IFIT1 Recombinant Rabbit mAb (S-5120)

IFIT1 (Interferon-Induced Protein with Tetratricopeptide Repeats 1, also known as ISG56) is a core member of the interferon-stimulated gene family and serves as a critical antiviral effector protein, playing a key inhibitory role in the host innate immune response. The canonical structural feature of this protein is its multiple tandem tetratricopeptide repeat (TPR) domains, which form a superhelical structure that mediates protein-protein interactions, enabling the recognition and binding of viral RNA molecules with atypical 5' ends. As a broad-spectrum antiviral factor, IFIT1 specifically recognizes and binds viral RNAs lacking 2'-O-methylation modification or possessing 5'-triphosphate groups, thereby competitively inhibiting the binding of viral mRNA to the host translation initiation complex and blocking viral protein synthesis. Unlike classical enzyme-active effector proteins, IFIT1 lacks catalytic function and instead sequesters foreign RNA molecules directly through a "molecular trapping" mechanism, a mode of action that confers inhibitory effects against a wide range of RNA viruses, including influenza virus, dengue virus, and hepatitis C virus. Furthermore, the expression of IFIT1 is tightly regulated by the type I interferon signaling pathway, and its expression level directly influences the host's ability to resist viral infection. Clinical studies have shown that certain viruses, such as SARS-CoV-2, can encode specific proteases to cleave IFIT1 and evade immune responses, while polymorphisms in the IFIT1 gene are closely associated with susceptibility to various viral infectious diseases and autoimmune disorders, highlighting the dual role of this protein in infection immunity and inflammatory regulation.