IFIT5 Recombinant Rabbit mAb (S-4213-30)

IFIT5 (Interferon-Induced Tetratricopeptide Repeat Protein 5) is a key effector protein in the human innate immune system. It is induced by interferon stimulation and functions as an RNA-binding protein that directly recognizes and binds to viral RNA molecular patterns, thereby blocking viral replication. Its unique feature lies in its ability to specifically bind single-stranded RNA carrying a 5'-triphosphate group (5'-PPP) or lacking the typical 2'-O-methylation modification found on host mRNAs—an important molecular signature for distinguishing "self" from "non-self" RNA. Structurally, IFIT5 consists of multiple TPR domains that form a positively charged binding groove, which tightly encloses the 5' end of viral RNA in a sequence-independent manner. Beyond direct viral RNA binding, IFIT5 also acts as a positive regulator that activates the canonical NF-κB signaling pathway, further potentiating the immune response. Moreover, studies have revealed a dual-faced nature of IFIT5 function: in certain cancers, its aberrant overexpression may promote tumor metastasis by degrading tumor-suppressive microRNA precursors.