epitope mapping near the C-terminus of Mms2 of mouse origin
recommended for detection of Mms2 of mouse, rat and human origin by WB, IP, IF and ELISA; also reactive with additional species, including equine, canine, bovine, porcine and avian
Mms2 Background Information Uev1A (also designated ubiquitin-conjugating enzyme E2 variant 1 (UEV1) and CROC1) and Mms2 (UEV2) proteins are similar in sequence and in predicted structure to the ubiquitin-conjugating enzymes or E2s, but lack a critical cysteine residue essential for the catalytic activity of E2 enzymes. Therefore, Uev1A does not have ubiquitin-conjugating activity in vitro. However, constitutive expression of exogenous Uev1A in colon carcinoma cells inhibits their capacity to differentiate upon confluence. Studies on recombinant Uev1A show that it localizes to the nucleus, excluding the nucleolar regions. Uev1A functions with TRAF6, a RING domain protein, to catalyze the synthesis of unique polyubiquitin chains linked through Lysine 63 of ubiquitin. UBC13 (ubiquitin-conjugating enzyme E2N (UBE2N)) may be involved in protein degradation mainly in the muscles and testis. In yeast, Mms2/UBC13 complex assembles novel polyubiquitin chains for signaling in DNA repair, and suggests that UEV proteins may act to increase diversity and selectivity in ubiquitin conjugation.
