| 货号 | MAB1589-SP |
| 别名 | sclerostin; VBCHsclerosteosis |
| 反应种属 | Mouse |
| 应用 | Western Blot(1 µg/mL) |
| 目标/特异性 | Detects mouse SOST in direct ELISAs and Western blots. In direct ELISAs, this antibody does not cross-react with recombinant human SOST. |
| 使用方法 | Western Blot: 1 µg/mL |
| 来源 | Reconstitute at 0.5 mg/mL in sterile PBS. |
| 产品组分 |
| 供应商 | R&D Systems |
| Entrez Gene IDs | 50964 (Human); 74499 (Mouse) |
| 应用文献 | |
| R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions. Mechanical stimulation of bone in vivo reduces osteocyte expression of Sost/sclerostin. | |
| 纯化方式 | Protein A or G purified from hybridoma culture supernatant |
| 免疫原 | Mouse myeloma cell line NS0-derived recombinant mouse SOST Gln24-Tyr211 Accession # AAI37834 |
| 生物活性 | Mouse |
| 标记 | Unconjugated |
| 溶解方法 | Reconstitute at 0.5 mg/mL in sterile PBS. |
| 背景 | 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 homeostasis. 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). |
| 运输条件 | Blue Ice |
| 存放说明 | 4℃ |
| 参考文献 |
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