Western blot shows lysates of C2C12 mouse myoblast cell line and mouse placenta tissue. PVDF membrane was probed with 0.2 µg/mL of Goat Anti-Mouse SPARC Antigen Affinity-purified Polyclonal Antibody (Catalog # ...read more
SPARC/Osteonectin was detected in immersion fixed frozen sections of mouse embryo (E15) using Mouse SPARC/Osteonectin Antigen Affinity-purified Polyclonal Antibody (Catalog # AF942) at 1.7 µg/mL overnight at 4 °C. ...read more
SPARC was detected in immersion fixed C2C12 mouse myoblast cell line using Goat Anti-Mouse SPARC Antigen Affinity-purified Polyclonal Antibody (Catalog # AF942) at 5 µg/mL for 3 hours at room temperature. Cells ...read more
SPARC, an acronym for “secreted protein, acidic and rich in cysteine”, is also known as osteonectin or BM-40 (1-5). It is the founding member of a family of secreted matricellular proteins with similar domain structure. The 302 amino acid (aa), 43 kDa protein contains a 17 aa signal sequence, an N-terminal acidic region that binds calcium, a follistatin domain containing Kazal-like sequences, and a C-terminal extracellular calcium (EC) binding domain with two EF-hand motifs (1-5). Crystal structure shows that residues implicated in cell binding, inhibition of cell spreading and disassembly of focal adhesions cluster on one face of SPARC, while a collagen binding epitope and an N-glycosylation site are opposite this face (6). SPARC is produced by fibroblasts, capillary endothelial cells, platelets, and macrophages, especially in areas of tissue morphogenesis and remodeling (3, 7). SPARC shows context-specific effects, but generally inhibits adhesion, spreading and proliferation, and promotes collagen matrix formation (3-5). For endothelial cells, SPARC disrupts focal adhesions and binds and sequesters PDGF and VEGF (3-5). SPARC is abundantly expressed in bone, where it promotes osteoblast differentiation and inhibits adipogenesis (5, 8). SPARC is potentially cleaved by metalloproteinases, producing an angiogenic peptide that includes the copper-binding sequence KGHK (7). Paradoxically, SPARC is highly expressed in many tumor types, yet expression mainly decreases the likelihood of metastasis and confers sensitivity to chemotherapy and radiation (4, 9, 10). Stabilin-1, which is expressed on alternately activated macrophages, is the first SPARC receptor to be identified. It binds the SPARC EC domain and mediates endocytosis for degradation (11). Mature mouse SPARC shows 97%, 92%, 92%, 92%, and 83% aa identity with rat, human, dog, cow, and chick SPARC, respectively.
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This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
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