Phospho-EGF Receptor (Tyr1045) Antibody [F16D14]

Application: Reactivity: Human

Usage Information

Dilution
WB1:1000 IF1:100 FCM1:1000

Application
WB, IF, FCM

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
134 kDa

Positive Control	A431 cells (EGF, 100ng/mL, 30 min)
Negative Control	A431 cells

Datasheet & SDS

Biological Description

Specificity
Phospho-EGF Receptor (Tyr1045) Antibody [F16D14] detects endogenous levels of total EGF Receptor protein only when it is phosphorylated at Tyr1045.

Clone
F16D14

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

Background
Phospho-EGF Receptor (Tyr1045) designates EGFR specifically phosphorylated at tyrosine 1045 within its C-terminal tail, a modification triggered by ligand binding (EGF). EGFR, an ErbB/HER family receptor tyrosine kinase, consists of an extracellular ligand-binding domain, a single transmembrane helix, a cytoplasmic kinase domain, and a C-terminal tail rich in regulatory tyrosines. Tyr1045 lies within a key docking motif (amino acids 1042-1054) recognized by the TKB domain of the E3 ubiquitin ligase c-Cbl. Upon phosphorylation, Tyr1045 recruits c-Cbl, initiating mono- and poly-ubiquitination of EGFR, which targets the receptor for clathrin-mediated endocytosis, endosomal trafficking, lysosomal degradation, and thus, signal termination. This negative feedback loop prevents sustained RTK signaling that could otherwise chronically activate RAS-MAPK, PI3K/AKT, and PLCγ pathways involved in cell proliferation, survival, and motility. Mutations at Tyr1045 (such as Y1045F) disrupt c-Cbl binding, impair EGFR degradation, promote receptor recycling, and prolong oncogenic signaling in cancers with EGFR overexpression. This site also interfaces with broader regulatory circuits involving Grb2/SOS and Shc, as adjacent phosphotyrosines (Tyr1068, Tyr1148, Tyr1173) mediate MAPK pathway activation.

Background

Phospho-EGF Receptor (Tyr1045) designates EGFR specifically phosphorylated at tyrosine 1045 within its C-terminal tail, a modification triggered by ligand binding (EGF). EGFR, an ErbB/HER family receptor tyrosine kinase, consists of an extracellular ligand-binding domain, a single transmembrane helix, a cytoplasmic kinase domain, and a C-terminal tail rich in regulatory tyrosines. Tyr1045 lies within a key docking motif (amino acids 1042-1054) recognized by the TKB domain of the E3 ubiquitin ligase c-Cbl. Upon phosphorylation, Tyr1045 recruits c-Cbl, initiating mono- and poly-ubiquitination of EGFR, which targets the receptor for clathrin-mediated endocytosis, endosomal trafficking, lysosomal degradation, and thus, signal termination. This negative feedback loop prevents sustained RTK signaling that could otherwise chronically activate RAS-MAPK, PI3K/AKT, and PLCγ pathways involved in cell proliferation, survival, and motility. Mutations at Tyr1045 (such as Y1045F) disrupt c-Cbl binding, impair EGFR degradation, promote receptor recycling, and prolong oncogenic signaling in cancers with EGFR overexpression. This site also interfaces with broader regulatory circuits involving Grb2/SOS and Shc, as adjacent phosphotyrosines (Tyr1068, Tyr1148, Tyr1173) mediate MAPK pathway activation.

References
https://pubmed.ncbi.nlm.nih.gov/21617115/ https://pubmed.ncbi.nlm.nih.gov/15475003/

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%