The Ubiquitin Proteasome System (UPS) controls the principal functions of almost all the cellular proteins of human cells and failures in this system often contribute directly or indirectly to the pathogenesis of many diseases, including cancer, inflammation, and neurodegeneration. There are ~700 E3 ubiquitin ligases encoded in human genome and the functions of most of these E3s remain unknown. E3 ligases build diverse ubiquitin chain linkages on substrates that can determine the fate of the substrate. Whereas K48-linked ubiquitin chains promote proteasomal degradation of substrates, K63-linked ubiquitin chains are associated with signaling and localization. Identification of the type of ubiquitin linkage as well as the substrate lysines modified with ubiquitin can provide insights into the cellular functions of E3s. Lifesensors can perform these studies very efficiently and in a timely manner for the clients.
- Cell-based assays to identify endogenous substrate ubiquitination
- Type of ubiquitin chain linkages as well as substrate lysines that are modified with ubiquitin
- With over expression of E3s and/or Knockout/Knockdown of E3s
Coated polymeric high-capacity magnetic beads to allow superior enrichment of polyubiquitinated proteins along with minimizing non-specific binding to proteins in tissue and cellular lysates.
TUBEs display up to a 1000-fold increase in affinity for polyubiquitin moieties over the single ubiquitin binding associated domain (UBA). In addition, TUBEs protect polyubiquitinated proteins from deubiquitination and proteasomal degradation, allowing for detection at relatively low abundance.
Monoclonal antibodies that recognize polyubiquitylated proteins and free ubiquitin. VU-1 has been shown to recognize all ubiquitin linkages (mono, K6, K11, K27, K29, K33, K48, K63, and linear) by Western blotting. VU-1 is an excellent antibody for immunostaining applications generating robust ubiquitin detection and low background with an ability to detect subcellular ubiquitin localization.