H-Ala-Ala-Phe-AMC (free base)

Description:

Fluorogenic substrate for tripeptidyl peptidases I and II and for tripeptide aminopeptidase EC 3.4.11.4.

Sequence:

AAF-AMC

General

References

Comments (0)

Name	H-Ala-Ala-Phe-AMC (free base)
Category	Enzyme Substrates and Inhibitors
One Letter Code	AAF-AMC
Three Letter Code	{Ala}{Ala}{Phe}-AMC
Molecular Weight	464.520
Application

Berman, Jonathan M., and Mouhamed S. Awayda. "Redox artifacts in electrophysiological recordings." American Journal of Physiology-Cell Physiology 304.7 (2013): C604-C613.

Vidal-Donet, José Manuel, et al. "Alterations in ROS activity and lysosomal pH account for distinct patterns of macroautophagy in LINCL and JNCL fibroblasts." PLoS One 8.2 (2013).

Bhosale, Manoj, et al. "Characterization of two M17 family members in Escherichia coli, peptidase A and peptidase B." Biochemical and biophysical research communications 395.1 (2010): 76-81.

Autefage, Hélène, et al. "Lysosomal Serine Protease CLN2 Regulates Tumor Necrosis Factor-α-mediated Apoptosis in a Bid-dependent Manner." Journal of Biological Chemistry 284.17 (2009): 11507-11516.

Bhutani, N., P. Venkatraman, and A. L. Goldberg. "Puromycin‐sensitive aminopeptidase is the major peptidase responsible for digesting polyglutamine sequences released by proteasomes during protein degradation." The EMBO journal 26.5 (2007): 1385-1396.