Osteonectin, Recombinant, Human (SPARC, Secreted Protein, Acidic, Cysteine-rich, ON, OSN, BM-40)

SPARC/Osteonectin is a secreted, evolutionarily conserved collagen-binding glycoprotein that is involved in a variety of cellular activities.It is highly expressed in tissues undergoing morphogenesis, remodeling and wound repair.SPARC/Osteonectin and its related peptides bind to numerous proteins of the extracellular matrix (ECM), affect ECM protein expression, influence cellular adhesion and migration, and modulate growth factor-induced cell proliferation and angiogenesis.SPARC/Osteonectin consists of three domains an N-terminal acidic region that binds calcium ions with low affinity, a module containing two EF-hand motifs that bind calcium with high affinity, and a cysteine-rich follistatin-like domain. Recombinant human SPARC/Osteonectin is a glycoprotein containing 286 amino acids that migrates at an apparent MW of 43.7kD by SDS-PAGE analysis due to the effect of glycosylation.\n\nBiological Activity:\nDetermined by its ability to increase alkaline phosphatase activity in differentiating MC3T3 cells using a concentration of 0.5-0.7ug/ml.\n\nAA Sequence:\nAPQQEALPDE TEVVEETVAE VTEVSVGANP VQVEVGEFDD GAEETEEEVV AENPCQNHHC KHGKVCELDE NNTPMCVCQD PTSCPAPIGE FEKVCSNDNK TFDSSCHFFA TKCTLEGTKK GHKLHLDYIG PCKYIPPCLD SELTEFPLRM RDWLKNVLVT LYERDEDNNL LTEKQKLRVK KIHENEKRLE AGDHPVELLA RDFEKNYNMY IFPVHWQFGQ LDQHPIDGYL SHTELAPLRA PLIPMEHCTT RFFETCDLDN DKYIALDEWA GCFGIKQKDI DKDLVI\n\nQuality Control:\nVerified by N-terminal and Mass Spectrometry analyses (when applicable).\n\nEndotoxin:\n<0.1ng/ug of protein (<1EU/ug).\n\nProtein Content:\nVerified by UV Spectroscopy and/or SDS-PAGE gel.\n\nStorage and Stability:\nStore lyophilized products at -20 degrees C. For reconstituted solutions of most products, we recommend short-term storage at 4 degrees C. For longer term storage the protein solution should be stored with a carrier protein (eg. 0.1% BSA) in working aliquots and stored frozen at -20 degrees C. Additional freeze/thaw cycles may cause some denaturation of the protein.

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