Anti-Propionyl-Histone H4 (Lys12) Mouse mAb

Primary Antibodies

Histone H4

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

Stable for 12 months from date of receipt/reconstitution.

Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Lysine propionylation (Kpr), structurally similar to lysine acetylation, is a newly identified reversible modification controlling protein activity. Lysine propionylation is abundant in both prokaryotes and eukaryotes and has been found in wide ranges of proteins including histones and non-histone substrates, such as p53. Similar to acetylation of histone H3 at Lys12, propionylation of histone H4 at Lys12 may play a vital role in the epigenetic modulation, includingchromatin remodeling and transcriptional regulation.

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

Propionyl

Propionylated human histone H4 (Lys12) peptide

Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Lysine propionylation (Kpr), structurally similar to lysine acetylation, is a newly identified reversible modification controlling protein activity. Lysine propionylation is abundant in both prokaryotes and eukaryotes and has been found in wide ranges of proteins including histones and non-histone substrates, such as p53. Similar to acetylation of histone H3 at Lys12, propionylation of histone H4 at Lys12 may play a vital role in the epigenetic modulation, including
chromatin remodeling and transcriptional regulation.