Render Target: STATIC
Render Timestamp: 2024-11-21T13:04:42.499Z
Commit: 5c4accf06eb7154018ba3f54329c7590f97f534a
XML generation date: 2024-09-30 01:54:39.577
Product last modified at: 2024-10-16T12:00:14.812Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77

Phospho-β-Arrestin 1 (Ser412) (6-24) Mouse mAb #2416

Filter:
  • WB
  • IP

    Supporting Data

    REACTIVITY H M R Mk
    SENSITIVITY Endogenous
    MW (kDa) 50
    Source/Isotype Mouse IgG1
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 
    • Mk-Monkey 

    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, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    Phospho-β-Arrestin 1 (Ser412) (6-24) Mouse mAb detects endogenous levels of β-arrestin 1 only when phosphorylated at serine 412. The antibody does not cross-react with beta-arrestin 2.

    Species Reactivity:

    Human, Mouse, Rat, Monkey

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser412 of human β-arrestin 1.

    Background

    Arrestin proteins function as negative regulators of G protein-coupled receptor (GPCR) signaling. Cognate ligand binding stimulates GPCR phosphorylation, which is followed by binding of arrestin to the phosphorylated GPCR and the eventual internalization of the receptor and desensitization of GPCR signaling (1). Four distinct mammalian arrestin proteins are known. Arrestin 1 (also known as S-arrestin) and arrestin 4 (X-arrestin) are localized to retinal rods and cones, respectively. Arrestin 2 (also known as β-arrestin 1) and arrestin 3 (β-arrestin 2) are ubiquitously expressed and bind to most GPCRs (2). β-arrestins function as adaptor and scaffold proteins and play important roles in other processes, such as recruiting c-Src family proteins to GPCRs in Erk activation pathways (3,4). β-arrestins are also involved in some receptor tyrosine kinase signaling pathways (5-8). Additional evidence suggests that β-arrestins translocate to the nucleus and help regulate transcription by binding transcriptional cofactors (9,10).
    Erk1/2 constitutively phosphorylates β-arrestin 1 at carboxy-terminal Ser412, which promotes cytosolic localization of the scaffold protein (11). Agonist stimulation of β2-adrenergic receptors results in recruitment of β-arrestin 1 to the plasma membrane and rapid dephosphorylation of arrestin. Dephosphorylation is an essential step of β-arrestin 1-mediated receptor endocytosis, but it is not required for receptor desensitization (12).
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