Render Target: STATIC
Render Timestamp: 2024-12-13T12:20:45.055Z
Commit: 611277b6de3cd1bb065350b6ef8d63df412b7185
XML generation date: 2024-11-19 23:03:09.821
Product last modified at: 2024-11-20T08:00:57.031Z
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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-LAT (Tyr220) (E3S5L) Rabbit mAb #20172

Filter:
  • WB
  • IP

    Supporting Data

    REACTIVITY H M
    SENSITIVITY Endogenous
    MW (kDa) 40
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    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.

    For a carrier free (BSA and azide free) version of this product see product #84593.

    Protocol

    Specificity / Sensitivity

    Phospho-LAT (Tyr220) (E3S5L) Rabbit mAb recognizes endogenous levels of LAT protein when phosphorylated at Tyr220. This antibody shows cross-reactivity with phosphorylated EGFR, and detects a 70 kDa band of unknown origin in some treated cell lines. Tyr220 of LAT, long isoform corresponds to Tyr191 of LAT, short isoform. Weak cross-reactivity with phosphorylated tyrosines 171 and 255 of LAT has been observed.

    Species Reactivity:

    Human, Mouse

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Tyr220 of human LAT protein.

    Background

    LAT, a transmembrane adaptor protein expressed in T, NK, and mast cells, is an important mediator for T cell receptor (TCR) signaling (1). Upon TCR engagement, activated Zap-70 phosphorylates LAT at multiple conserved tyrosine residues within SH2 binding motifs, exposing these motifs as the docking sites for downstream signaling targets (2,3). The phosphorylation of LAT at Tyr171 and Tyr220 enables the binding of Grb2, Gads/SLP-76, PLCγ1, and PI3 kinase through their SH2 domain and translocates them to the membrane. This process eventually leads to activation of the corresponding signaling pathways (1-4).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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