Anti-BMP-7 (Hu) aus Kaninchen – unkonj.

Bone morphogenetic protein 7 (BMP-7), also known as osteogenic protein 1 (OP1), is a widely expressed TGFb superfamily member with important functions during embryogenesis, in the adult, and in disease. Human BMP-7 is synthesized with a 29 amino acid (aa) signal sequence, a 263 aa propeptide, and a 139 aa growth factor domain. The growth factor domain of human BMP-7 shares 98% aa sequence identity with mouse and rat BMP-7. The BMP-7 propeptide is cleaved intracellularly but often remains associated with the mature C-terminus. Based on in vivo and in vitro studies, BMP-7 has the potential to be secreted as a disulfide-linked mature homodimer, or particularly as a heteromeric complex that consists of two propeptides noncovalently associated with a mature disulfide linked homodimer. The presence of the propeptides in BMP-7 appears to stabilize the molecule and provide a docking mechanism for extracellular storage on molecules such as fibrillin1 and 2. The propeptides themselves do not impart latency to the complex. BMP-7 binding to type II receptors rapidly displaces the prodomain: mature molecule interaction and has no effect on activity.BMP-7 plays a role in a variety of organ systems. It promotes new bone formation and nephron development, inhibits the branching of prostate epithelium, and antagonizes epithelial mesenchymal transition (EMT). In pathological conditions, BMP-7 inhibits tumor growth and metastasis, ameliorates fibrotic damage in nephritis, and promotes neuro regeneration following brain ischemia.