Phospho-EGFR (Tyr1101) Antibody [A24A1]

Application: Reactivity: Human

Usage Information

Dilution
WB1:1000 IF1:200

Application
WB, IF

Reactivity
Human

Source
Mouse 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
134 kDa 180 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight.

Positive Control	A431 cells (EGF, 100 ng/ml, 5 min)
Negative Control	A431 cells

Datasheet & SDS

Biological Description

Specificity
Phospho-EGFR (Tyr1101) Antibody [A24A1] detects endogenous levels of total EGFR protein only when it is phosphorylated at Tyr1101.

Clone
A24A1

Synonym(s)
ERBB; ERBB1; HER1; EGFR; Epidermal growth factor receptor; Proto-oncogene c-ErbB-1; Receptor tyrosine-protein kinase erbB-1

Background
Phospho-EGFR (Tyr1101) refers to phosphorylation at tyrosine residue 1101 within the C-terminal tail of the Epidermal Growth Factor Receptor (EGFR), a receptor tyrosine kinase belonging to the ErbB family that orchestrates cell proliferation, survival, and migration upon ligand binding such as EGF. Unlike classical EGFR autophosphorylation sites like Tyr1068 and Tyr1173, Tyr1101 is predominantly phosphorylated by the non-receptor tyrosine kinase c-Src, often in conjunction with Tyr845 in the activation loop, enabling Src-mediated hyperactivation of EGFR kinase activity in cancer cells such as MDA-MB-468 breast carcinoma where Src is overexpressed. Tyr1101 is located in the unstructured C-terminal regulatory domain, downstream of the kinase domain (which spans approximately residues 712-979). This site serves as a docking motif (pYXXφ consensus) for SH2 domains, recruiting not only Src itself but also other SH2-containing adaptors like Grb2 and Shc, thus amplifying signaling without requiring direct EGFR autophosphorylation at this residue. Tyr1101 phosphorylation is the enhancement of EGFR kinase potency for substrate phosphorylation, including downstream targets like PLCγ and STAT5, thereby promoting mitogenic DNA synthesis, tumor progression, and invasion through pathways such as MAPK/ERK and PI3K/AKT. Phosphorylation at Tyr1101 also sustains prolonged signaling by stabilizing Src-EGFR complexes, integrating EGFR with Src-family kinase crosstalk in response to growth factors or cellular stress. This modification contributes to processes like epithelial-mesenchymal transition and angiogenesis, and is associated with aggressive cancers, particularly breast and lung, characterized by Src overexpression, resistance to EGFR tyrosine kinase inhibitors, and poor prognosis.

Background

Phospho-EGFR (Tyr1101) refers to phosphorylation at tyrosine residue 1101 within the C-terminal tail of the Epidermal Growth Factor Receptor (EGFR), a receptor tyrosine kinase belonging to the ErbB family that orchestrates cell proliferation, survival, and migration upon ligand binding such as EGF. Unlike classical EGFR autophosphorylation sites like Tyr1068 and Tyr1173, Tyr1101 is predominantly phosphorylated by the non-receptor tyrosine kinase c-Src, often in conjunction with Tyr845 in the activation loop, enabling Src-mediated hyperactivation of EGFR kinase activity in cancer cells such as MDA-MB-468 breast carcinoma where Src is overexpressed. Tyr1101 is located in the unstructured C-terminal regulatory domain, downstream of the kinase domain (which spans approximately residues 712-979). This site serves as a docking motif (pYXXφ consensus) for SH2 domains, recruiting not only Src itself but also other SH2-containing adaptors like Grb2 and Shc, thus amplifying signaling without requiring direct EGFR autophosphorylation at this residue. Tyr1101 phosphorylation is the enhancement of EGFR kinase potency for substrate phosphorylation, including downstream targets like PLCγ and STAT5, thereby promoting mitogenic DNA synthesis, tumor progression, and invasion through pathways such as MAPK/ERK and PI3K/AKT. Phosphorylation at Tyr1101 also sustains prolonged signaling by stabilizing Src-EGFR complexes, integrating EGFR with Src-family kinase crosstalk in response to growth factors or cellular stress. This modification contributes to processes like epithelial-mesenchymal transition and angiogenesis, and is associated with aggressive cancers, particularly breast and lung, characterized by Src overexpression, resistance to EGFR tyrosine kinase inhibitors, and poor prognosis.

References
https://pubmed.ncbi.nlm.nih.gov/17671194/ https://pubmed.ncbi.nlm.nih.gov/25573954/

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%