20S Proteasome, rat RBC

Catalog Number: SBB-PP0086, 50 μg

Highly active protein complex that has been purified from rat red blood cells (RBC). The rat 20S proteasome is able to proteolytically degrade substrates in an ATP-independent manner. The 20S core can be activated chemically with SDS (0.035%) or by the addition of PA28. Initial experiments should be carried out at 20S proteasome concentrations between 2-5 nM.[1][2][3][4][5]

In stock


The ubiquitin-proteasome pathway is the major proteolytic system in eukaryotic cells, where it catalyzes the selective degradation of short-lived regulatory proteins or the rapid turnover of misfolded proteins. One of the most important proteases in this pathway is the 26S proteasome, an ATP-dependent proteolytic complex, which is formed by the association of the barrel-shaped 20S proteasome (700-kDa) and two 19S (700-kDa) regulatory complexes. The 20S catalytic core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 20S catalytic core is able to degrade a variety of peptide substrates and poly-ubiquitinated proteins involved with apoptosis, DNA repair, endocytosis, and cell cycle control. The 20S proteasome can be activated chemically by the addition of the detergent SDS at a concentration not exceeding 0.035% or by the proteinaceous activator PA28.


Product Overview
Quantity: 50 μg
Molecular Weight: >700 kDa
Purity: >93% by SDS-PAGE
Storage Buffer: 50 mM HEPES pH 7.5, 100 mM NaCl,1 mM TCEP.
Storage Store at -80 ̊C. Avoid multiple freeze thaw cycles.

Citations & References

  • 1)Smith DM,Chang SC, Park S, Finley D,Cheng Y, Goldberg AL (Sep 2007).“Docking of the proteasomal ATPases’ carboxyl termini in the 20S proteasome’s alpha ring open the gate for substrate entry”. Molecular Cell. 27 (5): 731–44. doi:10.1016/j.molcel.2007.06.033. PMC 2083707Freely accessible. PMID 17803938.
  • 2) Wilk S, Orlowski M (Mar 1983). “Evidence that pituitary cation-sensitive neutral endopeptidase is a multicatalytic protease complex”. Journal of Neurochemistry. 40 (3):842–9. doi:10.1111/j.1471-4159.1983.tb08056.x. PMID 6338156.
  • 3) Haas AL, Warms JV, Hershko A, Rose IA (Mar 1982). “Ubiquitin-activating enzyme. Mechanism and role in protein-ubiquitin conjugation”. The Journal of Biological Chemistry. 257(5): 2543–8. PMID 62779
  • 4) Lodish H, Berk A, Matsudaira P, Kaiser CA, Krieger M, Scott MP, Zipursky SL, Darnell J (2004). “3”. Molecular cell biology (5th ed.). New York: W.H. Freeman and CO.pp. 66–72. ISBN 978-0-7167-4366-8.
  • 5) G.N. DeMartino & C.A. Slaughter (1999)”The proteasome, a novel protease regulated by multiplemechanisms”. J. Biol. Chem. 274, 22123 (1999) PMID: 10428