SPARC Antibody (122511) [Alexa Fluor® 594] Summary
Mouse myeloma cell line NS0-derived recombinant human SPARC
Accession # P09486
Detects human SPARC/Osteonectin in direct ELISAs. In direct ELISAs, no cross-reactivity with recombinant mouse SPARC/Osteonectin is observed.
Test in a species/application not listed above to receive a full credit towards a future purchase.
- Intracellular Staining by Flow Cytometry 0.25-1 ug/10^6 cells
Flow Cytometry: Please use 0.25-1 ug of conjugated antibody per 10e6 cells.
Packaging, Storage & Formulations
Store the unopened product at 2 - 8 °C. Do not use past expiration date.
Supplied 0.2 mg/mL in a saline solution containing BSA and Sodium Azide.
0.09% Sodium Azide
Please see the vial label for concentration. If unlisted please contact technical services.
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for SPARC Antibody (122511) [Alexa Fluor® 594]
- Basement-membrane protein 40
- ONcysteine-rich protein
- Secreted protein acidic and rich in cysteine
- secreted protein, acidic, cysteine-rich (osteonectin)
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 286 amino acid (aa), 43 kDa protein contains an N-terminal acidic region that binds calcium, a follistatin domain that contains Kazal-like sequences, and a C-terminal extracellular calcium (EC) binding domain with two EF-hand motifs (1-5). Crystal structure modeling 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 undergoing an endothelial to mesenchymal transition; its expression, however, mainly decreases the likelihood of metastasis and confers sensitivity to chemotherapy and radiation (4, 9-11). 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 (12). Mature human SPARC shows 92%, 92%, 97%, 99%, 96% and 85% aa identity with mouse, rat, canine, bovine, porcine and chick SPARC, respectively.
- Lankat-Buttgereit, B. et al. (1988) FEBS Lett. 236:352.
- Sweetwyne, M. T. et al. (2004) J. Histochem. Cytochem. 52:723.
- Sage, H. et al. (1989) J. Cell Biol. 109:341.
- Framson, P. E. and E. H. Sage (2004) J. Cell. Biochem. 92:679.
- Alford, A. I. and K. D. Hankenson (2006) Bone 38:749.
- Hohenester, E et al. (1997) EMBO J. 16:3778.
- Sage, E. H. et al. (2003) J. Biol. Chem. 278:37849.
- Delany, A. M. et al. (2003) Endocrinology 144:2588.
- Robert, G. et al. (2006) Cancer Res. 66:7516.
- Koblinski, J. E. et al. (2005) Cancer Res. 65:7370.
- Tai, I. T. et al. (2005) J. Clin. Invest. 115:1492.
- Kzhyshkowska, J. et al. (2006) J. Immunol. 176:5825.
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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