• Purity

  >85%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

• Endotoxin Level

  <0.10 EU per 1 μg of the protein by the LAL method.  

• Activity

  Measured by its ability to inhibit the cell growth of DU145 human prostate carcinoma cells. Miyazaki, H.     et al. (2004) Oncogene     23:9326. The ED    ₅₀ for this effect is 0.7-3.5 μg/mL.

• Source

  Chinese Hamster Ovary cell line, CHO-derived Ala264-His402

• Accession #

• N-terminal Sequence    
  Analysis

  Ala264

• Structure / Form

  Disulfide-linked homodimer

• Predicted Molecular Mass

  16 kDa

• SDS-PAGE

  17-20 kDa, reducing conditions

Background: BMP-8b

BMP-8, also known as osteogenic protein 2 (OP-2), was first isolated from a hippocampal library in a screen to identify relatives of BMP-7/OP-1 (1). BMPs are a family of structurally and functionally related proteins and represent a subfamily of the transforming growth factor beta (TGF-beta ) superfamily. BMPs are involved in a wide range of processes including embryogenesis, tissue morphogenesis, cell differentiation and migration, and tumorigenesis. Cellular responses to BMPs are mediated by hetero-oligomeric complexes of type I and type II serine/threonine kinase receptors (2-4). BMP-8a and BMP-8b, produced from separate genes, share 98% aa sequence identity in human but only 74% in mouse within the mature regions. Human BMP-8b is synthesized as a 402 aa precursor protein that is cleaved between Arg263 and Ala264 to release the C-terminal mature protein. Mature human BMP-8b shares 91% and 71% aa sequence identity with mouse mature BMP-8a and -8b, respectively. BMP-8a is expressed during pregnancy in the deciduum and trophoblast cells, by inner root sheath cells of developing hair follicles, and by the epididymis and spermatids (5-7). In the mouse it cooperates with BMP-7 in the maintenance of spermatogenesis but is not required for the initiation of spermatogenesis (7, 8). BMP-8b, in contrast, is required for both the initiation and maintenance of spermatogenesis (9). BMP-8a is induced during osteoblast differentiation at the onset of mineralization and during the osteogenic phase of bone repair in osteoblasts and osteocytes (10-12). BMP-8b is also highly expressed in osteosarcomas and pancreatic cancer, and it contributes to tumor progression (13, 14). BMP-8b is also expressed in adipose tissue and the hypothalamus where it contributes to the regulation of energy balance and thermogenesis (15, 16).

• References:

1. Ozkaynak, E. et al. (1992) J. Biol. Chem. 267:25220.

2. Chen, D. et al. (2004) Growth Factors 22:233.

3. Bragdon, B. et al. (2010) Cell Signal. Oct 16 epub.

4. Singh, A. and R.J. Morris (2010) Cytokine Growth Factor Rev. 21:299.

5. Zhao, G.-Q. and B.L. Hogan (1996) Mech. Dev. 57:159.

6. Ying, Y. and G.-Q. Zhao (2000) Biol. Reprod. 63:1781.

7. Zhao, G.-Q. et al. (1998) Development 125:1103.

8. Zhao, G.-Q. et al. (2001) Dev. Biol. 240:212.

9. Zhao, G.-Q. et al. (1998) Genes Dev. 10:1657.

10. van der Horst, G. et al. (2002) Bone 31:661.

11. Cho, T.-J. et al. (2002) J. Bone Miner. Res. 17:513.

12. Paic, F. et al. (2009) Bone 45:682.

13. Sulzbacher, I. et al. (2002) J. Clin. Pathol. 55:381.

14. Cheng, Z. et al. (2014) Oncol. Rep. 32:1861.

15. Whittle, A.J. et al. (2012) Cell 149:871.

16. Martins, L. et al. (2016) Cell Rep. 16:2231.

• Long Name:

  Bone Morphogenetic Protein 8b

• Entrez Gene IDs:

  656 (Human); 12164 (Mouse)

• Alternate Names:

  BMP-8; BMP-8b; bone morphogenetic protein 8b; MGC131757; OP-3