Render Target: STATIC
Render Timestamp: 2024-11-21T13:20:49.919Z
Commit: 5c4accf06eb7154018ba3f54329c7590f97f534a
XML generation date: 2024-09-20 06:15:05.632
Product last modified at: 2024-09-20T07:04:01.719Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

Phospho-GKAP (Ser346) Antibody #13638

Filter:
  • WB

    Supporting Data

    REACTIVITY M R
    SENSITIVITY Endogenous
    MW (kDa) 90-150
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • M-Mouse 
    • R-Rat 

    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-GKAP (Ser346) Antibody recognizes endogenous levels of GKAP protein only when phosphorylated at Ser346.

    Species Reactivity:

    Mouse, Rat

    The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.

    Species predicted to react based on 100% sequence homology:

    Human

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser346 of human GKAP protein. Antibodies are purified by protein A and peptide affinity chromatography.

    Background

    Guanylate kinase-associated protein (GKAP, DLGAP1 or SAPAP1) is part of the postsynaptic scaffolding complex that includes the PSD-95, SAP90, and SHANK proteins (1-3). GKAP links the synaptic protein SHANK to a PSD-95 complex that includes NMDA glutamate receptors (3,4). Synaptic activity induces ubiquitination of GKAP protein by the E3 ubiquitin ligase TRIM3, which results in decreased GKAP protein levels through degradation (5,6). GKAP protein turnover is regulated by a CaMKII-dependent, bidirectional mechanism. Synaptic over-excitation leads to CaMKIIα-mediated GKAP phosphorylation at Ser346, which induces polyubiquitination of GKAP and removal of the scaffold protein from synapses. In contrast, during low-level synaptic activity CaMKIIβ phosphorylates GKAP, which triggers dissociation of GKAP from the motor protein complex responsible for GKAP transport to the base of the synapse and its subsequent incorporation into the postsynaptic density (7).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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