The ubiquitin-proteasome pathway is the principle pathway of proteolysis in eukaryotic cells and may
contribute to controlling the intracellular levels of a variety of short-lived proteins, in addition to
degrading abnormal proteins in the cytosol and nucleus. Protein substrates are marked with a poly-ubiquitin chain and then degraded to peptides and free ubiquitin by a large multicatalytic complex, the proteasome, which exists within all eukaryotic cells. Numerous examples of regulatory proteins have been found to undergo ubiquitin-dependent proteolysis.
Protein substrates of the ubiquitin-proteasome pathway include a number of cell regulatory molecules,
such as cyclins, the Myc oncogene protein, and p53, and the regulated degradation of these molecules
has been linked to the control of cell proliferation and cell cycle progression. By controlling the
intracellular levels of such proteins, the activity of the ubiquitin-proteasome pathway might also be
linked to apoptosis.
CycLex Proteasome Enrichment & Activity Assay Kit is for the isolation and study of intracellular proteasome proteins. Through the use of a hHR23B ubiquitin-like domain resin(UbL-Resin), 20S proteasome are isolated from cell or tissue lysate. The bound 20S proteasome protease activity can be measured by fluorogenic Proteasome Substrate (Suc-LLVY-AMC). In addition, this kit can be used to study 20S proteasome function and interactions with other proteins. Since the amino acid sequence of ubiquitin-like domain in hHR23B is well conserved among mammalian, this kit can be used for all mammalian cells.
Proteasome Enrichment & Activity Assay Kit
CycLex Poly-Ubiquitinated Protein ELISA Kit is designed to detect and quantify the level of total poly-ubiquitinated proteins in cell lysate. Since the amino acid sequence of ubiquitin is well conserved among mammal, this ELISA kit can be used for any mammalian cells. This assay is intended for the detection of poly-ubiquitinated proteins in cell lysate.
Poly-Ubiquitinated Protein ELISA Kit