Anti-Trim29 (Clone: ABM43D2)

TRIM29 (Tripartite motif-containing 29) is a member of the tripartite motif (TRIM) family of transcription factors, characterized by the conserved RING finger, B-box, and coiled-coil domains. The TRIM family has been implicated in a variety of physiologic processes including development, apoptosis and epithelial-mesenchymal transition (EMT). Depending on a tumor types, TRIM29 also may function as an oncogene or a tumor suppressor. As an oncogene, it facilitates tumor cell proliferation and invasion through stabilization of Beta-catenin. The mechanisms may also involve deactivation of p53 activity and promoting cell survival by inhibiting proapoptotic genes regulated by p53. As a histone binding protein TRIM29 is responsible for DDR (DNA damage response). It functions as a scaffold protein to assemble DNA repair proteins into chromatin followed by efficient activation of DDR. TRIM29 binds to modified histone H3 and H4 tails in the context of nucleosomes. Furthermore, chromatin binding of TRIM29 is required for the phosphorylation of H2AX nucleosomes and cell viability in response to ionizing radiation. Protein function: Plays a crucial role in the regulation of macrophage activation in response to viral or bacterial infections within the respiratory tract. Mechanistically, TRIM29 interacts with IKBKG/NEMO in the lysosome where it induces its 'Lys-48' ubiquitination and subsequent degradation. In turn, the expression of type I interferons and the production of proinflammatory cytokines are inhibited. Additionally, induces the 'Lys-48' ubiquitination of TMEM173/STING in a similar way, leading to its degradation. [The UniProt Consortium]