Recombinant Mouse Wnt-3/sFRP-1 Complex Protein, CF

Recombinant Mouse Wnt-3/sFRP-1 Complex (Catalog # 11200-WN) activates Wnt induced TCF reporter activity in HEK293 human embryonic kidney cells. The ED50 for this effect is 7.00-63.0 ng/mL.

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

Recombinant Mouse Wnt-3/sFRP-1 Complex Protein, CF Summary

• Details of Functionality: Measured by its ability to activate Wnt induced TCF reporter activity in HEK293 human embryonic kidney cells. The ED₅₀ for this effect is 7.00-63.0 ng/mL.
• Source: Chinese Hamster Ovary cell line, CHO-derived mouse Wnt-3 protein
  

  Mouse Wnt-3 (Gly22-Lys355) Accession # P17553.1

  Mouse sFRP-1 (Ser32-Lys314) Accession # Q8C4U3.3
  N-terminus	C-terminus

• Accession #: P17553.1, Q8C4U3.3
• N-terminal Sequence: Gly22 (Wnt-3) & Ser32 (sFRP-1)
• Structure / Form: Non-covalent complex
• Protein/Peptide Type: Recombinant Proteins
• Purity: >90%, 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: 37 kDa (Wnt-3) & 33 kDa (sFRP-1).
  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: 36-45 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 °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 MOPS and NaCl with Trehalose.
• Purity: >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 100 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 Wnt-3/sFRP-1 Complex Protein, CF

• INT4
• INT4Proto-oncogene Int-4 homolog
• MGC131950
• MGC138321
• MGC138323
• proto-oncogene Wnt-3
• TETAMS
• wingless-type MMTV integration site family, member 3
• WNT-3 proto-oncogene protein
• WNT3
• Wnt-3

Background

Wnt-3 is one of 19 vertebrate members of the Wingless-type MMTV integration site (Wnt) family of highly conserved cysteine-rich secreted glycoproteins that are important for normal developmental processes (1). Mouse Wnt-3 shares 99% and 100% amino acid (aa) identity with human and rat Wnt-3, respectively. It also shares 87% aa identity with mouse Wnt3a. Wnts bind to the cell surface Frizzled family receptors in conjunction with low-density lipoprotein receptor-related protein family receptors (LRP5 or 6) resulting in the stabilization of intracellular beta -catenin levels (4). As intracellular beta -catenin levels rise, it binds to TCF/LEF transcription factors, leading to expression of Wnt target genes (5). Wnts are known to bind to sFRPs, a family of secreted molecules that contain an N-terminal cysteine-rich domain (CRD) highly similar to the CRDs of the Frizzled family receptors (6,7). More than one molecule of sFRP is suggested to participate in the interaction with each Wnt molecule (7). Both sFRP-1 and sFRP-2 can inhibit Wnt-3a activity while sFRP-3 cannot (8). R&D Systems produces biologically active mouse Wnt-3 protein in a complex with mouse sFRP-1, and this Wnt-3/sFRP-1 complex is stable in the physiological buffer without detergent.

1. Willert, K. and R. Nusse (2012) Cold Spring Harb. Perspect. Biol. 4:a007864.
2. Van Ooyen, A. et al. (1985) EMBO J. 4:2905.
3. Burrus, L.W. and A.P. McMahon (1995) Exp. Cell Res. 220:363.
4. MacDonald, B.T. and X. He (2012) Cold Spring Harb. Perspect. Biol. 4:a007880.
5. Korinek, V. et al. (1997) Science 275:1784.
6. Dennis, S. et al. (1999) J. Cell Sci. 112:3815.
7. Bafico, A. et al. (1999) J. Biol. Chem. 274:16180.
8. Galli, L.M. et al. (2006) Dev. Dyn. 235:681.

Bioinformatics

• Uniprot:
  • P17553.1, Q8C4U3.3()