E3 ubiquitin ligases are standards in most antibody catalogs. These proteins are essential to the process of ubiquitination, which is expressed in protein pathways throughout the body and is often linked to disease states. It is widely used as a biomarker, with ubiquitin antibodies being widely used to identify the protein accumulations (inclusion bodies) which occur in conditions such as Alzheimer’s, Parkinson’s and Huntington's disease.
The E3 ligases target specific proteins and are important in apoptosis and proteolysis. Their function is generally to assist polyubiquitination – the binding of multiple ubiquitin molecules to the same target protein – which is the signal for degradation (i.e. destruction) by the proteasome to begin. In combination with an E2 ubiquitin-conjugating enzyme, E3 ligases trigger the attachment of ubiquitin to lysine on their target proteins, via isopeptide bonding. Further ubiquitin molecules are then attached, one to the next.
Immunocytochemistry/Immunofluorescence: IBRDC2 Antibody
The IBR (In Between Ring fingers) family of proteins are so-called because of a specific domain, found between pairs of ring fingers. Other names include C6HC and DRIL (double ring finger linked) domain. Also called RBR proteins, they are found in all eukaryotic organisms. They are thought to play an indirect role in regulating DNA transcription and protein quality control.
In recent times, it has been discovered that IBR-type ligases play a part in ubiquitination, often forming part of cullin-containing ubiquitin ligase complexes. Mutated forms of the Parkin IBR ligase is known to be expressed in familial forms of Parkinson's disease. Recently, IBRDC2, one of the IBR-type E3 ubiquitin ligases covered by our antibody database at Novus Biologicals, has been suspected of regulating apoptosis and Bax activation.
Novus Biologicals offers many IBRDC2 reagents for your research needs including: