
20S Immunoproteasome Kit, human PBMC
Catalog number: SBB-KP0037
This kit is designed to test for specific activity of 20S immunoproteasome. The kit provides purified 20S immunoproteasome and is designed to test for Chymotrypsin-like activity (Suc-LLVY-AMC), and Caspase-like activity of the immunoproteasome subunits ß1i/ PSMB9 (PAL-AMC), and ß5i/PSMB8 (ANW-AMC).[1][2][3][4][5][6]
Description
This kit is designed to test for specific activity of 20S immunoproteasome. The kit provides purified 20S immunoproteasome and is designed to test for Chymotrypsin-like activity (Suc-LLVY-AMC), and Caspase-like activity of the immunoproteasome subunits ß1i/ PSMB9 (PAL-AMC), and ß5i/PSMB8 (ANW-AMC). Additionally, we have included the compound, ONX-0914, which can be used to inhibit specifically the subunit ß5i/LMP7 20S immunoproteasome. All peptide substrates are conjugated to AMC, which upon proteasome catalyzed hydrolyses display fluorescence at Excitation = 345 nm, Emission = 445 nm; allowing for a real-time read out of 20S immunoproteasome specific activity.
For Research Use Only, Not For Use In Humans.
Specifications
Quantity: | 100 x 50 μL reactions |
---|---|
Purity: | > 95% |
Readout: | Endpoint / Kinetic |
Label or Dye: | 7-Amino-4-methylcoumarin |
Detection Method: | Fluorescence |
Substrate Properties: | Protein-Based Substrate |
Excitation/Emission (nm): | 345/445 |
Storage | -80C, Avoid multiple freeze / thaw cycles. It is recommended to make aliquots of each reaction component upon first time use. |
Figures & Data
20S Immunoproteasome Activity

Figure 1. 20S Immunoproteasome Activity Raw Data Output: Several wells of Immunoproteasome shown digesting LLVY, PAL, and ANW-AMC over time +/- 1x (40μM) inhibitor (ONX-0914).
Certificates of Analysis (COA)
Citations & References
1) Singh, Pradeep K., et al. “Immunoproteasome
ß5iSelective Dipeptidomimetic Inhibitors.”
ChemMedChem 11.19 (2016): 2127-2131.
2) De Groot, Karina A., et al. “Pharmacodynamic
monitoring of (immuno) proteasome inhibition during
bortezomib treatment of a critically ill patient with lupus
nephritis and myocarditis.” Lupus science & medicine
2.1 (2015): e000121.
3) Cornish Carmony, Kimberly, et al. “Elucidating the
Catalytic Subunit Composition of Distinct Proteasome
Subtypes: A Crosslinking Approach Employing
Bifunctional Activity Based Probes.” ChemBioChem
16.2 (2015): 284-292.
4) 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.
5) Miller, Zachary, et al. “Inhibitors of the
immunoproteasome: current status and future
directions.” Current pharmaceutical design 19.22 (2013):
4140-4151.
6) Dubiella, Christian. Development and Characterization
of Selective Immunoproteasome Inhibitors. Diss.
Universität München, 2015.