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Ubiquitin is a highly conserved globular 76 amino acid protein of about 8.5 kDa molecular weight. It has an important role in the targeting of proteins for proteolytic degradation. Proteins to be degraded are covalently coupled to the C-terminus of ubiquitin by means of ubiquitin ligases. The ubiquitin itself is frequently also ubiquitinated, producing a polyubiquitin chain. The polyubquitinated complex is then recognized by a complex of degradative enzymes which together form the proteosome. Interestingly, ubiquitin also becomes covalently bonded to many types of pathological inclusions seen in serious human disease states which appear to be resistant to normal degradation, so that ubiquitin antibodies are very useful for studies of these inclusions. For example the neurofibrillary tangles and paired helical filaments diagnostic of Alzheimer’s disease, the Lewy bodies seen in Parkinson’s disease, and Pick bodies found in Pick’s disease are all heavily ubiquitinated and can all be readily visualized with ubiquitin antibodies of appropriate specificity.
Image: MO22152 staining of cerebral cortex of an Alzheimer patient. Neurofibrillary tangles and dystrophic neurites associated with senile plaques stain strongly with this antibody. In the center is a typical neurofibrillary tangle containing neuron
Image: Blots of mono and polyubiquitin (lane 1), monoubiquitin only (2), and 100 μg total wet weight of cerebellum , cortex and brain stem respectively (lane 3-5). Material was run out on 20% SDS-PAGE and transferred electrophoretically to PVDF
MO22152 was raised against purified ubiquitin conjugated with glutaraldehyde to keyhole limpet hemocyanin. This antibody can used to study ubiquitinated inclusions seen in Alzheimer’s and other kinds of disease; such as such as the Lewy bodies of Parkinson’s disease and the Pick bodies in Pick’s disease in formalin fixed tissues. It can be used on mildly fixed histological sections of human brain, and paraffin embedded material.