Catalog number: SBB-UP0013,10 mg
Ubiquitin, human recombinant, is a small (8.5 kDa) regulatory protein that has been found in almost all tissues of eukaryotic organisms. The addition of ubiquitin to a substrate protein is called ubiquitination or ubiquitylation. Ubiquitination can affect proteins in many ways: it can signal for their degradation via the proteasome, alter their cellular location, affect their activity, and promote or prevent protein interactions. [1][2][3][4][5]
Ubiquitin, human recombinant
Ubiquitin is a 76 amino acid post-translational modifier expressed throughout all tissues in eukaryotic organisms. The many roles of ubiquitin modification include proteasomal degradation, signal transduction, inflammatory response, and DNA damage repair. Ubiquitin modification occurs through a pyramidal cascade of an E1 activating enzyme, E2 conjugating enzymes, and an E3 ubiquitin ligases. This enzymatic cascade results in modification of a ɜ-amine of a lysine reside on a substrate protein. Substrates may either be mono or poly-ubiquitinated by M1, K6, 11, 27, 29, 33, 48 or 63 linkages. Removal of ubiquitin from a substrate protein occurs via deconjugating enzymes, of which there are nearly 100 known enzymes with various linkage specificities. This product consists of a full-length human, mature ubiquitin polypeptide (amino acids 1-76), expressed in E.coli. Typical working concentrations range from 250 to 750 µM.