DATASHEET
Host:
Mouse
Target Protein:
H3K27ac
Clonality:
Monoclonal
Isotype:
IgG1
Source:
Monoclonal antibody raised in mouse against histone H3 acetylated at lysine 27 (H3K27ac), using a KLHconjugated synthetic peptide.
Purification:
Protein A purified monoclonal antibody in PBS containing 0.05% azide.
Storage Buffer:
0.01M TBS(pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.
Storage:
Store at -20°C for 12 months.
Background:
Histones are the main constituents of the protein part of chromosomes of eukaryotic cells. They are rich in the amino acids arginine and lysine and have been greatly conserved during evolution. Histones pack the DNA into tight masses of chromatin. Two core histones of each class H2A, H2B, H3 and H4 assemble and are wrapped by 146 base pairs of DNA to form one octameric nucleosome. Histone tails undergo numerous post-translational modifications, which either directly or indirectly alter chromatin structure to facilitate transcriptional activation or repression or other nuclear processes. In addition to the genetic code, combinations of the different histone modifications reveal the so-called histone code. Histone methylation and demethylation is dynamically regulated by respectively histone methyl transferases and histone demethylases.
VALIDATION IMAGES
HeLa cells were stained with H3K27ac (1A3) Monoclonal Antibody (bsm-53022M) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labelled with the H3K27ac antibody (left) diluted 1:500 in blocking solution followed by an anti-mouse antibody conjugated to Alexa594. The middle panel shows staining of the nuclei with DAPI. A merge of the two staining is shown on the right.
To test the specificity an ELISA was performed using a serial dilution of H3K27ac (1A3) Monoclonal Antibody (bsm-53022M). The wells were coated with peptides containing the unmodified H3K27 region as well as the acetylated H3K27 and the acetylated H3K9. Figure shows a high specificity of the antibody for the peptide containing the modification of interest.