Human BMP-8 Antibody
Human BMP-8 Antibody Summary
Accession # AAP74559
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
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‑8a 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‑8a shares 90% and 68% 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‑8a/b is also highly expressed in osteosarcomas (13).
- Ozkaynak, E. et al. (1992) J. Biol. Chem. 267:25220.
- Chen, D. et al. (2004) Growth Factors 22:233.
- Bragdon, B. et al. (2011) Cell Signal. 23:609.
- Singh, A. and R.J. Morris (2010) Cytokine Growth Factor Rev. 21:299.
- Zhao, G.-Q. and B.L. Hogan (1996) Mech. Dev. 57:159.
- Ying, Y. and G.-Q. Zhao (2000) Biol. Reprod. 63:1781.
- Zhao, G.-Q. et al. (1998) Development 125:1103.
- Zhao, G.-Q. et al. (2001) Dev. Biol. 240:212.
- Zhao, G.-Q. et al. (1998) Genes Dev. 10:1657.
- van der Horst, G. et al. (2002) Bone 31:661.
- Cho, T.-J. et al. (2002) J. Bone Miner. Res. 17:513.
- Paic, F. et al. (2009) Bone 45:682.
- Sulzbacher, I. et al. (2002) J. Clin. Pathol. 55:381.
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