Recombinant Mouse SPARC Protein, CF

Catalog # Availability Size / Price Qty
942-SP-050
R&D Systems Recombinant Proteins and Enzymes
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Citations (6)
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Recombinant Mouse SPARC Protein, CF Summary

Product Specifications

Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
Measured by its ability to inhibit the cell growth of Mv1Lu mink lung epithelial cells. Schiemann, B.J. et al. (2003) Mol. Biol. Cell. 14:3977. The ED50 for this effect is 0.6‑2.4 µg/mL.
Optimal dilutions should be determined by each laboratory for each application.
Source
Mouse myeloma cell line, NS0-derived mouse SPARC protein
Ala18-Ile302, with a C-terminal 10-His tag
Accession #
N-terminal Sequence
Analysis
Ala18
Predicted Molecular Mass
34 kDa
SDS-PAGE
42 kDa, reducing conditions

Product Datasheets

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942-SP

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

942-SP

Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 100 μg/mL in sterile PBS.
Shipping The product is shipped with polar packs. 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.
  • 3 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 302 amino acid (aa), 43 kDa protein contains a 17 aa signal sequence, an N-terminal acidic region that binds calcium, a follistatin domain containing Kazal-like sequences, and a C-terminal extracellular calcium (EC) binding domain with two EF-hand motifs (1 - 5). Crystal structure 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, yet expression mainly decreases the likelihood of metastasis and confers sensitivity to chemotherapy and radiation (4, 9, 10). 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 (11). Mature mouse SPARC shows 97%, 92%, 92%, 92% and 83% aa identity with rat, human, dog, cow and chick SPARC, respectively.

References
  1. Lankat-Buttgereit, B. et al. (1988) FEBS Lett. 236:352.
  2. McVey, J.H. et al. (1988) J. Biol. Chem. 263:11111.
  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. Koblinski, J.E. et al. (2005) Cancer Res. 65:7370.
  10. Tai, I.T. et al. (2005) J. Clin. Invest. 115:1492.
  11. 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

Citations for Recombinant Mouse SPARC Protein, CF

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.

6 Citations: Showing 1 - 6
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  1. SPARC promotes insulin secretion through down-regulation of RGS4 protein in pancreatic &beta cells
    Authors: L Hu, F He, M Huang, Q Zhao, L Cheng, N Said, Z Zhou, F Liu, YS Dai
    Sci Rep, 2020-10-16;10(1):17581.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Cell Culture
  2. Regulation of the bi-directional cross-talk between ovarian cancer cells and adipocytes by SPARC
    Authors: B John, C Naczki, C Patel, A Ghoneum, S Qasem, Z Salih, N Said
    Oncogene, 2019-02-14;0(0):.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  3. Implication of SPARC in the modulation of the extracellular matrix and mitochondrial function in muscle cells
    Authors: A Melouane, A Carbonell, M Yoshioka, J Puymirat, J St-Amand
    PLoS ONE, 2018-02-08;13(2):e0192714.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  4. SPARC and GluA1-Containing AMPA Receptors Promote Neuronal Health Following CNS Injury
    Authors: EV Jones, Y Bernardine, JG Zarruk, S Chierzi, KK Murai
    Front Cell Neurosci, 2018-02-01;12(0):22.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  5. SPARC deficiency affects bone marrow stromal function, resulting in impaired B lymphopoiesis.
    Authors: Luo Z, Zhou Y, Luo P, Zhao Q, Xiao N, Yu Y, Yan Q, Lu G, Cheng L
    J Leukoc Biol, 2014-03-05;96(1):73-82.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  6. Astrocytes control glutamate receptor levels at developing synapses through SPARC-beta-integrin interactions.
    Authors: Jones EV, Bernardinelli Y, Tse YC, Chierzi S, Wong TP, Murai KK
    J. Neurosci., 2011-03-16;31(11):4154-65.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay

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Recombinant Mouse SPARC Protein, CF
By Anonymous on 01/09/2018
Application: Binding assay/Protein-protein interaction

Recombinant Mouse SPARC Protein, CF
By Emma Jones on 01/04/2018
Application: In vitro bioactivity in cell culture