Recombinant Human BMP-10 Protein, CF


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Reactivity HuSpecies Glossary
Applications Bioactivity

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Recombinant Human BMP-10 Protein, CF 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 15-60 ng/mL.
Chinese Hamster Ovary cell line, CHO-derived human BMP-10 protein
Accession #
N-terminal Sequence
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.


  • Bioactivity
Theoretical MW
12.2 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.
13 kDa, reducing conditions
Read Publications using
2926-BP/CF in the following applications:

Packaging, Storage & Formulations

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.
Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA.
>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile 4 mM HCI.


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

Alternate Names for Recombinant Human BMP-10 Protein, CF

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


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
non-glycosylated homodimers (4, 5). Mature human BMP-10 shares 98% amino acid sequence identity with mouse and rat BMP-10 and 49% - 63% with human BMP-9, GDF-5, -6, and -7. BMP-10 is critical for the proper development of the heart but is not expressed until after cardiac patterning or looping are completed (6-8). BMP-10 production appears at the onset of trabeculation and chamber formation and is restricted to the right atrium in the adult heart (6-8). Homozygous BMP-10 knockout mice die in utero due to arrested cardiac development (7). BMP-10 is required for the expression of the cardiogenic transcription factors NKX2.5 and MEF2C in developing myocardium and the growth of embryonic cardiomyocytes (7, 10). 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 over-expression (7). BMP-10 in the postnatal heart promotes increased cardiomyocyte and heart size (8). BMP-10 has been shown to signal 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 causes similar cardiac morphogenetic abnormalities (11). 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. 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. Gaussin, V. et al. (2002) Proc. Natl. Acad. Sci. 99:2878.

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Publications for BMP-10 (2926-BP/CF)(15)

We have publications tested in 2 confirmed species: Human, Mouse.

We have publications tested in 5 applications: Binding Assay, Bioassay, Cell Culture, Surface Plasmon Resonance, Western Blot.

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Binding Assay
Cell Culture
Surface Plasmon Resonance
Western Blot
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Showing Publications 1 - 10 of 15. Show All 15 Publications.
Publications using 2926-BP/CF Applications Species
C Ivaldo, M Passalacqu, AL Furfaro, C d'Abramo, S Ruiz, PK Chatterjee, CN Metz, M Nitti, P Marambaud Oxidative stress-induced MMP- and gamma-secretase-dependent VE-cadherin processing is modulated by the proteasome and BMP9/10 Scientific Reports, 2023;13(1):597. 2023 [PMID: 36631513] (Cell Culture, Human) Cell Culture Human
Z Shonibare, M Monavarian, K O'Connell, D Altomare, A Shelton, S Mehta, R Jaskula-Sz, R Phaeton, MD Starr, R Whitaker, A Berchuck, AB Nixon, RC Arend, NY Lee, CR Miller, N Hempel, K Mythreye Reciprocal SOX2 regulation by SMAD1-SMAD3 is critical for anoikis resistance and metastasis in cancer Oncogene, 2022;40(4):111066. 2022 [PMID: 35905726] (Bioassay, Human) Bioassay Human
J Guo, B Liu, M Thorikay, M Yu, X Li, Z Tong, RM Salmon, RJ Read, P Ten Dijke, NW Morrell, W Li Crystal structures of BMPRII extracellular domain in binary and ternary receptor complexes with BMP10 Nature Communications, 2022;13(1):2395. 2022 [PMID: 35504921] (Surface Plasmon Resonance, Human) Surface Plasmon Resonance Human
R Kumar, AV Grinberg, H Li, TH Kuo, D Sako, L Krishnan, K Liharska, J Li, R Grenha, MC Maguire, SD Briscoe, RS Pearsall, BR Herrin, RNVS Suragani, R Castonguay Functionally diverse heteromeric traps for ligands of the transforming growth factor-beta superfamily Scientific Reports, 2021;11(1):18341. 2021 [PMID: 34526551] (Bioassay, Human) Bioassay Human
M Subileau, G Merdzhanov, D Ciais, V Collin-Fau, JJ Feige, S Bailly, D Vittet Bone Morphogenetic Protein 9 Regulates Early Lymphatic-Specified Endothelial Cell Expansion during Mouse Embryonic Stem Cell Differentiation Stem Cell Reports, 2018;0(0):. 2018 [PMID: 30595547] (Bioassay, Mouse) Bioassay Mouse
E Tillet, M Ouarné, A Desroches-, C Mallet, M Subileau, R Didier, A Lioutsko, G Belthier, JJ Feige, S Bailly A heterodimer formed by bone morphogenetic protein 9 (BMP9) and BMP10 provides most BMP biological activity in plasma J. Biol. Chem., 2018;0(0):. 2018 [PMID: 29789425] (Western Blot) Western Blot
CG Mitrofan, SL Appleby, GB Nash, Z Mallat, ER Chilvers, PD Upton, NW Morrell Bone morphogenetic protein (BMP) 9 and BMP10 enhance tumor necrosis factor-?-induced monocyte recruitment to the vascular endothelium mainly via activin receptor-like kinase 2 J. Biol. Chem., 2017;0(0):. 2017 [PMID: 28646109] (Bioassay, Human) Bioassay Human
Y Tachida, N Izumi, T Sakurai, H Kobayashi Mutual interaction between endothelial cells and mural cells enhances BMP9 signaling in endothelial cells Biol Open, 2017;6(3):370-380. 2017 [PMID: 28298363] (Bioassay, Human) Bioassay Human
Levet S, Ouarne M, Ciais D, Coutton C, Subileau M, Mallet C, Ricard N, Bidart M, Debillon T, Faravelli F, Rooryck C, Feige J, Tillet E, Bailly S BMP9 and BMP10 are necessary for proper closure of the ductus arteriosus. Proc Natl Acad Sci U S A, 2015;112(25):E3207-15. 2015 [PMID: 26056270] (Bioassay, Human) Bioassay Human
Tate C, Mc Entire J, Pallini R, Vakana E, Wyss L, Blosser W, Ricci-Vitiani L, D'Alessandris Q, Morgante L, Giannetti S, Larocca L, Todaro M, Benfante A, Colorito M, Stassi G, De Maria R, Rowlinson S, Stancato L A BMP7 Variant Inhibits Tumor Angiogenesis In Vitro and In Vivo through Direct Modulation of Endothelial Cell Biology. PLoS ONE, 2015;10(4):e0125697. 2015 [PMID: 25919028] (Bioassay, Human) Bioassay Human
Show All 15 Publications.

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Gene Symbol BMP10