| Application | Recommended Dilution |
|---|---|
| IF | 1:50-1:200 |
| FC | 1:50-1:200 |
KDM5A, also known as JARID1A or RBP2, functions as a histone demethylase that specifically removes methyl groups from tri- and di-methylated lysine 4 on histone H3. This enzymatic activity plays a central role in transcriptional regulation, with KDM5A serving as a key modulator of gene expression programs involved in cell cycle control, differentiation, and cellular senescence. Originally identified through its interaction with the retinoblastoma tumor suppressor protein, KDM5A has emerged as an important factor in cancer biology, where its dysregulation contributes to altered epigenetic landscapes in multiple tumor types.
This recombinant monoclonal antibody, clone 23B11, offers the reproducibility and consistency that demanding epigenetics research requires. Developed using recombinant technology with a defined sequence, it eliminates the lot-to-lot variability that can compromise longitudinal studies or multi-site collaborations. The rabbit IgG format, raised against a synthetic peptide derived from human KDM5A, provides reliable detection in human samples.
Validation studies demonstrate robust performance in both immunofluorescence and flow cytometry applications. Immunofluorescence analysis of HeLa cells reveals clear nuclear localization consistent with KDM5A's chromatin-associated function, with optimal staining achieved at dilutions between 1:50 and 1:200. Flow cytometry validation in HeLa cells confirms specific detection with distinct signal separation from isotype controls, supporting quantitative analysis of KDM5A expression at the single-cell level.
For researchers investigating histone modification dynamics, transcriptional regulation, or the epigenetic mechanisms underlying disease states, this antibody provides a dependable tool for characterizing KDM5A expression and localization across experimental systems.
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