anti-Ubiquitin antibody: Ubiquitin (Ub) is a small, 76-residue, protein (8.5 kDa) found both as free monomer and covalently attached to itself and other proteins in eukaryotic cells. Free Ub is a very compact and stable molecule that is easily refolded after being denatured. It is therefore recommended that for detection of free Ub on Westerns, the Tris-Tricine SDS-PAGE is used and nitrocellulose filters are autoclaved after the transfer and before blocking and addition of anti-Ub antibodies. The C-terminus of ubiquitin forms an isopeptide bond with the e-amino group of a lysine side chain in a target protein. In this way proteins can be covalently modified by the addition of ubiquitin which may alter the target protein's function. Monoubiquitination generally targets proteins for internalization, endocytosis and lysosomal degradation, or modifies the surface charge of histones and affects chromatin compaction. Conjugation of ubiquitin (Ub) involves a three-step mechanism whereby specific enzymes (or enzyme complexes) activate and covalently link Ub to their substrates.
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