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 ED 50 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-terminus | | C-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 |
|
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
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).
-
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.
- Swiss-Prot Accession # Q6UXX9.
- 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.
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