Catalog number: SBB-PS0007, 2 mg
Ac-PAL-AMC is a fluorogenic peptidyl substrate for measuring caspase-like activity of the immunoproteasome. Hydrolysis of this substrate by the β1i subunit of the immunoproteasome is monitored by observing fluorescence at an Excitation wavelength of 345nm and Emission at 445nm. 
Ac-PAL-AMC (Acetyl-Pro-Ala-Leu-AMC) is a 7-amino-4-methylcoumarin labeled fluorogenic peptidyl substrate hydrolyzed by the β1i subunit of the 20S immunoproteasome. Peptidylglutamyl-peptide hydrolyzing (Caspase-like) activity can be measured using a working concentration of 20-50μM substrate. This substrate is specific to the immunoproteasome, and is not hydrolyzed efficiently by the constitutive proteasome. Cleavage of this peptide by the immunoproteasome or other enzymes liberates the fluorophore AMC causing a strong fluorescent signal which is detected at an Excitation wavelength of 345nm and Emission wavelength of 445nm. 20S Proteasome enzyme requires activation with 0.035% SDS in the assay buffer.
For Research Use Only, Not For Use In Humans.
|Molecular Weight:||498.6 Da|
|Purity:||>99% by HPLC|
|Readout:||Endpoint / Kinetic|
|Label or Dye:||7-Amino-4-methylcoumarin|
|Substrate Properties:||Protein-Based Substrate, C26H34N4O6|
|Storage||Store at 4°C after product arrival. After preparing a stock in DMSO ( ≥10 mM) store product at -20°C to −80°C. It is recommended to make multiple aliquots after the first thaw to ensure best performance.|
Figures & Data
Figure 1. Ac-PAL-AMC, Chemical Structure.
Structure of Ac-PAL-AMC.
Figure 2. 20S Immunoproteasome vs. 20S Constitutive Proteasome Activity.
PAL-AMC exhibits a high specific activity and preference for 20S immunoproteasome compared to constitutive 20S proteasome.
Certificates of Analysis (COA)
Citations & References
1) Park, Ji Eun, et al. "PSMB9 codon 60 polymorphisms have no impact on the activity of the immunoproteasome catalytic subunit B1i expressed in multiple types of solid cancer." PloS one 8.9 (2013): e73732.
2) Miller, Zachary, et al. "Inhibitors of the immunoproteasome: current status and future directions." Current pharmaceutical design 19.22 (2013): 4140-4151.
3) Dubiella, Christian. Development and Characterization of Selective Immunoproteasome Inhibitors. Diss. Universität München, 2015.