• Target：
• Pan Methylated Lysine

• Immunogen：
• Conjugated Protein

• Specificity：
• The antibody detects endogenous Pan Methylated Lysine protein.

• Formulation：
• PBS, pH 7.4, containing 0.5%BSA, 0.02% sodium azide as Preservative and 50% Glycerol.

• Source：
• Monoclonal, Mouse

• Dilution：
• WB 1:1000-2000 IHC 1:200-500. IF 1:50-200

• Purification：
• The antibody was affinity-purified from mouse ascites by affinity-chromatography using epitope-specific immunogen.

• Storage Stability：
• -15°C to -25°C/1 year(Do not lower than -25°C)

• Background：
• 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. 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.

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