Recombinant Mouse Frizzled-10 Fc Chimera Protein, CF

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Recombinant Mouse Frizzled-10 Fc Chimera (Catalog # 9247-FZ) binds to Biotinylated Recombinant MouseWnt-3a in an ELISA Binding Assay. When Biotinylated Recombinant Mouse Wnt-3a is coated on a streptavidin coated ELISA ...read more

Product Details

Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Mouse Frizzled-10 Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its ability to bind biotinylated recombinant mouse Wnt-3a in a functional ELISA with an ED50 of 10-60 ng/mL.
Source
Mouse myeloma cell line, NS0-derived mouse Frizzled-10 protein
Mouse Frizzled-10
(Ile22-Phe166)
Accession # Q8BKG4
IEGRMDP Mouse IgG2a
(Glu98-Lys330)
N-terminusC-terminus
Accession #
N-terminal Sequence
Ile22
Structure / Form
Disulfide-linked homodimer
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
44 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
53-61 kDa, 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 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 200 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 Mouse Frizzled-10 Fc Chimera Protein, CF

  • CD350 antigen
  • CD350
  • frizzled (Drosophila) homolog 10
  • frizzled homolog 10 (Drosophila)
  • Frizzled10
  • Frizzled-10
  • Fz10
  • Fz-10
  • FZD10
  • FzE7
  • hFz10

Background

Frizzled-10, also known as CD350, is a 68 kDa seven pass transmembrane glycoprotein in the frizzled family of Wnt receptors (1, 2). The N-terminal extracellular region of Frizzled-10 contains a cysteine-rich domain that comprises the Wnt binding domain and mediates receptor oligomerization (3-5). The C-terminal cytoplasmic tail contains a PDZ-interaction motif (3). Within the cysteine-rich domain, human Frizzled-10 shares 94% and 99% aa sequence identity with human and rat Frizzled-10, respectively. Frizzled-10 is expressed during embryogenesis in the primitive streak, dorsal neural tube, developing brain, limb bud, and airway epithelium (6-12). It is induced by Shh and colocalizes with Shh and Wnt-7a in the neural tube (13, 14). In the adult, Frizzled-10 is expressed in placenta, gastric glands, and colon and renal tubule epithelial cells (4). Frizzled-10 associates with LRP5 and transduces Wnt-1, -7a, -7b, and -8 signals, resulting in the stabilization of cytoplasmic beta-Catenin (11, 12, 14). It is important for the differentiation of sensory neurons (12). Frizzled-10 is also up-regulated in some cancers and transformed cell lines (4, 15). It binds hypoxia inducible gene 2, which promotes oncogenic Wnt signaling and functions as an autocrine growth factor for renal cell carcinomas (16).
  1. Kikuchi, A. et al. (2007) Cell. Signal. 19:659.
  2. Wang, H. et al. (2006) Cell. Signal. 18:934.
  3. Koike, J. et al. (1999) Biochem. Biophys. Res. Commun. 262:39.
  4. Nagayama, S. et al. (2005) Oncogene 24:6201.
  5. Dann, C.E. et al. (2001) Nature 412:86.
  6. Kemp, C.R. et al. (2007) Dev. Dyn. 236:2011.
  7. Kawakami, Y. et al. (2000) Mech. Dev. 91:375.
  8. Nasevicius, A. et al. (2000) Mech. Dev. 92:311.
  9. Moriwaki, J. et al. (2000) Biochem. Biophys. Res. Commun. 278:377.
  10. Stark, M.R. et al. (2000) Mech. Dev. 93:195.
  11. Wang, Z. et al. (2005) Mol. Cell. Biol. 25:5022.
  12. Garcia-Morales, C. et al. (2009) Dev. Biol. 335:143.
  13. Nunnally, A.P. and B.A. Parr (2004) Dev. Genes Evol. 214:144.
  14. Kawakami, Y. et al. (2000) Dev. Growth Differ. 42:561.
  15. Saitoh, T. et al. (2002) Int. J. Oncol. 20:117.
  16. Togashi, A. et al. (2005) Cancer Res. 65:4817.

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