Product: Phospho-FGFR1/2/3/4 (Tyr653+Tyr654) Antibody
Catalog: AF8210
Description: Rabbit polyclonal antibody to Phospho-FGFR1/2/3/4 (Tyr653+Tyr654)
Application: WB IHC
Reactivity: Human, Mouse, Rat, Monkey
Prediction: Bovine, Horse, Sheep, Rabbit, Dog, Chicken, Xenopus
Mol.Wt.: 92KD; 92kD,88kD(Calculated).
Uniprot: P11362 | P21802 | P22607 | P22455
RRID: AB_2840272

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 100ul $350 In stock
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Product Info

Source:
Rabbit
Application:
WB 1:1000-3000, IHC 1:50-1:200
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human,Mouse,Rat,Monkey
Prediction:
Bovine(100%), Horse(100%), Sheep(100%), Rabbit(100%), Dog(100%), Chicken(100%), Xenopus(100%)
Clonality:
Polyclonal
Specificity:
Phospho-FGFR1/2/3/4 (Tyr653+Tyr654) Antibody detects endogenous levels of FGFR1/2/3/4 only when phosphorylated at Tyr653+Tyr654.
RRID:
AB_2840272
Cite Format: Affinity Biosciences Cat# AF8210, RRID:AB_2840272.
Conjugate:
Unconjugated.
Purification:
The antibody is from purified rabbit serum by affinity purification via sequential chromatography on phospho-peptide and non-phospho-peptide affinity columns.
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

Basic fibroblast growth factor receptor 1; bFGF-R-1; BFGFR; CD331; CEK; FGFBR; FGFR 1; FGFR-1; FGFR1; FGFR1/PLAG1 fusion; FGFR1_HUMAN; fibroblast growth factor receptor 1; FLG; FLT-2; FLT2; Fms-like gene; Fms-like tyrosine kinase 2; fms-related tyrosine kinase 2; HBGFR; heparin-binding growth factor receptor; HH2; HRTFDS; hydroxyaryl-protein kinase; KAL2; N-SAM; OGD; Proto-oncogene c-Fgr; bacteria-expressed kinase; BBDS; BEK; BEK fibroblast growth factor receptor; BFR1; CD332; CD332 antigen; CEK3; CFD1; Craniofacial dysostosis 1; ECT1; FGF receptor; FGFR 2; FGFR-2; Fgfr2; FGFR2_HUMAN; Fibroblast growth factor receptor 2; Hydroxyaryl protein kinase; Jackson Weiss syndrome; JWS; K SAM; K-sam; Keratinocyte growth factor receptor 2; Keratinocyte growth factor receptor; KGFR; KSAM; protein tyrosine kinase, receptor like 14; soluble FGFR4 variant 4; TK14; TK25; ACH; CD 333; CD333; CD333 antigen; CEK 2; CEK2; FGFR 3; FGFR-3; FGFR3; FGFR3_HUMAN; Fibroblast growth factor receptor 3 (achondroplasia thanatophoric dwarfism); Fibroblast growth factor receptor 3; Heparin binding growth factor receptor; HSFGFR3EX; Hydroxyaryl protein kinase; JTK 4; JTK4; MFR 3; SAM 3; Tyrosine kinase JTK 4; Tyrosine kinase JTK4; Z FGFR 3; CD 334; CD334; CD334 antigen; fc13h 10; fc13h10; Fgfr 4; FGFR-4; Fgfr4; FGFR4_HUMAN; Fibroblast growth factor receptor 4; Hydroxyaryl protein kinase; JTK 2; JTK2; MGC20292; Protein tyrosine kinase; TKF; Tyrosine kinase related to fibroblast growth factor receptor; Tyrosylprotein kinase;

Immunogens

Immunogen:
Uniprot:
Gene(ID):
Expression:
P11362 FGFR1_HUMAN:

Detected in astrocytoma, neuroblastoma and adrenal cortex cell lines. Some isoforms are detected in foreskin fibroblast cell lines, however isoform 17, isoform 18 and isoform 19 are not detected in these cells.

P22607 FGFR3_HUMAN:

Expressed in brain, kidney and testis. Very low or no expression in spleen, heart, and muscle. In 20- to 22-week old fetuses it is expressed at high level in kidney, lung, small intestine and brain, and to a lower degree in spleen, liver, and muscle. Isoform 2 is detected in epithelial cells. Isoform 1 is not detected in epithelial cells. Isoform 1 and isoform 2 are detected in fibroblastic cells.

P22455 FGFR4_HUMAN:

Expressed in gastrointestinal epithelial cells, pancreas, and gastric and pancreatic cancer cell lines.

Sequence:
MWSWKCLLFWAVLVTATLCTARPSPTLPEQAQPWGAPVEVESFLVHPGDLLQLRCRLRDDVQSINWLRDGVQLAESNRTRITGEEVEVQDSVPADSGLYACVTSSPSGSDTTYFSVNVSDALPSSEDDDDDDDSSSEEKETDNTKPNRMPVAPYWTSPEKMEKKLHAVPAAKTVKFKCPSSGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVALGSNVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHSAWLTVLEALEERPAVMTSPLYLEIIIYCTGAFLISCMVGSVIVYKMKSGTKKSDFHSQMAVHKLAKSIPLRRQVTVSADSSASMNSGVLLVRPSRLSSSGTPMLAGVSEYELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGLEYCYNPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPGVPVEELFKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIVALTSNQEYLDLSMPLDQYSPSFPDTRSSTCSSGEDSVFSHEPLPEEPCLPRHPAQLANGGLKRR

MVSWGRFICLVVVTMATLSLARPSFSLVEDTTLEPEEPPTKYQISQPEVYVAAPGESLEVRCLLKDAAVISWTKDGVHLGPNNRTVLIGEYLQIKGATPRDSGLYACTASRTVDSETWYFMVNVTDAISSGDDEDDTDGAEDFVSENSNNKRAPYWTNTEKMEKRLHAVPAANTVKFRCPAGGNPMPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDVVERSPHRPILQAGLPANASTVVGGDVEFVCKVYSDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKAAGVNTTDKEIEVLYIRNVTFEDAGEYTCLAGNSIGISFHSAWLTVLPAPGREKEITASPDYLEIAIYCIGVFLIACMVVTVILCRMKNTTKKPDFSSQPAVHKLTKRIPLRRQVTVSAESSSSMNSNTPLVRITTRLSSTADTPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILTLTTNEEYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQYPHINGSVKT

MGAPACALALCVAVAIVAGASSESLGTEQRVVGRAAEVPGPEPGQQEQLVFGSGDAVELSCPPPGGGPMGPTVWVKDGTGLVPSERVLVGPQRLQVLNASHEDSGAYSCRQRLTQRVLCHFSVRVTDAPSSGDDEDGEDEAEDTGVDTGAPYWTRPERMDKKLLAVPAANTVRFRCPAAGNPTPSISWLKNGREFRGEHRIGGIKLRHQQWSLVMESVVPSDRGNYTCVVENKFGSIRQTYTLDVLERSPHRPILQAGLPANQTAVLGSDVEFHCKVYSDAQPHIQWLKHVEVNGSKVGPDGTPYVTVLKTAGANTTDKELEVLSLHNVTFEDAGEYTCLAGNSIGFSHHSAWLVVLPAEEELVEADEAGSVYAGILSYGVGFFLFILVVAAVTLCRLRSPPKKGLGSPTVHKISRFPLKRQVSLESNASMSSNTPLVRIARLSSGEGPTLANVSELELPADPKWELSRARLTLGKPLGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLVEYAAKGNLREFLRARRPPGLDYSFDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVLTVTSTDEYLDLSAPFEQYSPGGQDTPSSSSSGDDSVFAHDLLPPAPPSSGGSRT

MRLLLALLGVLLSVPGPPVLSLEASEEVELEPCLAPSLEQQEQELTVALGQPVRLCCGRAERGGHWYKEGSRLAPAGRVRGWRGRLEIASFLPEDAGRYLCLARGSMIVLQNLTLITGDSLTSSNDDEDPKSHRDPSNRHSYPQQAPYWTHPQRMEKKLHAVPAGNTVKFRCPAAGNPTPTIRWLKDGQAFHGENRIGGIRLRHQHWSLVMESVVPSDRGTYTCLVENAVGSIRYNYLLDVLERSPHRPILQAGLPANTTAVVGSDVELLCKVYSDAQPHIQWLKHIVINGSSFGADGFPYVQVLKTADINSSEVEVLYLRNVSAEDAGEYTCLAGNSIGLSYQSAWLTVLPEEDPTWTAAAPEARYTDIILYASGSLALAVLLLLAGLYRGQALHGRHPRPPATVQKLSRFPLARQFSLESGSSGKSSSSLVRGVRLSSSGPALLAGLVSLDLPLDPLWEFPRDRLVLGKPLGEGCFGQVVRAEAFGMDPARPDQASTVAVKMLKDNASDKDLADLVSEMEVMKLIGRHKNIINLLGVCTQEGPLYVIVECAAKGNLREFLRARRPPGPDLSPDGPRSSEGPLSFPVLVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDNVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGHRMDRPPHCPPELYGLMRECWHAAPSQRPTFKQLVEALDKVLLAVSEEYLDLRLTFGPYSPSGGDASSTCSSSDSVFSHDPLPLGSSSFPFGSGVQT

Predictions

Predictions:

Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Species
Results
Score
Horse
100
Bovine
100
Sheep
100
Dog
100
Xenopus
100
Chicken
100
Rabbit
100
Pig
0
Zebrafish
0
Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - P11362/P21802/P22607/P22455 As Substrate

Site PTM Type Enzyme
Phosphorylation
S347 Phosphorylation
S437 Phosphorylation
S440 Phosphorylation
T442 Phosphorylation
T448 Phosphorylation
T449 Phosphorylation
S452 Phosphorylation
S453 Phosphorylation
T454 Phosphorylation
T457 Phosphorylation
Y466 Phosphorylation P21802 (FGFR2)
S533 Phosphorylation
K539 Acetylation
Y586 Phosphorylation P21802 (FGFR2)
S587 Phosphorylation
Y588 Phosphorylation P21802 (FGFR2)
Y608 Phosphorylation
Y616 Phosphorylation
Y656 Phosphorylation P21802 (FGFR2)
Y657 Phosphorylation P21802 (FGFR2)
Y733 Phosphorylation
K751 Ubiquitination
Y769 Phosphorylation P21802 (FGFR2)
S780 Phosphorylation
S782 Phosphorylation Q02156 (PRKCE)
S788 Phosphorylation
S789 Phosphorylation
S791 Phosphorylation
S792 Phosphorylation
Y805 Phosphorylation
Y812 Phosphorylation
Site PTM Type Enzyme
S408 Phosphorylation
T410 Phosphorylation
K413 Ubiquitination
S424 Phosphorylation
S444 Phosphorylation
S445 Phosphorylation
T450 Phosphorylation
S524 Phosphorylation
K530 Acetylation
Y577 Phosphorylation P22607 (FGFR3)
S578 Phosphorylation
S596 Phosphorylation
Y599 Phosphorylation
Y607 Phosphorylation
K632 Ubiquitination
Y647 Phosphorylation P22607 (FGFR3)
Y648 Phosphorylation P22607 (FGFR3)
Y724 Phosphorylation P22607 (FGFR3)
Y760 Phosphorylation P22607 (FGFR3)
Y770 Phosphorylation P22607 (FGFR3)
S771 Phosphorylation
T777 Phosphorylation
S787 Phosphorylation
Site PTM Type Enzyme
S91 Phosphorylation
Y154 Phosphorylation P11362 (FGFR1)
K164 Acetylation
K172 Acetylation
Y210 Phosphorylation
Y280 Phosphorylation P11362 (FGFR1)
N296 N-Glycosylation
Y307 Phosphorylation P11362 (FGFR1)
T403 Phosphorylation
S410 Phosphorylation
K416 Ubiquitination
T428 Phosphorylation
S439 Phosphorylation
S447 Phosphorylation
S450 Phosphorylation
S451 Phosphorylation
S452 Phosphorylation
T454 Phosphorylation
Y463 Phosphorylation P11362 (FGFR1)
K482 Ubiquitination
K510 Ubiquitination
Y572 Phosphorylation
Y583 Phosphorylation P11362 (FGFR1)
Y585 Phosphorylation P11362 (FGFR1)
S588 Phosphorylation
S602 Phosphorylation
Y605 Phosphorylation P11362 (FGFR1)
Y613 Phosphorylation
K638 Ubiquitination
Y653 Phosphorylation P51813 (BMX) , P11362 (FGFR1)
Y654 Phosphorylation P51813 (BMX) , P11362 (FGFR1)
K655 Ubiquitination
Y677 Phosphorylation
Y730 Phosphorylation P11362 (FGFR1)
K748 Ubiquitination
Y766 Phosphorylation P11362 (FGFR1)
Y776 Phosphorylation
S777 Phosphorylation P28482 (MAPK1) , Q16539 (MAPK14) , P27361 (MAPK3)
S779 Phosphorylation Q02156 (PRKCE)
S789 Phosphorylation P51812 (RPS6KA3)
Site PTM Type Enzyme
T167 Phosphorylation
S232 Phosphorylation
T368 Phosphorylation
Y390 Phosphorylation
K408 Ubiquitination
S410 Phosphorylation
S419 Phosphorylation
S422 Phosphorylation
S439 Phosphorylation
S440 Phosphorylation
S441 Phosphorylation
K471 Ubiquitination
S519 Phosphorylation
S573 Phosphorylation
K627 Ubiquitination
Y642 Phosphorylation P22455 (FGFR4)
Y643 Phosphorylation P22455 (FGFR4)
K644 Ubiquitination
Y719 Phosphorylation
Y754 Phosphorylation P22455 (FGFR4)
Y764 Phosphorylation

PTMs - P11362/P21802/P22607/P22455 As Enzyme

Substrate Site Source
P21802 (FGFR2) Y466 Uniprot
P21802 (FGFR2) Y586 Uniprot
P21802 (FGFR2) Y588 Uniprot
P21802 (FGFR2) Y656 Uniprot
P21802 (FGFR2) Y657 Uniprot
P21802 (FGFR2) Y769 Uniprot
P35222 (CTNNB1) Y142 Uniprot
P60484 (PTEN) Y240 Uniprot
P62993 (GRB2) Y209 Uniprot
Substrate Site Source
P22607-3 (FGFR3) Y465 Uniprot
P22607-3 (FGFR3) Y535 Uniprot
P22607-3 (FGFR3) Y536 Uniprot
P22607-1 (FGFR3) Y577 Uniprot
P22607-3 (FGFR3) Y612 Uniprot
P22607 (FGFR3) Y647 Uniprot
P22607 (FGFR3) Y648 Uniprot
P22607-3 (FGFR3) Y658 Uniprot
P22607-1 (FGFR3) Y724 Uniprot
P22607 (FGFR3) Y760 Uniprot
P22607 (FGFR3) Y770 Uniprot
P35222 (CTNNB1) Y142 Uniprot
P40763-2 (STAT3) Y704 Uniprot
P40763 (STAT3) Y705 Uniprot
P42224 (STAT1) Y701 Uniprot
P51812 (RPS6KA3) Y488 Uniprot
P51812 (RPS6KA3) Y529 Uniprot
P51812 (RPS6KA3) Y707 Uniprot
P60484 (PTEN) Y240 Uniprot
Substrate Site Source
O60506 (SYNCRIP) Y373 Uniprot
P00338 (LDHA) Y10 Uniprot
P00338 (LDHA) Y83 Uniprot
P11362 (FGFR1) Y154 Uniprot
P11362 (FGFR1) Y280 Uniprot
P11362 (FGFR1) Y307 Uniprot
P11362 (FGFR1) Y463 Uniprot
P11362 (FGFR1) Y583 Uniprot
P11362 (FGFR1) Y585 Uniprot
P11362 (FGFR1) Y605 Uniprot
P11362 (FGFR1) Y653 Uniprot
P11362 (FGFR1) Y654 Uniprot
P11362 (FGFR1) Y730 Uniprot
P11362 (FGFR1) Y766 Uniprot
P16144 (ITGB4) Y1564 Uniprot
P51812 (RPS6KA3) Y707 Uniprot
P56945 (BCAR1) Y128 Uniprot
P56945 (BCAR1) Y249 Uniprot
P56945 (BCAR1) Y306 Uniprot
P56945 (BCAR1) Y327 Uniprot
P56945 (BCAR1) Y410 Uniprot
Q14247 (CTTN) Y446 Uniprot
Q15118 (PDK1) Y136 Uniprot
Q15118 (PDK1) Y243 Uniprot
Q15118 (PDK1) Y244 Uniprot
Q9P0J1 (PDP1) Y381 Uniprot
Q9UBW7 (ZMYM2) Y502 Uniprot
Q9UBW7 (ZMYM2) Y557 Uniprot
Q9UBW7 (ZMYM2) Y595 Uniprot
Q9UBW7 (ZMYM2) Y605 Uniprot
Q9UBW7 (ZMYM2) Y680 Uniprot
Q9UBW7 (ZMYM2) Y683 Uniprot
Q9UBW7 (ZMYM2) Y729 Uniprot
Q9Y2J4 (AMOTL2) Y107 Uniprot
Substrate Site Source
P22455 (FGFR4) Y642 Uniprot
P22455 (FGFR4) Y643 Uniprot
P22455-2 (FGFR4) Y714 Uniprot
P22455 (FGFR4) Y754 Uniprot
P40763-2 (STAT3) Y704 Uniprot
P40763 (STAT3) Y705 Uniprot
P42224-1 (STAT1) Y701 Uniprot

Research Backgrounds

Function:

Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of embryonic development, cell proliferation, differentiation and migration. Required for normal mesoderm patterning and correct axial organization during embryonic development, normal skeletogenesis and normal development of the gonadotropin-releasing hormone (GnRH) neuronal system. Phosphorylates PLCG1, FRS2, GAB1 and SHB. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Promotes phosphorylation of SHC1, STAT1 and PTPN11/SHP2. In the nucleus, enhances RPS6KA1 and CREB1 activity and contributes to the regulation of transcription. FGFR1 signaling is down-regulated by IL17RD/SEF, and by FGFR1 ubiquitination, internalization and degradation.

PTMs:

Autophosphorylated. Binding of FGF family members together with heparan sulfate proteoglycan or heparin promotes receptor dimerization and autophosphorylation on tyrosine residues. Autophosphorylation occurs in trans between the two FGFR molecules present in the dimer and proceeds in a highly ordered manner. Initial autophosphorylation at Tyr-653 increases the kinase activity by a factor of 50 to 100. After this, Tyr-583 becomes phosphorylated, followed by phosphorylation of Tyr-463, Tyr-766, Tyr-583 and Tyr-585. In a third stage, Tyr-654 is autophosphorylated, resulting in a further tenfold increase of kinase activity. Phosphotyrosine residues provide docking sites for interacting proteins and so are crucial for FGFR1 function and its regulation.

Ubiquitinated. FGFR1 is rapidly ubiquitinated by NEDD4 after autophosphorylation, leading to internalization and lysosomal degradation. CBL is recruited to activated FGFR1 via FRS2 and GRB2, and mediates ubiquitination and subsequent degradation of FGFR1.

N-glycosylated in the endoplasmic reticulum. The N-glycan chains undergo further maturation to an Endo H-resistant form in the Golgi apparatus.

Subcellular Location:

Cell membrane>Single-pass type I membrane protein. Nucleus. Cytoplasm>Cytosol. Cytoplasmic vesicle.
Note: After ligand binding, both receptor and ligand are rapidly internalized. Can translocate to the nucleus after internalization, or by translocation from the endoplasmic reticulum or Golgi apparatus to the cytosol, and from there to the nucleus.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Detected in astrocytoma, neuroblastoma and adrenal cortex cell lines. Some isoforms are detected in foreskin fibroblast cell lines, however isoform 17, isoform 18 and isoform 19 are not detected in these cells.

Subunit Structure:

Monomer. Homodimer after ligand binding. Interacts predominantly with FGF1 and FGF2, but can also interact with FGF3, FGF4, FGF5, FGF6, FGF8, FGF10, FGF19, FGF21, FGF22 and FGF23 (in vitro). Ligand specificity is determined by tissue-specific expression of isoforms, and differences in the third Ig-like domain are crucial for ligand specificity. Affinity for fibroblast growth factors (FGFs) is increased by heparan sulfate glycosaminoglycans that function as coreceptors. Likewise, KLB increases the affinity for FGF19, FGF21 and FGF23. Interacts (phosphorylated on Tyr-766) with PLCG1 (via SH2 domains). Interacts with FRS2. Interacts with RPS6KA1. Interacts (via C-terminus) with NEDD4 (via WW3 domain). Interacts with KL (By similarity). Interacts with SHB (via SH2 domain). Interacts with GRB10. Interacts with ANOS1; this interaction does not interfere with FGF2-binding to FGFR1, but prevents binding of heparin-bound FGF2. Interacts with SOX2 and SOX3. Interacts with FLRT1, FLRT2 and FLRT3 (By similarity). Found in a ternary complex with FGF1 and ITGAV:ITGB3.

Family&Domains:

The second and third Ig-like domains directly interact with fibroblast growth factors (FGF) and heparan sulfate proteoglycans. Isoforms lacking the first Ig-like domain have higher affinity for fibroblast growth factors (FGF) and heparan sulfate proteoglycans than isoforms with all three Ig-like domains.

Belongs to the protein kinase superfamily. Tyr protein kinase family. Fibroblast growth factor receptor subfamily.

Function:

Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of cell proliferation, differentiation, migration and apoptosis, and in the regulation of embryonic development. Required for normal embryonic patterning, trophoblast function, limb bud development, lung morphogenesis, osteogenesis and skin development. Plays an essential role in the regulation of osteoblast differentiation, proliferation and apoptosis, and is required for normal skeleton development. Promotes cell proliferation in keratinocytes and immature osteoblasts, but promotes apoptosis in differentiated osteoblasts. Phosphorylates PLCG1, FRS2 and PAK4. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. FGFR2 signaling is down-regulated by ubiquitination, internalization and degradation. Mutations that lead to constitutive kinase activation or impair normal FGFR2 maturation, internalization and degradation lead to aberrant signaling. Over-expressed FGFR2 promotes activation of STAT1.

PTMs:

Autophosphorylated. Binding of FGF family members together with heparan sulfate proteoglycan or heparin promotes receptor dimerization and autophosphorylation on several tyrosine residues. Autophosphorylation occurs in trans between the two FGFR molecules present in the dimer. Phosphorylation at Tyr-769 is essential for interaction with PLCG1.

N-glycosylated in the endoplasmic reticulum. The N-glycan chains undergo further maturation to an Endo H-resistant form in the Golgi apparatus.

Ubiquitinated. FGFR2 is rapidly ubiquitinated after autophosphorylation, leading to internalization and degradation. Subject to degradation both in lysosomes and by the proteasome.

Subcellular Location:

Cell membrane>Single-pass type I membrane protein. Golgi apparatus. Cytoplasmic vesicle.
Note: Detected on osteoblast plasma membrane lipid rafts. After ligand binding, the activated receptor is rapidly internalized and degraded.

Cell membrane>Single-pass type I membrane protein.
Note: After ligand binding, the activated receptor is rapidly internalized and degraded.

Cell membrane>Single-pass type I membrane protein.
Note: After ligand binding, the activated receptor is rapidly internalized and degraded.

Secreted.

Secreted.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Subunit Structure:

Monomer. Homodimer after ligand binding. Interacts predominantly with FGF1 and FGF2, but can also interact with FGF3, FGF4, FGF6, FGF7, FGF8, FGF9, FGF10, FGF17, FGF18 and FGF22 (in vitro). Ligand specificity is determined by tissue-specific expression of isoforms, and differences in the third Ig-like domain are crucial for ligand specificity. Isoform 1 has high affinity for FGF1 and FGF2, but low affinity for FGF7. Isoform 3 has high affinity for FGF1 and FGF7, and has much higher affinity for FGF7 than isoform 1 (in vitro). Affinity for fibroblast growth factors (FGFs) is increased by heparan sulfate glycosaminoglycans that function as coreceptors. Likewise, KLB increases the affinity for FGF19 and FGF21. Interacts with PLCG1, GRB2 and PAK4. Interacts with FLRT2 (By similarity).

Family&Domains:

The second and third Ig-like domains directly interact with fibroblast growth factors (FGF) and heparan sulfate proteoglycans. Alternative splicing events affecting the third Ig-like domain are crucial for ligand selectivity.

Belongs to the protein kinase superfamily. Tyr protein kinase family. Fibroblast growth factor receptor subfamily.

Function:

Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of cell proliferation, differentiation and apoptosis. Plays an essential role in the regulation of chondrocyte differentiation, proliferation and apoptosis, and is required for normal skeleton development. Regulates both osteogenesis and postnatal bone mineralization by osteoblasts. Promotes apoptosis in chondrocytes, but can also promote cancer cell proliferation. Required for normal development of the inner ear. Phosphorylates PLCG1, CBL and FRS2. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Plays a role in the regulation of vitamin D metabolism. Mutations that lead to constitutive kinase activation or impair normal FGFR3 maturation, internalization and degradation lead to aberrant signaling. Over-expressed or constitutively activated FGFR3 promotes activation of PTPN11/SHP2, STAT1, STAT5A and STAT5B. Secreted isoform 3 retains its capacity to bind FGF1 and FGF2 and hence may interfere with FGF signaling.

PTMs:

Autophosphorylated. Binding of FGF family members together with heparan sulfate proteoglycan or heparin promotes receptor dimerization and autophosphorylation on tyrosine residues. Autophosphorylation occurs in trans between the two FGFR molecules present in the dimer. Phosphorylation at Tyr-724 is essential for stimulation of cell proliferation and activation of PIK3R1, STAT1 and MAP kinase signaling. Phosphorylation at Tyr-760 is required for interaction with PIK3R1 and PLCG1.

Ubiquitinated. Is rapidly ubiquitinated after ligand binding and autophosphorylation, leading to receptor internalization and degradation. Subject to both proteasomal and lysosomal degradation.

N-glycosylated in the endoplasmic reticulum. The N-glycan chains undergo further maturation to an Endo H-resistant form in the Golgi apparatus.

Subcellular Location:

Cell membrane>Single-pass type I membrane protein. Cytoplasmic vesicle. Endoplasmic reticulum.
Note: The activated receptor is rapidly internalized and degraded. Detected in intracellular vesicles after internalization of the autophosphorylated receptor.

Cell membrane>Single-pass type I membrane protein.

Secreted.

Cell membrane>Single-pass type I membrane protein.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Expressed in brain, kidney and testis. Very low or no expression in spleen, heart, and muscle. In 20- to 22-week old fetuses it is expressed at high level in kidney, lung, small intestine and brain, and to a lower degree in spleen, liver, and muscle. Isoform 2 is detected in epithelial cells. Isoform 1 is not detected in epithelial cells. Isoform 1 and isoform 2 are detected in fibroblastic cells.

Subunit Structure:

Monomer. Homodimer after ligand binding. Interacts with FGF1, FGF2, FGF4, FGF6; FGF8, FGF9, FGF10, FGF17, FGF18, FGF19, FGF20 and FGF23 (in vitro). Interacts with KLB. Affinity for fibroblast growth factors (FGFs) is increased by heparan sulfate glycosaminoglycans that function as coreceptors. Likewise, KLB increases the affinity for FGF19 and FGF21. Interacts with PIK3R1, PLCG1, SOCS1 and SOCS3. Isoform 3 forms disulfide-linked dimers.

Family&Domains:

The second and third Ig-like domains directly interact with fibroblast growth factors (FGF) and heparan sulfate proteoglycans.

Belongs to the protein kinase superfamily. Tyr protein kinase family. Fibroblast growth factor receptor subfamily.

Function:

Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays a role in the regulation of cell proliferation, differentiation and migration, and in regulation of lipid metabolism, bile acid biosynthesis, glucose uptake, vitamin D metabolism and phosphate homeostasis. Required for normal down-regulation of the expression of CYP7A1, the rate-limiting enzyme in bile acid synthesis, in response to FGF19. Phosphorylates PLCG1 and FRS2. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Promotes SRC-dependent phosphorylation of the matrix protease MMP14 and its lysosomal degradation. FGFR4 signaling is down-regulated by receptor internalization and degradation; MMP14 promotes internalization and degradation of FGFR4. Mutations that lead to constitutive kinase activation or impair normal FGFR4 inactivation lead to aberrant signaling.

PTMs:

N-glycosylated. Full maturation of the glycan chains in the Golgi is essential for high affinity interaction with FGF19.

Ubiquitinated. Subject to proteasomal degradation when not fully glycosylated.

Autophosphorylated. Binding of FGF family members together with heparan sulfate proteoglycan or heparin promotes receptor dimerization and autophosphorylation on tyrosine residues. Autophosphorylation occurs in trans between the two FGFR molecules present in the dimer.

Subcellular Location:

Cell membrane>Single-pass type I membrane protein. Endosome. Endoplasmic reticulum.
Note: Internalized from the cell membrane to recycling endosomes, and from there back to the cell membrane.

Secreted.

Cytoplasm.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Expressed in gastrointestinal epithelial cells, pancreas, and gastric and pancreatic cancer cell lines.

Subunit Structure:

Monomer. Homodimer after ligand binding. Interacts with FGF1, FGF2, FGF4, FGF6, FGF8, FGF9, FGF16, FGF17, FGF18, FGF19, FGF21 and FGF23 (in vitro). Binding affinity for FGF family members is enhanced by interactions between FGFs and heparan sulfate proteoglycans. Interacts with KLB; this strongly increases the affinity for FGF19 and FGF23. Affinity for FGF19 is strongly increased by KLB and sulfated glycosaminoglycans. KLB and KL both interact with the core-glycosylated FGFR4 in the endoplasmic reticulum and promote its degradation, so that only FGFR4 with fully mature N-glycans is expressed at the cell surface. Identified in a complex with NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN. Interacts with MMP14 and HIP1. Interacts with STAT3.

Family&Domains:

Belongs to the protein kinase superfamily. Tyr protein kinase family. Fibroblast growth factor receptor subfamily.

Research Fields

· Cellular Processes > Transport and catabolism > Endocytosis.   (View pathway)

· Cellular Processes > Cellular community - eukaryotes > Adherens junction.   (View pathway)

· Cellular Processes > Cellular community - eukaryotes > Signaling pathways regulating pluripotency of stem cells.   (View pathway)

· Cellular Processes > Cell motility > Regulation of actin cytoskeleton.   (View pathway)

· Environmental Information Processing > Signal transduction > MAPK signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > Ras signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > Rap1 signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > PI3K-Akt signaling pathway.   (View pathway)

· Human Diseases > Drug resistance: Antineoplastic > EGFR tyrosine kinase inhibitor resistance.

· Human Diseases > Cancers: Overview > Pathways in cancer.   (View pathway)

· Human Diseases > Cancers: Overview > Proteoglycans in cancer.

· Human Diseases > Cancers: Overview > MicroRNAs in cancer.

· Human Diseases > Cancers: Specific types > Prostate cancer.   (View pathway)

· Human Diseases > Cancers: Specific types > Melanoma.   (View pathway)

· Human Diseases > Cancers: Specific types > Bladder cancer.   (View pathway)

· Human Diseases > Cancers: Specific types > Breast cancer.   (View pathway)

· Human Diseases > Cancers: Specific types > Gastric cancer.   (View pathway)

· Human Diseases > Cancers: Overview > Central carbon metabolism in cancer.   (View pathway)

References

1). A novel small molecule RK-019 inhibits FGFR2-amplification gastric cancer cell proliferation and induces apoptosis in vitro and in vivo. Frontiers in Pharmacology, 2022 (PubMed: 36210834) [IF=5.6]

2). Vascular Adventitial Fibroblasts-Derived FGF10 Promotes Vascular Smooth Muscle Cells Proliferation and Migration in vitro and the Neointima Formation in vivo. Journal of Inflammation Research, 2021 (PubMed: 34079328) [IF=4.5]

Application: IHC    Species: Rat    Sample: VSMCs

Figure 5 The activities of FGFR2 in VSMCs in vivo and in vitro. (A and C) Representative IHC images of P-FGFR2 staining (A) and its quantitative analysis (C) in rat LCA sections harvested at indicated times after balloon-injury. Scale bar=50μm, n=6. (B and D) Representative immunofluorescence images of P-FGFR2 staining (B) and its quantitative analysis (D) in cultured VSMCs under conditions as indicated. Scale bar=20μm, n=3. (E–G) The protein expression of P-FGFR2 in co-cultured VSMCs under conditions described in Figure 3D were analyzed by WB (E) and its quantitative analyses (F and G), n=3. *p<0.05; **p<0.01 vs Ctl. # p<0.05; ## p<0.01 between two groups as marked.

Application: IF/ICC    Species: Rat    Sample: VSMCs

Figure 5 The activities of FGFR2 in VSMCs in vivo and in vitro. (A and C) Representative IHC images of P-FGFR2 staining (A) and its quantitative analysis (C) in rat LCA sections harvested at indicated times after balloon-injury. Scale bar=50μm, n=6. (B and D) Representative immunofluorescence images of P-FGFR2 staining (B) and its quantitative analysis (D) in cultured VSMCs under conditions as indicated. Scale bar=20μm, n=3. (E–G) The protein expression of P-FGFR2 in co-cultured VSMCs under conditions described in Figure 3D were analyzed by WB (E) and its quantitative analyses (F and G), n=3. *p<0.05; **p<0.01 vs Ctl. # p<0.05; ## p<0.01 between two groups as marked.

Application: WB    Species: Rat    Sample: VSMCs

Figure 2 PDGF differentially regulates expression of FGF10 and FGFR2 in VECs, VSMCs and VAFs. VECs, VSMCs and VAFs were isolated from rat aorta and cultured. (A) Morphological features of VECs, VSMCs and VAFs in primary cultures. Bar=200μm. (B) Immunofluorescence staining of CD31, α-SMA and Vimentin in three types of cells. Nuclei were stained with DAPI. Bar=20μm. (C and D) Representative WB images (C) and summaries (D) of FGF10 and FGFR2 protein expressions in three types of cells with or with put treatment of PDGF (20ng/mL). n=3. *p<0.05 and **p<0.01. Abbreviation: ns, no significance.

3). Dapagliflozin promotes browning of white adipose tissue through the FGFR1-LKB1-AMPK signaling pathway. Molecular biology reports, 2024 (PubMed: 38644407) [IF=2.8]

Application: WB    Species: Mouse    Sample: 3T3-L1 cells

Fig. 5 Effects of DAPA on AMPK pathway in 3T3-L1 cells. After treatment with PD, Pim1, CC, and treatment with DAPA, heat shock protein levels and the protein expression of p-FGFR1, p-LKB1, and p-AMPK were measured (A). Heat shock protein expression and the protein expression of p-LKB1, and p-AMPK were also measured (B). Heat shock protein expression and the protein expression of p-AMPK were also measured (C). Data are presented as mean ± SD; **P 

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