Recombinant Mouse BMP-10 Protein


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Reactivity MuSpecies Glossary
Applications Bioactivity

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Recombinant Mouse BMP-10 Protein Summary

Details of Functionality
Measured by its ability to induce alkaline phosphatase production by MC3T3‑E1 mouse preosteoblast cells. The ED50 for this effect is 6-36 ng/mL.
Chinese Hamster Ovary cell line, CHO-derived mouse BMP-10 protein
Accession #
N-terminal Sequence
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
>95%, 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.


Theoretical MW
12.1 kDa (monomer).
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.
10 kDa, reducing conditions

Packaging, Storage & Formulations

  • 12 months from date of receipt, ≤ -20 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, ≤ -20 °C under sterile conditions after reconstitution.
Lyophilized from a 0.2 μm filtered solution in HCl with BSA as a carrier protein.
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 250 μg/mL in 4 mM HCl containing at least 0.1% human or bovine serum albumin.


This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse BMP-10 Protein

  • BMP10
  • BMP-10
  • bone morphogenetic protein 10
  • MGC126783


Bone morphogenetic protein 10 (BMP-10), along with BMP-9, GDF-5, -6, and -7, belongs to a subgroup of TGF-beta superfamily proteins that signal through heterodimeric complexes composed of type I and type II BMP receptors (1-3). Proteolytic removal of the propeptide from the 60 kDa proprotein yields a 12 kDa mature BMP-10 which forms disulfide-linked nonglycosylated homodimers (4, 5). In transfectants, BMP-10 can also be secreted as a proprotein which binds to matrix fibrillin (4, 6). Mature mouse BMP-10 shares 98% and 100% amino acid sequence identity with human and rat BMP-10, respectively, and 48%-64% with mouse BMP-9, GDF-5, -6, and -7. BMP-10 is critical for the proper development of the heart and first appears at the onset of trabeculation and chamber formation (7-9). Homozygous BMP-10 knockout mice die in utero due to arrested cardiac development (8). BMP-10 is required for maintaining expression of the cardiogenic transcription factors NKX2.5 and MEF2C in developing myocardium and promoting the Notch-dependent growth of embryonic cardiomyocytes (8, 10-12). NKX2.5 itself negatively regulates BMP-10 expression in cardiac myocytes (11). BMP-10 in the postnatal heart promotes increased cardiomyocyte and heart size and is upregulated in hypertrophied ventricles (9, 13). Mature BMP-10 accumulates within cardiomyocytes in association with the sarcomere protein Tcap (13). BMP-10 induces signaling through ALK-1, BMPR-IA, BMPR-IB, and BMPR-II in transfectants and non-cardiac cell lines (4, 5). Deletion of BMPR-IA or BMP-10 causes similar cardiac morphogenetic abnormalities (14). In dermal endothelial cells, BMP-10 induces migration, proliferation, and gene expression typically associated with ALK-1 (5).
  1. Chen, D. et al. (2004) Growth Factors 22:233.
  2. Miyazono, K. et al. (2005) Cytokine Growth Factor Rev. 16:251.
  3. Schneider, M.D. et al. (2003) Cytokine Growth Factor Rev. 14:1.
  4. Mazerbourg, S. et al. (2005) J. Biol. Chem. 280:32122.
  5. David, L. et al. (2007) Blood 109:1953.
  6. Sengle, G. et al. (2008) J. Biol. Chem. 283:13874.
  7. Neuhaus, H. et al. (1999) Mech. Dev. 80:181.
  8. Chen, H. et al. (2004) Development 131:2219.
  9. Chen, H. et al. (2006) J. Biol. Chem. 281:27481.
  10. Srivastava, D. and Olson, E.N. (2000) Nature 407:221.
  11. Pashmforoush, M. et al. (2004) Cell 117:373.
  12. Grego-Bessa, J. et al. (2007) Dev. Cell 12:415.
  13. Nakano, N. et al. (2007) Am. J. Heart Circ. Physiol. 293:H3396.
  14. Gaussin, V. et al. (2002) Proc. Natl. Acad. Sci. 99:2878.

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