Render Target: STATIC
Render Timestamp: 2024-12-26T12:00:32.429Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-08-01 15:24:33.688
Product last modified at: 2024-12-17T18:56:47.442Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

MDA-5 (D74E4) Rabbit mAb #5321

Filter:
  • WB
  • IP

    Supporting Data

    REACTIVITY H M
    SENSITIVITY Endogenous
    MW (kDa) 135
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:100

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    MDA-5 (D74E4) Rabbit mAb detects endogenous levels of total MDA-5 protein.

    Species Reactivity:

    Human, Mouse

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Arg470 of human MDA-5.

    Background

    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).
    MDA-5 (16,17), also named Ifih1 (interferon induced with helicase C domain 1), RH116 (RNA helicase-DEAD box protein 116) (18), or Helicard (19) is found to be induced by interferon. During apoptosis, MDA-5 is cleaved by caspases, separating the helicase and CARD domains (19). MDA-5 is uniquely activated by picornavirus (20) and measles virus (21).
    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.
    16. Kang, D.C. et al. (2002) Proc Natl Acad Sci U S A 99, 637-42.
    17. Kang, D.C. et al. (2004) Oncogene 23, 1789-800.
    18. Cocude, C. et al. (2003) J Gen Virol 84, 3215-25.
    19. Kovacsovics, M. et al. (2002) Curr Biol 12, 838-43.
    20. Kato, H. et al. (2006) Nature 441, 101-5.
    21. Berghäll, H. et al. (2006) Microbes Infect 8, 2138-44.
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