Recombinant Human R-Spondin 1 Biotinylated Protein, CF Summary
Additional Information |
Biotinylated |
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Human Lgr5/GPR49 Fc Chimera (Catalog #
8078-GP) is immobilized at 2 µg/mL (100 µL/well), Biotinylated Recombinant Human R-Spondin
1 (Catalog # BT4645B) binds with an ED 50 of 4.50-54.0 ng/mL. |
Source |
Chinese Hamster Ovary cell line, CHO-derived human R-Spondin 1 protein Ser21-Ala263 |
Accession # |
|
N-terminal Sequence |
Ser21 & Arg31 |
Structure / Form |
Biotinylated via amines |
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 |
|
Theoretical MW |
25.6 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 |
29-42 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 250 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 1 Biotinylated Protein, CF
Background
R-Spondin 1 (RSPO1), also known as Cristin 3, is a 27 kDa secreted protein in the R-Spondin family of Wnt/ beta -catenin signaling regulators (1). These proteins contain two adjacent cysteine-rich furin-like domains followed by a thrombospondin (TSP-1) motif and a region rich in basic residues. Mature human R-Spondin 1 shares 87% amino acid sequence identity with mouse and rat R-Spondin 1 (2). Alternative splicing generates additional isoforms that have a substituted N-terminus or lack the TSP-1 domain. R-Spondin 1 enhances canonical Wnt/ beta -catenin signaling by competing with the Wnt antagonist Dkk-1, binding to Frizzled-8, Kremen, LRP-6, Lgr4, Lgr5, and Lgr6, and enhancing cell surface availability of Wnt receptors (3-11). R-Spondin 1 functions in dorsal neural tube development (12) as well as male and female germ cell development (7, 10, 13). It also induces bone formation (6), intestinal crypt cell proliferation (14), angiogenesis (7, 15), and insulin secretion from pancreatic beta cells (11). Interest in R-Spondin 1 as a cell culture supplement
has grown with the expansion of the organoid field. R-Spondin 1 is widely used
in organoid cell culture workflows as a vital component that promotes both
growth and survival of 3D organoids (16). Over the last several
years, the understanding of the regulatory mechanisms and functional roles of
RSPOs in many biological contexts has increased. Particularly, because a
leucine-rich repeat containing G protein-coupled receptor 5 (LGR5), a stem cell
marker originally identified as a marker for intestinal stem cells, and two
closely related proteins, LGR4 and LGR6, were identified as cognate receptors
for RSPOs, significant research progress has been made in understanding the
functional roles of RSPO/LGR signaling in stem cell biology (17).
- Jin, Y.R. and J.K. Yoon (2012) Int. J. Biochem. Cell Biol. 44:2278.
- Chen, J-Z. et al. (2002) Mol. Biol. Rep. 29:287.
- 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.
- Kronke, G. et al. (2010) Arthritis Rheum. 62:2303.
- Caruso, M. et al. (2015) PLoS One 10:e0124213.
- Hao, H.-X. et al. (2012) Nature 485:195.
- de Lau, W. et al. (2011) Nature 476:293.
- Chassot, A.-A. et al. (2011) PLoS One 6:e25641.
- Wong, V.S.C et al. (2010) J. Biol. Chem. 285:21292.
- Kamata, T. et al. (2004) Biochim. Biophys. Acta 1676:51.
- Chassost, A.-A. et al. (2012) Development 139:4461.
- Kim, K.-A. et al. (2005) Science 309:1256.
- Gore, A.V. et al. (2011) Development 138:4875.
- Drost and Clevers. (2018) Nature Reviews Cancer 18:407.
- Raslan,
H. et al. (2019) J. Biochem. Biocell. 106:26-34.
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