Human SPARC Antibody

(2 citations)   
  • Species Reactivity
    Human
  • Specificity
    Detects human SPARC/Osteonectin in direct ELISAs. In direct ELISAs, no cross-reactivity with recombinant mouse SPARC/Osteonectin is observed.
  • Source
    Monoclonal Mouse IgG1 Clone # 122511
  • Purification
    Protein A or G purified from hybridoma culture supernatant
  • Immunogen
    Mouse myeloma cell line NS0-derived recombinant human SPARC
    Ala18-Ile303
    Accession # P09486
  • Formulation
    Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.
  • Label
    Unconjugated
Applications
  •  
    Recommended
    Concentration
    Sample
  • Immunohistochemistry
    8-25 µg/mL
    See below
  • CyTOF-ready
    Ready to be labeled using established conjugation methods. No BSA or other carrier proteins that could interfere with conjugation.
  • Intracellular Staining by Flow Cytometry
    0.25 µg/106 cells
    See below
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Data Examples
Immunohistochemistry
SPARC/Osteonectin in Human Ovary Cancer. SPARC/Osteonectin was detected in immersion fixed paraffin-embedded sections of human ovarian clear cell carcinoma tissue using Human SPARC/Osteonectin Monoclonal Antibody (Catalog # MAB941) at 25 µg/mL overnight at 4 °C. Tissue was stained using the Anti-Mouse HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS002) and counterstained with hematoxylin (blue). Lower panel shows a lack of labeling when primary antibodies are omitted and tissue is stained only with secondary antibody followed by incubation with detection reagents. View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.
Immunohistochemistry
SPARC/Osteonectin in Human Ovary Cancer Tissue. SPARC/Osteonectin was detected in immersion fixed paraffin-embedded sections of human ovarian clear cell carcinoma tissue using Human SPARC/Osteonectin Monoclonal Antibody (Catalog # MAB941) at 25 µg/mL overnight at 4 °C. Tissue was stained using the Anti-Mouse HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS002) and counterstained with hematoxylin (blue). View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.
Intracellular Staining by Flow Cytometry
Detection of SPARC in HT1080 Human Cell Line by Flow Cytometry. HT1080 human fibrosarcoma cell line was stained with Mouse Anti-Human SPARC Monoclonal Antibody (Catalog # MAB941, filled histogram) or isotype control antibody (Catalog # MAB002, open histogram), followed by Allophycocyanin-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # F0101B). To facilitate intracellular staining, cells were fixed with Flow Cytometry Fixation Buffer (Catalog # FC004) and permeabilized with Flow Cytometry Permeabilization/Wash Buffer I (Catalog # FC005). View our protocol for Staining Intracellular Molecules.
Preparation and Storage
  • Reconstitution
    Reconstitute at 0.5 mg/mL in sterile PBS.
  • Shipping
    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.
Background: SPARC

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.

  • References:
    1. Lankat-Buttgereit, B. et al. (1988) FEBS Lett. 236:352.
    2. Sweetwyne, M. T. et al. (2004) J. Histochem. Cytochem. 52:723.
    3. Sage, H. et al. (1989) J. Cell Biol. 109:341.
    4. Framson, P. E. and E. H. Sage (2004) J. Cell. Biochem. 92:679.
    5. Alford, A. I. and K. D. Hankenson (2006) Bone 38:749.
    6. Hohenester, E et al. (1997) EMBO J. 16:3778.
    7. Sage, E. H. et al. (2003) J. Biol. Chem. 278:37849.
    8. Delany, A. M. et al. (2003) Endocrinology 144:2588.
    9. Robert, G. et al. (2006) Cancer Res. 66:7516.
    10. Koblinski, J. E. et al. (2005) Cancer Res. 65:7370.
    11. Tai, I. T. et al. (2005) J. Clin. Invest. 115:1492.
    12. Kzhyshkowska, J. et al. (2006) J. Immunol. 176:5825.
  • Long Name:
    Secreted Protein Acidic and Rich in Cysteine
  • Entrez Gene IDs:
    6678 (Human); 20692 (Mouse)
  • Alternate Names:
    Basement-membrane protein 40; BM-40; ONcysteine-rich protein; Osteonectin; Secreted protein acidic and rich in cysteine; secreted protein, acidic, cysteine-rich (osteonectin); SPARC
Related Research Areas
Citations:

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

2 Citations: Showing 1 - 2
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Applications
Sample Type
  1. Insulin-like growth factor binding protein-4 (IGFBP-4) is a novel anti-angiogenic and anti-tumorigenic mediator secreted by dibutyryl cyclic AMP (dB-cAMP)-differentiated glioblastoma cells.
    Authors: Moreno MJ, Ball M, Andrade MF, McDermid A, Stanimirovic DB
    Glia, 2006;53(8):845-57.
    Species: Human
    Sample Type: Cell Culture Supernates
    Application: ELISA Development
  2. Biomarker discovery from pancreatic cancer secretome using a differential proteomic approach.
    Authors: Gronborg M, Kristiansen TZ, Iwahori A, Chang R, Reddy R, Sato N, Molina H, Jensen ON, Hruban RH, Goggins MG, Maitra A, Pandey A
    Mol. Cell Proteomics, 2006;5(1):157-71.
    Species: Human
    Sample Type: Cell Lysates
    Application: WB
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