Anti-Viperin

0.5 mg/ml antibody in PBS with 0.1 mg/ml BSA (US source) and 0.05% sodium azide. Viral infection induces the interferon (IFN) response which triggers the production of an array of anti-viral proteins. Viperin (Virus inhibitory protein, endoplasmic reticulum-associated, interferon-inducible) is expressed in response to IFN-b binding to the IFN receptor, inducing the formation of the IFN-stimulated gene factor 3 complex which then binds to the Viperin promoter. It inhibits many DNA and RNA viruses through a diverse range of mechanisms and is involved in the PRR-mediated innate immune response. Viperin has been shown to be produced in response to TLR3 and TLR4 activation, but not TLR2 and TLR5. It may be involved in the TLR7 and TLR9-induced production of type I IFN by plasmacytoid dendritic cells (pDCs). Protein function: Interferon-inducible iron-sulfur (4FE-4S) cluster- binding antiviral protein which plays a major role in the cell antiviral state induced by type I and type II interferon. Can inhibit a wide range of DNA and RNA viruses, including human cytomegalovirus (HCMV), hepatitis C virus (HCV), west Nile virus (WNV), dengue virus, sindbis virus, influenza A virus, sendai virus, vesicular stomatitis virus (VSV), and human immunodeficiency virus (HIV-1). Displays antiviral activity against influenza A virus by inhibiting the budding of the virus from the plasma membrane by disturbing the lipid rafts. This is accomplished, at least in part, through binding and inhibition of the enzyme farnesyl diphospate synthase (FPPS), which is essential for the biosynthesis of isoprenoid-derived lipids. Promotes TLR7 and TLR9-dependent production of IFN-beta production in plasmacytoid dendritic cells (pDCs) by facilitating Lys-63'-linked ubiquitination of IRAK1. Plays a role in CD4+ T-cells activation and differentiation. Facilitates T-cell receptor (TCR)-mediated GATA3 activation and optimal T-helper 2 (Th2) cytokine production by modulating NFKB1 and JUNB activities. Can inhibit secretion of soluble proteins. [The UniProt Consortium]