protein

Recombinant Human Fibroblast growth factor receptor 3

MBS952862

0.05 mg (E-Coli)

185 USD

Recombinant Protein

Recombinant Human Fibroblast growth factor receptor 3

Fibroblast growth factor receptor 3

CD333

fibroblast growth factor receptor 3 isoform 1; Fibroblast growth factor receptor 3; fibroblast growth factor receptor 3; fibroblast growth factor receptor 3; CD_antigen: CD333

FGFR3

FGFR3; FGFR3; ACH; CEK2; JTK4; CD333; HSFGFR3EX; JTK4; FGFR-3

FGFR3_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

23-375

791

ESLGTEQRVVGRAAEVPGPEPGQQEQLVFGSGDAVELSC
PPPGGGPMGPTVWVKDGTGLVPSERVLVGPQRLQVLNAS
HEDSGAYSCRQRLTQRVLCHFSVRVTDAPSSGDDEDGED
EAEDTGVDTGAPYWTRPERMDKKLLAVPAANTVRFRCPA
AGNPTPSISWLKNGREFRGEHRIGGIKLRHQQWSLVMES
VVPSDRGNYTCVVENKFGSIRQTYTLDVLERSPHRPILQ
AGLPANQTAVLGSDVEFHCKV

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Apoptosis

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

Isolation of an additional member of the fibroblast growth factor receptor family, FGFR-3.Keegan K., Johnson D.E., Williams L.T., Hayman M.J.Proc. Natl. Acad. Sci. U.S.A. 88:1095-1099(1991) Fibroblast growth factor receptor 3 lacking the Ig IIIb and transmembrane domains secreted from human squamous cell carcinoma DJM-1 binds to FGFs.Terada M., Shimizu A., Sato N., Miyakaze S.I., Katayama H., Kurokawa-Seo M.Mol. Cell Biol. Res. Commun. 4:365-373(2001) Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. NIEHS SNPs programGeneration and annotation of the DNA sequences of human chromosomes 2 and 4.Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.Nature 434:724-731(2005)

4503711

NP_000133.1

NM_000142.4

P22607

42.2kD

ARMS-mediated Activation Pathway (1269471); Adaptive Immune System Pathway (1269171); Axon Guidance Pathway (1270303); Bladder Cancer Pathway (83115); Bladder Cancer Pathway (527); Central Carbon Metabolism In Cancer Pathway (1059538); Central Carbon Metabolism In Cancer Pathway (1084231); Constitutive Signaling By Aberrant PI3K In Cancer Pathway (1268880); Cytokine Signaling In Immune System Pathway (1269310); DAP12 Interactions Pathway (1269283)

This gene encodes a member of the fibroblast growth factor receptor (FGFR) family, with its amino acid sequence being highly conserved between members and among divergent species. FGFR family members differ from one another in their ligand affinities and tissue distribution. A full-length representative protein would consist 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 acidic and basic fibroblast growth hormone and plays a role in bone development and maintenance. Mutations in this gene lead to craniosynostosis and multiple types of skeletal dysplasia. Three alternatively spliced transcript variants that encode different protein isoforms have been described. [provided by RefSeq, Jul 2009]

FGFR3: a receptor tyrosine kinase of the highly-conserved FGFR family that binds fibroblast growth factor (FGF). Mutations are associated with thanatophoric dysplasia (TD), craniosynostosis Adelaide type, many craniosynostotic syndromes and bone malformations. Three splice-variant isoforms have been described. Activating point mutations cause dwarfism, including achondroplasia, hypochrondroplasia and thanatophoric dysplasia, and facial and other morphogenetic disorders, including Crouzon syndrome, craniosynostosis Adelaide type, San Diego skeletal displasia and Muenke syndrome. Translocations t(4;14) involving the IgH region are common in multiple myeloma and frequently involve FGFR3. Activated FGFR3 found in 30% of bladder cancers and several cervical cancers, but not in other tumors. Two mutations found in colorectal cancer. Protein type: Membrane protein, integral; Kinase, protein; EC 2.7.10.1; Protein kinase, tyrosine (receptor); Protein kinase, TK; TK group; FGFR family. Chromosomal Location of Human Ortholog: 4p16.3. Cellular Component: cell surface; endoplasmic reticulum; extracellular region; focal adhesion; Golgi apparatus; integral to plasma membrane; internal side of plasma membrane; lysosome; nucleus; perinuclear region of cytoplasm; plasma membrane; transport vesicle. Molecular Function: ATP binding; fibroblast growth factor binding; fibroblast growth factor receptor activity; protein binding; protein-tyrosine kinase activity. Biological Process: activation of MAPKK activity; axon guidance; bone mineralization; cell-cell signaling; chondrocyte differentiation; digestive tract morphogenesis; endochondral ossification; epidermal growth factor receptor signaling pathway; fibroblast growth factor receptor signaling pathway; forebrain development; innate immune response; inner ear receptor cell differentiation; insulin receptor signaling pathway; JAK-STAT cascade; lens morphogenesis in camera-type eye; MAPKKK cascade; morphogenesis of an epithelium; myelination in the central nervous system; negative regulation of astrocyte differentiation; negative regulation of cell proliferation; negative regulation of developmental growth; negative regulation of mitosis; negative regulation of smoothened signaling pathway; negative regulation of transcription from RNA polymerase II promoter; nerve growth factor receptor signaling pathway; peptidyl-tyrosine phosphorylation; phosphoinositide-mediated signaling; positive regulation of cell differentiation; positive regulation of cell proliferation; positive regulation of endothelial cell proliferation; positive regulation of MAPKKK cascade; positive regulation of neuron apoptosis; positive regulation of phosphoinositide 3-kinase activity; positive regulation of protein ubiquitination; positive regulation of tyrosine phosphorylation of Stat1 protein; positive regulation of tyrosine phosphorylation of Stat3 protein; protein amino acid autophosphorylation; Ras protein signal transduction; response to axon injury; skeletal development; small GTPase mediated signal transduction; somatic stem cell maintenance; substantia nigra development; vascular endothelial growth factor receptor signaling pathway. Disease: Achondroplasia; Achondroplasia, Severe, With Developmental Delay And Acanthosis Nigricans; Bladder Cancer; Camptodactyly, Tall Stature, And Hearing Loss Syndrome; Cervical Cancer; Colorectal Cancer; Crouzon Syndrome With Acanthosis Nigricans; Hypochondroplasia; Lacrimoauriculodentodigital Syndrome; Muenke Syndrome; Nevus, Epidermal; Testicular Germ Cell Tumor; Thanatophoric Dysplasia, Type I; Thanatophoric Dysplasia, Type Ii

0.05 mg (E-Coli)

185 USD

0.2 mg (E-Coli)

420

0.5 mg (E-Coli)

680

1 mg (E-Coli)

1070