Anti-SPARC

0.5mg/ml if reconstituted with 0.2ml sterile DI water. SPARC, secreted protein acidic and rich in cysteine , also known as Osteonectin is a protein that in humans is encoded by the SPARC gene. The human SPARC gene is 26.5 kb long, and contains 10 exons and 9 introns and is located on chromosome 5q31-q33. SPARC is a glycoprotein of ~40 kDa. SPARC is an acidic, cysteine-rich glycoprotein consisting of a single polypeptide chain that can be broken into 4 domains: 1) an Ca++ binding domains near the glutamic acidic-rich region at the amino terminus (domain I), 2) a cysteine- rich (domain II), 3) a hydrophilic region (domain III) and 4) an EF hand motif at the carboxy terminus region (domain IV). Osteonectin is a glycoprotein in the bone that binds sodium. It is secreted by osteoblasts during bone formation, initiating mineralization and promoting mineral crystal formation. Osteonectin also shows affinity for collagen in addition to bone mineral calcium. A correlation between osteonectin over expression and ampullary cancers and chronic pancreatitis has been found. 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]