<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
103 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
100-145 kDa, reducing conditions
Publications
Read Publication using 8390-TH in the following applications:
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 Sodium Acetate, NaCl and CHAPS.
Purity
>90%, by SDS-PAGE with silver staining.
Reconstitution Instructions
Reconstitute at 200 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 Thrombospondin-3 Protein, CF
MGC119565
THBS3
thrombospondin 3
Thrombospondin3
Thrombospondin-3
TSP3
TSP3MGC119564
Background
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.
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