Anti-Acetylated Proteins antibody produced in rabbit

Protein acetylation on lysine is a reversible protein modification that regulates protein functions. Histone acetylation at N-epsilon-lysine residues can destabilize the nucleosome structure and render DNA more accessible to transcription factors. Protein acetylation controls the function of transcription factors such as p53, GATA-1, E2F, TFIIEb, TFIIF, and EKLF.
Staining of histone H4 in immunoblotting is specifically inhibited with acetylated histone H4 immunizing peptide (human, amino acids 1-20 with N-epsilon-acetylated lysines at positions 5, 8, 12, and 16). No inhibition with the non-acetylated histone H4 peptide (human, amino acids 1-20) is observed.

Reacts with several acetylated proteins (e.g., acetylated histone H4 [12 kDa], acetylated H1 and H2b and acetylated BSA). Does not recognize acetylated histone H3.

synthetic acetylated peptide corresponding to the N-terminus of human histone H4 (amino acids 1-20, with N-ε-acetylated lysines at positions 5,8,12 and 16) conjugated to KLH.

Rabbit anti-acetylated protein antibody can be used for microarrays, indirect immunofluorescence (1:1,000) and western blot (1:1,000) assays.

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% BSA and 15 mM sodium azide.

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