TRIM25 兔多克隆抗体-S0B6916

TRIM25 (tripartite motif-containing protein 25, also known as EFP) is a member of the TRIM family, characterized by an N-terminal RING finger domain (conferring E3 ubiquitin ligase activity), one or two B-box domains, a coiled-coil domain, and a C-terminal SPRY domain for substrate recognition. As an important E3 ubiquitin ligase, TRIM25 is best known for catalyzing the formation of K63-linked ubiquitin chains via its RING domain, thereby activating RIG-I (retinoic acid-inducible gene I) in the RIG-I signaling pathway and inducing type I interferon production, playing a central role in antiviral innate immune responses. Furthermore, TRIM25 is involved in regulating various cellular processes, including modulating estrogen receptor stability and transcriptional activity through ubiquitination, promoting cell proliferation and tumor development (often highly expressed in cancers such as breast and colorectal cancer), as well as regulating apoptosis, autophagy, and RNA metabolism. Notably, TRIM25 is also a key target of the influenza virus NS1 protein for antagonizing host immune responses; inhibition of its function leads to viral immune evasion. Additionally, abnormal expression or mutations in TRIM25 have been associated with the development of autoimmune diseases such as systemic lupus erythematosus.