Anti-Ubiquitin

Ubiquitin is a 76 amino acid, highly conserved protein of about 8.5kD which is highly conserved evolutionarily. All plant and animal species are observed to express ubiquitin. Ubiquitin is produced in response to stress. The formation of ubiquitin-protein conjugates is a signal for the selective degradation of proteins. To perform this function, the protein to be degraded is first covalently attached to the C-terminus of ubiquitin, and the ubiquitinated complex is then recognized by a complex of degradative enzymes. Ubiquitin also becomes covalently bonded to many types of pathological inclusions, which appear to be resistant to normal degradation. Ubiquitin has been immunohistochemically localized to a number of pathological inclusions, including: 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 in specific myopathy, and Rosenthal fibers within astrocytes. All are heavily ubiquitinated and can be readily visualized with ubiquitin antibodies. Applications: Suitable for use in Immunohistochemistry and Western Blot. Other applications have not been tested. Recommended Dilutions: Immunohistochemistry (Parafin/Frozen): 1:2000-1:5000 (human brain sections), Western Blot: 1:1000-1:2000, Optimal dilutions to be determined by the researcher. Storage and Stability: Lyophilized and reconstituted products are stable for 12 months after receipt at -20°C. Reconstitute with sterile ddH2O. Aliquot to avoid repeated freezing and thawing. Store at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.