Applications Key: W=Western Blotting IP=Immunoprecipitation Reactivity Key: H=Human M=Mouse R=Rat Mk=Monkey Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
UbcH5C (D60E2) Rabbit mAb detects endogenous levels of total UbcH5C protein.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Asp135 of human UbcH5C protein.
Western Blotting
Western blot analysis of extracts from various cell lines using UbcH5C (D60E2) Rabbit mAb.
Background
Protein ubiquitination requires the concerted action of the E1, E2 and E3 ubiquitin-conjugating enzymes. Ubiquitin is first activated through an ATP-dependent formation of a thiol ester with an E1 enzyme. The activated ubiquitin is then transferred to a thiol-group of an E2 ubiquitin-conjugation enzyme. The final step is the transfer of ubiquitin from E2 to an ε-amino group of a lysine residue on the target protein, a transfer mediated by ubiquitin-conjugating enzyme E3 (1). UbcH5C is a universally expressed E2 ubiquitin conjugating enzyme and member of the UbcH5 family that also includes UbcH5A and UbcH5B (2). Evidence suggests that UbcH5C plays an important role in regulating a number of signaling pathways by catalyzing the ubiquitination of key target proteins, including p53, PCNA, the IκB kinase protein NEMO, and the apoptosis inhibitor BRUCE (3-6). Gene expression profiles revealed increased expression of UbcH5C in meibomian cell carcinoma and oncocytic thyroid adenomas (7,8), while an RNAi screen reveals diffrential Ubc5HC in acute promyelocytic cells (9). These results suggest a potential role of UbcH5C in cell cycle control and tumorigenesis.