| Application | Recommended Dilution |
|---|---|
| WB | 1:500-1:2000 |
| IHC | 1:50-1:200 |
| FC | 1:50-1:200 |
EHMT2, also known as G9a, is a critical histone methyltransferase responsible for mono- and dimethylation of histone H3 at lysine 9, a modification central to transcriptional silencing and heterochromatin formation. This enzyme plays essential roles in embryonic development, cell differentiation, and the maintenance of cellular identity. Dysregulation of EHMT2 has been implicated in various cancers and developmental disorders, making it a compelling target for epigenetic research and therapeutic development.
This recombinant monoclonal antibody, clone 4A2, offers the reliability that demanding epigenetic studies require. Produced using recombinant technology in rabbit host, it provides sequence-defined consistency between lots, ensuring your experimental results remain comparable across extended research timelines. The antibody was raised against a synthetic peptide derived from human EHMT2 and purified by affinity chromatography for optimal specificity.
Validation across multiple platforms demonstrates this antibody's experimental versatility. Western blot analysis in HEK293 and HeLa whole cell lysates reveals bands at 160-170 kDa, larger than the predicted 132 kDa molecular weight. This size difference likely reflects post-translational modifications, including glycosylation and automethylation events characteristic of active EHMT2. Immunohistochemistry performed on paraffin-embedded human colorectal cancer tissue shows clear nuclear staining patterns consistent with EHMT2's chromatin-associated function. Flow cytometry analysis using MCF-7 cells further confirms the antibody's utility for quantitative single-cell studies of this methyltransferase.
Whether investigating epigenetic mechanisms in cancer biology, studying chromatin dynamics during differentiation, or exploring EHMT2 as a therapeutic target, this antibody provides the validated performance needed for meaningful discoveries in histone methylation research.
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