Recombinant fusion protein of human Pr-Set7. The exact sequence is proprietary.
Conjugation:
Unconjugated
Alternative Names:
KMT5A, PRSET7, SET07, SET8, N-lysine methyltransferase SETD8, H4-K20-HMTase SETD8, Histone-lysine N-methyltransferase SETD8, Lysine N-methyltransferase 5A, PR/SET domain-containing protein 07, PR-Set7, PR/SET07, SET domain-containing protein 8
SET domain-containing lysine methyltransferase 8 (SET8), also known as PR/SET domain-containing protein 7 (PR/SET7), is a member of a family of histone lysine methyltransferases, each of which contains a conserved catalytic SET domain originally identified in Drosophila Su[var]3-9, Enhancer of zeste, and Trithorax proteins. SET8 is a single-subunit enzyme that mono-methylates histone H4 on Lys20, preferably on nucleosomal substrates. SET8 protein levels and Histone H4 Lys20 methylation are cell cycle regulated, both increasing in S phase and peaking at G2/M phase. SET8 interacts with the PCNA protein, associates with sites of active DNA synthesis, and is required for DNA replication and genome stability during S phase. Inhibition of SET8 using shRNA or siRNA results in arrest of replication forks, induction of double-stranded DNA breaks, and a Chk1-mediated cell-cycle arrest in S and G2/M phases of the cell cycle. Furthermore, SET8 methylates p53 on Lys382, down regulating the pro-apoptotic and checkpoint activation functions of p53. In response to DNA damage, SET8 expression levels decrease, allowing p53 to activate checkpoints and/or apoptosis. Both the methylation of histone H4 Lys20 and p53 appear to be important for the functions of SET8 in S phase.
