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Anti-phospho-FGFR-1 (Tyr653/Tyr654), Cat. No. 06-1433, is a Rabbit polyclonal antibody that detects basic fibroblast growth factor receptor 1 phosphorylated on Tyr 653/654 and is tested for use in Peptide Inhibition Assay and use in Western Blotting.
More>>Anti-phospho-FGFR-1 (Tyr653/Tyr654), Cat. No. 06-1433, is a Rabbit polyclonal antibody that detects basic fibroblast growth factor receptor 1 phosphorylated on Tyr 653/654 and is tested for use in Peptide Inhibition Assay and use in Western Blotting. Less<<
Anti-phospho-FGFR-1 (Tyr653/Tyr654) Antibody: SDB (Sicherheitsdatenblätter), Analysenzertifikate und Qualitätszertifikate, Dossiers, Broschüren und andere verfügbare Dokumente.
Fibroblast growth factor receptor 1 (UniProt: P11362; also known as 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) is encoded by the FGFR1 (also known as BFGFR, CEK, FGFBR, FLG, FLT2, HBGFR) gene (Gene ID: 2260) in human. FGF-R1 is a single-pass type I membrane glycoprotein with serves as a receptor for fibroblast growth factor and plays a role in the regulation of embryonic development, cell proliferation, differentiation and migration. It is 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. FGFR-1 is synthesized with a signal peptide (aa 1-21), which is subsequently cleaved off to generate the mature form that contains an extracellular domain (aa 22-376), a transmembrane domain (aa 377-397), and a cytoplasmic domain (aa 398-822). FGF-R1 undergoes autophosphorylation and upon binding of FGF family members together with heparan sulfate proteoglycan or heparin promotes receptor dimerization and autophosphorylation on tyrosine residues. Initial autophosphorylation at tyrosine 653 increases the kinase activity by a factor of 50 to 100. Following this initial phosphorylation tyrosine 583 is phosphorylated followed by phosphorylation of tyrosines 463, 766, 583, and 585. In a third stage, tyrosine 654 is autophosphorylated, resulting in a further tenfold increase its kinase activity. Phosphotyrosine residues provide docking sites for interacting proteins and so are crucial for FGF-R1 function and its regulation. The downstream targets of PGF-R1 include phospholipase C g1 (PLCg1) FGF receptor substrate 2, GRB2-associated-binding protein 1 (GAB1), and SH2 domain-containing adapter protein B (SHB2). This ZooMAb® recombinant monoclonal antibody, generated by our propriety technology, offers significantly enhanced specificity, affinity, reproducibility, and stability over conventional monoclonals.
References
Product Information
Format
Affinity Purified
Control
Untreated and lambda phosphatase-treated HEK293T cells transfected with FGFR-1
Presentation
Purified rabbit polyclonal antibody in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
Anti-phospho-FGFR-1 (Tyr653/Tyr654), Cat. No. 06-1433, is a Rabbit polyclonal antibody that detects basic fibroblast growth factor receptor 1 phosphorylated on Tyr 653/654 and is tested for use in Peptide Inhibition Assay and use in Western Blotting.
Key Applications
Western Blotting
Peptide Inhibition Assay
Application Notes
Peptide Inhibition Analysis: A 1:5,000 dilution from a representative lot failed to detect the target band in lysate from HEK293 cells transfected with human FGFR1 when preblocked with the immunogen phosphopeptide, but not with a corresponding non-phosphopeptide.
Note: Actual optimal working dilutions must be determined by end user as specimens, and experimental conditions may vary with the end user
Biological Information
Immunogen
KLH-conjugated linear peptide corresponding to 12 amino acids surrounding phosphotyrosine 653/654 from the C-terminal, cytoplasmic domain of human Fibroblast growth factor receptor 1 (FGFR1).
Epitope
Phosphorylated Tyr653/Tyr654
Concentration
Please refer to the Certificate of Analysis for the lot-specific concentration.
Host
Rabbit
Specificity
This rabbit polyclonal antibody specifically detects Fibroblast growth factor receptor 1 (FGFR1) phosphorylated on tyrosine 653/654.
Species Reactivity
Human
Mouse
Rat
Chicken
Bovine
Xenopus
Species Reactivity Note
Human. Predicted to react with Bovine, Chicken, Mouse, Rat, Xenopus based on 100% sequence homology.
The protein encoded by this gene is a member of the fibroblast growth factor receptor (FGFR) family, where amino acid sequence is highly conserved between members and throughout evolution. FGFR family members differ from one another in their ligand affinities and tissue distribution. A full-length representative protein consists of an extracellular region, composed of three immunoglobulin-like domains, a single hydrophobic membrane-spanning segment and a cytoplasmic tyrosine kinase domain. The extracellular portion of the protein interacts with fibroblast growth factors, setting in motion a cascade of downstream signals, ultimately influencing mitogenesis and differentiation. This particular family member binds both acidic and basic fibroblast growth factors and is involved in limb induction. Mutations in this gene have been associated with Pfeiffer syndrome, Jackson-Weiss syndrome, Antley-Bixler syndrome, osteoglophonic dysplasia, and autosomal dominant Kallmann syndrome 2. Chromosomal aberrations involving this gene are associated with stem cell myeloproliferative disorder and stem cell leukemia lymphoma syndrome. Alternatively spliced variants which encode different protein isoforms have been described; however, not all variants have been fully characterized. [provided by RefSeq].
FUNCTION: Receptor for fibroblast growth factors FGF2 and FGF1. Receptor for FGF23 in the presence of KL (By similarity). Promotes mitogenesis in response to fibroblast growth factors. Activates PLCG1.
CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
SUBUNIT STRUCTURE: Homodimer. Interacts with KLB (By similarity). Interacts with KL and FGF23 (By similarity). Interacts with SHB and GRB10. Interacts with PLCG1 (via SH2 domains). Interacts with KAL1; this interaction does not interfere with FGF2-binding to FGFR1, but prevents binding of heparin-bound FGF2. Interacts with SOX2 and SOX3 (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
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.
PTM: Binding of FGF1 and heparin promotes autophosphorylation on tyrosine residues and activation of the receptor.
INVOLVEMENT IN DISEASE: Defects in FGFR1 are a cause of Pfeiffer syndrome (PS) [MIM:101600]; also known as acrocephalosyndactyly type V (ACS5). PS is characterized by craniosynostosis (premature fusion of the skull sutures) with deviation and enlargement of the thumbs and great toes, brachymesophalangy, with phalangeal ankylosis and a varying degree of soft tissue syndactyly.
Defects in FGFR1 are a cause of idiopathic hypogonadotropic hypogonadism (IHH) [MIM:146110]. IHH is defined as a deficiency of the pituitary secretion of follicle-stimulating hormone and luteinizing hormone, which results in the impairment of pubertal maturation and of reproductive function.
Defects in FGFR1 are the cause of Kallmann syndrome type 2 (KAL2) [MIM:147950]; also known as hypogonadotropic hypogonadism and anosmia. Anosmia or hyposmia is related to the absence or hypoplasia of the olfactory bulbs and tracts. Hypogonadism is due to deficiency in gonadotropin-releasing hormone and probably results from a failure of embryonic migration of gonadotropin-releasing hormone-synthesizing neurons. In some cases, midline cranial anomalies (cleft lip/palate and imperfect fusion) are present and anosmia may be absent or inconspicuous.
Defects in FGFR1 are the cause of osteoglophonic dysplasia (OGD) [MIM:166250]; also known as osteoglophonic dwarfism. OGD is characterized by craniosynostosis, prominent supraorbital ridge, and depressed nasal bridge, as well as by rhizomelic dwarfism and nonossifying bone lesions. Inheritance is autosomal dominant.
Defects in FGFR1 are the cause of trigonocephaly non-syndromic (TRICEPH) [MIM:190440]; also known as metopic craniosynostosis. The term trigonocephaly describes the typical keel-shaped deformation of the forehead resulting from premature fusion of the frontal suture. Trigonocephaly may occur also as a part of a syndrome.
Note=A chromosomal aberration involving FGFR1 may be a cause of stem cell leukemia lymphoma syndrome (SCLL). Translocation t(8;13)(p11;q12) with ZMYM2. SCLL usually presents as lymphoblastic lymphoma in association with a myeloproliferative disorder, often accompanied by pronounced peripheral eosinophilia and/or prominent eosinophilic infiltrates in the affected bone marrow.
Note=A chromosomal aberration involving FGFR1 may be a cause of stem cell myeloproliferative disorder (MPD). Translocation t(6;8)(q27;p11) with FGFR1OP. Insertion ins(12;8)(p11;p11p22) with FGFR1OP2. MPD is characterized by myeloid hyperplasia, eosinophilia and T-cell or B-cell lymphoblastic lymphoma. In general it progresses to acute myeloid leukemia. The fusion proteins FGFR1OP2-FGFR1, FGFR1OP-FGFR1 or FGFR1-FGFR1OP may exhibit constitutive kinase activity and be responsible for the transforming activity.
Note=A chromosomal aberration involving FGFR1 may be a cause of stem cell myeloproliferative disorder (MPD). Translocation t(8;9)(p12;q33) with CEP110. MPD is characterized by myeloid hyperplasia, eosinophilia and T-cell or B-cell lymphoblastic lymphoma. In general it progresses to acute myeloid leukemia. The fusion protein CEP110-FGFR1 is found in the cytoplasm, exhibits constitutive kinase activity and may be responsible for the transforming activity.
SEQUENCE SIMILARITIES: Belongs to the protein kinase superfamily. Tyr protein kinase family. Fibroblast growth factor receptor subfamily.
~130 kDa observed; 91.87 kDa calculated. Uncharacterized bands may be observed in some lysate(s).
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Quality Assurance
Evaluated by Western Blotting in HEK293 cells transfected with FGFR1.
Western Blotting Analysis: A 1:5,000 dilution of this antibody detected phospho-FGFR-1 (Tyr653/Tyr654) in HEK293 cells transfected with human FGFR1.
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
LTBP-2 Has a Single High-Affinity Binding Site for FGF-2 and Blocks FGF-2-Induced Cell Proliferation. Menz, C; Parsi, MK; Adams, JR; Sideek, MA; Kopecki, Z; Cowin, AJ; Gibson, MA PloS one
10
e0135577
2015
Latent transforming growth factor-beta-1 binding protein-2 (LTBP-2) belongs to the fibrillin-LTBP superfamily of extracellular matrix proteins. LTBPs and fibrillins are involved in the sequestration and storage of latent growth factors, particularly transforming growth factor β (TGF-β), in tissues. Unlike other LTBPs, LTBP-2 does not covalently bind TGF-β, and its molecular functions remain unclear. We are screening LTBP-2 for binding to other growth factors and have found very strong saturable binding to fibroblast growth factor-2 (FGF-2) (Kd = 1.1 nM). Using a series of recombinant LTBP-2 fragments a single binding site for FGF-2 was identified in a central region of LTBP-2 consisting of six tandem epidermal growth factor-like (EGF-like) motifs (EGFs 9-14). This region was also shown to contain a heparin/heparan sulphate-binding site. FGF-2 stimulation of fibroblast proliferation was completely negated by the addition of 5-fold molar excess of LTBP-2 to the assay. Confocal microscopy showed strong co-localisation of LTBP-2 and FGF-2 in fibrotic keloid tissue suggesting that the two proteins may interact in vivo. Overall the study indicates that LTBP-2 is a potent inhibitor of FGF-2 that may influence FGF-2 bioactivity during wound repair particularly in fibrotic tissues.
Postnatal and adult subventricular zone (SVZ) neurogenesis is believed to be primarily controlled by neural stem cell (NSC)-intrinsic mechanisms, interacting with extracellular and niche-driven cues. Although behavioral experiments and disease states have suggested possibilities for higher level inputs, it is unknown whether neural activity patterns from discrete circuits can directly regulate SVZ neurogenesis. We identified a previously unknown population of choline acetyltransferase (ChAT)(+) neurons residing in the rodent SVZ neurogenic niche. These neurons showed morphological and functional differences from neighboring striatal counterparts and released acetylcholine locally in an activity-dependent fashion. Optogenetic inhibition and stimulation of subependymal ChAT(+) neurons in vivo indicated that they were necessary and sufficient to control neurogenic proliferation. Furthermore, whole-cell recordings and biochemical experiments revealed direct SVZ NSC responses to local acetylcholine release, synergizing with fibroblast growth factor receptor activation to increase neuroblast production. These results reveal an unknown gateway connecting SVZ neurogenesis to neuronal activity-dependent control and suggest possibilities for modulating neuroregenerative capacities in health and disease.
