| Application | Recommended Dilution |
|---|---|
| IHC | 1:50-1:200 |
Histone H3.1, encoded by the HIST1H3A gene cluster, serves as a fundamental component of nucleosome structure and plays a central role in chromatin organization and epigenetic regulation. The lysine 27 position on histone H3 represents one of the most intensively studied epigenetic modification sites, where methylation and acetylation states directly influence gene expression programs, cell fate decisions, and developmental processes. Mutations at this critical residue, particularly the K27M substitution, have emerged as defining features of certain aggressive cancers, making detection of mutated HIST1H3A essential for both basic chromatin biology and translational oncology research.
This recombinant monoclonal antibody, generated from clone 35C11 in rabbit host, offers the reproducibility and consistency that demanding epigenetic studies require. Because the antibody sequence is defined and produced recombinantly, researchers can expect uniform performance across experiments and over time, eliminating the lot-to-lot variability that can complicate longitudinal studies or multi-site collaborations. Affinity chromatography purification ensures high specificity for the target epitope derived from human HIST1H3A.
Validation in immunohistochemistry demonstrates reliable performance in formalin-fixed, paraffin-embedded human gastric cancer tissue, with optimal staining achieved at 1:100 dilution using citrate buffer antigen retrieval. This tissue-based validation confirms the antibody's utility for examining histone H3 mutation status in clinical specimens and tumor samples. The antibody is also validated for ELISA applications, providing flexibility for quantitative detection workflows.
Researchers investigating chromatin dynamics, histone mutations in cancer, or epigenetic mechanisms in human samples will find this antibody a dependable tool for their experimental needs.
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