Render Target: STATIC
Render Timestamp: 2024-10-14T09:43:23.270Z
Commit: 56767fe525c928647c8401233a175d0d607d385d
XML generation date: 2024-09-30 01:53:54.540
Product last modified at: 2024-09-30T08:02:16.143Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

Phospho-DAPP1/BAM32 (Tyr139) (D7G4G) Rabbit mAb #13703

Filter:
  • WB
  • IP

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 29
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Simple Western™ 1:50 - 1:250
    Immunoprecipitation 1:200

    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-DAPP1/BAM32 (Tyr139) (D7G4G) Rabbit mAb recognizes endogenous levels of DAPP1/BAM32 protein only when phosphorylated at Tyr139.

    Species Reactivity:

    Human

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr139 of human DAPP1/BAM32 protein.

    Background

    The dual adaptor of phosphotyrosine and 3-phosphoinositides (DAPP1/BAM32) is a cytoplasmic adaptor protein that mediates the recruitment and interaction of molecules required for signal transduction downstream of the B cell receptor (BCR) (1). The DAPP1/BAM32 protein contains an amino-terminal SH2 domain and a carboxy-terminal pleckstrin homology (PH) domain that binds to PI3K-derived phosphoinositides (i.e., PIP3). Upon BCR activation, DAPP1/BAM32 is phosphorylated at specific tyrosine residues and translocated from the cytoplasm to the membrane. Research studies indicate that phosphorylation and translocation of DAPP1/BAM32 is strongly dependent upon PI3K signaling (2,3). The amino-terminal SH2 domain binds to PLCγ2 and other tyrosine-phosphorylated targets. As a result of these interactions, DAPP1/BAM32 can adjust the response to receptor activation by coordinating membrane-localized interactions among proteins of distinct signal transduction pathways (1,4). DAPP1/BAM32 is expressed most abundantly in B lymphocytes; high expression during dendritic cell (DC) maturation and localization to contact sites between DC and allogenic T cells suggest that the DAPP1/BAM32 adaptor may play a role in the activation of T cells through MHC class I-mediated signaling pathways (5).
    Research studies show that phosphorylation of DAPP1/BAM32 at Tyr139 is PI3K-dependent, requires an intact PH domain in DAPP1/BAM32, and is likely performed by Src-family kinases following membrane recruitment of DAPP1/BAM32 by phosphoinositides (6). Blocking phosphorylation of DAPP1/BAM32 at Tyr139 inhibits BCR internalization and reduces cellular F-actin levels, suggesting that phosphorylation of DAPP1/BAM32 may play a role in regulating actin-dependent internalization of the activated BCR (7,8).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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