TRIM16 (F3S3I) Rabbit Monoclonal Antibody #38910

Misfolded proteins are cleared in cells by ubiquitination and degradation using the proteasome and autophagy pathways (1-5). Various factors, including mutations, oxidative stress, and environmental conditions, can trigger increased protein misfolding and overwhelm cells, resulting in aggregation, accumulation, and disease (2,3). Tripartite Motif-Containing Protein 16 (TRIM16) was first discovered to regulate the NRF2 pathway (3) along with other autophagy proteins, such as Beclin-1, ULK1, and ATG16L, helping to facilitate protein aggregate clearing (1-3,6). TRIM16 plays an important role in cellular defense against oxidative stress and autophagy (4-6). The TRIM family of proteins is highly conserved and has been implicated in a diverse range of biological processes, including development, cell growth, differentiation, innate immune functions, and cancer (4). TRIMs most commonly have a RING finger domain, B-box domains, a coiled-coil domain, and a variable C-terminal domain (4). Specifically, TRIM16 lacks a RING domain but possesses two B-box domains and a C-terminal SPRY domain. TRIM16 has recently been shown to function as an E3 ubiquitin ligase (1,4). TRIM16 is also studied as a tumor suppressor, influencing cell differentiation and migration, and has been implicated in various cancers (7-9), including pancreatic, bladder (9), and breast cancer (7).