The bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules that can induce ectopic bone growth. Many BMPs are part of the transforming growth factor-beta (TGFB) superfamily. BMPs were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. Based on its expression early in embryogenesis, the BMP encoded by this gene has a proposed role in early development. In addition, the fact that this BMP is closely related to BMP5 and BMP7 has lead to speculation of possible bone inductive activity.
A synthesized peptide derived from human BMP7, corresponding to a region within the internal amino acids.
Bone morphogenetic protein 7 (BMP-7), also known as osteogenic protein 1 (OP-1), is a widely expressed TGF-beta 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.
A synthetic peptide from human BMP7
A synthesized peptide derived from human BMP8A, corresponding to a region within the internal amino acids.
A synthesized peptide derived from human BMP8B, corresponding to a region within the internal amino acids.
A synthesized peptide derived from human BMP9, corresponding to a region within the internal amino acids.
A synthesized peptide derived from human BMPER.
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