PRDM7 is a zinc finger protein with a PR/SET domain that catalyzes histone H3 lysine 4 trimethylation (H3K4me3), a hallmark of active chromatin . The antibody targets PRDM7 for applications including:
Western blot (WB)
Immunohistochemistry (IHC)
Immunofluorescence (IF/ICC)
Enzyme-linked immunosorbent assay (ELISA)
Key roles of PRDM7 in research include studying:
PRDM7 exhibits distinct enzymatic properties compared to its paralog PRDM9 :
| Parameter | PRDM7 Wild-Type | PRDM7 S357Y Mutant | PRDM9 Wild-Type |
|---|---|---|---|
| Primary Substrate | H3K4me2 → H3K4me3 | H3K4me2 → H3K4me3 | H3K4me2 → H3K4me3 |
| Secondary Activity | None | H3K36 methylation | H3K36 methylation |
| AdoMet K<sub>m</sub> | 1,000 μM | 250 μM | 50 μM |
The S357Y mutation restores PRDM9-like dual substrate specificity, linking evolutionary divergence to functional adaptation .
PRDM7 is implicated in cancer through:
Genomic instability: Loss of PRDM7 disrupts DNA repair mechanisms, promoting oncogenic mutations .
Histone code regulation: Altered H3K4me3 levels correlate with tumor progression in lung adenocarcinoma and leukemia .