Recombinant Human FGFR3 (IIIc) Fc Avi-tag Protein, CF

Measured by its binding ability in a functional ELISA. Biotinylated Recombinant Human FGFR3 Fc Chimera Avi-tag Protein (Catalog # AVI766) binds to Recombinant Human FGF acidic/FGF1 (aa 16-155) Protein (232-FA) with a ED50 of 0.250-2.50 µg/mL

2 μg/lane of Biotinylated Recombinant Human FGFR3 Fc Chimera Avi-tag Protein (Catalog # AVI766) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 94-104 kDa and 190-210 kDa, respectively.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human FGFR3 (IIIc) Fc Avi-tag Protein, CF Summary

• Additional Information: Biotinylated Fc Chimera
• Details of Functionality: Measured by its binding ability in a functional ELISA. Biotinylated Recombinant Human FGFR3 Fc Chimera Avi-tag (Catalog # AVI766) binds to Recombinant Human FGF acidic/FGF1 (aa16-155) Protein (Catalog # 232-FA) with a ED 50 of 0.250-2.50 µg/mL
• Source: Human embryonic kidney cell, HEK293-derived human FGFR3 protein

  Human FGFR3 (IIIc) (Glu23-Gly375) Accession # P22607.1

  IEGRMD

  Human IgG 1 (Pro100-Lys330)

  Avi-tag

  N-terminus

  C-terminus

• Accession #: P22607.1
• N-terminal Sequence: Glu23
• Structure / Form: Disulfide-linked homodimer
  Biotinylated via Avi-tag
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 67 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
• SDS-PAGE: 94-104 kDa, under reducing conditions.

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  12 months from date of receipt, -20 to -70 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after reconstitution. 3 months, -20 to -70 degreesC under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
• Reconstitution Instructions: Reconstitute at 500 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human FGFR3 (IIIc) Fc Avi-tag Protein, CF

• CD333
• CEK
• EC 2.7.10
• FGF R3
• FGFR3
• fibroblast growth factor receptor 3
• HSFGFR3EX
• JTK4
• JTK4thanatophoric dwarfism

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 alpha isoform, or only IgII and IgIII, referred to as the beta isoform. Only the alpha 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). A 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 FGF R1. Mutations in FGF R1-3 have been found in patients with birth defects involving craniosynostosis. 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. Our Avi-tag Biotinylated human FGFR3 Fc Chimera features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.

1. Galzie, Z. et al. (1997) Biochem. Cell Biol. 75:669.
2. Burke, D. et al. (1998) Trends Biochem. Sci. 23:59.

Bioinformatics

• Uniprot:
  • P22607.1()