Phospho-HER2/ErbB2 (Tyr1139) Antibody [L15E14]

Catalog No.: F2902

    Application: Reactivity:

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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
    1:500 - 1:1000
    1:30
    Application
    WB, IP
    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 Observed MW
    137 kDa 185 kDa
    *なぜ予測分子量と実際の分子量が異なるのか?
    下記の原因により、実際の分子量が予測と異なる:タンパク質の翻訳後修飾(リン酸化/糖鎖付加),スプライシングバリアント,イソフォーム,相対的な電荷,ポリマー。

    Datasheet & SDS

    生物学的記述

    Specificity
    Phospho-HER2/ErbB2 (Tyr1139) Antibody [L15E14] detects endogenous levels of total HER2/ErbB2 protein only when it is phosphorylated at Tyr1139.
    Clone
    L15E14
    Synonym(s)
    CD340, HER2, MLN19, NEU, NGL, ERBB2, Receptor tyrosine-protein kinase erbB-2, Metastatic lymph node gene 19 protein, Proto-oncogene Neu, Proto-oncogene c-ErbB-2, Tyrosine kinase-type cell surface receptor HER2, p185erbB2, MLN 19
    Background
    Phospho‑HER2/ErbB2 (Tyr1139) denotes the activated receptor tyrosine kinase ERBB2 phosphorylated at a specific C‑terminal tyrosine that serves as a docking site for SH2‑domain adaptors and shapes downstream signaling output. HER2 is a member of the EGFR/ErbB family that forms ligand‑independent homodimers when overexpressed or heterodimers with ligand‑bound partners such as EGFR and HER3, and autophosphorylation across multiple cytoplasmic tyrosines follows trans‑activation of its intracellular kinase domain. Tyr1139 lies within the intracellular tail among a cluster of autophosphorylation sites and, when phosphorylated, directly binds the SH2‑domain adaptor GRB7, creating a specific recruitment platform distinct from the ERBIN‑binding Tyr1248 or CBL‑binding Tyr1112 sites. GRB7 association with phospho‑Tyr1139 links activated HER2 to focal adhesion components and small GTPase signaling, and has been connected to cell migration, adhesion remodeling, and polarity disruption in HER2‑overexpressing models where Tyr1139 and Tyr1196 are robustly phosphorylated. HER2 overexpression in breast and other carcinomas results in constitutive phosphorylation of multiple tail tyrosines, including Tyr1139, and high levels of phosphorylated HER2 correlate with increased lymph node involvement, higher proliferation indices, and shorter disease‑free and disease‑specific survival compared with HER2 expression alone.
    References

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