Recombinant Mouse BMP-10 Protein

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Product Details

Summary
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.
Source
Chinese Hamster Ovary cell line, CHO-derived mouse BMP-10 protein
Asn314-Arg421
Accession #
N-terminal Sequence
Asn314
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Purity
>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.

Applications/Dilutions

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.
SDS-PAGE
10 kDa, reducing conditions

Packaging, Storage & Formulations

Storage
  • 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.
Buffer
Lyophilized from a 0.2 μm filtered solution in HCl with BSA as a carrier protein.
Purity
>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.

Notes

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

Background

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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