Recombinant Human Thrombospondin-3 Protein, CF Summary
Product Specifications
Ser22-Val956 with a C-terminal 10-His tag
Analysis
Product Datasheets
Carrier Free
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.
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.
8390-TH
| Formulation | Lyophilized from a 0.2 μm filtered solution in Sodium Acetate, NaCl and CHAPS. |
| Reconstitution | Reconstitute at 200 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.
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Reconstitution Calculator
Background: Thrombospondin-3
Thrombospondin-3 (TSP-3) is a 140-150 kDa heparin-binding protein in the thrombospondin family of matricellular adhesion proteins. Within this family, TSP-3, TSP-4, and TSP-5/COMP are secreted as pentamers, while TSP-1 and TSP-2 are homotrimeric (1). TSP-3 contains an N-terminal Laminin G-like globular domain, a flexible linker region, multiple tandem EGF-like repeats, multiple tandem TSP type-3 repeats, and a globular TSP C-terminal domain (2). Alternative splicing of human TSP-3 generates a short isoform with a deletion of approximately half of the Laminin-like domain and a portion of the linker. Mature human TSP-3 shares 98% and 97% amino acid sequence identity with mouse and rat TSP-3, respectively. In the disulfide-linked TSP-3 pentamer, the Laminin-like domains are clustered while the C-terminal globular domains are extended (3). TSP-3 is expressed during mouse embryogenesis in the brain, dorsal root ganglia, cartilage, lung, and gut (4, 5). In postnatal mice it is most highly expressed in the lung (6). TSP-3 is involved in the columnar organization of chondrocytes in developing growth plates of long bones (7). It is up-regulated in metastatic osteosarcoma and in the corneal stroma during wound healing (8, 9).
- Murphy-Ullrich, J.E. and R.V. Iozzo (2012) Matrix Biol. 31:152.
- Adolph, K.W. et al. (1995) Genomics 27:329.
- Qabar, A. et al. (1995) J. Biol. Chem. 270:12725.
- Iruela-Arispe, M.L. et al. (1993) Dev. Dyn. 197:40.
- Qabar, A. et al. (1994) J. Biol. Chem. 269:1262.
- Vos, H.L. et al. (1992) J. Biol. Chem. 267:12192.
- Posey, K.L. et al. (2008) Am. J. Pathol. 172:1664.
- Dalla-Torre, C.A. et al. (2006) BMC Cancer 6:237.
- Armstrong, D.J. et al. (2002) Int. J. Biochem. Cell Biol. 34:588.
Citation for Recombinant Human Thrombospondin-3 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.
1 Citation: Showing 1 - 1
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Thrombospondin-3 augments injury-induced cardiomyopathy by intracellular integrin inhibition and sarcolemmal instability
Authors: TG Schips, D Vanhoutte, A Vo, RN Correll, MJ Brody, H Khalil, J Karch, A Tjondrokoe, MA Sargent, M Maillet, RS Ross, JD Molkentin
Nat Commun, 2019-01-08;10(1):76.
Species: Human, Rat
Sample Types: Recombinant Protein, Whole Cells
Applications: Bioassay
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