N-α-Benzoyl-L-Arginine ethyl ester (hydrochloride) (Synonyms: BAEE, Bz-Arg-OEt, NSC 86159)

N-α-Benzoyl-L-arginine ethyl ester (BAEE) is a nonpeptide substrate of proteases and deiminases.1,2,3,4,5 It has been used as a substrate for the relative quantification of trypsin activity.1,2 BAEE has also been used as a substrate for the activity of subtilisins, kallikreins, and protein arginine deiminase 4 (PAD4).3,4,5

References
1. Crowell, A.M.J., Stewart, E.J., Take, Z.S., et al. Critical assessment of the spectroscopic activity assay for monitoring trypsin activity in organic-aqueous solvent. Anal. Biochem. 435(2), 131-136 (2013).
2. Rajabi, M., Shareghi, B., Farhadian, S., et al. Evaluation of maltose on conformation and activity parameters of trypsin. J. Biomol. Struct. Dyn. (2018).
3. Glazer, A.N. Esteratic reactions catalyzed by subtilisins. J. Biol. Chem. 242(3), 433-436 (1967).
4. Ran, X., Zhang, Q., and Wang, D.W. Tissue kallikrein activity, detected by a novel method, may be a predictor of recurrent stroke: A case-control study. Dis. Markers 159750 (2015).
5. Kearney, P.L., Bhatia, M., Jones, N.G., et al. Kinetic characterization of protein arginine deiminase 4: A transcriptional corepressor implicated in the onset and progression of rheumatoid arthritis. Biochemistry 44(31), 10570-10582 (2005).