Render Target: STATIC
Render Timestamp: 2024-12-26T10:41:42.836Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-09-30 01:58:52.933
Product last modified at: 2024-12-17T19:03:21.073Z
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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 (Tyr161) (E9Q2R) Rabbit mAb #88077

Filter:
  • WB
  • IP

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 40
    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
    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-LAT (Tyr161) (E9Q2R) Rabbit mAb recognizes endogenous levels of LAT protein only when phosphorylated at Tyr161. Tyr161 of LAT, long isoform corresponds to Tyr132 of LAT, short isoform. This antibody cross-reacts with phosphorylated EGFR.

    Species Reactivity:

    Human

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr161 of human LAT protein, long isoform.

    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).

    Research studies have shown that Zap-70 phosphorylates LAT at Tyr161, which creates an additional docking site to facilitate PLCγ1 recruitment, phosphorylation, and activation (3-5). Tyr161 is a relatively poor substrate for Zap-70 and following TCR engagement, phosphorylation of LAT at Tyr161 is delayed relative to the other distal tyrosine residues. Given the importance of PLCγ1 in regulating multiple T cell effector functions, it is posited that the delayed kinetics of Tyr161 phosphorylation serves as molecular rheostat in order to allow the TCR to effectively discriminate between autoantigens and foreign antigens (6,7).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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