Product Specifications for Recombinant Human Thrombospondin-4 Protein, CF
Chinese Hamster Ovary cell line, CHO-derived human Thrombospondin-4 protein Ala22-Asn961, with a C-terminal 10-His tag
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
<1.0 EU per 1 μg of the protein by the LAL method.
N-terminal sequence Analysis
Predicted Molecular Mass
145 kDa, reducing conditions
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.
Formulation, Preparation and Storage
What does CF mean?
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our
Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant
protein to be stored at a more dilute concentration.
The carrier free version does not contain BSA.
What formulation is right for me?
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or
as an ELISA standard.
In contrast, the carrier free protein is recommended for applications, in which the presence of BSA
Lyophilized from a 0.2 μm filtered solution in Tris and NaCl.
Reconstitute at 100 μg/mL in sterile PBS.
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.
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 alpha M, beta 2, or beta 3 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).
Murphy-Ullrich, J.E. and R.V. Iozzo (2012) Matrix Biol. 31:152.
Lawler, J. et al. (1995) J. Biol. Chem. 270:2809.
Narouz-Ott, L. et al. (2000) J. Biol. Chem. 275:37110.
Pluskota, E. et al. (2005) Blood 106:3970.
Frolova, E.G. et al. (2010) Circ. Res. 107:1313.
Sodersten, F. et al. (2007) Connect. Tiss. Res. 48:254.
Stenina, O.I. et al. (2003) Circulation 108:1514.
Arber, S. and P. Caroni (1995) J. Cell Biol. 131:1083.
Cingolani, O.H. et al. (2011) Circ. Res. 109:1410.
Stenina, O.I. et al. (2007) Arterioscler. Thromb. Vasc. Biol. 27:1886.
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