Ubiquitin is a 76 amino acid protein that is highly conserved.  It is found is all plant and animal species and is produced in response to stress.  The formation of ubiquitin-protein conjugates is a signal for the selective degradation of proteins.  Ubiquitin has been immunohistochemically localized to a number of pathological inclusions. These lesions include Lewy bodies of Parkinson's disease, neurofibrillary tangles of Alzheimer's disease, Pick bodies of Pick's disease, Mallory bodies of alcoholic liver disease, cytoplasmic bodies of a specific myopathy, and Rosenthal fibers within astrocytes.

A rabbit antiserum to a purified preparation of human ubiquitin protein is currently available.  This antiserum has been shown to be immunoreactive with the purified protein by ELISA. This antiserun reacts immunohistochemically with ubiquitin-containing lesions in formalin-fixed, paraffin-embedded tissue. This antiserum is especially useful for the immunohistochemical identification of Lewy bodies, which are not well differentiated by histochemical stains. It will also immunolabel ubiquitin on protein blots.  This antibody should be a valuable tool for scientists working to understand the role of ubiquitin in various neurological diseases.

Manufacturing Reference:

Sparkman, D.R., et al.  Prep. Biochem. 21:93-104, 1991.