Anti-Acetyl-Histone H4 (Lys12) Mouse mAb

PTM BIO

Anti-Acetyl-Histone H4 (Lys12) Mouse mAb

5

Anti-Acetyl-Histone H4 (Lys12) Mouse mAb detects histone H4 only when it is acetylated at Lys12.

ImmunoFluorescence, Western Blot, ChIP Chromatin ImmunoPrecipitation, ImmunoCytoChemistry, ImmunoHistoChemistry Paraffin

WB, IHC-P, ICC/IF, ChIP

Antibody

Research Use Only

Monoclonal

9A1

Unconjugated

Mouse

IgG

Histone H4

Histone post-translational modifications (PTMs) are key mechanisms of epigenetics that modulate chromatin structures, termed as “histone code”. The PTMs on histone including acetylation, methylation, Phosphorylatedrylation and novel acylations directly affect the accessibility of chromatin to transcription factors and other epigenetic regulators, altering genome stability, gene transcription, etc. Histone acetylation occurs primarily at multiple lysine residues on the amino-terminal of core histones, in response to various stimuli and plays vital roles in the regulation of gene expression, DNA damage repair, chromatin dynamics, etc. Mostly, histone H2A is primarily acetylated at Lys5, 9, 15, and 36; H2B is primarily acetylated at Lys5, 12, 15, 16, and 20. Histone H3 is primarily acetylated at Lys4, 9, 14, 18, 23, 27, 56, and 79. Histone H4 is primarily acetylated at Lys5, 8, 12, 16, and 20. Histone acetyltransferases (HATs) and histone deacetylases (HDACs) are major regulating factors.

Stable for 12 months from date of receipt/reconstitution.

Human, Mouse, Rat

Human, Mouse, Rat

Protein G and immunogen affinity purified

Store at -20°C. Avoid freeze/thaw cycles.

12352203