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Phospho-FGF Receptor (Tyr653/654) Antibody [F13P7]

Cat.No.: F0647

Application: Reactivity: Human, Monkey

Usage Information

Dilution
WB1:1000

Application
WB

Reactivity
Human, Monkey

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
120 kDa, 145 kDa

Datasheet & SDS

Biological Description

Specificity
Phospho-FGF Receptor (Tyr653/654) Antibody [F13P7] detects endogenous levels of total FGF Receptor protein only when it is phosphorylated at Tyr653/654.

Clone
F13P7

Synonym(s)
FGFR1; Fibroblast growth factor receptor 1; EC:2.7.10.1; FGFR-1; Basic fibroblast growth factor receptor 1 (BFGFR; bFGF-R-1); Fms-like tyrosine kinase 2 (FLT-2); N-sam; Proto-oncogene c-Fgr; CD331; BFGFR; CEK; FGFBR; FLG; FLT2; HBGFR

Background
Phospho-FGF Receptor (Tyr653/654) is the principal activation mark of FGFR1-4, driving the transition of these receptors from a low- to high-activity state upon ligand-induced dimerization, a process that underpins FGF-dependent control of cell proliferation, differentiation, migration, and survival. This phosphorylation occurs in the kinase activation loop, precisely between the DFG and APE motifs, and is absolutely required for full catalytic activity and efficient signal propagation. Tyr653 phosphorylation primes the kinase for activity, while subsequent Tyr654 phosphorylation fully stabilizes the active conformation, enabling broad substrate access and robust engagement of downstream signaling partners such as PLCγ, FRS2α, and Crk. These interactions relay signals to key pathways, including MAPK/ERK and PI3K/AKT, regulate gene expression, cytoskeletal dynamics, and cellular metabolism, and determine cell fate decisions during embryogenesis and tissue repair. Phospho-Tyr653/654 also integrates extracellular matrix cues and can be induced in a ligand-independent manner through receptor clustering or oncogenic mutations, contributing to aberrant FGFR signaling. Dephosphorylation by protein tyrosine phosphatases tightly regulates signal duration and amplitude. Mutations affecting Tyr653/654 or the activation loop are causative for skeletal dysplasias such as thanatophoric dysplasia, craniosynostosis syndromes, and dwarfism, by either constitutively activating or inactivating FGFR function. In cancer, persistent phosphorylation at these sites, often due to activating FGFR3 mutations or gene amplifications, drives uncontrolled proliferation, angiogenesis, and therapy resistance.

Background

Phospho-FGF Receptor (Tyr653/654) is the principal activation mark of FGFR1-4, driving the transition of these receptors from a low- to high-activity state upon ligand-induced dimerization, a process that underpins FGF-dependent control of cell proliferation, differentiation, migration, and survival. This phosphorylation occurs in the kinase activation loop, precisely between the DFG and APE motifs, and is absolutely required for full catalytic activity and efficient signal propagation. Tyr653 phosphorylation primes the kinase for activity, while subsequent Tyr654 phosphorylation fully stabilizes the active conformation, enabling broad substrate access and robust engagement of downstream signaling partners such as PLCγ, FRS2α, and Crk. These interactions relay signals to key pathways, including MAPK/ERK and PI3K/AKT, regulate gene expression, cytoskeletal dynamics, and cellular metabolism, and determine cell fate decisions during embryogenesis and tissue repair. Phospho-Tyr653/654 also integrates extracellular matrix cues and can be induced in a ligand-independent manner through receptor clustering or oncogenic mutations, contributing to aberrant FGFR signaling. Dephosphorylation by protein tyrosine phosphatases tightly regulates signal duration and amplitude. Mutations affecting Tyr653/654 or the activation loop are causative for skeletal dysplasias such as thanatophoric dysplasia, craniosynostosis syndromes, and dwarfism, by either constitutively activating or inactivating FGFR function. In cancer, persistent phosphorylation at these sites, often due to activating FGFR3 mutations or gene amplifications, drives uncontrolled proliferation, angiogenesis, and therapy resistance.

References
https://pubmed.ncbi.nlm.nih.gov/17901128/ https://pubmed.ncbi.nlm.nih.gov/25679016/

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%