Product: FGFR2 Antibody
Catalog: AF0159
Description: Rabbit polyclonal antibody to FGFR2
Application: WB IHC
Reactivity: Human, Mouse, Rat
Prediction: Pig, Zebrafish, Bovine, Horse, Rabbit, Dog, Chicken, Xenopus
Mol.Wt.: 90kD, 140kDa; 92kD(Calculated).
Uniprot: P21802
RRID: AB_2833340

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 100ul $280 In stock
 200ul $350 In stock

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Product Info

Source:
Rabbit
Application:
WB 1:500-1:3000, 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
Prediction:
Pig(88%), Zebrafish(88%), Bovine(100%), Horse(100%), Rabbit(100%), Dog(100%), Chicken(100%), Xenopus(100%)
Clonality:
Polyclonal
Specificity:
FGFR2 Antibody detects endogenous levels of total FGFR2.
RRID:
AB_2833340
Cite Format: Affinity Biosciences Cat# AF0159, RRID:AB_2833340.
Conjugate:
Unconjugated.
Purification:
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
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

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):
Description:
FGFR2 a receptor tyrosine kinase of the highly-conserved FGFR family that binds fibroblast growth factor (FGF). Mutations are associated with many craniosynostotic syndromes and bone malformations. Mutations cause syndromes with defects in facial and limb development, including Crouzon syndrome, Beare-Stevenson cutis gyrata syndrome, Pfeiffer syndrome, Apert syndrome, and Jackson-Weiss syndrome. Somatic mutations seen in gastric cancer. Amplified in gastric, breast and some B cell cancers, but deleted in glioblastoma Twenty splice-variant isoforms have been described. Note: This description may include information from UniProtKB.
Sequence:
MVSWGRFICLVVVTMATLSLARPSFSLVEDTTLEPEEPPTKYQISQPEVYVAAPGESLEVRCLLKDAAVISWTKDGVHLGPNNRTVLIGEYLQIKGATPRDSGLYACTASRTVDSETWYFMVNVTDAISSGDDEDDTDGAEDFVSENSNNKRAPYWTNTEKMEKRLHAVPAANTVKFRCPAGGNPMPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDVVERSPHRPILQAGLPANASTVVGGDVEFVCKVYSDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKAAGVNTTDKEIEVLYIRNVTFEDAGEYTCLAGNSIGISFHSAWLTVLPAPGREKEITASPDYLEIAIYCIGVFLIACMVVTVILCRMKNTTKKPDFSSQPAVHKLTKRIPLRRQVTVSAESSSSMNSNTPLVRITTRLSSTADTPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILTLTTNEEYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQYPHINGSVKT

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
Dog
100
Xenopus
100
Chicken
100
Rabbit
100
Pig
88
Zebrafish
88
Sheep
0
Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - 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

PTMs - 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

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 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 > 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: Specific types > Prostate 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). Shi HJ et al. A novel long noncoding RNA FAF inhibits apoptosis via upregulating FGF9 through PI3K/AKT signaling pathway in ischemia-hypoxia cardiomyocytes. JOURNAL OF CELLULAR PHYSIOLOGY 2019 Dec;234(12):21973-21987 (PubMed: 31093967) [IF=5.6]

Application: WB    Species: rat    Sample: cardiomyocytes

FIGURE 7| The effects of lncRNA FAF, FGF9, and FGFR2 in cardiomyocytes and heart tissues. (a,b) The FGF9 mRNA and the protein expression level were measured by RT‐PCR and western blot analysis in ischemia–hypoxia cardiomyocytes and control groups. (c,d) The results of FGF9 mRNA and protein expression level in AMI rats and healthy controls on RT‐PCR and western blot analysis analysis.(e) The expression level of FGF9 was measured in the plasma of patients with AMI and healthy groups (N = 20). (f,g) The results of FGF9 mRNA and protein expression level in cardiomyocytes after overexpression of lncRNA FAF. (h,i) RT‐PCR and western blot analysis of FGFR2 in ischemia–hypoxia cardiomyocytes and control groups.

2). Zhang N et al. Liraglutide regulates lipid metabolism via FGF21-LKB1-AMPK-ACC1 pathway in white adipose tissues and macrophage of type 2 diabetic mice. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 2021 Feb 25;548:120-126. (PubMed: 33640604) [IF=3.1]

Application: WB    Species: Mice    Sample: diabetic mice

Fig. 2. Effects of LRG on adipocyte size and the protein expression in WAT of diabetic mice. (A) Adipocyte size of the mice; (B) Quantification of Fig. 2A; (C) Immunohistochemical assay of WAT; (D) Quantification of Fig. 2C; (E) Protein expression in WAT; (F) Quantification of Fig. 3E n ¼ 6 mice/group. #p < 0.05, ##p < 0.01,###p < 0.001 vs CON; *p < 0.05,**p < 0.01, ***p < 0.001 vs DM.

3). Hai E et al. Chi-miR-370-3p regulates hair follicle development of Inner Mongolian cashmere goats. G3-Genes Genomes Genetics 2021 Mar 23;jkab091. (PubMed: 33755111) [IF=2.6]

Application: WB    Species: Goats    Sample: epithelial cell

Figure 3 Verification of the regulatory effect of chi-mir-370-3p on TGF-βR2 and FGFR2 at epithelial cell and dermal fibroblast levels. (A) Construction of chi-miR-370-3p (lo) and chi-miR-370-3p (hi) dermal fibroblast and epithelial cell lines. (B) Relative expression of chi-miR-370-3p in various cell lines. (C) Relative expression of TGF-βR2 and FGFR2 in various cell lines. (D) Expression of β-actin, TGF-βR2, and FGFR2 proteins in each cell line. (E) Relative abundance of TGF-βR2 and FGFR2 proteins in different epithelial cell lines. (F) Relative abundance of TGF-βR2 and FGFR2 proteins in different dermal fibroblast cell lines.

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