Measured by its ability to inhibit proliferation of HeLa human cervical epithelial carcinoma cells. Ko, L. et al. (2002) Exp. Cell Res. 280:280. The ED50 for this effect is 0.15‑0.75 µg/mL.
Source
Mouse myeloma cell line, NS0-derived human sFRP-1 protein Ser32-Lys314
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
32.6 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
33-40 kDa, reducing conditions
Publications
Read Publications using 5396-SF in the following applications:
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 Phosphate and NaCl.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 250 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human sFRP-1 Protein, CF
FRP1
FRP-1FrzA
FRPSARP-2
FrzA
SARP-2
SARP2sFRP-1
Secreted apoptosis-related protein 2
secreted frizzled-related protein 1
sFRP1
sFRP-1
Background
Secreted Frizzled Related Protein-1 (sFRP-1), also known as SARP-2, FRP, and FrzA, belongs to a family of Wnt-binding proteins with homology to the ligand-binding domain of the Frizzled transmembrane Wnt receptors. The sFRP proteins are approximately 30-35 kDa in size and contain an N-terminal Frizzled-like domain with 10 conserved cysteines and a Netrin-like C-terminal domain (1-3). Mature human sFRP-1 shares 97% and 96% amino acid sequence identity with mouse and rat sFRP-1, respectively. It binds to Wnt-1, -2, -3a, and -4 and prevents their activation of canonical beta-catenin signaling (4-7). sFRP-1 is up-regulated in the ischemic heart where it limits inflammation and the severity of tissue damage following myocardial infarction (8-10). During angiogenesis it induces endothelial cell migration, tube formation, and vessel formation (11). sFRP-1 is expressed by bone marrow stromal cells and osteoclasts (12). It binds to TRANCE/RANK Ligand, inhibits osteoclast and osteoblast formation and survival, and inhibits the formation of trabecular bone (13, 14). sFRP-1 additionally restricts kidney tubule formation (7), the inflammatory activation of leukocytes (10), early B lymphoid progression (12), and vitreous fluid outflow in the eye (15).
Cruciat, C.M. and C. Niehrs (2013) Cold Spring Harb. Perspect. Biol. 5:e015081.
van Amerongen, R. and R. Nusse (2009) Development 136:3205.
Finch, P.W. et al. (1997) Proc. Natl. Acad. Sci. USA 94:6770.
Bafico, A. et al. (1999) J. Biol. Chem. 274:16180.
Dennis, S. et al. (1999) J. Cell Sci. 112:3815.
Wawrzak, D. et al. (2007) Biochem. Biophys. Res. Commun. 357:1119.
Yoshino, K. et al. (2001) Mech. Dev. 102:45.
Barandon, L. et al. (2002) Circulation 108:2282.
Sklepkiewicz, P. et al. (2015) Circ. Heart Fail. 8:362.
Barandon, L. et al. (2011) Arterioscler. Thromb. Vasc. Biol. 31:e80.
Dufourcq, P. et al. (2002) Circ. Res. 106:3097.
Yokota, T. et al. (2008) J. Immunol. 181:6061.
Hausler, K.D. et al. (2004) J. Bone Miner. Res. 19:1873.
Bodine, P.V.N. et al. (2004) Mol. Endocrinol. 18:1222.
Wang, W.-H. et al. (2008) J. Clin. Invest. 118:1056.
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