Recombinant Human SOST/Sclerostin His-tag 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 1.50-6.00 μg/mL. |
Source |
Chinese Hamster Ovary cell line, CHO-derived human SOST/Sclerostin protein Gln24-Tyr213, with a N-terminal 7-His tag |
Accession # |
|
N-terminal Sequence |
His of Tag |
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 |
22 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 |
25-35 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. |
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 SOST/Sclerostin His-tag Protein, CF
Background
Sclerostin (SOST) is a member of the Cerberus/differential
screening-selected gene in neuroblastoma (DAN) family, a group of secreted
glycoproteins characterized by a cysteine-knot motif. The Cerberus/DAN family
consists of multiple members originally identified as putative BMP antagonists
including Dan, SOST, Cerberus, Gremlin, USAG-1, PRDC, and Coco (1, 2). While the
overall sequence identity between family members is low, they have conserved
spacing of six cysteine residues in the C-terminus which form the structurally
conserved cysteine-knot motif. Cerberus and Dan have an additional cysteine
residue used for dimerization; however, SOST does not and is secreted as a
monomer (1). Mature human SOST shares 90% amino acid sequence identity with
mouse and rat SOST. SOST appears to be the first example of a BMP antagonist predominately
localized to osteoclasts and functions as an important regulator of bone homeostasis
by inhibiting bone mineralization (3). SOST has been shown to have unique
ligand specificity by binding directly to BMP-5, -6, and -7 with high affinity
and BMP-2 and -4 with low affinity thereby repressing BMP-induced osteogenesis
(4). Mutations in the SOST gene can
cause several bone dysplasia disorders characterized by progressive skeletal
overgrowth including sclerosteosis and van Buchem disease (5). Additionally, SOST
has been shown to be a strong Wnt antagonist by directly binding the Wnt
co‑receptors LRP5 and LRP6 (6).
- Nolan, K. and Thompson, T.B. (2014) Protein Sci. 23:999.
- Balemans, W. et al. (2001) Hum. Mol. Genet. 10:537.
- van Bezooijen, R.L. et al. (2004) J. Exp. Med. 199:805.
- Kusu, N. et al. (2003) J. Biol. Chem. 278:24113.
- Brunkow, M.E. et al. (2001) Am. J. Hum. Genet. 68:577.
- Kim, J. et al. (2020) Nat Commun 11:5357.
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