Recombinant Human SPARC Protein, CF

Catalog #: 941-SP
7 Citations 2 Reviews Datasheet

Catalog #	Availability	Size / Price	Qty
941-SP-050

R&D Systems Recombinant Proteins and Enzymes

1 Image

All SPARC Proteins and Enzymes

Product Details

Citations (7)

FAQs

Supplemental Products

Reviews (2)

Summary Product Datasheets Carrier Free Data Images Reconstitution Calculator Background Related Research Areas

Recombinant Human SPARC Protein, CF Summary

Product Specifications

Purity

>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

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 0.75-3.0 µg/mL.

Source

Mouse myeloma cell line, NS0-derived human SPARC protein
Ala18-Ile303, with a C-terminal 10-His tag

Accession #

NP_003109

N-terminal Sequence
Analysis

Ala18

Predicted Molecular Mass

34 kDa

SDS-PAGE

40-50 kDa, reducing conditions

Product Datasheets

941-SP

Product Datasheet

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.

941-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 at ambient temperature. 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 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.

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

Related Research Areas

Citations for Recombinant Human 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.

7 Citations: Showing 1 - 7
Filter your results:

Filter by:

SPARC Aggravates Blood-Brain Barrier Disruption via Integrin alphaVbeta3/MAPKs/MMP-9 Signaling Pathway after Subarachnoid Hemorrhage
Authors: T Okada, H Suzuki, ZD Travis, O Altay, J Tang, JH Zhang
Oxidative Medicine and Cellular Longevity, 2021-11-11;2021(0):9739977.
Species: Rat
Sample Types: In Vivo
Applications: In Vivo
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.
Authors: Chih-Hau Chang, Meng-Chi Yen, Ssu-Hui Liao, Yu-Ling Hsu, Chung-Sheng Lai, Kao-Ping Chang, Ya-Ling Hsu
International Journal of Molecular Sciences, 2017-07-18;0(0):1422-0067.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay
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.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay
Collagen signaling enhances tumor progression after anti-VEGF therapy in a murine model of pancreatic ductal adenocarcinoma.
Authors: Aguilera K, Rivera L, Hur H, Carbon J, Toombs J, Goldstein C, Dellinger M, Castrillon D, Brekken R
Cancer Res, 2013-12-17;74(4):1032-44.
Species: Rat
Sample Types: Protein
Applications: ELISA Developmet
SPARC expression in CML is associated to imatinib treatment and to inhibition of leukemia cell proliferation.
Authors: Giallongo C, La Cava P, Tibullo D, Barbagallo I, Parrinello N, Cupri A, Stagno F, Consoli C, Chiarenza A, Palumbo G, Di Raimondo F
BMC Cancer, 2013-02-05;13(0):60.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay
SMOC1 is a tenascin-C interacting protein over-expressed in brain tumors.
Authors: Brellier F, Ruggiero S, Zwolanek D, Martina E, Hess D, Brown-Luedi M, Hartmann U, Koch M, Merlo A, Lino M, Chiquet-Ehrismann R
Matrix Biol., 2011-02-21;30(3):225-33.
Species: Human
Sample Types: Recombinant Protein
Applications: Surface Plasmon Resonance
Dynamic interaction networks in a hierarchically organized tissue.
Authors: Kirouac DC, Ito C, Csaszar E, Roch A, Yu M, Sykes EA, Bader GD, Zandstra PW
Mol. Syst. Biol., 2010-10-05;6(0):417.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay