Product Details
A highly purified preparation of ‘26S’ proteasomes, useful for carrying out in vitro protein degradation studies with suitably ubiquitinylated protein substrates.

Source: Purified from human blood cells by fractination. The highest activity, soluble and homogenous. Consists of a high purity mixture of ‘26S’ proteasomes singly (26S) and doubly (30S) capped with 19S regulatory subunit complexes in the ratio of 40% single cap : 60% double capped at the time of preparation.

Formulation: Suspended in TSD buffer (50μg in 10mM TRIS, containing 25mM potassium chloride, 1.1mM magnesium chloride, 0.1mM ethylenediaminetetraacetic acid, 1mM dithiothreitol, 1mM sodium azide, 2mM ATP, pH 7.0, and 35% glycerol).

Shipping: Shipped on Dry Ice

Long Term Storage: -80°C

 

Use/Stability

When ready for use the enzyme should be thawed by standing on ice. If the enzymatic acitivity of the 26S proteasome is to be measured, it should be used immediately after thawing since the enzyme complex is labile. After dissociaton of the 26S complex the 20S proteasome activity is relatively stable.

 

Product Literature Reference

- UBQLN2 Mediates Autophagy-Independent Protein Aggregate Clearance by the Proteasome Author links open overlay panel: Roland Hjerpe, John S.Bett, Matthew J.Keuss, Alexandra Solovyova, Thomas G. McWilliams, Clare Johnson, Indrajit Sahu, Joby Varghese, Nicola Wood, Melanie Wightman, Georgina Osborne, Gillian P. Bates, Michael H. Glickman, Matthias Trost, Axel Knebel, Francesco Marchesi, Thimo Kurz, Cell Volume 166, Issue 4, 11 August 2016, Pages 935-949, Full Text

- Structural Snapshots of 26S Proteasome Reveal Tetraubiquitin-Induced Conformations, Zhanyu Ding, Cong Xu, Indrajit Sahu, Yifan Wang, Zhenglin Fu, Min Huang, Catherine C.L. Wong, Michael H.Glickman, YaoCong: Molecular Cell Volume 73, Issue 6, 21 March 2019, Pages 1150-1161.e6, Full Text

- Synthetic Uncleavable Ubiquitinated Proteins Dissect Proteasome Deubiquitination and Degradation, and Highlight Distinctive Fate of Tetraubiquitin Sumeet K. Singh, Indrajit Sahu, Sachitanand M. Mali, Hosahalli P. Hemantha, Oded Kleifeld, Michael H. Glickman, and Ashraf Brik Journal of the American Chemical Society 2016 138 (49), 16004-16015, Full Text

- Proteasome lid bridges mitochondrial stress with Cdc53/Cullin1 NEDDylation status Author: L. Bramasole, A. Sinha, S. Gurevich, M. Radzinski, Y. Klein, N. Panat, E. Gefen, T. Rinaldi, D. Jimenez-Morales, J. Johnson, N.J. Krogan, N. Reis, D. Reichmann, M.H. Glickman, E. Pick, Redox Biology, Elsevier, January 2019, Full Text

- Tuning the proteasome to brighten the end of the journey: Thibault Mayor, Michal Sharon and Michael H. Glickman, American Journal of Physiology - Cell Physiology 11 NOV 2016, Full Text

- Polyubiquitin-Photoactivatable Crosslinking Reagents for Mapping Ubiquitin Interactome Identify Rpn1 as a Proteasome Ubiquitin-Associating Subunit: Michal Chojnacki, Wissam Mansour, Dharjath S. Hameed, Rajesh K. Singh, Farid El Oualid, Rina Rosenzweig, Mark A. Nakasone, Zanlin Yu, Fabian Glaser, Lewis E. Kay, David Fushman, Huib Ovaa, Michael H. Glickman, Cell Chemical Biology 20 April 2017, Full Text

- Proteasome in action: substrate degradation by the 26S proteasome: Indrajit Sahu, Michael H. Glickman, Biochem Soc Trans (2021) 49 (2): 629–644, Full Text

- The reaction of complement factors and proteasomes in experimental encephalitis: S. Lange, et al.; J. Neurovirol. 23, 313 (2017)
UBQLN2 Mediates Autophagy-Independent Protein Aggregate Clearance by the Proteasome: R. Hjerpe, et al.; Cell 166(4): 935-949 (2016), Full Text
- Molecular architecture of the 26S proteasome holo complex determined by an integrative approach: K. Lasker, et al.; Proc.Natl.Acad.Sci.31:109(5)1380-1387 (2012), Abstract