TRIM11 Recombinant Rabbit mAb (S-2960-11)

TRIM11 is an E3 ubiquitin ligase of the TRIM family that suppresses proteotoxicity by acting as a dual-function chaperone-disaggregase and proteasome activator: it binds misfolded or aggregation-prone proteins such as tau, α-synuclein and Atxn1-82Q, prevents their aggregation, dissolves pre-formed fibrils, and then targets them for SUMOylation and proteasomal degradation by displacing the de-ubiquitinase USP14 from the 26S proteasome, thereby enhancing overall proteolysis; concurrently TRIM11 ubiquitinates and destabilizes specific regulatory proteins (Axin1, PAX6, ARC105, PHOX2B, TBK1, PHLPP1) to modulate Wnt/β-catenin, neurogenesis, TGF-β, IFN-β and AKT signaling, and its expression is up-regulated in many cancers where it drives proliferation, invasion, glycolysis and ferroptosis resistance, while its down-regulation in Alzheimer’s disease contributes to toxic tau accumulation, positioning TRIM11 as a central node linking protein-quality-control, innate immunity and oncogenesis.