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Render Timestamp: 2024-12-10T21:51:42.227Z
Commit: 611277b6de3cd1bb065350b6ef8d63df412b7185
XML generation date: 2024-10-10 16:01:13.813
Product last modified at: 2024-12-03T22:15:08.706Z
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PDP - Template Name: Antibody Sampler Kit
PDP - Template ID: *******4a3ef3a

MAVS Signalosome Antibody Sampler Kit #40415

    Product Information

    Product Description

    The MAVS Signalosome Antibody Sampler Kit provides an economical means of detecting the activation of signaling pathways in which MAVS plays a critical role. The kit includes enough antibodies to perform two western blot experiments with each primary antibody.

    Specificity / Sensitivity

    Each antibody in the MAVS Signalosome Antibody Sampler Kit detects endogenous levels of its target protein. TRAF2 (C192) Antibody detects endogenous levels of total human TRAF2 protein. No cross-reactivity was detected with other family members at physiological conditions. Phospho-TBK1/NAK (Ser172) (D52C2) XP® Rabbit mAb detects endogenous levels of TBK1 only when phosphorylated at Ser172. This antibody may cross-react with phospho-IKKε. Phospho-IRF-3 (Ser386) (E7J8G) XP® Rabbit mAb recognizes endogenous levels of IRF-3 protein only when phosphorylated at Ser386. Phospho-IRF-3 (Ser396) (D6O1M) Rabbit mAb recognizes endogenous levels of IRF-3 protein only when phosphorylated at Ser396.

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Cys192 of human TRAF2. Antibodies are purified by protein A and peptide affinity chromatography. Monoclonal antibodies are produced by immunizing animals with recombinant human IRF-3 protein and recombinant protein specific to a central region of mouse TRAF6, or synthetic phosphopeptides corresponding to residues surrounding Ser172 of human TBK1, Ser386 of human IRF-3, and Ser396 of human IRF-3 protein, or synthetic peptides corresponding to residues surrounding Leu202 of human MAVS and Ala327 of human TRAF3, or near the carboxy terminus of human TBK1/NAK protein.

    Background

    Recognition of conserved molecular structures of viruses by host pattern-recognition receptors (PRRs) initiates innate antiviral immune responses. Several families of PRRs have been demonstrated to sense different microbial components (1,2). The RIG-I-like receptor (RLR) family, including RIG-I, MDA5, and LGP2, are the primary PRRs to recognize viral RNAs (3,4). Upon binding to viral RNA, these receptors undergo conformation change, leading to their interaction with mitochondrial antiviral signaling protein (MAVS). MAVS subsequently forms large prion-like polymers and serves as a platform to recruit multiple components, including TRAF proteins and TBK1, to form the so-called MAVS signalosome. MAVS signalosome, in turn, activates the IRF-3 and NF-kB pathways, leading to the production of type I IFNs and pro-inflammatory cytokines (5-9).
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