Recombinant Human Bone Sialoprotein (His tag C-Terminus)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Bone Sialoprotein (BSP) is a non-collagenous glycoprotein of the SIBLING (Small Integrin-Binding Ligand N-linked Glycoprotein) family with a mass around 70-80 kDa. Its expression mainly takes place in mineralized tissues like bone and dentin highlighting its importance in skeletal biology. BSP has a strong affinity for calcium and hydroxyapatite allowing it to play binding and structural roles in bone matrix formation.

Biological function summary

The protein influences the nucleation of hydroxyapatite crystals and helps regulate mineralization processes. It associates with collagenous and non-collagenous components in the bone and contributes to tissue integrity and repair. BSP functions as part of a complex matrix that orchestrates cell adhesion and signal transduction impacting osteoblast and osteoclast activity.

Pathways

Bone Sialoprotein interacts within the extracellular matrix organization pathway and the integrin signaling pathway. In the extracellular matrix pathway BSP plays a role together with proteins like osteopontin also from the SIBLING family to influence cellular adhesion. Through integrin signaling BSP modulates cell-surface interactions particularly affecting the behavior of osteoclasts and osteoblasts and their capacity to maintain bone homeostasis.

Bone Sialoprotein associates with pathological conditions such as osteosarcoma and osteoporosis. In osteosarcoma BSP overexpression correlates with aggressive tumor growth potentially linking it with the tumor protein osteopontin suggesting a marker for malignancy. In osteoporosis dysregulation of BSP expression may affect bone density contributing to weakened bone structure alongside changes in other bone matrix proteins.