Human Thrombospondin-2 Biotinylated Antibody

Catalog # Availability Size / Price Qty
BAF1635
Product Details
Citations (1)
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Human Thrombospondin-2 Biotinylated Antibody Summary

Species Reactivity
Human
Specificity
Detects human Thrombospondin‑2 in ELISAs and Western blots. In sandwich ELISAs, less than 0.2% cross-reactivity with recombinant human (rh) THBS-1 and rhTHBS-4 is observed.
Source
Polyclonal Goat IgG
Purification
Antigen Affinity-purified
Immunogen
Mouse myeloma cell line NS0-derived recombinant human Thrombospondin-2
Gly19-Ile1172
Accession # P35442
Formulation
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Label
Biotin

Applications

Recommended Concentration
Sample
Western Blot
0.1 µg/mL
Recombinant Human Thrombospondin‑2 (Catalog # 1635-T2)

Human Thrombospondin-2 Sandwich Immunoassay

Recommended Concentration
Reagent
ELISA Detection (Matched Antibody Pair)
0.1-0.4 µg/mL 

Use in combination with:

Capture Reagent: Human Thrombospondin‑2 Antibody (Catalog # MAB16351)

Standard: Recombinant Human Thrombospondin-2 Protein, CF (Catalog # 1635-T2)

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

Reconstitution
Reconstitute at 0.2 mg/mL in sterile PBS.
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Shipping
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
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.
  • 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).

References
  1. Elzie, C.A. and J.E. Murphy-Ullrich (2004) Int. J. Biochem. Cell Biol. 36:1090.
  2. Armstrong, L.C. and P. Bornstein (2003) Matrix Biol. 22:63.
  3. Murphy-Ullrich, J.E. (2001) J. Clin. Invest. 107:785.
  4. Bornstein, P. and E.H. Sage (2002) Curr. Opin. Cell Biol. 14:608.
  5. LaBell, T.L. and P.H. Byers (1993) Genomics 17:225.
  6. Kyriakides, T.R. et al. (1998) J. Histochem. Cytochem. 46:1007.
  7. Kyriakides, T.R. et al. (1998) J. Cell Biol. 140:419.
  8. Anilkumar, N. et al. (2002) J. Cell Sci. 115:2357.
  9. Misenheimer, T.M. et al. (2003) Biochemistry 42:5125.
  10. Murphy-Ullrich, J.E. et al. (1993) J. Biol. Chem. 268:26784.
  11. Calzada, M.J. et al. (2004) Circ. Res. 94:462.
  12. Calzada, M.J. et al. (2003) J. Biol. Chem. 278:40679.
  13. Noh, Y-H. et al. (2003) J. Invest. Dermatol. 121:1536.
  14. Simantov, R. et al. (2005) Matrix Biol. 24:27.
  15. Streit, M. et al. (1999) Proc. Natl. Acad. Sci. USA 96:14888.
  16. Yang, Z. et al. (2001) J. Biol. Chem. 276:8403.
Entrez Gene IDs
7058 (Human)
Alternate Names
THBS2; thrombospondin 2; Thrombospondin2; Thrombospondin-2; TSP-2; TSP2thrombospondin-2

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Citation for Human Thrombospondin-2 Biotinylated 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

  1. Thrombospondin‑2 is upregulated in patients with aortic dissection and enhances angiotensin II‑induced smooth muscle cell apoptosis
    Authors: Liping Qi, Kui Wu, Shutian Shi, Qingwei Ji, Huangtai Miao, Que Bin
    Experimental and Therapeutic Medicine

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