Ubiquitin (human, recombinant; His-tagged)

Ubiquitin is a regulatory protein encoded by three gene classes in humans, which code for fusion proteins between ubiquitin and zinc-finger proteins, ribosomal proteins, or ubiquitin repeats that are cleaved by esterases to release monomeric ubiquitin.^1,2 It is ubiquitously expressed and highly conserved among eukaryotic species. Ubiquitin is conjugated to misfolded, abnormal, short-lived, or foreign proteins by ubiquitin-conjugating enzymes (E2) and substrate-specific ubiquitin ligases (E3) to target them for degradation by the 26S proteasome or lysosome.^1,3 It is also conjugated to proteins to modify cell signaling through regulation of protein-protein interactions, activity, or subcellular localization.³ Dysregulation of ubiquitination has been implicated in the pathogenesis of neurodegenerative diseases, including Parkinson’s and Alzheimer’s diseases.⁴ Cayman’s Ubiquitin (human, recombinant; His-tagged) protein can be used as a substrate for enzyme activity assays, as well as for ELISA and Western blot (WB) applications.

WARNING This product is not for human or veterinary use.

1. Wilkinson, K.D. Roles of ubiquitinylation in proteolysis and cellular regulation. Annu. Rev. Nutr. 15, 161-189 (1995).

2. Bonifacino, J.S., and Weissman, A.M. Ubiquitin and the control of protein fate in the secretory and endocytic pathways. Annu. Rev. Cell Dev. Biol. 14, 19-57 (1998).

3. Komander, D., and Rape, M. The ubiquitin code. Annu. Rev. Biochem. 81, 203-209 (2012).

4. Ciechanover, A., and Brundin, P. The ubiquitin proteasome system in neurodegenerative diseases: Sometimes the chicken, sometimes the egg. Neuron 40(2), 427-446 (2003).