Ubiquitin is a small, highly conserved protein which plays an important role in protein breakdown, covalently bonding to proteins to mark them for proteolytic degradation in a process called ubiquitination. Ubiquitin also binds to inclusion bodies (accumulations of protein) in pathological conditions such as Parkinson’s and Alzheimer's disease. Ubiquitin antibody products are therefore useful for identifying inclusions in neuroscience research.
The Ubiquitin Proteasome Pathway, or UPP, is the principal method for protein degradation in normal cells, and central to the regulation of many cellular processes, including apoptosis; biogenesis; cell division; DNA transcription; cellular differentiation; modulation of ion channels, and DNA repair. Defects in the pathway have been linked to a number of important human diseases.
Protein degradation takes place in two stages: the protein is first covalently tagged by binding to multiple ubiquitin molecules, in a process known as conjugation, before being degraded by the 26S proteasome. Covalent linkage occurs as both single molecules and poly-ubiquitin chains, with the protein binding to lysine residues on the target protein via a series of enzymatically-controlled steps. Research with ubiquitin antibodies has shown the protein can also be conjugated to itself, resulting in diverse chain linkages. Initially, the protein was thought to play a “housekeeping” role, regulating antigenic-peptide generation and protein turnover. However, recent ubiquitin antibody studies have identified non-degenerative roles in, for example, endocytosis and DNA repair.
Ubiquitin antibodies are widely used in immunohistochemistry to identify abnormal protein inclusions. These include the neurofibrillary tangles of Alzheimer's disease; Lewy bodies of Parkinson's disease; Mallory bodies in alcoholic liver disease and Pick disease Pick bodies. The ubiquitin antibody can also identify the Rosenthal fibers of astrocytes.
Novus Biologicals offers many Ubiquitin reagents for your research needs including: