Render Target: STATIC
Render Timestamp: 2025-02-07T11:37:15.798Z
Commit: 1bba917eefc12d62e72a522121e2774ffbd0ee36
XML generation date: 2024-04-05 20:46:36.736
Product last modified at: 2025-01-01T09:04:19.854Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

OAS3 Antibody #41440

Filter:
  • WB
  • IP

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 120
    SOURCE Rabbit
    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 and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    OAS3 Antibody recognizes endogenous levels of total OAS3 protein. This antibody detects an 18 kDa band of unknown origin in some cell lines.

    Species Reactivity:

    Human

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human OAS3 protein. Antibodies are purified by peptide affinity chromatography.

    Background

    The 2'-5'-oligoadenylate synthetase (OAS) family of interferon-induced proteins play an important role in cellular innate immune response (1-4). When activated by double-stranded RNA, these proteins polymerize ATP into 2′-5′-linked oligomers (2,3,5). These 2’-5’-linked oligoadenylates bind to the ribonuclease RNase L, which then degrades viral and cellular RNA (2,3,5). In humans, the OAS family of proteins includes OAS1, OAS2, OAS3, and OASL (1-3). OAS3 is required to activate RNase L and to restrict the replication of four different human viruses (5). These findings suggest that OAS3 may provide a target for antiviral therapies (4,5).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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