Human BMP9 is a member of the BMP subgroup of the TGF-beta superfamily proteins that signal through heterodimeric complexes composed of type I and type II BMP receptors. BMP9 regulates the development and function of a variety of embryonal and adult tissues. The human BMP9 cDNA encodes a 429 amino acid (aa) precursor that includes a 22aa signal sequence, a 298aa propeptide, and a 111aa mature protein. Unlike with other BMP family proteins, the propeptide does not interfere with the biological activity of BMP9 and remains associated with the mature peptide after proteolytic cleavage. Human and mouse BMP9 share 96% aa sequence identity. Within the mature protein, human BMP9 shares 64% aa sequence identity with human BMP10 and less than 50% aa sequence identity with other BMPs. BMP9 is expressed by non-parenchymal cells in the liver, where it promotes lipid metabolism and inhibits glucose production. BMP9 exerts a prolonged hypoglycemic effect which may be due to an enhancement of insulin release. BMP9 interacts with a high affinity specific heteromeric receptor expressed on liver endothelial cells that has been identified as ALK-1. In the embryonal CNS, BMP9 functions in the development and maintenance of the cholinergic neuronal phenotype. BMP9 also induces the differentiation of mesenchymal stem cells into the chondrogenic lineage. At low concentrations, BMP9 is a proliferative factor for hematopoietic progenitor cells, but at higher concentrations, it enhances TGF-beta1 production and inhibits hematopoietic progenitor colony formation.
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