Recombinant Human BMP-7 Biotinylated Protein, CF

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When Biotinylated Recombinant Human BMP‑7 (BT354B/CF) is used at 0.25 μg/mL, it binds Recombinant Human Activin RIA/ALK‑2 Fc Chimera (Catalog # 637‑AR) with an ED50 of 0.15‑0.9 μg/mL.

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human BMP-7 Biotinylated Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. In a Streptavidin coated plate (Catalog # CP004), when Biotinylated Recombinant Human BMP‑7 is used at 0.25 μg/mL, it binds Recombinant Human Activin RIA/ALK-2 Fc Chimera (Catalog # 637-AR) with an ED50 of 0.15-0.9 μg/mL. 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 0.1-0.6 μg/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human BMP-7 protein
Ser293-His431
Accession #
N-terminal Sequence
Ser293
Structure / Form
Disulfide-linked homodimer. Biotinylated protein via amines
Protein/Peptide Type
Recombinant Proteins
Purity
>85%, 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.

Applications/Dilutions

Theoretical MW
16 kDa (unlabeled).
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
15-24 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 HCl.
Purity
>85%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in 4 mM HCl.

Notes

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

Alternate Names for Recombinant Human BMP-7 Biotinylated Protein, CF

  • BMP7
  • BMP-7
  • bone morphogenetic protein 7
  • Eptotermin alfa
  • OP-1
  • OP-1OP1
  • Osteogenic protein 1

Background

Bone morphogenetic protein 7 (BMP-7), also known as osteogenic protein 1 (OP-1), is a widely expressed TGF-beta superfamily member with important functions during embryogenesis, in the adult, and in disease (1, 2). Human BMP-7 is synthesized with a 29 amino acid (aa) signal sequence, a 263 aa propeptide, and a 139 aa growth factor domain (3, 4). The growth factor domain of human BMP-7 shares 98% aa sequence identity with mouse and rat BMP-7. The BMP-7 propeptide is cleaved intracellularly but remains in association with the growth factor domain. BMP-7 is subsequently secreted as a tetramer that consists of two propeptides and two disulfide-linked growth factor domains (5, 6). Mature BMP-7 can also form disulfide-linked heterodimers with BMP-2 or BMP-4, complexes that show increased potency and range of activity compared to BMP-7 homodimers (7-9). The presence of the propeptides in the BMP-7 tetramer does not diminish the bioactivity of the growth factor domains (6). Secreted BMP-7 is immobilized in the extracellular matrix as a result of interactions between the propeptide and matrix Fibrillin (5). BMP-7 exerts its biological effects through the type 2 receptors Activin RIIA, Activin RIIB, and BMPR-II and the type 1 receptors Activin RIA, BMPR-IA, and BMPR-IB (2, 6). BMP-7 plays a role in a variety of organ systems. It promotes new bone formation and nephron development (10, 11), inhibits the branching of prostate epithelium (12), and antagonizes epithelial-mesenchymal transition (EMT) (13-15). In pathological conditions, BMP-7 inhibits tumor growth and metastasis (14), ameliorates fibrotic damage in nephritis (13), and promotes neuroregeneration following brain ischemia (16).
  1. Carreira, A.C. et al. (2015) J. Dent. Res. 93:335.
  2. Weiskirchen, R. and S.K. Meurer (2013) Front. Biosci. (Landmark Ed.) 18:1407.
  3. Ozkaynak, E. et al. (1990) EMBO J. 9:2085.
  4. Celeste, A.J. et al. (1990) Proc. Natl. Acad. Sci. USA 87:9843.
  5. Gregory, K.E. et al. (2005) J. Biol. Chem. 280:27970.
  6. Sengle, G. et al. (2008) J. Mol. Biol. 381:1025.
  7. Israel, D.I. et al. (1996) Growth Factors 13:291.
  8. Aono, A. et al. (1995) Biochem. Biophys. Res. Commun. 210:670.
  9. Nishimatsu, S. and G.H. Thomsen (1998) Mech. Dev. 74:75.
  10. Sampath, T.K. et al. (1992) J. Biol. Chem. 267:20352.
  11. Kazama, I. et al. (2008) J. Am. Soc. Nephrol. 19:2181.
  12. Grishina, I.B. et al. (2005) Dev. Biol. 288:334.
  13. Zeisberg, M. et al. (2003) Nat. Med. 9:964.
  14. Buijs, J.T. et al. (2007) Am. J. Pathol. 171:1047.
  15. Yu, M.-A. et al. (2009) J. Am. Soc. Nephrol. 20:567.
  16. Chou, J. et al. (2006) J. Neurol. Sci. 240:21.

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