Ubiquitination Cascade Pathway

Ubiquitin is a highly conserved globular 76-residue eukaryotic protein found in the cytoplasm and nucleus of cells. Ubiquitin can be covalently attached (conjugated) to proteins in a process termed ubiquitination that utilizes Ubiquitin-activating (E1), Ubiquitin-conjugating (E2) and Ubiquitin Ligase (E3) enzymes. Ubiquitination affects protein stability, subcellular localization, and the ability to interact with other proteins. Ubiquitin can be attached to substrate proteins in three different manners: monoubiquitination, multi-monoubiquitination, and polyubiquitination. Eight residues within ubiquitin can be utilized to form polyubiquitin chains [K6, K11, K27, K29, K33, K48, K63, and Met1 (linear)] and linkage type directs the modified proteins to different cellular fates. Polyubiquitin chains of all linkages listed above have been detected in vivo and have been shown to differentially affect many cellular processes, signaling pathways, and disease states. R&D Systems reagents allow you to discover if a protein of interest is ubiquitinated and investigate how ubiquitination affects the function of that protein.

To learn more, please visit our Ubiquitin and Ubiquitin-like Modifiers Research Area.