RIG-I Antibody (2M6F10)

RIG-I, an RNA helicase of the DEAD/H box family, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), is implicated in a number of cellular processes involving RNA binding and alteration of RNA secondary structure and in innate immune defense against viruses. It acts as a specific sensor for dsRNA, which is absent in uninfected cells but known to be accumulated in virus-infected cells. It contains two CARD domains, one helicase ATP-binding domain and the other helicase C-terminal domain. The CARD domains actually inhibit the activity of RIG-I in normal cell, but once the cell gets infected, RIG I directly binds uncapped 5-prime-triphosphate RNA present in viruses triggering an immune response signal. The signaling cascade involves MAVS/IPS1 which induces the expression of antiviral cytokines such as IFN-beta and RANTES (CCL5) during viral replication through activation of NF-kappa-B, IRF3 and IRF7. The ability of RIG I to sense 5-prime-phosphorylated RNA evolved in the innate immune system as a means of discriminating between self and nonself.

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

We have publications tested in 2 confirmed species: Human, Porcine.

We have publications tested in 1 application: WB.

Showing Publications 1 - 2 of 2.

Publications using NBP2-27109	Applications	Species
De Luna N, Suarez-Calvet X, Lleixa C et al. Hypoxia triggers IFN-I production in muscle: Implications in dermatomyositis Sci Rep 2017-08-17 [PMID: 28819164] (WB, Human)	WB	Human
Pei J, Deng J, Ye Z et al. Absence of autophagy promotes apoptosis by modulating the ROS-dependent RLR signaling pathway in classical swine fever virus-infected cells Autophagy 2016-07-27 [PMID: 27463126] (WB, Porcine)	WB	Porcine

Array NBP2-27109

• RIG-I Antibodies
• RIG-I Lysate
• RIG-I Protein