Render Target: STATIC
Render Timestamp: 2024-11-04T09:47:44.208Z
Commit: 23cb9f61fe67e1e9093fd644a533c4ff516a6463
XML generation date: 2024-08-01 15:23:30.938
Product last modified at: 2024-08-20T12:15:09.870Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

Phospho-eNOS (Ser113) Antibody #9575

Filter:
  • WB

    Supporting Data

    REACTIVITY H B
    SENSITIVITY Endogenous
    MW (kDa) 140
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 
    • B-Bovine 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000

    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

    Phospho-eNOS (Ser113) Antibody detects endogenous levels of eNOS only when phosphorylated at serine 113.

    Species Reactivity:

    Human, Bovine

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser113 of human eNOS. Antibodies are purified by protein A and peptide affinity chromatography.

    Background

    Endothelial nitric-oxide synthase (eNOS) is an important enzyme in the cardiovascular system. It catalyzes the production of nitric oxide (NO), a key regulator of blood pressure, vascular remodeling, and angiogenesis (1,2). The activity of eNOS is regulated by phosphorylation at multiple sites. The two most thoroughly studied sites are the activation site Ser1177 and the inhibitory site Thr495 (3). Several protein kinases including Akt/PKB, PKA, and AMPK activate eNOS by phosphorylating Ser1177 in response to various stimuli (4,5). In contrast, bradykinin and H2O2 activate eNOS activity by promoting both Ser1177 phosphorylation and Thr495 dephosphorylation (6,7).
    eNOS is activated by VEGF, and this activation is associated with dephsophorylation of eNOS at serine 113. Cyclosporin A blocks this dephosphorylation of eNOS upon VEGF stimulation (8).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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