Recombinant Human R-Spondin 3 Fc Chimera Protein, CF New
Recombinant Human R-Spondin 3 Fc Chimera Protein, CF Summary
Product Specifications
| Human RSPO3 (Met33-Gly209) Accession # Q9BXY4.1 | IEGRMD | Human IgG1 (Pro100-Lys330) |
| N-terminus | C-terminus | |
Analysis
Product Datasheets
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.
11506-RS
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
| Reconstitution | Reconstitute the 20 μg size at 200 μg/mL in PBS. Reconstitute all other sizes at 500 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.
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Scientific Data
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Recombinant Human R-Spondin 3 Fc Chimera Protein (Catalog # 11506-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 effect is 0.500‑10.0 ng/mL.
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2 μg/lane of Recombinant Human R‑Spondin 3 Fc Chimera Protein (Catalog # 11506-RS) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 53-69 kDa and 110-140 kDa, respectively.
Reconstitution Calculator
Background: R-Spondin 3
R-Spondin 3 (RSPO3, roof plate-specific spondin 3), also called cysteine-rich and single thrombospondin domain containing-1 (Cristin 1), is a 31-kDa secreted protein that shares ~40% amino acid (aa) identity with the other three R-Spondin family members (1, 2). All are positive modulators of Wnt/ beta-catenin signaling, but has a distinct expression pattern (1-4). Like other R-spondins, R-Spondin 3 contains two adjacent cysteine-rich furin-like domains (aa 35-135) with one potential N-glycosylation site (aa 36), followed by a thrombospondin (TSP-1) motif (aa 147-207) and a region rich in basic residues (aa 211-269). Only the furin-like domains are needed for beta-catenin stabilization (2). Within aa 21-209, human R-Spondin 3 shares 93%, 92%, 97%, 96% and 92% aa identity with mouse, rat, equine, bovine and canine R-Spondin 3, respectively. Potential isoforms of 279 and 297 aa diverge at aa 210 and 276, respectively (5). Mouse R-Spondin 3 is critical for development of the placental labyrinthine layer, probably by promoting VEGF expression and thus vascular development (6, 7). It is also essential for expression of the placenta-specific transcription factor, Gcm1. In the mouse embryo, R-Spondin 3 is often expressed by or located near endothelial cells (6). It is found in the roof plate, tail, somites, otic vesicles, cephalic mesoderm, truncus arteriosus, atrioventricular canal of the developing heart, and strongly but transiently in developing limbs (4, 7). R‑Spondins regulate Wnt/ beta-catenin by competing with the Wnt antagonist DKK-1 for binding to the Wnt co-receptors LRP-6 and Kremen, reducing their DKK‑1‑mediated internalization (8, 9). Reports differ on whether R‑Spondins bind LRP-6 directly (8‑10). R‑Spondin 3 has also been identified as an oncogene (11).
- Chen, J-Z. et al. (2002) Mol. Biol. Rep. 29:287.
- Kim, K.-A. et al. (2008) Mol. Biol. Cell 19:2588.
- Hendrickx, M. and L. Leyns (2008) Develop. Growth Differ. 50:229.
- Nam, J.-S. et al. (2007) Gene Expr. Patterns 7:306.
- Entrez Accession # EAW48114 and EAW48116.
- Kazanskaya, O. et al. (2008) Development 135:3655.
- Aoki, M. et al. (2007) Dev. Biol. 301:218.
- Binnerts, M.E. et al. (2007) Proc. Natl. Acad. Sci. USA 104:14700.
- Nam, J.-S. et al. (2006) J. Biol. Chem. 281:13247.
- Wei, Q. et al. (2007) J. Biol. Chem. 282:15903.
- Theodorou, V. et al. (2007) Nat. Genet. 6:759.
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