Measured by its ability to induce alkaline phosphatase production by ATDC5 mouse chondrogenic cells. Nakamura, K. et al. (1999) Exp. Cell Res. 250:351. The ED50 for this effect is 0.5-4 ng/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived mouse BMP-9 protein Ser319-Arg428
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
12.1 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
13 kDa, reducing conditions
Publications
Read Publications using 5566-BP 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 Acetonitrile and TFA with BSA as a carrier protein.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 100 μg/mL in 4 mM HCl containing at least 0.1% human or bovine serum albumin.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse BMP-9 Protein
BMP9
BMP-9
BMP9BMP-9Bone morphogenetic protein 9
GDF2
GDF-2
growth differentiation factor 2
growth/differentiation factor 2
Background
Bone morphogenetic protein 9 (BMP-9), also known as growth and differentiation factor 2 (GDF-2), is a member of the BMP family of TGF-beta superfamily proteins that signal through heterodimeric complexes composed of type I and type II BMP receptors. BMP-9 regulates the development and function of a variety of embryonal and adult tissues (1, 2). Mouse BMP-9 consists of a 22 amino acid (aa) signal sequence, a 296 aa propeptide, and a 110 aa mature protein. Unlike other BMP family propeptides, the BMP-9 propeptide does not interfere with the biological activity of BMP-9, and remains associated with the mature peptide after proteolytic cleavage (3). Mouse and human BMP-9 share 96% aa sequence identity. Within the mature protein, mouse BMP-9 shares 64% aa sequence identity with mouse BMP-10 and approximately 50% aa sequence identity with other BMPs. BMP-9 is expressed by non-parenchymal cells in the liver where it promotes lipid metabolism and inhibits glucose production (4 - 6). It exerts a prolonged hypoglycemic effect which may be due to an enhancement of insulin release (6). BMP-9 interacts with the high affinity ALK-1 receptor on liver endothelial cells (3 - 5). It induces a cholinergic neuronal phenotype as well as the differentiation of mesenchymal stem cells into the chondrogenic lineage (7 - 11). At low concentrations, BMP-9 is a proliferative factor for hematopoietic progenitor cells, but at higher concentrations it enhances TGF-beta 1 production, and inhibits hematopoietic progenitor colony formation (12). BMP-9 also inhibits angiogenesis and the invasiveness of prostate carcinoma cells (13, 14).
Chen, D. et al. (2004) Growth Factors 22:233.
Miyazono, K. et al. (2005) Cytokine Growth Factor Rev. 16:251.
Brown, M.A. et al. (2005) J. Biol. Chem. 280:25111.
Song, J.J. et al. (1995) Endocrinology 136:4293.
Miller, A.F. et al. (2000) J. Biol. Chem. 275:17937.
Chen, C. et al. (2003) Nat. Biotechnol. 21:294.
Lopez-Coviella, I.et al. (2000) Science 289:313.
Lopez-Coviella, I.et al. (2005) Proc. Natl. Acad. Sci. 102:6984.
Lopez-Coviella, I.et al. (2002) J. Physiol. Paris 96:53.
Majumdar, M.K. et al. (2001) J. Cell. Physiol. 189:275.
Hills, R.L. et al. (2005) J. Orthoped. Res. 23:611.
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