Datasheet

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.
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.

Specificity

Phospho-HER2/ErbB2 (Tyr1139) Antibody [L15E14] detects endogenous levels of total HER2/ErbB2 protein only when it is phosphorylated at Tyr1139.

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.

使用情報

Application

WB, IP

Dilution

WB	IP
1:500 - 1:1000	1:30

Reactivity

Human

Source

Rabbit Monoclonal Antibody

MW

137 kDa

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

プロトコール

References

https://pubmed.ncbi.nlm.nih.gov/21966491/
https://pubmed.ncbi.nlm.nih.gov/17274834/

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

生物学的記述

使用情報

References

Application Data