Sclerostin (SOST) 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 homeostasis. 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.
| 説明 |
Sclerostin (SOST) 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 homeostasis. 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. |
| Species |
Mouse
|
| Expression Host |
HEK293 Cells
|
| Tag |
C-6xHis
|
| Accession Number |
Q99P68
|
| 別名 |
Sost, Sclerostin
|
| Amino Acid |
Gln24-Tyr211
|
| Construction |
Gln24-Tyr211
|
| Protein Purity |
Greater than 95% as determined by reducing SDS-PAGE. Greater than 95% as determined by SEC-HPLC.
|
| 分子量 |
32 KDa (reducing condition)
|
| Endotoxin |
< 0.1 ng/µg (1 EU/µg) as determined by LAL test.
|
| Formulation |
Lyophilized from a solution filtered through a 0.22 μm filter, containing PBS, pH 7.4.
|
| Reconstitution |
Reconstitute the lyophilized protein in distilled water. The product concentration should not be less than 100 μg/ml. Before opening, centrifuge the tube to collect powder at the bottom. After adding the reconstitution buffer, avoid vortexing or pipetting for mixing.
|
| Stability & Storage |
Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at-80℃. For reconstituted proteinsolutions, the solution can be stored at -20°c to -80'c for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.
|
| Shipping |
In general, Lyophilized powders are shipping with blue ice. Solutions are shipping with dry ice.
|
| Research Background |
Sclerostin (SOST) 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 homeostasis. 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.
|
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