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Recombinant Human Latent BMP-9 Protein

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Recombinant Human Latent BMP-9 (Catalog # 9624-BP) induces alkalinephosphatase production in the ATDC5 mouse chondrogenic cell line. The ED50 forthis effect is 1‑6 ng/mL.

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Summary
Reactivity HuSpecies Glossary
Applications Bioactivity

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Recombinant Human Latent BMP-9 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 1-6 ng/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human BMP-9 protein
Lys23-Arg319 (pro) & Ser320-Arg429 (mature)
Accession #
N-terminal Sequence
Lys23 (pro) & Ser320 (mature)
Structure / Form
Non covalent complex between the prodomain and mature domain.
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

Dilutions
  • Bioactivity
Theoretical MW
33 kDa (pro) & 12 kDa (mature).
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
39-44 kDa (pro) & 11 kDa (mature)

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 PBS with BSA as a carrier protein.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 250 μg/mL in PBS.

Notes

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

Alternate Names for Recombinant Human Latent BMP-9 Protein

  • BMP9
  • BMP-9
  • BMP9BMP-9Bone morphogenetic protein 9
  • GDF2
  • GDF-2
  • growth differentiation factor 2
  • growth/differentiation factor 2

Background

Human BMP-9, also known as growth and differentiation factor 2 (GDF2), is a member of the BMP subgroup of the TGF beta superfamily proteins that signal through heterodimeric complexes composed of type I and type II BMP receptors. BMP-9 regulates the development and function of a variety of embryonal and adult tissues (1, 2). The human BMP-9 cDNA encodes a 429 amino acid (aa) precursor that includes a 22 aa signal sequence, a 298 aa propeptide, and a 111 aa mature protein (3). Unlike with other BMP family proteins, the propeptide does not interfere with the biological activity of BMP-9 and remains associated with the mature peptide after proteolytic cleavage (4). Human and mouse BMP-9 share 96% aa sequence identity. Within the mature protein, human BMP-9 shares 64% aa sequence identity with human BMP-10 and less than 50% aa sequence identity with other BMPs. BMP-9 is expressed by nonparenchymal cells in the liver, (5, 6) where it promotes lipid metabolism and inhibits glucose production (7). BMP-9 exerts a prolonged hypoglycemic effect which may be due to an enhancement of insulin release (7). BMP-9 interacts with a high affinity specific heteromeric receptor expressed on liver endothelial cells that has been identified as ALK1 (4, 6). In the embryonal CNS, BMP-9 functions in the development and maintenance of the cholinergic neuronal phenotype (8, 10). BMP-9 also induces the differentiation of mesenchymal stem cells into the chondrogenic lineage (11, 12). At low concentrations, BMP-9 is a proliferative factor for hematopoietic progenitor cells, but at higher concentrations, it enhances TGF-beta 1 production and inhibits hematopoietic progenitor colony formation (13).
  1. Chen, D. et al. (2004) Growth Factors 22:233.
  2. Miyazono, K. et al. (2005) Cytokine Growth Factor Rev. 16:251.
  3. Celeste, A.J. et al. (1994) J. Bone Miner. Res. 9:S136.
  4. Brown, M.A. et al. (2005) J. Biol. Chem. 280:25111.
  5. Song, J.J. et al. (1995) Endocrinology 136:4293.
  6. Miller, A.F. et al. (2000) J. Biol. Chem. 275:17937.
  7. Chen, C. et al. (2003) Nat. Biotechnol. 21:294.
  8. LopezCoviella,I. et al. (2000) Science 289:313.
  9. LopezCoviella,I. et al. (2005) Proc. Natl. Acad. Sci. 102:6984.
  10. LopezCoviella,I. et al. (2002) J. Physiol. Paris 96:53.
  11. Majumdar, M.K. et al. (2001) J. Cell. Physiol. 189:275.
  12. Hills, R.L. et al. (2005) J. Orthoped. Res. 23:611.
  13. Ploemacher, R.E. et al. (1999) Leukemia 13:428.

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