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Recombinant Human BMP-4 Protein, CF

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Recombinant Human BMP‑4 (Catalog # 314-BP/CF) induces BMP responsive SEAP reporter activity in HEK293 human embryonic kidney cells. The ED50 for this effect is 0.70-7.00 ng/mL.

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free
Datasheet
Reviews & Publications
Protocols & FAQs
Support & Research

Recombinant Human BMP-4 Protein, CF Summary

Details of Functionality
Measured by its ability to induce BMP responsive SEAP reporter activity in HEK293 human embryonic kidney cells. The ED50 for this effect is 0.70-7.00 ng/mL. 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 3.00-30.0 ng/mL.
Source
Mouse myeloma cell line, NS0-derived human BMP-4 protein
Ser293-Arg408
Accession #
N-terminal Sequence
Ser293
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
BMP4
Purity
>95%, 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

Dilutions
  • Bioactivity
  • Bioactivity2
Theoretical MW
13 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.
SDS-PAGE
19-24 kDa, reducing conditions
35-41 kDa, non-reducing conditions
Publications
Read Publications using
314-BP/CF in the following applications:

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 50-200 μg/mL in sterile 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 Protein, CF

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

Background

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). The human BMP-4 precursor contains a 273 amino acid (aa) propeptide and a 116 aa mature protein (6). 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 (7-9). 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. Compared to BMP-4 homodimers, BMP-4/BMP-7 heterodimers exhibit a greater potency in inducing osteogenic differentiation (9). In Xenopus, the heterodimers can also induce the formation of mesoderm, whereas BMP-4 homodimers only provide ventralizing signals for existing mesoderm (10). 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 (11, 12). The bioavailability of BMP-4 is regulated by its interaction with multiple proteins and glycosaminoglycans (13-15).

 

  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. Wozney, J. et al. (1988) Science 242:1528.
  7. Cui, Y. et al. (1998) EMBO J. 17:4735.
  8. Cui, Y. et al. (2001) Genes Dev. 15:2797.
  9. Aono, A. et al. (1995) Biochem. Biophys. Res. Commun. 210:670.
  10. Nishimatsu, S. and G.H. Thomsen (1998) Mech. Dev. 74:75.
  11. Chen, D. et al. (2004) Growth Factors 22:233.
  12. Lavery, K. et al. (2008) J. Biol. Chem. April 24 epub.
  13. Rosen, V. (2006) Ann. N.Y. Acad. Sci. 1068:19.
  14. Jones, C.M. and J.C. Smith (1998) Dev. Biol. 194:12.
  15. Takada, T. et al. (2003) J. Biol. Chem. 278:43229.

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Bioinformatics

Gene Symbol BMP4
Uniprot