Anti-Acetyl-Histone H4 (Lys12) Rabbit mAb

Histone & Histone Modification Antibodies

Ambient temperature

11

Histone post-translational modifications (PTMs), known as the “histone code”, are key mechanisms of epigenetics that modulate chromatin structures. The PTMs on histone including acetylation, methylation, phosphorylation, and novel acylations directly affect the accessibility of chromatin to transcription factors and other epigenetic regulators, altering genome stability and gene transcription. Histone acetylation, tightly controlled by the opposing action of histone acetyltransferases (HATs) and histone deacetylases (HDACs), occurs primarily at lysine residues on the N-terminal tails of histones H2A (Lys5, 9, and 15), H2B (Lys5, 12, 15, 16, and 20), H3 (Lys4, 9, 14, 18, 23, 27, and 36), and H4 (Lys5, 8, 12, 16, and 20), and plays vital roles in the regulation of gene expression, DNA damage repair, chromatin dynamics, etc.

Anti-Acetyl-Histone H4 (Lys12) Rabbit mAb detects histone H4 only when it is acetylated at Lys12. This antibody has been shown to selectively recognize acetylated H4 peptide at Lys12, but not the structurally similar crotonylated, butyrylated, propionylated, β-hydroxybutyrylated, or 2-hydroxyisobutyrylated H4 peptide at Lys12.

Acetyl

Acetylated human histone H4 (Lys12) peptide

Stable for 12 months from date of receipt/reconstitution.

Nucleus