Home / SPARC / Human SPARC/Osteonectin Biotinylated Antibody

Human SPARC/Osteonectin Biotinylated Antibody

Catalog #: BAF941
2 Citations Datasheet / COA / SDS
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BAF941
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Citations (2)
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Human SPARC/Osteonectin Biotinylated Antibody Summary

Species Reactivity
Human
Specificity
Detects human SPARC in Western blots. In Western blots, less than 1% cross-reactivity with recombinant mouse SPARC is observed.
Source
Polyclonal Goat IgG
Purification
Antigen Affinity-purified
Immunogen
Mouse myeloma cell line NS0-derived recombinant human SPARC/Osteonectin
Ala18-Ile303
Accession # P09486
Formulation
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Label
Biotin

Applications

Recommended Concentration
Sample
Western Blot
0.1 µg/mL
Recombinant Human SPARC/Osteonectin (Catalog # 941-SP)
Intracellular Staining by Flow Cytometry
2.5 µg/106 cells
MG‑63 human osteosarcoma cell line fixed with paraformaldehyde and permeabilized with saponin

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.

Reconstitution Calculator

Reconstitution Calculator

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Preparation and Storage

Reconstitution
Reconstitute at 0.2 mg/mL in sterile PBS.
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Shipping
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
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 transistion; 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

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Citations for Human SPARC/Osteonectin Biotinylated Antibody

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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  1. Elevated plasma SPARC levels are associated with insulin resistance, dyslipidemia, and inflammation in gestational diabetes mellitus.
    Authors: Xu, Lu, Ping, Fan, Yin, Jinhua, Xiao, Xinhua, Xiang, Hongding, Ballantyne, Christie, Wu, Huaizhu, Li, Ming
    PLoS ONE, 2013-12-09;8(12):e81615.
    Species: Human
    Sample Types: Plasma
    Applications: ELISA Development
  2. 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, 2006-06-01;53(8):845-57.
    Species: Human
    Sample Types: Cell Culture Supernates
    Applications: ELISA Development

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