Recombinant Human SOST/Sclerostin Protein, CF Summary
Details of Functionality
Measured by its ability to inhibit Wnt-3a-induced alkaline phosphatase production by MC3T3‑E1 mouse preosteoblast cells. The ED50 for this effect is 1.5-6 μg/mL in the presence of 3 ng/mL Recombinant Mouse Wnt‑3a (Catalog # 1324-WN).
Source
Mouse myeloma cell line, NS0-derived human SOST/Sclerostin protein Gln24-Tyr213, with an N-terminal 7-His tag
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
22.5 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
28-32 kDa, reducing conditions
Publications
Read Publications using 1406-ST/CF 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 PBS.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 200 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 SOST/Sclerostin Protein, CF
sclerostin
SOST
VBCHsclerosteosis
Background
SOST, also known as sclerostin, is a member of the cerberus/DAN family, a group of secreted glycoproteins characterized by a cysteine-knot motif. Cerberus/DAN family members are putative BMP antagonists, and include Dan, Cerberus, Gremlin, PRDC, and Caronte. While the overall sequence identity between members of the family is low, they have conserved spacing of six cysteine residues. Cerberus and dan have an additional cysteine residue used for dimerization; however, SOST does not and is secreted as a monomer. SOST was originally identified as an important regulator of bone homesotasis. Positional cloning studies identified that mutations in the SOST gene can cause sclerosteosis and van Buchem disease, bone dysplasia disorders characterized by progressive skeletal overgrowth. Significant levels of SOST expression are detected in bone, cartilage, kidney, and liver. SOST is expressed by osteoclasts in developing bones of mouse embryos, including both intramembranously forming skull bones and endochondrally forming long bones. SOST plays a physiological role as a negative regulator of bone formation by repressing BMP-induced osteogenesis. SOST has been shown to have unique ligand specificity, binding BMP-5, -6, and -7 with high affinity and BMP-2 and -4 with low affinity. This seems to be the first example of a BMP antagonist being localized to osteoclasts, cells derived from the hematopoietic lineage, that function to degrade bone matrix. Recombinant human SOST preparations from R&D Systems bind BMP-5 and BMP-6 in a functional ELISA. Human and mouse SOST share 88% amino acid identity (1-3).
Kusu, N. et al. (2003) J. Biol. Chem. 278:24113.
Balemans, W. et al. (2001) Hum. Mol. Genet. 10:537.
Brunkow, M.E. et al. (2001) Am. J. Hum. Genet. 68:577.
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