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Recombinant Human R-Spondin 2 Fc Chimera Protein, CF

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Recombinant Human R-Spondin 2 Fc Chimera Protein (Catalog # 11427-RS) activates TCF reporter activity in HEK293 human embryonic kidney cells in the presence of Recombinant Human Wnt-3a (5036-WN). The ED50 for this ...read more
2 μg/lane of Recombinant Human R‑Spondin 2 Fc Chimera Protein (Catalog # 11427-RS) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human R-Spondin 2 Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its ability to activate TCF reporter activity in HEK293 human embryonic kidney cells in the presence of Recombinant Human Wnt-3a (Catalog # 5036-WN). The ED50 for this effect is 0.400-4.80 ng/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human R-Spondin 2 protein
Human R-Spondin 2
(Ala32-Gly205)
Accession # Q6UXX9.2
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminusC-terminus
Accession #
N-terminal Sequence
Ala32
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
47 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
53-60 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 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 R-Spondin 2 Fc Chimera Protein, CF

  • Cristin 2
  • CRISTIN2
  • hRspo2
  • MGC35555
  • MGC43342
  • Roof plate-specific spondin-2
  • RSPO2
  • R-spondin 2 homolog (Xenopus laevis)
  • RSpondin 2
  • R-Spondin 2
  • R-spondin-2

Background

Roof plate-specific Spondin 2 isoform 1 (R‑Spondin 2, RSPO2), also known as cysteine‑rich and single thrombospondin domain containing protein 2 (Cristin 2), is a 33 kDa secreted protein that belongs to the R-Spondin family (1‑3). The four R‑Spondins regulate Wnt/ beta -catenin signaling and overlap in expression and function (1‑3). Like other R‑Spondins, RSPO2 contains two adjacent cysteine‑rich furin-like domains (aa 90‑134) followed by a thrombospondin (TSP-1) motif (aa 144‑204) and a C-terminal region rich in basic residues (aa 207‑243). The basic region binds heparin and mediates cell surface retention and extracellular matrix attachment while the furin‑like domains are required for Wnt/ beta -catenin signaling (1, 3, 4). RSPO2 contains one potential N‑glycosylation site. Mature human RSPO2 shares 97‑98% aa identity with mouse, rat, equine, canine and bovine RSPO2 and ~40% aa identity with RSPO1, RSPO3 and RSPO4. Of the three reported splice isoforms of human R‑Spondin 2, isoform 2 lacks residues 1‑67 of isoform 1, while isoform 3 has a glycine substitution for residues 32‑95 of isoform 1 (5). Human RSPO2 is expressed in organs of endodermal origin in adults, including intestine and lung, and is down‑regulated in tumors of these tissues (1). In the embryonic mouse, RSPO2 expression is concentrated in the apical epidermal ridge, hippocampus, and developing muscle, teeth and bones (1, 6). Deletion of RSPO2 results in down‑regulation of Wnt activity in these areas, malformations of the facial skeleton and limbs, and respiratory failure at birth (7‑9). RSPO2 is an extracellular potentiator of Wnt/ beta -catenin signaling (3, 4). It functions at least in part by binding LRP‑6, stimulating its long-term phosphorylation and down‑regulating its internalization (3, 4). RSPO proteins, especially RSPO2 and RSPO3, also antagonize DKK1 activity by interfering with DKK1‑mediated LRP‑6 and Kremen association (10).
  1. Kazanskaya, O. et al. (2004) Dev. Cell 7:525.
  2. Kim, K.-A. et al. (2006) Cell Cycle 5:23.
  3. Nam, J.-S. et al. (2006) J. Biol. Chem. 281:13247.
  4. Li, S-J. et al. (2009) Cell Signal. 21:916.
  5. Swiss-Prot Accession # Q6UXX9.
  6. Nam, J.-S. et al. (2007) Gene Expr. Patterns 7:306.
  7. Yamada, W. et al. (2009) Biochem. Biophys. Res. Commun. 381:453.
  8. Jin, Y.-R. et al. (2011) Dev. Biol. 352:1.
  9. Nam, J.-S. et al. (2007) Dev. Biol. 311:124.
  10. Kim, K.-A. et al. (2007) Mol. Biol. Cell 19:2588.

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