Human Thrombospondin-2 Antibody Summary
Gly19-Ile1172
Accession # P35442
Applications
Human Thrombospondin-2 Sandwich Immunoassay
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: Thrombospondin-2
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.
- Yang, Z. et al. (2001) J. Biol. Chem. 276:8403.
Product Datasheets
Citation for Human Thrombospondin-2 Antibody
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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Digital Decoding of Single Extracellular Vesicle Phenotype Differentiates Early Malignant and Benign Lung Lesions
Authors: Li J, Sina AAI, Antaw F et al.
Advanced science (Weinheim, Baden-Wurttemberg, Germany)
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