Render Target: STATIC
Render Timestamp: 2024-11-21T12:44:14.265Z
Commit: 5c4accf06eb7154018ba3f54329c7590f97f534a
XML generation date: 2024-09-30 01:53:58.936
Product last modified at: 2024-11-13T13:30:10.803Z
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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.

Viperin (D5T2X) Rabbit mAb #13996

Filter:
  • WB
  • IP

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 42
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    Species Cross-Reactivity Key:
    • H-Human 

    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

    Viperin (D5T2X) Rabbit mAb recognizes endogenous levels of total viperin protein.

    Species Reactivity:

    Human

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Val270 of human viperin protein.

    Background

    The antiviral protein viperin (RSAD2) is induced by viral infection, lipopolysaccharides (LPS), polyriboinosinic polyribocytidylic acid [poly(I:C)], and interferons (1,2). Viperin protein localizes to the ER and redistributes to the Golgi and then to lipid droplets following viral infection (1,3). Viruses are known to use lipid droplets for replication, and the localization of the antiviral viperin protein to these lipid droplets is likely part of a cellular mechanism to inhibit these pathogens (4). Research studies indicate that induction of viperin by HIV in human macrophages inhibits virus production, and that siRNA targeting viperin reduced the inhibition of HIV replication observed in poly(I:C) treated astrocytes (5,6). Additional research suggests that human cytomegalovirus (HCMV) co-opts viperin protein function, resulting in an interaction between viperin and the viral protein vMIA. This association leads to relocalization of viperin to mitochondria, resulting in disruption of ATP generation and the actin cytoskeleton, and increased viral infection (7). The viperin protein also contributes to innate immune signaling by recruiting IRAK1 ant TRAF6 to lipid droplets, which results in activation of IRF7 and induction of type I interferon (8).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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