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Render Timestamp: 2024-07-26T09:59:21.143Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

IKKβ (L570) Antibody #2678

Filter:
  • WB
  • IP

    Supporting Data

    REACTIVITY H M R Hm Mk B GP
    SENSITIVITY Endogenous
    MW (kDa) 87
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 
    • Hm-Hamster 
    • Mk-Monkey 
    • B-Bovine 
    • GP-Guinea Pig 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:50

    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

    IKKβ (L570) Antibody detects endogenous levels of total IKKβ protein.


    Species Reactivity:

    Human, Mouse, Rat, Hamster, Monkey, Bovine, Guinea Pig

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Leu570 of IKKβ protein. Antibodies are purified by protein A and peptide affinity chromatography.

    Background

    The NF-κB/Rel transcription factors are present in the cytosol in an inactive state, complexed with the inhibitory IκB proteins (1-3). Most agents that activate NF-κB do so through a common pathway based on phosphorylation-induced, proteasome-mediated degradation of IκB (3-7). The key regulatory step in this pathway involves activation of a high molecular weight IκB kinase (IKK) complex whose catalysis is generally carried out by three tightly associated IKK subunits. IKKα and IKKβ serve as the catalytic subunits of the kinase and IKKγ serves as the regulatory subunit (8,9). Activation of IKK depends upon phosphorylation at Ser177 and Ser181 in the activation loop of IKKβ (Ser176 and Ser180 in IKKα), which causes conformational changes, resulting in kinase activation (10-13).

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