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Ubiquitin Chains - Why To Use Ubiquigent Reagents
? Fully annotated protein sequence
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Validation and Experimental Utility of the E2scan™ Kit version 2
"Linking Ubiquitin Research to Drug Discovery"
Ubiquigent - E3 Ligases
E3 ligases confer specificity to the ubiquitylation pathway by recognizing target substrates and mediating transfer of ubiquitin or ubiquitin like modifiers (UBLs) from an E2 conjugating enzyme to a substrate. There are estimated to be >700 E3 ligases forming several classes of enzyme; N-end rule ubiquitin E3 ligases, Homology to E6AP C-Terminus (HECT) domain E3s, Really Interesting New Gene (RING) domain E3s, U-Box containing E3s, Inhibitor of Apoptosis (IAP) E3s, and Cullin-RING E3 ligases (CRLs). The classes of E3 ligases are continually expanding. HECT E3 ligases form a thioester intermediate with the C-terminus of activated ubiquitin via a catalytic cysteine residue on the E3. In this case, ubiquitin is transferred from an E2 via the E3 to a substrate protein lysine side chain. RING and U-Box E3 ligases do not possess a catalytic cysteine residue and bring the E2-ubiquitin complex and substrate into close proximity to mediate the transfer of the ubiquitin directly from the E2 to the substrate.