Anti-TRIP12 Antibody

Thyroid hormone receptors (TRs) are transcription factors that regulate the expression of specific genes in a hormone-dependent manner (1) . TRIP12 (thyroid hormone receptor interactor 12) is an ATP-dependent E3 ubiquitin ligase involved in the human ubiquitin fusion degradation (UFD) pathway and also modulates the NEDD8 pathway (2,3) . TRIP12 contains one WWE domain and a single HECT (E6AP-type E3 ubiquitin-protein ligase) domain suggested to contain a noncovalent ubiquitin-binding site (4) . TRIP12 acts as a key regulator of DNA damage response and the ubiquitin ligase activity of TRIP12 is essential for mouse development (5) .

TRIP12 antibody was raised against a 18 amino acid peptide near the carboxy terminus of human TRIP12. The immunogen is located within amino acids 1930 - 1980 of TRIP12.

E3 ubiquitin-protein ligase involved in ubiquitin fusion degradation (UFD) pathway and regulation of DNA repair. Part of the ubiquitin fusion degradation (UFD) pathway, a process that mediates ubiquitination of protein at their N-terminus, regardless of the presence of lysine residues in target proteins. In normal cells, mediates ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A, a lysine-less tumor suppressor required for p53/TP53 activation under oncogenic stress. In cancer cells, however, isoform p19ARF/ARF and TRIP12 are located in different cell compartments, preventing isoform p19ARF/ARF ubiquitination and degradation. Does not mediate ubiquitination of isoform p16- INK4a of CDKN2A. Also catalyzes ubiquitination of NAE1 and SMARCE1, leading to their degradation. Ubiquitination and degradation of target proteins is regulated by interaction with proteins such as MYC, TRADD or SMARCC1, which disrupt the interaction between TRIP12 and target proteins. Acts as a key regulator of DNA damage response by acting as a suppressor of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites, thereby acting as a guard against excessive spreading of ubiquitinated chromatin at damaged chromosomes.