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REACTIVITY SENSITIVITY MW (kDa) SOURCE
102 Rabbit

Product Usage Information

Storage: Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

Specificity / Sensitivity

Rig-I Antibody detects endogenous levels of total Rig-I protein.


Species predicted to react based on 100% sequence homology: Monkey

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues at the carboxyl terminus of human Rig-I. Antibodies were purified by protein A and peptide affinity chromatography.

Antiviral innate immunity depends on the combination of parallel pathways triggered by virus detecting proteins in the Toll-like receptor (TLR) family and RNA helicases, such as Rig-I (retinoic acid-inducible gene I) and MDA-5 (melanoma differentiation-associated antigen 5), which promote the transcription of type I interferons (IFN) and antiviral enzymes (1-3). TLRs and helicase proteins contain sites that recognize the molecular patterns of different virus types, including DNA, single-stranded RNA (ssRNA), double-stranded RNA (dsRNA), and glycoproteins. These antiviral proteins are found in different cell compartments; TLRs (i.e. TLR3, TLR7, TLR8, and TLR9) are expressed on endosomal membranes and helicases are localized to the cytoplasm. Rig-I expression is induced by retinoic acid, LPS, IFN, and viral infection (4,5). Both Rig-I and MDA-5 share a DExD/H-box helicase domain that detects viral dsRNA and two amino-terminal caspase recruitment domains (CARD) that are required for triggering downstream signaling (4-7). Rig-I binds both dsRNA and viral ssRNA that contains a 5'-triphosphate end not seen in host RNA (8,9). Though structurally related, Rig-I and MDA-5 detect a distinct set of viruses (10,11). The CARD domain of the helicases, which is sufficient to generate signaling and IFN production, is recruited to the CARD domain of the MAVS/VISA/Cardif/IPS-1 mitochondrial protein, which triggers activation of NF-κB, TBK1/IKKε, and IRF-3/IRF-7 (12-15).


1.  Yoneyama, M. and Fujita, T. (2007) J Biol Chem 282, 15315-8.

2.  Meylan, E. and Tschopp, J. (2006) Mol Cell 22, 561-9.

3.  Thompson, A.J. and Locarnini, S.A. (2007) Immunol Cell Biol 85, 435-45.

4.  Imaizumi, T. et al. (2002) Biochem Biophys Res Commun 292, 274-9.

5.  Zhang, X. et al. (2000) Microb Pathog 28, 267-78.

6.  Yoneyama, M. et al. (2005) J Immunol 175, 2851-8.

7.  Yoneyama, M. et al. (2004) Nat Immunol 5, 730-7.

8.  Hornung, V. et al. (2006) Science 314, 994-7.

9.  Pichlmair, A. et al. (2006) Science 314, 997-1001.

10.  Kato, H. et al. (2006) Nature 441, 101-5.

11.  Childs, K. et al. (2007) Virology 359, 190-200.

12.  Meylan, E. et al. (2005) Nature 437, 1167-72.

13.  Xu, L.G. et al. (2005) Mol Cell 19, 727-40.

14.  Kawai, T. et al. (2005) Nat Immunol 6, 981-8.

15.  Seth, R.B. et al. (2005) Cell 122, 669-82.


Entrez-Gene Id 23586
Swiss-Prot Acc. O95786


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