Recombinant Human BMP-4 (E. coli-expressed) Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human BMP-4 (E. coli-expressed) Protein, CF 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 6-48 ng/mL.
Source
E. coli-derived human BMP-4 protein
Lys303-Arg408
Accession #
N-terminal Sequence
Lys303
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
12 kDa.
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
8-9 kDa, under 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, -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA.
Purity
>95%, 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-4 (E. coli-expressed) Protein, CF

  • BMP2B
  • BMP-2B
  • BMP2B1
  • BMP2BMCOPS6
  • BMP4
  • BMP-4
  • Bone morphogenetic protein 2B
  • bone morphogenetic protein 4
  • DVR4
  • MCOPS6
  • OFC11
  • ZYME

Background

Bone morphogenetic protein 4 (BMP-4) is a TGF-beta superfamily ligand that is widely expressed from early embryogenesis through adulthood. It plays an important role in mesenchyme formation, epidermal determination, suppression of neural induction, the development of multiple organs, and tissue repair (1-5). It is an integral part of many stem cell differentiation pathways, including lung tissue, (6), adipogenesis (7) and osteogenesis (8, 9). The human BMP-4 precursor contains a 273 amino acid (aa) propeptide and a 116 amino acid (aa) mature protein (10). Processing of the propeptide by furin or proprotein convertase 6 enables the formation of the mature disulfide-linked homodimeric BMP-4 and facilitates its secretion. Similar intracellular processes may lead to the formation and recreation of BMP4/BMP7 disulfide-linked heterodimer (11-13). Mature human and mouse BMP-4 share 98% aa sequence identity. Human BMP-4 shares 85% aa sequence identity with human BMP-2 and less than 50% with other human BMPs. In Xenopus, BMP-4 dimers provide ventralizing signals for existing mesoderm (14). BMP-4 signals through tetrameric complexes composed of type I (primarily Activin RIA or BMPR-IA) and type II (primarily Activin RIIA or BMPR-II) receptors (15, 16). The bioavailability of BMP-4 is regulated by its interaction with multiple proteins and glycosaminoglycans (17-19).
  1. Zhang, P. et al. (2008) Blood 111:1933.
  2. Gambaro, K. et al. (2006) Cell Death Differ. 13:1075.
  3. Simic, P. and S. Vukicevic (2005) Cytokine Growth Factor Rev. 16:299.
  4. Sadlon, T.J. et al. (2004) Stem Cells 22:457.
  5. Frank, D.B. et al. (2005) Circ. Res. 97:496.
  6. Lee, J-H. et al. (2014) Cell. 156:440.
  7. Tang, QQ. et Lane MD. (2012) Annu Rev. Biochem. 81:715.
  8. Urist, MR. (1965). Science. 150:893.
  9. Bandyopadhyay, A. et al. (2006) Plos Genetics. 2:e216.
  10. Wozney, J. et al. (1988) Science 242:1528.
  11. Cui, Y. et al. (1998) EMBO J. 17:4735.
  12. Cui, Y. et al. (2001) Genes Dev. 15:2797.
  13. Aono, A. et al. (1995) Biochem. Biophys. Res. Commun. 210:670.
  14. Nishimatsu, S. and G.H. Thomsen (1998) Mech. Dev. 74:75.
  15. Chen, D. et al. (2004) Growth Factors 22:233.
  16. Lavery, K. et al. (2008) J. Biol. Chem. April 24 epub.
  17. Rosen, V. (2006) Ann. N.Y. Acad. Sci. 1068:19.
  18. Jones, C.M. and J.C. Smith (1998) Dev. Biol. 194:12.
  19. Takada, T. et al. (2003) J. Biol. Chem. 278:43229.

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