Ubiquitination is a type of post-translational modification (PTM) that involves the attachment of Ubiquitin to a protein's lysine residue. Ubiquitin is a highly conserved protein of approximately 8.5 kDa which has a normal role in the targeting of proteins for proteolytic degradation. In order to perform this function, Ubiquitin is appended to the target protein to be degraded via the C-terminal glycine of Ubiquitin. The ubiquitinated complex is then recognized by a complex of degradative enzymes. Proteins may be monoubiquitinated or polyubiquitinated; the latter are recognized by the 26S proteasome, which catalyzes the degradation of the target protein. The 26S proteasome is also responsible for recycling Ubiquitin after the target protein's degradation.
Ubiquitination Bioinformatics Tool
Laverne is a handy bioinformatics tool to help facilitate scientific exploration of related genes, diseases and pathways based on co-citations. Explore more on Ubiquitination below!
For more information on how to use Laverne, please read the How to Guide.
We have 2980 products for the study of Ubiquitination that can be applied to Western Blot, Chromatin Immunoprecipitation, Flow Cytometry, Immunocytochemistry/Immunofluorescence, Chromatin Immunoprecipitation (ChIP), Immunohistochemistry from our catalog of antibodies and ELISA kits.
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