FGFR1 Human, (22-285)
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| Amount : | 10 µg |
| Purification : | Greater than 90.0% as determined by SDS-PAGE. |
| Content : | The FGFR1 solution (0.25mg/1ml) contains phosphate buffered Saline (pH7.4), and 10% glycerol. |
| Storage condition : | Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles. |
| AA sequence : | RPSPTLPEQD ALPSSEDDDD DDDSSSEEKE TDNTKPNPVA PYWTSPEKME KKLHAVPAAK TVKFKCPSSG TPNPTLRWLK NGKEFKPDHRIGGYKVRYAT WSIIMDSVVP SDKGNYTCIV ENEYGSINHT YQLDVVERSP HRPILQAGLP ANKTVALGSN VEFMCKVYSD PQPHIQWLKH IEVNGSKIGP DNLPYVQILK TAGVNTTDKE MEVLHLRNVS FEDAGEYTCL AGNSIGLSHH SAWLTVLEAL EERPAVMTSP LYLELEHHHH HH. |
| Alternative Name : | FGFR-1, bFGF-R, C-FGR, CD331, fms-related tyrosine kinase 2, Pfeiffer syndrome, CEK, FLG, FLT2, KAL2, BFGFR, FGFBR, HBGFR, FGFR1/FGFR1OP2 FUSION GENE, FGFR1/ZNF198 FUSION GENE, FLG FGFR1/BCR FUSION GENE, FLG protein, FMS-LIKE GENE, N-sam tyrosine kinase, basic fibroblast growth factor receptor 1. |
Source: Sf9, Baculovirus cells.Â
Sterile Filtered colorless solution.
Fibroblast Growth Factors (FGFs) comprise a family of at least 18 structurally related proteins that are involved in a multitude of physiological and pathological cellular processes, including cell growth, differentiation, angiogenesis, wound healing and tumorigenesis. The biological activities of the FGFs are mediated by a family of type I transmembrane tyrosine kinases which undergo dimerization and autophosphorylation after ligand binding. Multiple forms of FGFR-1 to -3 are generated by alternative splicing of the mRNAs. A frequent splicing event involving FGFR-1 and -2 results in receptors containing all three Ig domains, referred to as the alpha isoform, or only IgII and IgIII, referred to as the isoform. Only the alpha isoform has been identified for FGFR-3 and FGFR-4. Additional splicing events for FGFR-1 to -3, involving the C-terminal half of the IgIII domain encoded by two mutually exclusive alternative exons, generate FGF receptors with alternative IgIII domains (IIIb and IIIc). An IIIa isoform which is a secreted FGF binding protein containing only the N-terminal half of the IgIII domain plus some intron sequences has also been reported for FGFR-1. Mutations in FGFR-1 to -3 have been found in patients with birth defects involving craniosynostosis.
FGFR1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 272 amino acids (22-285) and having a molecular mass of 30.4kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). FGFR1 is fused to a 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Sterile Filtered colorless solution.
Fibroblast Growth Factors (FGFs) comprise a family of at least 18 structurally related proteins that are involved in a multitude of physiological and pathological cellular processes, including cell growth, differentiation, angiogenesis, wound healing and tumorigenesis. The biological activities of the FGFs are mediated by a family of type I transmembrane tyrosine kinases which undergo dimerization and autophosphorylation after ligand binding. Multiple forms of FGFR-1 to -3 are generated by alternative splicing of the mRNAs. A frequent splicing event involving FGFR-1 and -2 results in receptors containing all three Ig domains, referred to as the alpha isoform, or only IgII and IgIII, referred to as the isoform. Only the alpha isoform has been identified for FGFR-3 and FGFR-4. Additional splicing events for FGFR-1 to -3, involving the C-terminal half of the IgIII domain encoded by two mutually exclusive alternative exons, generate FGF receptors with alternative IgIII domains (IIIb and IIIc). An IIIa isoform which is a secreted FGF binding protein containing only the N-terminal half of the IgIII domain plus some intron sequences has also been reported for FGFR-1. Mutations in FGFR-1 to -3 have been found in patients with birth defects involving craniosynostosis.
FGFR1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 272 amino acids (22-285) and having a molecular mass of 30.4kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). FGFR1 is fused to a 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
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