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045257 Mouse Anti-RIG-I (RIG-1, Retinoic Acid-inducible Gene 1 Protein, DEAD-box Protein 58, Probable ATP-dependent RNA Helicase DDX58)

Specifications
References
Clone Type
Monoclonal
Host
Mouse
Source
Human
Swiss Prot
Q96C10
Isotype
IgG1
Clone Number
Alme-1
Grade
Affinity Purified
Applications
IHC IP WB
Crossreactivity
Hu Mo
Shipping Temp
Blue Ice
Storage Temp
-20°C
RIG-1, Retinoic Acid-inducible Gene 1 Protein, DEAD-box Protein 58, Probable ATP-dependent RNA Helicase DDX58

RIG-I and MDA5 are highly conserved helicases involved in the innate immune response to virus. RIG-I is a member of the DEAD-box RNA helicases and is activated by cytoplasmic dsRNA and 5'-ppp RNA produced during the viral replication. The protein is characterized by a N-terminal region with two caspase recruitment domains (CARD) and a C-terminal region harboring potential ATP-dependent RNA helicase activity. RIG-I recruits the CARD adaptor inducing IFN-beta (Cardif) in a CARD-CARD-dependent manner resulting in NF-kappaB and IRF3 activation.

Applications
Suitable for use in Immunohistochemistry, Immunoprecipitation and Western Blot. Other applications not tested.
Recommended Dilution
Immunohistochemistry: paraffin sections Immunoprecipitation: 1:200 Western Blot: 1:1000 Optimal dilutions to be determined by researcher.
Storage and Stability
May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 12 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Immunogen
Recombinant protein corresponding to aa201-713 from human RIG-I.
Form
Supplied as a liquid in PBS, 0.02% sodium azide, 10% glycerol.
Purity
Purified by Protein G affinity chromatography from concentrated hybridoma tissue culture supernatant. >95% (SDS-PAGE)
Specificity
Recognizes human RIG-I. Species Crossreactivity: mouse.
References
1. The antiviral adaptor proteins Cardif and Trif are processed and inactivated by caspases: M. Rebsamen, et al.; Cell Death Differ. 15:1804 (2008) 2. Phosphorylation-mediated negative regulation of RIG-I antiviral activity: M.U. Gack, et al.; J. Virol. 84:3220 (2010) 3. Incoming RNA Virus Nucleocapsids Containing a 5’-Triphosphorylated Genome Activate RIG-I and Antiviral Signaling: M. Weber, et al.; Cell Host Microbe 13:336 (2013) 4. Lymphocytic choriomeningitis virus differentially affects the virus-induced type I interferon response and mitochondrial apoptosis mediated by RIG-I/MAVS: C. Pythoud, et al.; J. Virol. 89:6240 (2015) 5. A hosphomimetic-based mechanism of dengue virus to antagonize innate immunity: Y.K. Chan & M.U. Gack; Nat. Immunol. 17:523 (2016) 6. Sensing of latent EBV infection through exosomal transfer of 5’pppRNA: S.R. Baglio, et al.; PNAS 113:E587 (2016) 7. RNAs Containing Modified Nucleotides Fail To Trigger RIG-I Conformational Changes for Innate Immune Signaling: A. Fiegen Durbin, et al.; MBio 7, e00833 (2016) 8. Viral unmasking of cellular 5S rRNA pseudogene transcripts induces RIG-I-mediated immunity: J.J. Chiang, et al.; Nat. Immunol. 19:53 (2018) 9. RIG-I recognizes the 5′ region of dengue and zika virus genomes: M. Chazal, et al.; Cell Rep. 24:320 (2018)
USBio References
No references available
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