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Recombinant Mouse SPARC Protein, CF

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Product Details

Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Mouse 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 0.6‑2.4 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
Ala18
Protein/Peptide Type
Recombinant Proteins
Gene
Sparc
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
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
42 kDa, reducing conditions
Publications
Read Publications using
942-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 under reducing conditions and visualized by silver stain
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 Mouse 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 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.

  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.

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Publications for SPARC (942-SP)(6)

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

We have publications tested in 2 applications: Bioassay, Cell Culture.


Filter By Application
Bioassay
(5)
Cell Culture
(1)
All Applications
Filter By Species
Human
(1)
Mouse
(5)
All Species
Showing Publications 1 - 6 of 6.
Publications using 942-SP Applications Species
L Hu, F He, M Huang, Q Zhao, L Cheng, N Said, Z Zhou, F Liu, YS Dai SPARC promotes insulin secretion through down-regulation of RGS4 protein in pancreatic &amp;beta cells Sci Rep, 2020-10-16;10(1):17581. 2020-10-16 [PMID: 33067534] (Cell Culture, Mouse) Cell Culture Mouse
B John, C Naczki, C Patel, A Ghoneum, S Qasem, Z Salih, N Said Regulation of the bi-directional cross-talk between ovarian cancer cells and adipocytes by SPARC Oncogene, 2019-02-14;0(0):. 2019-02-14 [PMID: 30765860] (Bioassay, Mouse) Bioassay Mouse
EV Jones, Y Bernardine, JG Zarruk, S Chierzi, KK Murai SPARC and GluA1-Containing AMPA Receptors Promote Neuronal Health Following CNS Injury Front Cell Neurosci, 2018-02-01;12(0):22. 2018-02-01 [PMID: 29449802] (Bioassay, Mouse) Bioassay Mouse
A Melouane, A Carbonell, M Yoshioka, J Puymirat, J St-Amand Implication of SPARC in the modulation of the extracellular matrix and mitochondrial function in muscle cells PLoS ONE, 2018-02-08;13(2):e0192714. 2018-02-08 [PMID: 29420632] (Bioassay, Mouse) Bioassay Mouse
Luo Z, Zhou Y, Luo P, Zhao Q, Xiao N, Yu Y, Yan Q, Lu G, Cheng L SPARC deficiency affects bone marrow stromal function, resulting in impaired B lymphopoiesis. J Leukoc Biol, 2014-03-05;96(1):73-82. 2014-03-05 [PMID: 24598056] (Bioassay, Mouse) Bioassay Mouse
Jones EV, Bernardinelli Y, Tse YC, Chierzi S, Wong TP, Murai KK Astrocytes control glutamate receptor levels at developing synapses through SPARC-beta-integrin interactions. J. Neurosci., 2011-03-16;31(11):4154-65. 2011-03-16 [PMID: 21411656] (Bioassay, Human) Bioassay Human

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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