Detection of Mouse SPARC by Western Blot.
Western blot shows lysates of C2C12 mouse myoblast cell line and mouse placenta tissue. PVDF membrane was probed with 2 µg/mL of Rat Anti-Mouse SPARC Monoclonal Antibody (Catalog # MAB942) followed by HRP-conjugated Anti-Rat IgG Secondary Antibody (Catalog # HAF005). A specific band was detected for SPARC at approximately 35-37 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
SPARC/Osteonectin in Mouse Ovary.
SPARC/Osteonectin was detected in perfusion fixed frozen sections of mouse ovary using Mouse SPARC/Osteonectin Monoclonal Antibody (Catalog # MAB942) at 25 µg/mL overnight at 4 °C. Tissue was stained using the Anti-Rat HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS017) and counterstained with hematoxylin (blue). View our protocol for Chromogenic IHC Staining of Frozen Tissue Sections.
Preparation and Storage
Reconstitute at 0.5 mg/mL in sterile PBS.
Reconstitution Buffer Available
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
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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Delany, A.M. et al. (2003) Endocrinology 144:2588.
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Secreted Protein Acidic and Rich in Cysteine
Entrez Gene IDs:
6678 (Human); 20692 (Mouse)
Basement-membrane protein 40; BM-40; ONcysteine-rich protein; Osteonectin; Secreted protein acidic and rich in cysteine; secreted protein, acidic, cysteine-rich (osteonectin); SPARC
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