Recombinant Human BMP-2/BMP-7 Heterodimer Protein Summary
Details of Functionality
Measured by its ability to induce alkaline phosphatase production by ATDC5 mouse chondrogenic cells. Nakamura, K. et al. (1999) Exp. Cell Res. 250:351. The ED50 for this effect is 15.0-120 ng/mL.
Source
E. coli-derived human BMP-2/BMP-7 Heterodimer protein
Human BMP-2 (Ala284 - Arg396) Accession # NP_001191
Human BMP-7 (Ser293 - His431) Accession # NP_001710
>97%, 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.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
12.9 kDa (BMP-2), 15.8 kDa (BMP-7). 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.
Publications
Read Publications using 3229-BM in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after opening.
3 months, -20 to -70 °C under sterile conditions after opening.
Buffer
Supplied as 0.2 μm filtered solution in 30%(v/v) Acetonitrile and 0.1%(v/v) TFA with 50
μg BSA per 1 μg as a carrier protein.
Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human BMP-2/BMP-7 Heterodimer Protein
BDA2;BMP2A;Bone morphogenetic protein 2;SSFSC;SSFSC1
BMP-2/BMP-7 Heterodimer
Background
Human BMP-7, also known as osteogenic protein 1 (OP-1), and BMP-2 are members of the BMP subgroup of the TGF-beta superfamily and signal through heterodimeric complexes composed of type I and type II BMP receptors. BMP-2 and BMP-7 influence a variety of morphogenic processes, particularly during skeletal and renal development (1 - 3). The human BMP-2 cDNA encodes a 396 amino acid (aa) precursor that contains a 23 aa signal sequence, a 259 propeptide, and a 114 aa mature protein (4). The human BMP-7 cDNA encodes a 431 aa precursor that contains a 29 aa signal sequence, a 263 aa propeptide, and a 139 aa mature protein (5). BMP propeptides are removed by proteolysis, enabling mature BMPs to form active disulfide linked homodimers or heterodimers (1). Human and mouse BMP-2 and BMP-7 are 100% and 98% identical, respectively, at the amino acid level. Human BMP-2 shares 85% aa sequence identity with human BMP-4 and less than 51% aa sequence identity with other BMPs. Human BMP-7 shares approximately 60% - 70% aa sequence identity with BMP-5, -6, and -8, and less than 50% aa sequence identity with other BMPs. BMP-2 and BMP-7 are co-expressed in some embryonic tissues (6, 7) and associate into a functional 38 kDa osteogenic dimer (8). In in vitro osteoblast differentiation assays and in vivo bone formation models, a BMP-2/BMP-7 heterodimer is significantly more potent than either homodimer (9 - 12). Considering that BMP-2 preferentially binds BMPRIA/ALK-3 and BMPRIB/ALK-6, while BMP-7 is selective for ALK-2, the observed increase in heterodimer activity may be due to the triggering of additional receptor subtypes.
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Wozney, J. et al. (1988) Science 242:1528.
Gregory, K.E. et al. (2005) J. Biol. Chem. 280:27970.
Lyons, K.M. et al. (1995) Mech. Dev. 50:71.
Knosp, W.M. et al. (2004) Development 131:4581.
Sampath, T.K. et al. (1990) J. Biol. Chem. 265:13198.
Hazama, M. et al. (1995) Biochem. Biophys. Res. Commun. 209:859.
Zhu, W. et al. (2004) J. Bone Miner. Res. 19:2021.
Zhao, M. et al. (2005) J. Cell. Biochem. 95:1.
Israel, D.I. et al. (1996) Growth Fact ors 13:291.
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