Browse hundreds of high-quality research products, including proteins and antibodies, for activating enzymes (E1s), conjugating enzymes (E2s), ligases (E3s) and deconjugating enzymes (DCEs), plus an innovative range of ubiquitin-, SUMO-, NEDD8-, ISG15- and FAT10-associated proteins and derivatives. Discover ubiquitin- and Ubl-reactive antibodies, kits for the study of ubiquitin, SUMO, and NEDD8 conjugation, and our easy-to-use UBIQAPTURE™ and SUMO-QAPTURE™ kits for the detection and isolation of ubiquitinylated and SUMOylated proteins.
Ubiquitinylation of cellular proteins is a highly complex and tightly regulated process that targets, in a specific manner, thousands of cellular proteins. It is carried out by a modular cascade of enzymes with high specificity towards target proteins. Conjugation of ubiquitin can serve a variety of non-proteolytic functions, including activation of enzymes, modulation of membrane dynamics, or routing of the tagged proteins to their sub-cellular destination (Figure 1).
Figure 1. Differing ubiquitin modification resulting in distinct functions.
There are at least 10 conjugatable ‘cousins’ of ubiquitin including, amongst others, SUMO, NEDD8, ISG15 and FAT10. These ubiquitin-like proteins (Ubls) can be covalently attached to target proteins for a variety of signalling processes in the cell and may function as critical regulators of many cellular processes, including transcription, DNA repair, signal transduction, autophagy, and cell-cycle control. There is a growing body of data implicating the dysregulation of Ubl-substrate modification and mutations in the Ubl-conjugation machinery in the etiology and progression of a number of human diseases.
The complexity of the ubiquitin and ubiquitin-like protein cascades is considerable. In mammals, there are some ten activating enzymes (E1s) known, some twenty plus conjugating enzymes (E2s), over eight hundred ligases (E3s), and approaching one hundred deconjugating enzymes. These varied components work in a hierarchical context and, for appropriate modification with ubiquitin or a Ubl to occur, the correct combination of E1, E2, E3, substrate, and deconjugating enzyme must all work in concert. The cascades for the ubiquitin-like proteins appear not to be as complex as that of ubiquitin with a reduced number of component possibilities.
Deconjugating enzymes (DCEs) can hydrolyse a peptide, amide, ester or thioester bond at the C-terminus of ubiquitin, including the post translationally formed isopeptide bonds found in mono-, multi-, and polyubiquitinylated conjugates. DCEs thus have the potential to regulate any ubiquitin/Ubl-mediated cellular process. Their conservation and widespread occurrence in eukaryotes, prokaryotes and viruses shows that these proteases constitute an essential class of enzymes.
For isolation and enrichment of ubiquitinylated proteins. The UBIQAPTURE-Q® Kit is an efficient tool for the selective isolation of ubiquitinylated proteins. The Kit facilitates the isolation of both mono- and poly-ubiquitinylated proteins (independent of lysine residue chain linkage) from cell extracts, tissue lysates and in vitro assay solutions through use of a high-binding affinity matrix.
Applications:
Enzo Life Sciences offers hundreds of antibodies against ubiquitin and related targets including the antibody for detection of ubiquitinylated proteins, Mono- and polyubiquitinylated conjugates, mAb (UBCJ2).
Backed by thousands of peer-reviewed citations, our Worry-free Antibody Trial Program, and expert technical support, you can count on Enzo antibodies to deliver reliable, consistent, accurate data.
Diglycyl Lysine, mAb (GX41)
Highly specific monoclonal for ubiquitin remnant profiling via immunoprecipitation.
Identification of exact ubiquitinylation sites is challenging under physiological conditions, but the recent development of an immunoprecipitation approach allows for enrichment and identification of peptides derived from the ubiquitinated portion of proteins.
UPS and Diabetes: Disrupting the logistics of glucokinase regulation
2013 October 4 | Tags:
Epigenetics,
Proteasome
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Autophagy,
Cancer,
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