Pan Methylated Lysine Monoclonal Antibody (Mix)

Gel pack with blue ice.

Methylation of lysine residues is a common regulatory posttranslational modification (PTM) that results in the mono-, di-, or tri-methylation of lysine at epsilon-amine groups by protein lysine methyltransferases (PKMTs). Two PKMT groups are recognized based on structure and catalytic mechanism: class I methyltransferases or seven beta strand enzymes, and SET domain-containing class V methyltransferases. Both use the methyl donor S-adenosyl-L-methionine to methylate histone and non-histone proteins. Class I methyltransferases methylate amino acids, DNA, and RNA. Six methyl-lysine-interacting protein families are distinguished based on binding domains: mBT, PHD finger, Tudor, PWWP, WD40 repeat, and chromodomains. Many of these display differential binding preferences based on lysine methylation state. KDM1 subfamily lysine demethylases catalyze demethylation of mono- and di-methyl lysines, while 2-oxoglutarate-dependent JmjC (KDM2-7) subfamily enzymes also modify tri-methyl lysine residues.

Conjugated Protein

The antibody was affinity-purified from mouse ascites by affinity-chromatography using epitope-specific immunogen

The antibody detects endogenous Pan Methylated Lysine protein.