Name :
Human FGFR1 Protein, ECD (Extracellular Domain), Fc-fusion, Recombinant
Description :
FGFR1 (fibroblast growth factor receptor 1), also known as FLT-2 and CD331, is a single-pass type I transmembrane protein that belongs to the FGFR subfamily of the receptor tyrosine kinase (RTK) family. There are 4 distinct members (FGFR1-4) that differ from one another in their ligand affinities, tissue distribution and biological functions. FGFRs mediate the biological activities of a group of at least 23 structurally related FGFs, including cell growth, differentiation, angiogenesis, wound healing, and tumorigenesis. All 4 FGFR members are composed of a signal peptide, 3 immunoglobulin (Ig)like domains, an acidbox region, a transmembrane domain and a cytoplasmic tyrosinekinase domain. FGFR1 is the receptor for FGF basic and also interacts with GRB14, SHB, FRS2. The extracellular region of FGFR1 interacts with FGFs, setting in motion a cascade of downstream signals, ultimately leading to mitogenesis and differentiation. FGFR1 plays an essential 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. Defects in FGFR1 are the cause of several diseases, such as Kallmann syndrome type 2 (KAL2), osteoglophonic dysplasia (OGD), and Pfeiffer syndrome (PF). Chromosomal aberrations involving FGFR1 are associated with stem cell leukemia lymphoma syndrome (SCLL) and stem cell myeloproliferative disorder (MPD).
Gene Symbol :
The recombinant human FGFR1-Fc fusion protein is expressed as a 492 amino acid protein consisting of Arg22 – Glu285 region of FGFR1 (Uniprot accession #P11362 – isoform 15) and a C-terminal Fc fusion from human IgG1, which exists as a dimer under non-reducing condition.
NCBI Gene ID :
2260
Uniprot Entry :
P11362
Construct Details :
The recombinant human FGFR1-Fc fusion protein is expressed as a 492 amino acid protein consisting of Arg22 – Glu285 region of FGFR1 (Uniprot accession #P11362 – isoform 15) and a C-terminal Fc fusion from human IgG1, which exists as a dimer under non-reducing condition.
Source :
Human cells stably expressing FGFR1-Fc and growing in chemical-defined media with no animal components or antibiotics
Amino Acid Sequence: :
RPSPTLPEQDALPSSEDDDDDDDSSSEEKETDNTKPNPVAPYWTSPEKMEKKLHAVPAAKTVK FKCPSSGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGS INHTYQLDVVERSPHRPILQAGLPANKTVALGSNVEFMCKVYSDPQPHIQWLKHIEVNGSKIG PDNLPYVQILKTAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHSAWLTVLEALEE RPAVMTSPLYLESTGTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHED PEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIE KTISKAKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPP VLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK
M.W. :
Calculated molecular mass (kDa): 55.0; Estimated by SDS-PAGE under reducing condition (kDa): 70-80
Calculated PI :
5.85
Calculated Extinction Coefficients :
(M-1 cm-1, at 280nm): 78435
Endotoxin Level :
>95% judged by SDS-PAGE under reducing condition (see the gel image above, labeled as DTT: “+” and “M”)
Formulation :
Supplied at 0.5 mg/ml in sterile PBS pH7.4 (carrier free).
Endotoxin Level :
<0.1 EU per 1 μg of purified recombinant protein determined by the LAL method
Biological Activity :
Binds and inhibits aFGF / FGF-acidic dependent proliferation of mouse fibroblast cells with an ED50 of 0.02 – 0.15 μg/mL
Molecule Class :
Receptor Tyrosine Kinase (RTK)
Gene Synonym :
<0.1 EU per 1 μg of purified recombinant protein determined by the LAL method
Gene Family :
FGFR1; CD331; FGFR-1; CEK; FLG; HH2; OGD; c-Fgr; FLT2; KAL2; BFGFR; FGFBR; FLT-2; HBGFR; N-SAM; HRTFDS; bFGF-R-1
Research Area :
Development
Pathway/Disease :
FGF/FGFR Signaling Pathway
Species :
Human
CD Antigen :
CD331
References :
1. J. Biol. Chem. 271: 1726-1731 (1996). 2. Biochem. Cell Biol. 75:669 (1997). 3. Proc. Natl. Acad. Sci. 97: 49-54 (2000). 4. Nature. 407: 1029-1034 (2000). 5. Nature Genetics. 39: 870-874 (2007).
Related category websites: https://www.medchemexpress.com/recombinant-proteins.html
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