Human SPARC Alexa Fluor® 700-conjugated Antibody

Catalog #: IC941N Datasheet / COA / SDS

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IC941N-100UG

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Human SPARC Alexa Fluor® 700-conjugated Antibody Summary

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

Supplied 0.2 mg/mL in a saline solution containing BSA and Sodium Azide.

Label

Alexa Fluor 700 (Excitation= 675-700 nm, Emission= 723 nm)

Applications

Recommended Concentration

Sample

Intracellular Staining by Flow Cytometry

0.25-1 µg/10⁶ cells

HT1080 human fibrosarcoma cell line fixed with Flow Cytometry Fixation Buffer (Catalog # FC004) and permeabilized with Flow Cytometry Permeabilization/Wash Buffer I (Catalog # FC005)

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

Preparation and Storage

Shipping

The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.

Stability & Storage

Store the unopened product at 2 - 8 °C. Do not use past expiration date.

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

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.

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

Product Datasheets

Product Datasheet

COA

SDS

Product Specific Notices

This product is provided under an agreement between Life Technologies Corporation and R&D Systems, Inc, and the manufacture, use, sale or import of this product is subject to one or more US patents and corresponding non-US equivalents, owned by Life Technologies Corporation and its affiliates. The purchase of this product conveys to the buyer the non-transferable right to use the purchased amount of the product and components of the product only in research conducted by the buyer (whether the buyer is an academic or for-profit entity). The sale of this product is expressly conditioned on the buyer not using the product or its components (1) in manufacturing; (2) to provide a service, information, or data to an unaffiliated third party for payment; (3) for therapeutic, diagnostic or prophylactic purposes; (4) to resell, sell, or otherwise transfer this product or its components to any third party, or for any other commercial purpose. Life Technologies Corporation will not assert a claim against the buyer of the infringement of the above patents based on the manufacture, use or sale of a commercial product developed in research by the buyer in which this product or its components was employed, provided that neither this product nor any of its components was used in the manufacture of such product. For information on purchasing a license to this product for purposes other than research, contact Life Technologies Corporation, Cell Analysis Business Unit, Business Development, 29851 Willow Creek Road, Eugene, OR 97402, Tel: (541) 465-8300. Fax: (541) 335-0354.