Progression of the mammalian cell cycle is regulated mainly by phosphorylation/dephosphorylation and synthesis/degradation of many key proteins. Ubiquitin, a soluble protein of 76 amino acids, is enzymatically attached to an ε-NH2-Lys in a target protein. Ubiquitination is a hallmark for rapid protein degradation of the target protein in the proteosome-a cytoplasmic complex of proteases. Several human homologs of the yeast ubiquitin-conjugating enzymes (Ubc) have been identified and found involved in critical processes such as cell cycle progression and apoptosis. UbcH7 was characterized as an E6-AP-interacting protein required for the ubiquitination of p53. E6-AP is the ubiquitin ligase used as bait in the search for interacting proteins required for the proper ubiquitination of cellular targets. UbcH7 interacts with the C-terminal region of E6-AP named the hect domain. Therefore, UbcH7 is another protein, like Ubc9, involved in the degradation and regulation of critical proteins in the cell cycle.
This antibody is routinely tested by western blot analysis. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.