IBSP/Sialoprotein II: Lysates

IBSP (integrin-binding sialoprotein; also BSP or bone sialoprotein II) is a 55 - 75 kDa, secreted, variably glycosylated, monomeric noncollagenous member of the SIBLING family of extracellular matrix (ECM) proteins. It is principally associated with the early stages of bone mineralization. IBSP is synthesized as a 317 amino acid (aa) precursor that contains a 16 aa signal sequence and a 301 aa mature region. The mature segment is divided into a basic N-terminus (aa 17 - 62), a central region (aa 63 - 233), and an acidic C-terminus (aa 234 - 317).

HAp formation requires a IBSP nucleation site composed of at least eight consecutive glutamic acid residues and, likely, a contribution from a BSP-associated co-nucleator. IBSP is highly glycosylated, sulfated, and phosphorylated. Phosphorylation may impact HAp growth, while carbohydrate may regulate cell adhesion. Mature human IBSP is 70%, 72%, 78%, and 72% aa identical to porcine, rat, canine, and mouse IBSP, respectively. IBSP is synthesized by megakaryocytes/platelets, osteoblasts, osteocytes, odontoblasts, osteoclasts, and bone marrow stromal cells.