ] Have you included a loading control (e.g., total H3) for Western blot?
- [ ] Have you included an input sample and negative control region for ChIP?
- [ ] Have you checked the antibody's lot number and expiration date?
- [ ] Have you stored the antibody correctly and avoided freeze-thaw cycles?
- [ ] Have you considered potential epitope masking by neighboring modifications?

## Frequently Asked Questions

### What is a histone antibody?

A histone antibody is an immunoglobulin that specifically binds to a histone protein, a histone variant, or a specific post-translational modification on a histone. These antibodies are essential tools in epigenetics research, used to detect and localize histone modifications in cells and across genomes.

### How do histone antibodies work?

Histone antibodies work through the standard antibody-antigen interaction. The antibody's variable region recognizes a specific epitope—typically 5–10 amino acids on a histone tail, with the modified residue (e.g., methylated lysine) playing a central role in binding. The antibody binds with high affinity and specificity, allowing researchers to capture or visualize the target modification.

### What are histone antibodies used for?

Histone antibodies are used in chromatin immunoprecipitation (ChIP) to map the genomic locations of histone modifications, in Western blotting to detect modification levels, in immunofluorescence to visualize nuclear distribution, and in ELISA to detect anti-histone autoantibodies in patient serum for clinical diagnosis.

### Are histone antibodies specific?

High-quality histone antibodies are specific for their intended target, but specificity must be validated. Cross-reactivity with related modifications, other histone proteins, or non-histone proteins is possible. Validation by peptide competition, dot blot, and genetic perturbation is essential before drawing conclusions from experiments.

### What is the difference between monoclonal and polyclonal histone antibodies?

Monoclonal antibodies are derived from a single B cell clone and recognize a single epitope. They offer unlimited supply and consistent quality but may be more sensitive to epitope masking. Polyclonal antibodies are derived from multiple B cell clones and recognize multiple epitopes. They are often more sensitive but are limited in supply and subject to batch-to-batch variability.

### Why do histone antibodies sometimes fail in ChIP?

Histone antibodies can fail in ChIP for several reasons: the epitope may be masked by cross-linked proteins or neighboring modifications; the antibody may not recognize its target in the context of cross-linked chromatin; the antibody may have low affinity, leading to loss of chromatin during washing; or the antibody may be non-specific, pulling down background chromatin. Optimization of antibody amount, wash stringency, and chromatin fragmentation can help.

### Can histone antibodies detect histone modifications in living cells?

Standard histone antibodies cannot penetrate living cells. However, recent advances include nanobodies (single-domain antibodies) that can be expressed intracellularly and used to track modifications in live cells, and intrabodies that recognize specific modifications. These tools are still in development and are not yet widely available for all modifications. For most applications, cells must be fixed or lysed before antibody staining.

## Further Reading

- Kupai A et al. *Analysis of histone antibody specificity directly in sequencing data using siQ-ChIP*. bioRxiv : the preprint server for biology. 2023. [PubMed 36945621](https://doi.org/10.1101/2023.03.08.531745)
- Cornett EM, Dickson BM, Rothbart SB. *Analysis of Histone Antibody Specificity with Peptide Microarrays*. Journal of visualized experiments : JoVE. 2017. [PubMed 28809825](https://doi.org/10.3791/55912)
- Zwiers E et al. *Inhibition of EETosis with an anti-citrullinated histone antibody: a novel therapeutic approach for eosinophilic inflammatory disorders*. Frontiers in immunology. 2025. [PubMed 40051617](https://doi.org/10.3389/fimmu.2025.1533407)
- Hui M et al. *Anti-histone H3.3K36M Antibody is a Highly Sensitive and Specific Immunohistochemistry Marker for the Diagnosis of Chondroblastoma. A Validation Based on Study 136 Cases Comprising Chondroblastoma and its Mimics from Single a Centre in India*. International journal of surgical pathology. 2023. [PubMed 35786027](https://doi.org/10.1177/10668969221105614)
- Jha AK, Sunder A. *An unusual association between anti-histone antibody seropositive SLE, autoimmune hemolytic anemia, and herpetic rash: A case report*. Journal of family medicine and primary care. 2022. [PubMed 35516673](https://doi.org/10.4103/jfmpc.jfmpc_1324_21)
- Prabu G et al. *Monoclonal antibody produced against calf thymus histone*. Hybridoma (2005). 2009. [PubMed 19663700](https://doi.org/10.1089/hyb.2009.0005)

## Related Clinical & Scientific Guides

* [MAPK Pathway: Mechanism, Function, and Clinical Relevance](/knowledge/molecular-biology/mapk-pathway)
* [Mammalian Cell Culture Bioreactors: A Practical Guide](/knowledge/molecular-biology/mammalian-cell-culture-bioreactor)
* [Nucleotide Formation: Biosynthesis and Assembly of DNA/RNA Building Blocks](/knowledge/molecular-biology/nucleotide-formation)