Recombinant Human FGF R3 (C-6His)

Description

EnkiLife provides the Recombinant Human FGF R3 (C-6His) protein,aslo know as Fibroblast growth factor receptor 3,FGFR-3,CD333,FGFR3,JTK4,IIIc, which features high purity, high activity, and high stability. It can be applied in scientific research, biopharmaceuticals, and other fields.Purity:Greater than 95% as determined by reducing SDS-PAGE;Endotoxin Level:<1 EU/µg as determined by LAL test.;Construction:Recombinant Human Fibroblast Growth Factor Receptor 3 is produced by our Mammalian expression system and the target gene encoding Glu23-Gly375 is expressed with a 6His tag at the C-terminus.Accession:P22607. Expression Host:Human Cells.Species:Human.Predicted Molecular Mass:39 KDa. Background:Fibroblast growth factors (FGFs) comprise a family of at least eighteen structurally related proteins that are involved in a multitude of physiological and pathological cellular processes, including cell growth, differentiation, angiogenesis, wound healing and tumorgenesis. 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. Four distinct genes encoding closely related FGF receptors, FGF R1-4, are known. All four genes for FGF Rs encode proteins with an N-terminal signal peptide, three immunoglobulin (Ig)-like domains, an acid-box region containing a run of acidic residues between the IgI and IgII domains, a transmembrane domain and the split tyrosine-kinase domain. Multiple forms of FGF R1-3 are generated by alternative splicing of the mRNAs. A frequent splicing event involving FGF R1 and 2 results in receptors containing all three Ig domains, referred to as the α isoform, or only IgII and IgIII, referred to as the β isoform. Only the α isoform has been identified for FGF R3 and FGF R4. Additional splicing events for FGF R1-3, 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). The complex patterns of expression of these receptors as well as the specificity of their interactions with the various FGF ligand family members are under investigation.