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Name :
Human FGFR2 Protein, ECD (Extracellular Domain), Fc-fusion, Biotinylated, Recombinant

Description :
FGFR2 (fibroblast growth factor receptor 2), also known as KGFR and CD332, 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. FGFR2 is a high-affinity receptor for acidic, basic and/or keratinocyte growth factor, depending on the isoform. The extracellular portion of FGFR2 interacts with FGFs, setting in motion a cascade of downstream signals, ultimately leading to mitogenesis and differentiation. FGFR2 plays an essential role in the regulation of cell proliferation, differentiation, migration and apoptosis, and in the regulation of embryonic development. It is required for normal embryonic patterning, trophoblast function, limb bud development, lung morphogenesis, osteogenesis and skin development. Mutations in the FGFR2 gene are associated with Crouzon syndrome, Pfeiffer syndrome, Craniosynostosis, Apert syndrome, Jackson-Weiss syndrome, Beare-Stevenson cutis gyrata syndrome, Saethre-Chotzen syndrome, and syndromic craniosynostosis.

Gene Symbol :
The recombinant human FGFR2-Fc fusion protein is expressed as a 584 amino acid protein consisting of Arg22 – Glu377 region of FGFR2 (Uniprot accession #P21802 – isoform 1) and a C-terminal Fc fusion from human IgG1, which exists as a dimer under non-reducing condition.

NCBI Gene ID :
2263

Uniprot Entry :
P21802

Construct Details :
The recombinant human FGFR2-Fc fusion protein is expressed as a 584 amino acid protein consisting of Arg22 – Glu377 region of FGFR2 (Uniprot accession #P21802 – isoform 1) and a C-terminal Fc fusion from human IgG1, which exists as a dimer under non-reducing condition.

Source :
Human cells stably expressing FGFR2-Fc and growing in chemical-defined media with no animal components or antibiotics

Amino Acid Sequence: :
RPSFSLVEDTTLEPEEPPTKYQISQPEVYVAAPGESLEVRCLLKDAAVISWTKDGVHLGPNNR TVLIGEYLQIKGATPRDSGLYACTASRTVDSETWYFMVNVTDAISSGDDEDDTDGAEDFVSEN SNNKRAPYWTNTEKMEKRLHAVPAANTVKFRCPAGGNPMPTMRWLKNGKEFKQEHRIGGYKVR NQHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDVVERSPHRPILQAGLPANASTVVGGD VEFVCKVYSDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKAAGVNTTDKEIEVLYIRNVTFED AGEYTCLAGNSIGISFHSAWLTVLPAPGREKEITASPDYLESTGTHTCPPCPAPELLGGPSVF LFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVS VLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLTC LVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHE ALHNHYTQKSLSLSPGK

M.W. :
Calculated molecular mass (kDa): 65.1; Estimated by SDS-PAGE under reducing condition (kDa): 85-95

Calculated PI :
5.78

Calculated Extinction Coefficients :
(M-1 cm-1, at 280nm): 98500

Endotoxin Level :
>95% judged by SDS-PAGE under reducing condition (see the gel image above, labeled as DTT “+”)

Formulation :
Supplied at 0.5 mg/ml in sterile PBSpH7.4 (carrier free). The purified recombinant protein was labeled with Biotin (3-5 Biotin per molecule) using the standard procedure.

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 0.15 – 0.35 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 :
FGFR2; CD332; FGFR-2; BEK; JWS; BBDS; CEK3; CFD1; ECT1; KGFR; TK14; TK25; BFR-1; K-SAM; KSAM

Research Area :
Development

Pathway/Disease :
FGF/FGFR Signaling Pathway

Species :
Human

CD Antigen :
CD332

References :
1. Science 251:72 (1991). 2. Proc. Natl. Acad. Sci. 89:3305 (1992). 3. J. Biol. Chem. 271:15292 (1996). 4. Nature. 407 (6807): 1029-34 (2000). 5. Cytokine Growth Factor Rev. 16:107 (2005).

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