20S Immunoproteasome, mouse Spleen

Catalog Number: SBB-PP0083, 50 μg

Highly active protein complex that has been purified from mouse spleen and is supplied at >95% purity. Immunoproteasome is recognized as a strong drug target for autoimmune disease and cancer.  This immunoproteasome is supplied at >95% purity and experiments should be carried out at 20S immunoproteasome concentrations between 2-5 nM.  [1][2][3][4]

In stock
SKU
0127
$189.00

Description

The immunoproteasome is structurally similar to constitutive 26S proteasome. The 20S core of immunoproteasome contains two outer rings composed of alpha subunits, and two internal 7-subunit containing rings each possessing 3 specific subunits responsible for proteasome catalytic activity.  In immunoproteasome these subunits (ß1, ß2, ß5) are replaced by three inducible subunits: PSMB9, PSMB10, and PSMB8, (ß1i, ß2i, ß5i).  These stress-induced subunits allow for the production of MHC-1 associating peptides, which are displayed as antigens on the cell surface.  These displayed peptides can then be recognized by immune surveillance CD8 T-Cells. 20S Immunoproteasome is recognized as a strong drug target for autoimmune disease and cancer.  This immunoproteasome is purified from mouse spleen and is supplied at >95% purity. The immunoproteasome is commonly associated with the 19S, PA28 α/ß, or the PA28γ regulatory complexes. If choosing to omit PA28 during use, 20S must be chemically activated by addition of 0.035%SDS in final assay buffers.

Specifications

Product Overview
Quantity: 50 μg
Molecular Weight: >700 kDa
Purity: >92% 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