|Detection of Human RIG-I by Western Blot. Western blot shows lysates of A172 human glioblastoma cell line and Nalm‑6 human Pre‑B acute lymphocytic leukemia cell line. PVDF membrane was probed with 1 µg/mL of Goat Anti-Human RIG-I Antigen Affinity-purified Polyclonal Antibody (Catalog # AF4859) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF019). A specific band was detected for RIG-I at approximately 105 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 8.|
RIG-I (Retinoic-acid inducible gene I; also Dead-box protein 58) is a 100 kDa member of the DexH-box family of proteins. It is expressed in smooth muscle cells and endothelium. RIG-I is normally an inactive monomer. Upon Sendai and Hepatitis C virus infection, RIG-I binds to dsRNA, initiating homodimerization and downstream activation of IRF3 and KF kappa B genes. Human RIG-I is 925 amino acids (aa) in length. It contains two CARD domains (aa 1‑172), one helicase ATP-binding region (aa 251‑430), and one C-terminal repressor domain (aa 735‑925). There are three potential splice variants. One shows an alternate start site at Met204, while another shows deletion of aa 3‑80, and a third shows a deletion of aa 36‑80 plus 749‑925. Over aa 724‑925, human RIG-I is 76% aa identical to mouse RIG-I.
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