Render Target: STATIC
Render Timestamp: 2024-12-26T11:20:45.141Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-09-20 06:15:33.229
Product last modified at: 2024-12-17T18:49:57.399Z
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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.

MAVS (D5A9E) Rabbit mAb (PE Conjugate) #18930

Filter:
  • F

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa)
    Source/Isotype Rabbit IgG
    Application Key:
    • F-Flow Cytometry 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Description

    This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometric analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated MAVS (D5A9E) Rabbit mAb #24930.

    Product Usage Information

    Application Dilution
    Flow Cytometry (Fixed/Permeabilized) 1:50

    Storage

    Supplied in PBS (pH 7.2), less than 0.1% sodium azide and 2 mg/ml BSA. Store at 4°C. Do not aliquot the antibodies. Protect from light. Do not freeze.

    Protocol

    Specificity / Sensitivity

    MAVS (D5A9E) Rabbit mAb (PE Conjugate) recognizes endogenous levels of total MAVS protein.

    Species Reactivity:

    Human

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Leu202 of human MAVS protein.

    Background

    The mitochondrial antiviral signaling protein (MAVS, VISA) contributes to innate immunity by triggering IRF-3 and NF-κB activation in response to viral infection, leading to the production of IFN-β (1). The MAVS protein contains an N-terminal CARD domain and a C-terminal mitochondrial transmembrane domain. The MAVS adaptor protein plays a critical and specific role in viral defenses (2). MAVS acts downstream of the RIG-I RNA helicase and viral RNA sensor, leading to the recruitment of IKKε, TRIF, and TRAF6 (3,4). Some viruses have evolved strategies to circumvent these innate defenses by using proteases that cleave MAVS to prevent its mitochondrial localization (5,6).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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