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AdipoGen Life Sciences
anti-Cardif (human), mAb (Adri-1)
Picture courtesy of Prof. Darius Moradpour, CHUV, Lausanne.
Product Details | |
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Synonyms | CARD Adapter Inducing Interferon-β; IPS-1; MAVS; Mitochondrial Antiviral Signaling Protein; VISA; Virus-induced Signaling Adapter; Interferon-β Promoter Stimulator Protein 1 |
Product Type | Monoclonal Antibody |
Properties | |
Clone | Adri-1 |
Isotype | Mouse IgG2b |
Source/Host | Purified from concentrated hybridoma tissue culture supernatant. |
Immunogen/Antigen | Recombinant human Cardif (aa 160-450). |
Application |
Immunocytochemistry: (1:100) |
Crossreactivity | Human |
Specificity |
Recognizes human Cardif. |
Purity | ≥95% (SDS-PAGE) |
Purity Detail | Protein G-affinity purified. |
Concentration | 1mg/ml |
Formulation | Liquid. In PBS containing 10% glycerol and 0.02% sodium azide. |
Isotype Negative Control | |
Shipping and Handling | |
Shipping | BLUE ICE |
Short Term Storage | +4°C |
Long Term Storage | -20°C |
Handling Advice |
After opening, prepare aliquots and store at -20°C. Avoid freeze/thaw cycles. |
Use/Stability | Stable for at least 1 year after receipt when stored at -20°C. |
Documents | |
MSDS | Download PDF |
Product Specification Sheet | |
Datasheet | Download PDF |
RIG-I (retinoic acid-inducible gene I; Ddx58) and MDA5 (melanoma differentiation-associated gene 5, also known as Ifih1 or Helicard) are proteins that sense viral replication intermediates, such as double-stranded RNA and triggers the host antiviral programs. These molecules signal the downstream activation of NF-κB and IFN regulatory factor (IRF) -3, which coordinately regulate the expression of type-I interferons. Cardif (also called VISA/IPS-1/MAVS) is a new CARD (caspase activation and recruitment domain)-containing adaptor protein that interacts with the CARD domain of RIG-I and MDA5, leading to the activation of NF-κB and IRF3. Cardif is located to the mitochondrial outer membrane. Removal of the mitochondrial-targeting domain of cardif abolishes its ability to induce IFNs. Cardif is cleaved and inactivated by NS3-4A, a serine protease from hepatitis C virus known to block interferon-β production.
- TRADD Protein Is an Essential Component of the RIG-like Helicase Antiviral Pathway: M.C. Michallet, et al.; Immunity 28, 651 (2008)
- Cleavage of mitochondrial antiviral signaling protein in the liver of patients with chronic hepatitis C correlates with a reduced activation of the endogenous interferon system: P. Bellecave, et al.; Hepatology 51, 1127 (2010)
- Quantitative proteomics identifies the membrane-associated peroxidase GPx8 as a cellular substrate of the hepatitis C virus NS3-4A protease: K. Morikawa, et al.; Hepatology 59, 423 (2014)
- Hepatitis C virus variants resistant to macrocyclic NS3-4A inhibitors subvert IFN-β induction by efficient MAVS cleavage: C. Welsch, et al.; J. Hepatol. 62, 779 (2015)
- Extended interaction networks with HCV protease NS3-4A substrates explain the lack of adaptive capability against protease inhibitors: G. Dultz, et al.; J. Biol. Chem. 295, 13862 (2020)
- Deficiency in coatomer complex I causes aberrant activation of STING signalling: A. Steiner, et al.; Nature Comm. 13, 2321 (2022)