SPARC Protein
Quick Overview for SPARC Protein (ABIN925110)
Target
See all SPARC ProteinsProtein Type
Origin
Host
Purity
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Characteristics
- Cellular Localization: Bone, platelets, plasma (0.9 µg/mLl), serum (2.6 µg/mL).
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Secreted Protein, Acidic, Cysteine-Rich (Osteonectin) (SPARC) (AA 18-303) protein (His tag)
SPARC Origin: Human Host: HEK-293 Cells Recombinant > 95 % as determined by Tris-Bis PAGE,> 95 % as determined by HPLC
Secreted Protein, Acidic, Cysteine-Rich (Osteonectin) (SPARC) (AA 18-303) protein (His tag)SPARC Origin: Cynomolgus Host: HEK-293 Cells Recombinant > 95 % as determined by Tris-Bis PAGE,> 95 % as determined by HPLC
Secreted Protein, Acidic, Cysteine-Rich (Osteonectin) (SPARC) (AA 18-302) protein (His tag)SPARC Origin: Mouse Host: HEK-293 Cells Recombinant > 95 % as determined by Tris-Bis PAGE,> 95 % as determined by HPLC
Secreted Protein, Acidic, Cysteine-Rich (Osteonectin) (SPARC) (AA 18-297) protein (His tag)SPARC Origin: Human Host: Escherichia coli (E. coli) Recombinant Greater than 95 % as determined by SDS-PAGE WB, ELISA
Secreted Protein, Acidic, Cysteine-Rich (Osteonectin) (SPARC) protein (Fc Tag)SPARC Origin: Human Host: HEK-293 Cells Recombinant The purity of the protein is greater than 95 % as determined by SDS-PAGE and Coomassie blue staining.
Secreted Protein, Acidic, Cysteine-Rich (Osteonectin) (SPARC) (AA 1-303) protein (GST tag)SPARC Origin: Human Host: Wheat germ Recombinant WB, ELISA, AP, AA
Secreted Protein, Acidic, Cysteine-Rich (Osteonectin) (SPARC) (AA 18-303), (full length) protein (GST tag)SPARC Origin: Human Host: Escherichia coli (E. coli) Recombinant 90 % ELISA
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Restrictions
- For Research Use only
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Format
- Liquid
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Buffer
- Supplied as solution in 0.02 M Tris, 0.15 M NaCl, pH 7.4.
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Storage
- -80 °C
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- SPARC (Secreted Protein, Acidic, Cysteine-Rich (Osteonectin) (SPARC))
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Alternative Name
- Osteonectin
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Background
- Osteonectin is an acidic, noncollagenous glycoprotein originally isolated from fetal and adult bovine bone matrix. In vitro bovine bone osteonectin binds type I collagen, calcium (Kd=3x10 -7 M) and hydroxyapatite (Kd=8x10 -8 M) and has been shown to be a potent inhibitor of hydroxyapatite-seeded crystal growth. In this context it has been suggested that osteonectin may play an important role in the regulation of bone metabolism by binding hydroxyapatite to collagen. Recently, proteins homologous to osteonectin have been identified in a number of cell types, most of which are associated with extracellular matrix production. The amino acid sequence (from cDNA sequences) of one of these proteins, human placental SPARC is identical to human bone osteonectin. Osteonectin has also been identified as an alpha granule component of human platelets and is secreted during activation. A small portion of the secreted osteonectin is expressed on the platelet cell surface in an activation dependent manner. Purified platelet osteonectin is a single chain molecule which exhibits a slightly larger apparent molecular weight than that of osteonectin derived from bone. The NH2- terminal sequences of platelet- and bone- derived osteonectin are identical, but the two proteins differ with regard to the extent of glycosylation.
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Molecular Weight
- 29,000 (by sedimentation equilibrium)
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Pathways
- Autophagy
Target
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