RSAD2 (Radical S-adenosyl methionine domain-containing protein 2), also known as CIG5 (Cytomegalovirus-induced gene 5 protein), vig1, viperin or CIG33, is a 361 amino acid protein that is involved in antiviral defense against pathogens such as Hep C, Cytomegalovirus and HIV-1. Localized to the cytosolic side of the endoplasmic reticulum and relocated to the Golgi apparatus upon viral infection, RSAD2 is thought to prevent viral budding by disrupting lipid rafts at the plasma membrane and supporting the Interferon-induced antiviral state of the cell. Additionally, RSAD2 can bind to and inactivate FDPS (an enzyme that is crucial for the synthesis of cholesterol and geranylated and farnesylated proteins), thereby playing a role in lipid synthesis. Overexpression of RSAD2 leads to abnormal lipid accumulation that is associated with atherosclerosis, a chronic inflammatory disease characterized by hardened arteries.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFIHCELISA
recommended for detection of RSAD2 of mouse, human, canine and zebra fish origin by WB, IP, IF, IHC(P) and ELISA