SPARC Antibody (122511) [Alexa Fluor® 594]

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Flow
Clone
122511
Clonality
Monoclonal
Host
Mouse
Conjugate
Alexa Fluor 594
Concentration
Please see the vial label for concentration. If unlisted please contact technical services.

SPARC Antibody (122511) [Alexa Fluor® 594] Summary

Immunogen
Mouse myeloma cell line NS0-derived recombinant human SPARC
Ala18-Ile303
Accession # P09486
Specificity
Detects human SPARC/Osteonectin in direct ELISAs. In direct ELISAs, no cross-reactivity with recombinant mouse SPARC/Osteonectin is observed.
Isotype
IgG1
Clonality
Monoclonal
Host
Mouse
Gene
SPARC
Innovator's Reward
Test in a species/application not listed above to receive a full credit towards a future purchase.

Applications/Dilutions

Dilutions
  • Intracellular Staining by Flow Cytometry 0.25-1 ug/10^6 cells
Application Notes
Flow Cytometry: Please use 0.25-1 ug of conjugated antibody per 10e6 cells.

Packaging, Storage & Formulations

Storage
Store the unopened product at 2 - 8 °C. Do not use past expiration date.
Buffer
Supplied 0.2 mg/mL in a saline solution containing BSA and Sodium Azide.
Preservative
0.09% Sodium Azide
Concentration
Please see the vial label for concentration. If unlisted please contact technical services.

Notes

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
  • BM-40
  • ONcysteine-rich protein
  • Osteonectin
  • Secreted protein acidic and rich in cysteine
  • secreted protein, acidic, cysteine-rich (osteonectin)
  • SPARC

Background

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.

  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.

Limitations

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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Bioinformatics Tool for SPARC Antibody (IC941T)

Discover related pathways, diseases and genes to SPARC Antibody (IC941T). Need help? Read the Bioinformatics Tool Guide for instructions on using this tool.
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Blogs on SPARC.

Caspase 8 - a key mediator of apoptosis
Programmed cell death via apoptosis is a key controlled physiological process instigated by the cell death receptor family, their ligands, and the caspase cysteine protease family. All caspases exist in a precursor form that contains a prodomain, a...  Read full blog post.

GAPDH: More than a housekeeping gene
GAPDH is a 146kD tetramer glycolytic pathway metabolic enzyme composed of four 30-40 kDa subunits. It is responsible for reversibly phosphorylating its substrate glyceraldehyde 3-phosphate within the glycolytic pathway.  Apart from its role in gl...  Read full blog post.

GAPDH (Glyceraldehyde 3-Phosphate Dehydrogenase)
GAPDH is a 146 kD tetramer glycolytic pathway metabolic enzyme responsible for reversibly phosphorylating glyceraldehyde 3-phosphate. It may have other possible functions in transcriptional activation. GAPDH is highly expressed due to this housekeepin...  Read full blog post.

FLICE, FLICE, baby
Cell death via apoptosis is a fundamental cellular function triggered by the cell death receptor family and their ligands which signal through downstream adaptor molecules and the caspase protease family. All caspases exist in a precursor form compose...  Read full blog post.

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Bioinformatics

Gene Symbol SPARC
Uniprot