Recombinant Human BMP-8b Protein, CF

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human BMP-8b Protein, CF Summary

• Details of Functionality: Measured by its ability to inhibit the cell growth of DU145 human prostate carcinoma cells. Miyazaki, H. et al. (2004) Oncogene 23:9326. The ED₅₀ for this effect is 0.7-3.5 μg/mL.
• Source: Chinese Hamster Ovary cell line, CHO-derived human BMP-8b protein
  Ala264-His402
• Accession #: P34820
• N-terminal Sequence: Ala264
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Purity: >85%, 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: 16 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: 17-20 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 250 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-8b Protein, CF

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

Background

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).

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.

Publications for BMP-8b (9316-BP)(3)

Publications using 9316-BP

• K Tan, MF Wilkinson Regulation of both transcription and RNA turnover contribute to germline specification Oncogene, 2022-07-22;0(0):. 2022-07-22 [PMID: 35776114] (Bioassay, Mouse)
• E Rial-Pensa, O Freire-Agu, M Ríos, DF Guo, C Contreras, P Seoane-Col, S Tovar, R Nogueiras, C Diéguez, K Rahmouni, M López Obesity induces resistance to central action of BMP8B through a mechanism involving the BBSome Molecular Metabolism, 2022-02-23;0(0):101465. 2022-02-23 [PMID: 35218946] (In Vivo, Mouse)
• R Zhao, Q Zuo, X Yuan, K Jin, J Jin, Y Ding, C Zhang, T Li, J Jiang, J Li, M Zhang, X Shi, H Sun, Y Zhang, Q Xu, G Chang, Z Zhao, B Li, X Wu, Y Zhang, J Song, G Chen, B Li Production of viable chicken by allogeneic transplantation of primordial germ cells induced from somatic cells Nature Communications, 2021-05-20;12(1):2989. 2021-05-20 [PMID: 34017000] (Bioassay, Chicken)

Bioinformatics

• Uniprot:
  • P34820()