Recombinant Human Thrombospondin-4 Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 2390-TH

R&D Systems, part of Bio-Techne
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2390-TH-050
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Key Product Details

Source

CHO

Accession #

P35443

Conjugate

Unconjugated

Applications

Bioactivity

View all Thrombospondin-4 Proteins and Enzymes »

Product Specifications

Source

Chinese Hamster Ovary cell line, CHO-derived human Thrombospondin-4 protein
Ala22-Asn961, with a C-terminal 10-His tag

Purity

>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.

Endotoxin Level

<1.0 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Ala22

Predicted Molecular Mass

105 kDa

SDS-PAGE

145 kDa, reducing conditions

Activity

Measured by the ability of the immobilized protein to support the adhesion of SVEC4-10 mouse vascular endothelial cells.
Recombinant Human Thrombospondin‑4 (rhThrombospondin-4) is coated to 96 well plates at 10 µg/mL (100 µL/well) overnight then reduced with 20 mM DTT for 30 minutes. When 2 x 104 cells/well are added to rhThrombospondin‑4 coated plates, ≥50% will adhere after one hour at 37 °C.
Optimal dilutions should be determined by each laboratory for each application.

Reviewed Applications

Read 2 reviews rated 5 using 2390-TH in the following applications:

Formulation, Preparation and Storage

2390-TH
Formulation Lyophilized from a 0.2 μm filtered solution in Tris and NaCl.
Reconstitution
Reconstitute at 100 μg/mL in sterile PBS.

Reconstitution Buffer Available:
Size / Price
Qty
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.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.

Background: Thrombospondin-4

Thrombospondin-4 (TSP-4) is an approximately 140 kDa matricellular protein that is secreted as a disulfide-linked pentamer. Within the Thrombospondin family, TSP-3 and TSP-5/COMP are also pentameric, while TSP-1 and TSP-2 are trimeric. TSP-4 regulates cell-cell and cell matrix interactions and plays a role in cardiovascular physiology and neuronal development (1, 2). Mature human TSP-4 consists of an N-terminal heparin-binding domain, a coiled coil motif, four EGF-like repeats, seven TSP type-3 repeats (one with an RGD motif), and a TSP C-terminal domain (2). Human TSP-4 shares 93% amino acid sequence identity with mouse and rat TSP-4. TSP-4 binds a variety of matrix proteins including Collagens I, II, III, V, Laminin-1, Fibronectin, and Matrilin-2 (3). Interactions of TSP-4 with non-collagenous proteins are independent of divalent cations, whereas interactions with collagenous proteins are enhanced in the presence of zinc (3). TSP-4 binds to cell surface Integrins containing the alphaM, beta2, or beta3 chains (4, 5). It is expressed in skeletal muscle and tendon as well as by vascular smooth muscle and endothelial cells (6‑8). It is up‑regulated in cardiomyocytes during pressure overload and is required for mediating the responsive increase in cardiac contractility (9). In humans, a polymorphism of TSP-4 (A387P) is associated with myocardial infarction (10). TSP-4 contributes to the development of inflammation and atherosclerosis by promoting macrophage and neutrophil adhesion to the vasculature (4, 5). In the nervous system, TSP-4 is expressed by astrocytes and neurons and is enriched at neuromuscular junctions and synapse-rich layers of the brain and retina (8, 11, 12). It promotes neuronal adhesion, neurite outgrowth, and excitatory synaptogenesis (8, 12, 13). TSP-4 is
up‑regulated in the spinal cord following peripheral nerve injury where it contributes to presynaptic hypersensitivity and hyperalgesia (11). It is also up‑regulated in muscle following denervation (8). TSP-4 is additionally secreted by tumor-associated fibroblasts in gastric adenocarcinoma, particularly in regions of tumor cell invasion (14).

References

  1. Murphy-Ullrich, J.E. and R.V. Iozzo (2012) Matrix Biol. 31:152.
  2. Lawler, J. et al. (1995) J. Biol. Chem. 270:2809.
  3. Narouz-Ott, L. et al. (2000) J. Biol. Chem. 275:37110.
  4. Pluskota, E. et al. (2005) Blood 106:3970.
  5. Frolova, E.G. et al. (2010) Circ. Res. 107:1313.
  6. Sodersten, F. et al. (2007) Connect. Tiss. Res. 48:254.
  7. Stenina, O.I. et al. (2003) Circulation 108:1514.
  8. Arber, S. and P. Caroni (1995) J. Cell Biol. 131:1083.
  9. Cingolani, O.H. et al. (2011) Circ. Res. 109:1410.
  10. Stenina, O.I. et al. (2007) Arterioscler. Thromb. Vasc. Biol. 27:1886.
  11. Kim, D.-S. et al. (2012) J. Neurosci. 32:8977.
  12. Dunkle, E.T. et al. (2007) Exp. Eye Res. 84:707.
  13. Eroglu, C. et al. (2009) Cell 139:380.
  14. Forster, S. et al. (2011) Mod. Pathol. 24:1390.

Alternate Names

THBS4, Thrombospondin4, TSP-4

Entrez Gene IDs

7060 (Human); 21828 (Mouse)

Gene Symbol

THBS4

UniProt

P35443

Additional Thrombospondin-4 Products

Product Documents for Recombinant Human Thrombospondin-4 Protein, CF

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Product Specific Notices for Recombinant Human Thrombospondin-4 Protein, CF

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