Anti-Propionyl-Histone H2A (Lys125) Rabbit mAb

Primary Antibodies

Histone H2A

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 (Kprop) is 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 H2A at Lys125 may play a vital role in the epigenetic modulation, including chromatin remodeling and transcriptional regulation.

Anti-Propionyl-Histone H2A (Lys125) Rabbit mAb detects histone H2A only when it is propionylated at Lys125, but not the crotonylated and unmodified H2A peptide at Lys125.

Propionyl

Propionylated human histone H2A (Lys125) peptide

Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Lysine propionylation (Kprop) is 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 H2A at Lys125 may play a vital role in the epigenetic modulation, including chromatin remodeling and transcriptional regulation.