I know it reacts with the alpha-amino group, but I'm only interested in the side chains. I think it reacts with lysine, but what about glutamine or asparagine?
OPA reacts in presence of thiols specifically with primary amines above their isoelectric point. Amino acid esters and amides including glutamine and asparginine fail to produce strong fluorescence following their reaction with o-phthalaldehyde (OPA) in the presence of β-mercaptoethanol. The lack of luminescence appears to arise from a quenching phenomenon rather than from reduced reactivity of these substrates toward OPA. The amido hydrogen in the peptide linkage has been implicated in the loss in fluorescence yield.
OPA reacts with primary AA (except cysteine or cystine) in the presence of 2-mercaptoethanol or 3-mercaptopropionic acid to form a highly fluorescent adduct.