Anti-SPARC / Osteonectin, clone OSTN/3761

1 mg/ml in 1X PBS, BSA free, sodium azide free. SPARC (for secreted protein acidic and rich in cysteine) is a phosphorylated, acidic, glycine-rich glycoprotein that is secreted by endothelial cells and is present in large amounts in the parietal endoderm of mouse embryos and in human placenta. It is identical to osteonectin, a protein important to bone calcification that is highly conserved between species. SPARC, which can be selectively expressed by the endothelium in response to certain types of injury, induces rounding in adherent endothelial cells in vitro. It regulates endothelial barrier function through F-Actin-dependent changes in cell shape, coincident with the appearance of intercellular gaps, which provide a paracellular pathway for extravasation of macromolecules. Protein function: Appears to regulate cell growth through interactions with the extracellular matrix and cytokines. Binds calcium and copper, several types of collagen, albumin, thrombospondin, PDGF and cell membranes. There are two calcium binding sites, an acidic domain that binds 5 to 8 Ca(2+) with a low affinity and an EF-hand loop that binds a Ca(2+) ion with a high affinity. [The UniProt Consortium]