Anti-Butyryl-Histone H3 (Lys18) Rabbit mAb

WB, ICC/IF

Histone H3

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. Butyrylation of lysine, structurally similar to lysine acetylation and propionylation, is a newly identified reversible modification controlling chromosome structure and gene transcription. With integrated proteomic approaches and biochemistry analysis, lysine butyrylation has been well demonstrated in both prokaryotes and eukaryotes. The unique structure and genomic localization of histone lysine butyrylation suggest that it is mechanistically and functionally different from histone lysine acetylation. Butyrylation of histone H3 at Lys18 may play a vital role in the epigenetic modulation, including chromatin remodeling and DNA transcriptional regulation.

Anti-Butyryl-Histone H3 (Lys18) Rabbit mAb detects histone H3 only when it is butyrylated at Lys18. 

Butyryl

Butyrylated human histone H3 (Lys18) peptide

Histones are subject to a variety of enzyme catalyzed modifications, including acetylation, methylation, phosphorylation, ubiquitylation, etc. Butyrylation of lysine, structurally similar to lysine acetylation and propionylation, is a newly identified reversible modification controlling chromosome structure and gene transcription. With integrated proteomic approaches and biochemistry analysis, lysine butyrylation has been well demonstrated in both prokaryotes and eukaryotes. The unique structure and genomic localization of histone lysine butyrylation suggest that it is mechanistically and functionally different from histone lysine acetylation. Butyrylation of histone H3 at Lys18 may play a vital role in the epigenetic modulation, including chromatin remodeling and DNA transcriptional regulation.