Recombinant Human BMP-3 Protein, CF


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Reactivity HuSpecies Glossary
Applications Bioactivity

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Recombinant Human BMP-3 Protein, CF Summary

Details of Functionality
Measured by its ability to inhibit BMP-2-induced activity in MC3T3‑E1 mouse preosteoblast cells. Daluiski, A. et al. (2001) Nature Genetics 27:84. 30 µg/mL of hBMP-3 will antagonize hBMP-2 (0.25 µg/mL) induction of alkaline phosphatase in MC3T3E1 cells by >50%.
E. coli-derived human BMP-3 protein
Gln363-Arg472, with an N-terminal Met
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
<0.10 EU per 1 μg of the protein by the LAL method.


  • Bioactivity
Theoretical MW
12.5 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.
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113-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.
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 1 mg/mL in sterile 35% Acetonitrile and 0.1% TFA.


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

Alternate Names for Recombinant Human BMP-3 Protein, CF

  • BMP3
  • BMP-3
  • BMP3A
  • BMP-3A
  • bone morphogenetic protein 3 (osteogenic)
  • bone morphogenetic protein 3
  • Bone morphogenetic protein 3A
  • bone morphogenetic protein-3
  • Osteogenin


BMP-3, also known as osteogenin, the most abundant BMP in adult bone, is one of at least 15 structurally and functionally related BMPs, which are members of the TGF-  beta superfamily (1 - 3). BMPs were originally identified as protein regulators of cartilage and bone formation. They have since been shown to be involved in embryogenesis and morphogenesis of various tissues and organs. BMPs also regulate the growth, differentiation, chemotaxis, and apoptosis of various cell types. Similar to most other TGF-beta family proteins, BMPs are highly conserved across animal species. At the amino acid sequence level, mature human and rat BMP-3 are 98% identical. BMP-3 is synthesized as a large precursor protein that is cleaved at the dibasic cleavage site (RXXR) to release the carboxy-terminal domain. Biologically active BMP-3 is a disulfide-linked homodimer of the carboxy-terminal 110 amino acid residues that contains the characteristic seven conserved cysteine residues involved in the formation of the cysteine knot and the single interchain disulfide bond (4). The role of BMP-3 in bone is contradictory since, unlike osteogenin purified from bone, recombinant BMP-3 has not shown osteogenic function (5). Several studies indicate that BMP-3 is an inhibitor of osteogenic BMPs. BMP-3 dorsalizes Xenopus embryos, the opposite effect of BMP-2 or 4, which cause ventralization. BMP-3 inhibits alkaline phosphatase production and induction of osteoblastic target genes in undifferentiated mesenchymal and osteogenic cell lines that have been treated with BMP-2. BMP-3 also induces the expression of TGF-beta /activin responsive genes, but not BMP-responsive genes. Since the inhibitory effect is not due to direct competition with osteogenic BMPs, it has been suggested that BMP-3 activates signaling through an activin pathway, resulting in antagonism of osteogenesis induced by other BMPs.

  1. Chen, D. et al. (2004) Growth Factors 22:233.
  2. Hino, J. et al. (2004) Front. Biosci. 9:1520.
  3. Bahamonde, M.E. and K.M. Lyons (2001) J. Bone and Joint Surgery 83-A (suppl 1):S156.
  4. Wozney, J.M. et al. (1998) Science 242:1528.
  5. Daluiski, A. et al. (2001) Nature Genetics 27:84.

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Publications for BMP-3 (113-BP/CF)(4)

We have publications tested in 3 confirmed species: Human, Mouse, Xenopus.

We have publications tested in 3 applications: Bioassay, In Vivo, Surface Plasmon Resonance.

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Gene Symbol BMP3