Millipore Sigma Vibrant Logo
 
Life Science Research
 

Ubiquitin Antibodies

 Request Information

Featured Ubiquitination Assay
Measurement of 20S proteasome activity using the proteasome activity assay kit.
20S Proteasome Activity Assay
Merck’s Proteasome Activity Assay Kit provides a simple and convenient means for assaying proteasome activity that recognizes the substrate LLVY. The assay is based on detection of the fluorophore 7-Amino-4-methylcoumarin (AMC) after cleavage from the labeled substrate LLVY-AMC. 
A protein marked for degradation is covalently attached to multiple molecules of ubiquitin, a highly conserved 76 aa (8.6 kda) protein, which escorts it for rapid hydrolysis to the 26S proteasome.
The ubiquitin-proteasome pathway has been implicated in several forms of malignancy, in the pathogenesis of several genetic diseases, and in the pathology of muscle wasting. It is also involved in the destruction of proteins that participate in cell cycle progression, transcription control, signal transduction, proliferation, apoptosis and metabolic regulation. Merck’s tools for studying ubiquitin signaling have helped immensely in understanding the biological role and importance of the ubiquitin-proteasome pathway. Merck is also the first provider of lead discovery services to target the ubiquitination pathway: visit our Lead Discovery Ubiquitin page.
Featured Ubiquitination Antibodies
Anti-ubiquitinylated proteins.
Anti-Ubiquitinylated proteins, clone FK2
Ubiquitin is a polypeptide of 76 amino acid residues, being a very highly conserved and widely distributed protein in all eukaryotic cells. In these processes, ubiquitin functions as both a signal for protein degradation and as a chaperone promoting the formation of organelles. Recognizes mono- and poly ubiquitinylated proteins, but not free ubiquitin.

Learn More 
Anti-ubiquitinylated proteins.
Anti-Ubiquitinylated proteins, clone FK21
Ubiquitin is a polypeptide of 76 amino acid residues, being a very highly conserved and widely distributed protein in all eukaryotic cells. In these processes, ubiquitin functions as both a signal for protein degradation and as a chaperone promoting the formation of organelles. Recognizes only poly-ubiquitinylated proteins and not mono-ubiquitinylated proteins or free ubiquitin.

Learn More 


Histone H3 modification sites including ubiquitinylation sites.
Histone Ubiquitination in Nuclear Signaling
Ubiquitination is required for certain histone methylation events and involves ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s), and ubiquitin-protein ligases (E3s). Our wide range of products for measuring ubiquitination, includes unique antibodies for specific ubiquitin linkages and modified histone residues.