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

Application: Reactivity: Human

Usage Information

Dilution
WB1:500 - 1:1000 IP1:30

Application
WB, IP

Reactivity
Human

Source
Rabbit Monoclonal Antibody

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
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

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.

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

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

Tech Support

Handling Instructions

Tel: +1-832-582-8158 Ext:3

If you have any other enquiries, please leave a message.

Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%