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PRODUCT DETAILS
Product specifications
The 26S proteasome is a large, ATP-dependent proteolytic complex responsible for the selective degradation of ubiquitinated proteins in eukaryotic cells. It consists of a 20S catalytic core particle capped at one or both ends by a 19S regulatory particle.
The 19S complex recognizes ubiquitin-tagged substrates, removes ubiquitin chains, unfolds target proteins, and translocates them into the 20S core for proteolytic degradation.
Through this process, the 26S proteasome plays a central role in maintaining cellular protein homeostasis and regulating numerous essential cellular processes.
A highly purified preparation of 26S proteasomes, useful for carrying out in vitro protein degradation studies with suitably ubiquitinylated protein substrates. Consists of a high purity mixture of 26S proteasomes singly (26S) and doubly (30S) capped with 19S regulatory subunit complexes.
SOURCE
Purified by fractionation from human erythrocytes.
Highly active, soluble, and homogeneous
FORMULATION
Liquid.
In 20mM Tris-HCl, 25mM KCl, 1.1mM MgCl₂, 0.1mM EDTA,
1mM DTT, 1mM sodium azide, 2mM ATP, pH 7.0, and 35% glycerol
Buffer ingredients can be adjusted to customer needs
SHIPPING
Shipped on dry ice
LONG-TERM STORAGE
Store at −80°C. Avoid repeated freeze/thaw cycles
PACKAGE
50 μg standard one unit quantity.
Contact us for larger quantities and custom requirements
UNIT PRICE
260 $ USD per 50 μg unit
PRODUCT QUALITY
Product quality assessment
(A) Coomassie-stained 12% SDS-PAGE of purified human 26S proteasome. (B) Purified human 26S proteasomes were separated by 4% native-PAGE and analyzed by overlay assays using Suc-LLVY-AMC. (C) Coomassie-stained 4% native-PAGE of purified human 26S proteasome. (D) Immunoblotting described cleavage of Di-Ub (K63) by 26S as a 19S activity assay. (E) Coomassie-stained 12% SDS-PAGE of human untagged 26S proteasome samples. (F) Western blot analysis of human 26S proteasome samples targeted with Rpt-5 and alpha-4 antibodies.
LITERATURE
Selected literature
Roland Hjerpe, Thimo Kurz et al. • Cell Volume 166, Issue 4, 11, 935-949 • 2016
Zhanyu Ding, Michael H. Glickman, Yao Cong et al. • Molecular Cell Volume 73, Issue 6,1150-1161.e6 • 2019
Sumeet K. Singh, Ashraf Brik et al. • Journal of the American Chemical Society 138 (49), 16004-16015 • 2016
L. Bramasole, E. Pick et al. • Redox Biology, Elsevier, 20:533-543 • 2019
Thibault Mayor, Michal Sharon and Michael H. Glickman • American Journal of Physiology - Cell Physiology, 311(5):C793-C804 • 2016
Michal Chojnacki, Michael H. Glickman et al. • Cell Chemical Biology 24(4):443-457.e6. • 2017
Indrajit Sahu and Michael H. Glickman • Biochem. Soc. Trans.49 (2): 629–644 • 2021
Stefan Lange, Ivar Lönnroth et al. • J. Neurovirol. 23, 313-318 • 2017
Keren Lasker, Wolfgang Baumeister et al. • Proc. Natl. Acad. Sci. 31:109(5)1380-1387 • 2012