Recombinant Human BMP-2/BMP-6 Heterodimer Protein


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Recombinant Human BMP-2/BMP-6 Heterodimer Protein Summary

Details of Functionality
Measured by its ability to induce alkaline phosphatase production by ATDC5 mouse chondrogenic cells. Binnerts, M.E. et al. (2004) Biochem. Biophys. Res. Commun. 315(2):272.

The ED50 for this effect is 4-20 ng/mL.

E. coli-derived human BMP-2/BMP-6 Heterodimer protein
Human BMP-2
(Ala284 - Arg396), with an N-terminal Met
Accession # P12643
Human BMP-6
(Gln382 - His513), with an N-terminal Met
Accession # P22004
N-terminus C-terminus
Accession #
N-terminal Sequence
Ala284 (BMP-2) & Met (BMP-6)
Structure / Form
Disulfide-linked heterodimer
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.


  • Bioactivity
Theoretical MW
12.8 kDa (BMP-2) & 15 kDa (BMP-6).
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.
11 kDa & 14 kDa, reducing conditions
Read Publications using
7145-BP 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 HCl with BSA as a carrier protein.
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 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 Human BMP-2/BMP-6 Heterodimer Protein

  • BMP-2/BMP-6 Heterodimer


Bone Morphogenetic Protein 6 (BMP-6), also known as Vgr-1, and BMP-2 are members of the BMP family of structurally and functionally related proteins and represent a subfamily of the transforming growth factor beta (TGF-beta ) superfamily. BMPs are involved in a wide range of processes including embryogenesis, tissue morphogenesis, cell differentiation and migration, and tumorigenesis. Cellular responses to BMPs are mediated by hetero‑oligomeric complexes of type I and type II serine/threonine kinase receptors (1 - 4). Human BMP-2 is synthesized as a 396 amino acid (aa) preproprotein that contains a 23 aa signal sequence, a 259 aa prosegment, and a 114 aa mature region (5). Human BMP-6 is synthesized as a 513 aa precursor protein that contains a 20 aa signal sequence, a 354 aa prosegment, and a 139 aa mature region (6). BMP prosegments are removed by proteolysis, enabling the glycosylated 18 kDa mature BMPs to form active disulfide-linked homodimers or heterodimers (1, 2). Mature human BMP-2 shares 100% aa sequence identity with mouse and rat BMP-2, and mature human BMP-6 shares 96% and 98% aa sequence identity with mouse and rat BMP-6, respectively. They share 48% aa sequence identity with each other. Both BMP-2 and BMP-6 induce osteogenic and chondrogenic differentiation in mesenchymal stem cells (4). Heterodimers of BMP-2 and BMP-6 show increased potency at inducing osteoblastic calcium deposition, chondrogenesis, and in vivo bone formation compared to either BMP-2 or BMP-6 homodimers (7, 8). BMP-2/6 heterodimers also show increased activity at inducing trophoectodermal and endodermal differentiation of embryonic stem cells compared to either homodimer (9).
  1. Chen, D. et al. (2004) Growth Factors 22:233.
  2. Bragdon, B. et al. (2010) Cell Signal. 23:609.
  3. Singh, A. and R.J. Morris (2010) Cytokine Growth Factor Rev. 21:299.
  4. Lavery, K. et al. (2008) J. Biol. Chem. 283:20948.
  5. Wozney, J. et al. (1988) Science 242:1528.
  6. Celeste, A.J. et al. (1990) Proc. Natl. Acad. Sci. 87:9843.
  7. Isaacs, M.J. et al. (2010) Mol. Endocrinol. 24:1469.
  8. Israel, D.I. et al. (1996) Growth Factors 13:291.
  9. Valera, E. et al. (2010) PLoS ONE 5:e11167.

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