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Recombinant Human SPARC Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human SPARC Protein, CF Summary

Details of Functionality
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 0.75-3.0 µg/mL.
Source
Mouse myeloma cell line, NS0-derived human SPARC protein
Ala18-Ile303, with a C-terminal 10-His tag
Accession #
N-terminal Sequence
Ala18
Protein/Peptide Type
Recombinant Proteins
Gene
SPARC
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
34 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
40-50 kDa, reducing conditions
Publications
Read Publications using
941-SP in the following applications:

Packaging, Storage & Formulations

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.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human SPARC Protein, CF

  • 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 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.

  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.

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Publications for SPARC (941-SP)(7)

We have publications tested in 2 confirmed species: Human, Rat.

We have publications tested in 4 applications: Bioassay, ELISA Developmet, In Vivo, Surface Plasmon Resonance.


Filter By Application
Bioassay
(4)
ELISA Developmet
(1)
In Vivo
(1)
Surface Plasmon Resonance
(1)
All Applications
Filter By Species
Human
(5)
Rat
(2)
All Species
Showing Publications 1 - 7 of 7.
Publications using 941-SP Applications Species
T Okada, H Suzuki, ZD Travis, O Altay, J Tang, JH Zhang SPARC Aggravates Blood-Brain Barrier Disruption via Integrin alphaVbeta3/MAPKs/MMP-9 Signaling Pathway after Subarachnoid Hemorrhage Oxidative Medicine and Cellular Longevity, 2021-11-11;2021(0):9739977. 2021-11-11 [PMID: 34804372] (In Vivo, Rat) In Vivo Rat
Chih-Hau Chang, Meng-Chi Yen, Ssu-Hui Liao, Yu-Ling Hsu, Chung-Sheng Lai, Kao-Ping Chang, Ya-Ling Hsu Secreted Protein Acidic and Rich in Cysteine (SPARC) Enhances Cell Proliferation, Migration, and Epithelial Mesenchymal Transition, and SPARC Expression is Associated with Tumor Grade in Head and Neck Cancer. International Journal of Molecular Sciences, 2017-07-18;0(0):1422-0067. 2017-07-18 [PMID: 28718842] (Bioassay, Human) Bioassay Human
SPARC expression by cerebral microvascular endothelial cells in vitro and its influence on blood-brain barrier properties J Neuroinflammation, 2016-08-31;13(1):225. 2016-08-31 [PMID: 27581191] (Bioassay, Human) Bioassay Human
Aguilera K, Rivera L, Hur H, Carbon J, Toombs J, Goldstein C, Dellinger M, Castrillon D, Brekken R Collagen signaling enhances tumor progression after anti-VEGF therapy in a murine model of pancreatic ductal adenocarcinoma. Cancer Res, 2013-12-17;74(4):1032-44. 2013-12-17 [PMID: 24346431] (ELISA Developmet, Rat) ELISA Developmet Rat
Giallongo C, La Cava P, Tibullo D, Barbagallo I, Parrinello N, Cupri A, Stagno F, Consoli C, Chiarenza A, Palumbo G, Di Raimondo F SPARC expression in CML is associated to imatinib treatment and to inhibition of leukemia cell proliferation. BMC Cancer, 2013-02-05;13(0):60. 2013-02-05 [PMID: 23383963] (Bioassay, Human) Bioassay Human
Brellier F, Ruggiero S, Zwolanek D, Martina E, Hess D, Brown-Luedi M, Hartmann U, Koch M, Merlo A, Lino M, Chiquet-Ehrismann R SMOC1 is a tenascin-C interacting protein over-expressed in brain tumors. Matrix Biol., 2011-02-21;30(3):225-33. 2011-02-21 [PMID: 21349332] (Surface Plasmon Resonance, Human) Surface Plasmon Resonance Human
Kirouac DC, Ito C, Csaszar E, Roch A, Yu M, Sykes EA, Bader GD, Zandstra PW Dynamic interaction networks in a hierarchically organized tissue. Mol. Syst. Biol., 2010-10-05;6(0):417. 2010-10-05 [PMID: 20924352] (Bioassay, Human) Bioassay Human

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Bioinformatics

Gene Symbol SPARC
Uniprot