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Recombinant Human BMP-10 Propeptide Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human BMP-10 Propeptide Protein, CF Summary

Details of Functionality
Measured by its ability to inhibit BMP-10-induced alkaline phosphatase production by MC3T3‑E1 mouse preosteoblast cells. The ED50 for this effect is 0.75-3 µg/mL in the presence of 100 ng/mL of rhBMP-10.
Source
Mouse myeloma cell line, NS0-derived human BMP-10 protein
Human BMP-10 Propeptide
(Ser20 - Arg313) & (Pro23 - Arg313)
Accession # O95393
RR 6-His tag
N-terminus C-terminus
Accession #
N-terminal Sequence
Ser20 & Pro23
Protein/Peptide Type
Recombinant Proteins
Gene
BMP10
Purity
>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
34.6 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
42-50 kDa, reducing conditions

Packaging, Storage & Formulations

Storage
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 PBS.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 250 μg/mL in sterile PBS.

Notes

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

Alternate Names for Recombinant Human BMP-10 Propeptide Protein, CF

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

Background

BMP-10, along with BMP-9, GDF-5, -6, and -7, belongs to a subgroup of sequence related 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 non-glycosylated homodimers (4, 5). In transfectants, BMP-10 is secreted as a cleaved mature dimer, an uncleaved proform dimer, and an uncleaved proform monomer (4). The propeptide of human BMP-10 shares 82% amino acid sequence identity with mouse and rat proBMP-10 and 19% - 34% with the propeptides of human 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 (6 - 8). Homozygous BMP-10 knockout mice die in utero due to arrested cardiac development (7). BMP-10 is required for maintaining expression of the cardiogenic transcription factors NKX2.5 and MEF2C in developing myocardium and promoting the growth of embryonic cardiomyocytes (7, 9, 10). The BMP-10 mediated proliferation of these cells requires Notch signaling (11). NKX2.5 itself negatively regulates BMP-10 expression in cardiac myocytes (10). Multiple human congenital heart defects result from mutations in NKX2.5 and require BMP-10 expression (10). In mice, genetic knockout of ErbB leads to a similar phenotype but appears not to involve BMP-10, and knockout of the calcium channel subunit FKBP12 induces BMP-10 overexpression (7). BMP-10 in the postnatal heart promotes increased cardiomyocyte and heart size (8). BMP-10 has been shown to induce signaling through ALK-1, BMPR-IA, BMPR-IB, and BMPR-II in transfectants and non-cardiac cell lines (4, 5). A functional BMP-10 receptor in the heart has not yet been identified, although deletion of BMPR-IA or BMP-10 causes similar cardiac morphogenetic abnormalities (12).

  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. Neuhaus, H. et al. (1999) Mech. Dev. 80:181. 
  7. Chen, H. et al. (2004) Development 131:2219.
  8. Chen, H. et al. (2006) J. Biol. Chem. 281:27481.
  9. Srivastava, D. and E.N. Olson (2000) Nature 407:221.
  10. Pashmforoush, M. et al. (2004) Cell 117:373.
  11. Grego-Bessa, J. et al. (2007) Dev. Cell 12:415.
  12. Gaussin, V. et al. (2002) Proc. Natl. Acad. Sci. 99:2878.

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Bioinformatics

Gene Symbol BMP10
Uniprot