Phospho-HER3/ErbB3 (Tyr1197) Antibody [F15P3]

Application: Reactivity: Human, Mouse

Lane 1: T47D, Lane 2: T47D (NRG treated)

Usage Information

Dilution
WB1:1000

Application
WB

Reactivity
Human, Mouse

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
185 kDa

Datasheet & SDS

Biological Description

Specificity
Phospho-HER3/ErbB3 (Tyr1197) Antibody [F15P3] detects endogenous levels of total HER3/ErbB3 protein only when it is phosphorylated at Tyr1197.

Clone
F15P3

Synonym(s)
Receptor tyrosine-protein kinase erbB-3; Proto-oncogene-like protein c-ErbB-3; Tyrosine kinase-type cell surface receptor HER3; ERBB3; HER3

Background
Phospho-HER3/ErbB3 (Tyr1197) signifies the activated state of HER3, a member of the ErbB receptor tyrosine kinase family notable for its catalytically impaired kinase domain. Unlike its relatives, HER3 cannot autophosphorylate and instead depends on heterodimerization with active ErbB partners such as EGFR or HER2, which phosphorylate key tyrosine residues in its C-terminal tail, including Tyr1197. Following ligand engagement, such as by neuregulin-1, HER3 dimerizes, and its tail tyrosines (Tyr1197, Tyr1222, Tyr1289) are transphosphorylated, establishing high-affinity binding sites for SH2 domain-containing effectors, especially the p85 subunit of PI3K via YXXM motifs. This triggers robust activation of the PI3K/AKT/mTOR pathway, driving cellular survival, proliferation, migration, and metabolic adaptation, functions that are critical in both normal development and tumorigenesis. In HER2-amplified breast cancers and various adenocarcinomas, phospho-Tyr1197 HER3 is a major signaling hub, enabling sustained oncogenic signaling, resistance to EGFR/HER2-targeted therapies, and tumor progression.

Background

Phospho-HER3/ErbB3 (Tyr1197) signifies the activated state of HER3, a member of the ErbB receptor tyrosine kinase family notable for its catalytically impaired kinase domain. Unlike its relatives, HER3 cannot autophosphorylate and instead depends on heterodimerization with active ErbB partners such as EGFR or HER2, which phosphorylate key tyrosine residues in its C-terminal tail, including Tyr1197. Following ligand engagement, such as by neuregulin-1, HER3 dimerizes, and its tail tyrosines (Tyr1197, Tyr1222, Tyr1289) are transphosphorylated, establishing high-affinity binding sites for SH2 domain-containing effectors, especially the p85 subunit of PI3K via YXXM motifs. This triggers robust activation of the PI3K/AKT/mTOR pathway, driving cellular survival, proliferation, migration, and metabolic adaptation, functions that are critical in both normal development and tumorigenesis. In HER2-amplified breast cancers and various adenocarcinomas, phospho-Tyr1197 HER3 is a major signaling hub, enabling sustained oncogenic signaling, resistance to EGFR/HER2-targeted therapies, and tumor progression.

References
https://pubmed.ncbi.nlm.nih.gov/38835349/ https://pubmed.ncbi.nlm.nih.gov/28114269/

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

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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%