<0.10 EU per 1 μg of the protein by the LAL method.
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.
100-145 kDa, reducing conditions
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.
Lyophilized from a 0.2 μm filtered solution in Sodium Acetate, NaCl and CHAPS.
>90%, by SDS-PAGE with silver staining.
Reconstitute at 200 μg/mL in sterile PBS.
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
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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PRODUCT AVAILABILITY: Update Regarding the Evolving COVID-19 Situation
Bio-Techne appreciates the critical role that you and our products and services play in research efforts to further scientific innovation and discovery. We are continually assessing our manufacturing and supplier capabilities during the COVID-19 situation and are implementing precautionary measures to ensure uninterrupted supply of products and services. Currently, and as we abide by local shelter in place orders across the world, we are fully operational and do not anticipate any material supply disruptions across our Bio-Techne brands and product lines. As the situation evolves, our goal is to utilize preventive measures to reduce the threat that COVID-19 poses to our ability to meet the needs of our customers globally.