PRMT5 (Protein Arginine Methyltransferase 5) is an important epigenetic enzyme involved in gene expression, RNA processing, DNA repair, and cancer biology. PRMT5 functions together with its cofactor MEP50 (also known as WDR77) to methylate arginine residues on histones and other regulatory proteins, using SAM as a methyl donor.
MTAP deletion can result in the accumulation of MTA, an endogenous metabolic product that modulates PRMT5 activity. This creates a biologically relevant context for studying PRMT5/MEP50 inhibitors in MTAP-deficient cancer models. ICE Bioscience provides an integrated PRMT5 drug discovery platform covering biochemical, biophysical, cell-based, degradation, and in vivo pharmacology studies.
By combining PRMT5/MEP50 binding analysis, enzymatic assays, selectivity profiling, cellular models, degradation assays, and in vivo pharmacology, ICE Bioscience supports integrated evaluation of PRMT5-targeting strategies in MTAP-deficient cancer research.
Study design, assay configuration, model selection, and data layers can be customized according to the mechanism and development stage of the program.
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