Product: FGFR1/2 Mouse Monoclonal Antibody
Catalog: BF8264
Description: Mouse monoclonal antibody to FGFR1/2
Application: WB IF/ICC
Reactivity: Human
Mol.Wt.: 92kD(Calculated).
Uniprot: P11362 | P21802

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Product Info

Source:
Mouse
Application:
WB 1:500-1:3000, IF/ICC 1:100-1:500
*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
Clonality:
Monoclonal [AFfirm8264]
Specificity:
FGFR1/2 Mouse Monoclonal Antibody detects endogenous levels of total FGFR1/2
Conjugate:
Unconjugated.
Purification:
Affinity-chromatography.
Storage:
Mouse IgG1 in phosphate buffered saline (without Mg2+ and Ca2+), 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;

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.

Sequence:
MWSWKCLLFWAVLVTATLCTARPSPTLPEQAQPWGAPVEVESFLVHPGDLLQLRCRLRDDVQSINWLRDGVQLAESNRTRITGEEVEVQDSVPADSGLYACVTSSPSGSDTTYFSVNVSDALPSSEDDDDDDDSSSEEKETDNTKPNRMPVAPYWTSPEKMEKKLHAVPAAKTVKFKCPSSGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVALGSNVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHSAWLTVLEALEERPAVMTSPLYLEIIIYCTGAFLISCMVGSVIVYKMKSGTKKSDFHSQMAVHKLAKSIPLRRQVTVSADSSASMNSGVLLVRPSRLSSSGTPMLAGVSEYELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGLEYCYNPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPGVPVEELFKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIVALTSNQEYLDLSMPLDQYSPSFPDTRSSTCSSGEDSVFSHEPLPEEPCLPRHPAQLANGGLKRR

MVSWGRFICLVVVTMATLSLARPSFSLVEDTTLEPEEPPTKYQISQPEVYVAAPGESLEVRCLLKDAAVISWTKDGVHLGPNNRTVLIGEYLQIKGATPRDSGLYACTASRTVDSETWYFMVNVTDAISSGDDEDDTDGAEDFVSENSNNKRAPYWTNTEKMEKRLHAVPAANTVKFRCPAGGNPMPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDVVERSPHRPILQAGLPANASTVVGGDVEFVCKVYSDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKAAGVNTTDKEIEVLYIRNVTFEDAGEYTCLAGNSIGISFHSAWLTVLPAPGREKEITASPDYLEIAIYCIGVFLIACMVVTVILCRMKNTTKKPDFSSQPAVHKLTKRIPLRRQVTVSAESSSSMNSNTPLVRITTRLSSTADTPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILTLTTNEEYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQYPHINGSVKT

PTMs - P11362/P21802 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
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)

PTMs - P11362/P21802 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
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

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.

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: Specific types > Prostate cancer.   (View pathway)

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

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