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Recombinant Mouse R-Spondin 2 Protein (25 ug)
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咨询Recombinant Mouse R-Spondin 2 Protein Summary
- R&D Systems CHO-derived Recombinant Mouse R-Spondin 2 Protein (6946-RS)
- Quality control testing to verify active proteins with lot specific assays by in-house scientists
- All R&D Systems proteins are covered with a 100% guarantee
Product Specifications
Met1-Gly205
Analysis
Product Datasheets
6946-RS (with carrier)
6946-RS/CF (carrier free)
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
6946-RS
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein. |
| Reconstitution | Reconstitute at 100 μg/mL in PBS containing at least 0.1% human or bovine serum albumin. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
6946-RS/CF
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
| Reconstitution | Reconstitute at 100 μg/mL in PBS. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Reconstitution Calculator
Background: R-Spondin 2
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 mouse RSPO2 shares 97‑98% aa identity with human, rat, equine, canine and bovine RSPO2 and ~40% aa identity with RSPO1, RSPO3 and RSPO4. One potential 237 aa mouse isoform diverges after aa 206 and lacks a basic region (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).
- Kazanskaya, O. et al. (2004) Dev. Cell 7:525.
- Kim, K.-A. et al. (2006) Cell Cycle 5:23.
- Nam, J.-S. et al. (2006) J. Biol. Chem. 281:13247.
- Li, S-J. et al. (2009) Cell Signal. 21:916.
- Entrez accession # EDL08755.
- Nam, J.-S. et al. (2007) Gene Expr. Patterns 7:306.
- Yamada, W. et al. (2009) Biochem. Biophys. Res. Commun. 381:453.
- Jin, Y.-R. et al. (2011) Dev. Biol. 352:1.
- Nam, J.-S. et al. (2007) Dev. Biol. 311:124.
- Kim, K.-A. et al. (2007) Mol. Biol. Cell 19:2588.
Background: R-Spondin 2
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 mouse RSPO2 shares 97‑98% aa identity with human, rat, equine, canine and bovine RSPO2 and ~40% aa identity with RSPO1, RSPO3 and RSPO4. One potential 237 aa mouse isoform diverges after aa 206 and lacks a basic region (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).
- Kazanskaya, O. et al. (2004) Dev. Cell 7:525.
- Kim, K.-A. et al. (2006) Cell Cycle 5:23.
- Nam, J.-S. et al. (2006) J. Biol. Chem. 281:13247.
- Li, S-J. et al. (2009) Cell Signal. 21:916.
- Entrez accession # EDL08755.
- Nam, J.-S. et al. (2007) Gene Expr. Patterns 7:306.
- Yamada, W. et al. (2009) Biochem. Biophys. Res. Commun. 381:453.
- Jin, Y.-R. et al. (2011) Dev. Biol. 352:1.
- Nam, J.-S. et al. (2007) Dev. Biol. 311:124.
- Kim, K.-A. et al. (2007) Mol. Biol. Cell 19:2588.