A major advantage of ABPP is the ability to monitor the availability of the enzyme active site directly, rather than being limited to protein or mRNA abundance. With classes of enzymes such as the serine proteases and metalloproteases that often interact with endogenous inhibitors or that exist as inactive zymogens, this technique offers a valuable advantage over traditional techniques that rely on abundance rather than activity.
Finally, in recent years ABPP has been combined with tandem mass spectrometry enabling the identification of hundreds of active enzymes from a single sample. This technique, known as ABPP-MudPIT (multidimensional protein identification technology) is especially useful for profiling inhibitor selectivity as the potency of an inhibitor can be tested against hundreds of targets simultaneously.
ABPP were first reported in the 1990s in the study of proteases.
^Kam CM, et al. Biotinylated isocoumarins, new inhibitors and reagents for detection, localization, and isolation of serine proteases.Bioconjugate chemistry 1993 
^Abuelyaman AS, et al. Fluorescent derivatives of diphenyl [1-(N-peptidylamino)alkyl]phosphonate esters: synthesis and use in the inhibition and cellular localization of serine proteases.Bioconjugate chemistry 1994