货号 | 14117S |
反应种属 | All |
来源宿主 | Rabbit |
应用 | W/IP |
使用方法 | WB(1:1000) IP (1:100) |
供应商 | CST |
背景 | Methylation of lysine residues is a common regulatory posttranslational modification (PTM) that results in the mono-, di-, or tri-methylation of lysine at ε-amine groups by protein lysine methyltransferases (PKMTs). Two PKMT groups are recognized based on structure and catalytic mechanism: class I methyltransferases or seven β 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 (1,2). 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 (3). 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 (4). |
存放说明 | -20C |
A peptide ELISA was used to determine the specificity of Di-Methyl Lysine Motif [dme-K] Rabbit mAb. The figure demonstrates that the antibody is specific to di-methyl lysine and will not cross-react with mono- or tri-methyl lysine or mono- or di-methyl arginine. | |
Western blot analysis of HeLa cells, untreated (-) or treated with adenosine-2,3-dialdehyde (AdOx, 100 μM, 24 hr; +), using Di-Methyl Lysine Motif [dme-K] Rabbit mAb (upper) and GAPDH (D16H11) XP® Rabbit mAb #5174 (lower). |