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I am looking for a 'positive control' that would bind to proteins that contain bromodomains(which recognizesacetylatedlysineresidues) for Biacore binding assays. I thought perhaps an acetylated peptide fragment derived from histones 3H or 4H would be perfect for the assay.
Asked on Feb 23 2012
We do have a few acetylated peptides taken from histone sequences, but since these are short peptide sequences I don't expect them to have any functional activity. However, if the bromodomain binds the acetylated lysine in a passive way (i.e. the tertiary structure or functional activity of the peptide is not a concern) then perhaps a short peptide would be suitable.
I've looked through some literature and it seems that the bromodomain recognizes the acetyl lysine moiety supported by the flanking sequences (PMID:15382140). Our acetylated histone peptides are intended mostly to be used as blocking peptides, so they are around 15 amino acids long. If this is a long enough sequence for bromodomain recognition, then again perhaps it is suitable. We unfortunately don't have any information for any of these acetylated histone peptides regarding Kd and we can't guarantee them to work in a binding assay since we haven't tested them for such an assay.
I am sorry that I don't have more information at this time, but if you have any further questions or if there is anything else that I can do for you, please let me know and I'll be happy to help.
Answered on Feb 23 2012