Measured by the ability of the immobilized protein to support the adhesion of SVEC4‑10 mouse vascular endothelial cells. The ED50 for this effect is 0.1-0.5 μg/mL.
Source
Mouse myeloma cell line, NS0-derived mouse Thrombospondin-1 protein
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
129 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
130-155 kDa, reducing conditions
Publications
Read Publications using 7859-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 PBS.
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse Thrombospondin-1 Protein, CF
THBS
THBS1
THBS-1
thrombospondin 1
Thrombospondin1
Thrombospondin-1
thrombospondin-1p180
TSP-1
TSP1thrombospondin-1
TSPTSP-1
Background
Thrombospondin‑1 (TSP‑1) is a 150‑180 kDa calcium‑sensitive protein that is secreted as a disulfide‑linked homotrimer. Within the Thrombospondin family, TSP‑2 is also homotrimeric, while TSP-3, -4, and -5/COMP are pentameric. TSP‑1 regulates a wide range of cellular functions including their interactions with other cells and with the extracellular matrix (ECM). TSP-1 contains an N‑terminal Laminin G‑like globular domain, an extended central region with one vWF‑C domain, 3 TSP type 1 repeats, 3 EGF‑like domains, and 8 TSP type‑3 repeats, and a globular C‑terminal lectin domain. Distinct regions of TSP‑1 have been associated with binding to particular ECM or cellular molecules (1, 2). Mature mouse TSP‑1 shares 95% and 99% amino acid sequence identity with human and rat TSP‑1, respectively. TSP‑1 counteracts the angiogenic, hypotensive, and anti‑thrombotic effects of nitric oxide (NO) (3). It binds and neutralizes VEGF, blocks VEGF R2 signaling on vascular endothelial cells (EC), and destabilizes adhesive contacts between EC (4‑6). TSP‑1’s actions on vascular smooth muscle cells support arterial tone and blood pressure in the presence of vasodilatory stimulation (7). It is released from activated platelets and enhances platelet aggregation and adhesion (8). TSP-1 also plays an important role in wound repair and tissue fibrosis by binding latent TGF‑beta and inducing release of the active cytokine from the latency associated peptide (LAP) (9, 10). TSP‑1 dampens adaptive immune responses by inducing the differentiation of regulatory T cells and inhibiting TCR signaling (11, 12). In the nervous system, it promotes excitatory synapse formation (13, 14) and supports the integration of neural progenitor cells into the olfactory bulb (15). In addition, TSP‑1 is released by apoptotic cells and promotes macrophage-mediated debris clearance (16).
Murphy-Ullrich, J.E. and R.V. Iozzo (2012) Matrix Biol. 31:152.
Laherty, C.D. et al. (1992) J. Biol. Chem. 267:3274.
Roberts, D.D. et al. (2012) Matrix Biol. 31:162.
Gupta, K. et al. (1999) Angiogenesis 3:147.
Kaur, S. et al. (2010) J. Biol. Chem. 285:38923.
Garg, P. et al. (2011) Am. J. Physiol. Lung Cell. Mol. Physiol. 301:L79.
Isenberg, J.S. et al. (2009) Matrix Biol. 28:110.
Isenberg, J.S. et al. (2008) Blood 111:613.
Schultz-Cherry, S. et al. (1994) J. Biol. Chem. 269:26775.
Sweetwyne, M.T. and J.E. Murphy-Ullrich (2012) Matrix Biol. 31:178.
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