PA1-187 detects both the ubiquitin monomer as well as poly-ubiquitinated proteins of various molecular weights.
Ubiquitin is a conserved 76 amino acid polypeptide and can affect proteasomal degradation of the protein it is bound to, or mediate interactions with other proteins related to post-translational modifications. The degradation of cellular regulatory proteins by the Uubiquitin pathway is important as it controls the cellular growth and proliferation. Ubiquitin-dependent proteolysis occurs after a covalent attachment of the peptide to a lysine residue of a protein, which involves three enzymatic reactions: E1, E2 and E3. The first reaction involves ubiquitin-activating enzyme. The third reaction uses enzyme ubiquitin ligase (E3) to transfer the activated ubiquitin from E2 to a lysine residue on a protein, or directly transfers the ubiquitin from E2 to the substrate.
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Protein Aliases: 40S ribosomal protein S27a; epididymis luminal protein 112; epididymis secretory protein Li 50; Polyubiquitin B; Polyubiquitin-B; Small ribosomal subunit protein eS31; Ubiquitin; ubiquitin and ribosomal protein S27a; Ubiquitin B; ubiquitin C; Ubiquitin carboxyl extension protein 80; Ubiquitin-40S ribosomal protein S27a; ubiquitin-40S ribosomal protein S27a-like; ubiquitin-CEP80
Gene Aliases: 0610006J14Rik; AL033289; CEP80; HEL-S-50; HEL112; RPS27A; S27A; Uba52; UBA80; UBB; Ubb2; UBC; UBCEP1; UBCEP80