Phospho-ALK (Tyr1507) Antibody [P14J22]

Catalog No.: F9572

    Application: Reactivity:
    • Lane 1: KARPAS-299, Lane 2: KARPAS-299 (Crizotinib, 1 μM, 1 h)
    1/

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    代表番号: 045-509-1970|電子メール:sales@selleck.co.jp

    使用情報

    Dilution
    1:1000
    1:100
    1:400
    1:200
    Application
    WB, IP, IF, FCM
    Source
    Rabbit Monoclonal Antibody
    Reactivity
    Human
    Storage Buffer
    PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3
    Storage (from the date of receipt)
    -20°C (avoid freeze-thaw cycles), 2 years
    Predicted MW
    80 kDa

    Datasheet & SDS

    生物学的記述

    Specificity
    Phospho-ALK (Tyr1507) Antibody [P14J22] detects endogenous levels of total ALK protein only when it is phosphorylated at Tyr1507.
    Clone
    P14J22
    Synonym(s)
    ALK tyrosine kinase receptor; Anaplastic lymphoma kinase; CD246; ALK
    Background
    Phospho‑ALK (Tyr1507) marks a functionally critical autophosphorylation site on the intracellular tyrosine kinase domain of anaplastic lymphoma kinase (ALK), a neuronal‑type receptor tyrosine kinase activated by ligands such as pleiotrophin and ALKAL family proteins in the nervous system and by oncogenic ALK‑fusion proteins in cancer. In the full‑length receptor, tyrosine‑1507 lies within a canonical NPXpY motif that, when phosphorylated, recruits SH2‑domain‑ and PTB‑domain‑containing adaptor proteins, most notably the docking proteins Shc, FRS2‑α, and FRS2‑β, which in turn bridge activated ALK to the Ras‑ERK (MAPK) and PI3K‑Akt signaling axes. Antibody‑mediated or ligand‑dependent activation of ALK drives phosphorylation at Tyr1507, promotes Shc and FRS2 recruitment and phosphorylation, and supports sustained ERK activation that underlies neuronal‑like differentiation and mitogenic responses. The equivalent phospho‑site (Tyr567) in the NPM‑ALK fusion is constitutively phosphorylated and required for efficient engagement of Shc and FRS2, thereby sustaining downstream proliferative and survival‑signaling pathways that contribute to lymphoma pathogenesis.
    References

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