SMYD2 Protein, Human (sf9, His)

The SMYD2 protein is a multifunctional methyltransferase that can modify histones and non-histone proteins, including p53/TP53 and RB1. Notably, it trimethylates H3 at "Lys-4" (H3K4me3), which is critical for gene activation. SMYD2 Protein, Human (sf9, His) is the recombinant human-derived SMYD2 protein, expressed by Sf9 insect cells , with N-His labeled tag. The total length of SMYD2 Protein, Human (sf9, His) is 433 a.a., with molecular weight of ~48 kDa.

SMYD2 protein, a versatile protein-lysine N-methyltransferase, exhibits the capability to methylate both histones and non-histone proteins, such as p53/TP53 and RB1. Notably, it specifically trimethylates histone H3 at 'Lys-4' (H3K4me3) in vivo, a crucial modification associated with gene activation. The enzymatic activity of SMYD2 requires interaction with HSP90alpha, further highlighting its functional dependence on cellular regulatory networks. Strikingly, SMYD2 demonstrates heightened methyltransferase activity on p53/TP53, where it monomethylates 'Lys-370,' leading to a consequential reduction in DNA-binding activity and subsequent transcriptional regulation. Furthermore, SMYD2 plays a role in the epigenetic modification of RB1 by monomethylating 'Lys-860,' showcasing its broad impact on both histone and non-histone proteins, thereby contributing to the intricate landscape of epigenetic regulation within the cellular milieu.

Human

Sf9 insect cells

N-His

Q9NRG4 (M1-H433)

56950  [NCBI]

Approximately 48 kDa

Greater than 95% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.