Recombinant Human Thrombospondin-2 His-tag (Catalog # 1635-T2) supports the adhesion of SVEC4-10 vascular endothelial cells. The ED50 for this effect is 0.07-0.7 μg/mL.
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<1.0 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
170-176 kDa, reducing conditions
Publications
Read Publications using 1635-T2 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 MES and NaCl.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 100 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-2 Protein, CF
THBS2
thrombospondin 2
Thrombospondin2
Thrombospondin-2
TSP-2
TSP2thrombospondin-2
Background
Thrombospondin-2 (TSP-2) is a 150 kDa calcium-binding protein that modulates cellular interactions with extracellular matrix. Thrombospondin-1 and -2 constitute subgroup A thrombospondin family members and form disulfide-linked homotrimers, whereas Thrombospondin-3, -4, and -5/COMP constitute subgroup B and form homopentamers (1‑4). The human TSP-2 cDNA encodes a 1172 amino acid (aa) precursor that includes an 18 aa signal sequence followed by an N-terminal heparin‑binding domain, an oligomerization motif, one vWF-C domain, three TSP type-1 repeats, three EGF-like repeats, seven TSP type-3 repeats, and a lectin-like TSP C‑terminal domain (5). Human TSP-2 shares 88‑90% aa sequence identity with bovine, mouse, and rat TSP-2. Within the TSP type-3 repeats and TSP C-terminal domain, human TSP-2 shares 80% aa sequence identity with human TSP-1 and approximately 60% aa sequence identity with human TSP-3, -4, and -5/COMP. TSP-2 regulates collagen matrix formation by altering fibroblast behavior during development and in areas of tissue remodeling in the adult (6, 7). Trimerization of TSP-2 is required for the calcium-dependent cell attachment and spreading functions, while the heparin‑binding domain is responsible for the destabilization of focal adhesion sites (8‑10). The heparin‑binding domain also mediates binding to Integrins alpha 3 beta 1 and alpha 6 beta 1 on microvascular endothelial cells (EC) and Integrin alpha 4 beta 1 on large blood vessel EC (11, 12). A fragment of TSP-2 (heparin‑binding domain, oligomerization motif, and vWF-C domain) promotes EC survival, proliferation, and chemotaxis (11). Inclusion of the three TSP type-1 domains results in a molecule that inhibits VEGF-induced EC migration and vascular tube formation (13, 14). In vivo, full length TSP-2 blocks tumor angiogenesis and induces vascular EC apoptosis (13, 15). HPRG functions as an apparent decoy receptor by preventing interaction of TSP-2 with CD36 on macrophages and microvasculature EC (14). TSP-2 also binds MMP-2 and facilitates MMP-2 clearance by the scavenger receptor LRP (16).
Elzie, C.A. and J.E. Murphy-Ullrich (2004) Int. J. Biochem. Cell Biol. 36:1090.
Armstrong, L.C. and P. Bornstein (2003) Matrix Biol. 22:63.
Murphy-Ullrich, J.E. (2001) J. Clin. Invest. 107:785.
Bornstein, P. and E.H. Sage (2002) Curr. Opin. Cell Biol. 14:608.
LaBell, T.L. and P.H. Byers (1993) Genomics 17:225.
Kyriakides, T.R. et al. (1998) J. Histochem. Cytochem. 46:1007.
Kyriakides, T.R. et al. (1998) J. Cell Biol. 140:419.
Anilkumar, N. et al. (2002) J. Cell Sci. 115:2357.
Misenheimer, T.M. et al. (2003) Biochemistry 42:5125.
Murphy-Ullrich, J.E. et al. (1993) J. Biol. Chem. 268:26784.
Calzada, M.J. et al. (2004) Circ. Res. 94:462.
Calzada, M.J. et al. (2003) J. Biol. Chem. 278:40679.
Noh, Y.-H. et al. (2003) J. Invest. Dermatol. 121:1536.
Simantov, R. et al. (2005) Matrix Biol. 24:27.
Streit, M. et al. (1999) Proc. Natl. Acad. Sci. 96:14888.
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