ENCAB000AQM

Antibody against Mus musculus H3K27ac

Homo sapiens
any cell type or tissue
characterized to standards with exemption
Mus musculus
any cell type or tissue
characterized to standards with exemption
Status
released
Source (vendor)
Active Motif
Product ID
39133
Lot ID
21311004
Characterized targets
H3K27ac (Mus musculus)
Host
rabbit
Clonality
polyclonal
Purification
Protein A
Isotype
IgG
Antigen description
Histone H3 acetyl Lys27 antibody was raised against a peptide including acetyl-lysine 27 of histone H3
External resources

Characterizations

H3K27ac (Mus musculus)
Method: dot blot assay
Attachment from submitter
exempt from standards
Caption
Dot blot analysis performed by Active Motif to confirm the specificity of Histone H3 acetyl Lys27 antibody (cat#39133, lot#21311004) for acetyl Lys27 histone H3. Peptides were spotted onto the membrane in the following concentrations: 50pmol (top row), 10pmol (middle row), 2pmol (bottom row). The blot was then probed with the antibody at 0.5ug/mL. The antibody recognized the H3K27ac peptide with >10-fold enrichment in binding signal relative to other peptides when peptides were used at 10pmol and 2pmol. At 50pmol, the antibody showed a 2.5-fold enrichment of H3K27ac relative to unmodified H3K27 and >10-fold enrichment of H3K27ac relative to H3K18ac.
Submitter comment
There is no more of this antibody lot to carry out an additional dot-blot, but there are other H3K27ac antibodies from Active Motif used by this lab which have shown similar ChIP-seq and characterization results.
Reviewer comment
We agree that this antibody should be approved via exemption due to lack of additional antibody lot to test and comparable results with other H3K27ac antibodies.
Submitted by
Jean Davidson
Lab
Bing Ren, UCSD
H3K27ac (Mus musculus)
A375embryonic fibroblastHEK293ES-Bruce4
Method: immunoblot
Attachment from submitter
compliant
Caption
An immunoblot using whole cell extract of two human cell lines and two mouse cell lines shows positive bands at the size of the histone (17kDa), while the recombinant unmodified version of that histone shows a lack of reactivity. The histone bands detected in the extracts constitute 100% of the protein signal and show at least 10-fold enrichment relative to any other band. This signal is also at least 10-fold enriched relative to that detected using the unmodified recombinant histone.
Submitted by
David Gorkin
Lab
Bing Ren, UCSD