Bovine Vitronectin Protein, CF

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Product Details
Citations (2)
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Bovine Vitronectin Protein, CF Summary

Product Specifications

>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Measured by the ability of the immobilized protein to support the adhesion of B16‑F1 mouse melanoma cells. When 5 x 104 cells/well are added to Vitronectin coated plates (5 µg/mL with 100 µL/well), approximately >55% will adhere after 30 minutes at 37 °C.
Optimal concentration depends on cell type as well as the application or research objectives.
Bovine plasma-derived Vitronectin protein
N-terminal Sequence
58 kDa, 68 kDa and 80 kDa, reducing conditions

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Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. 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 could interfere.


Formulation Lyophilized from a 0.2 μm filtered solution in PBS and Urea.
Reconstitution Reconstitute at 100 μg/mL in sterile PBS.
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.
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Background: Vitronectin

Vitronectin is a larger glycoprotein found in blood and in the extracellular matrix (ECM). The amino terminal segment of vitronectin harbors a binding site (aa 1 ‑ 44) for plasminogen activator inhibitor-1 (PAI‑1) and urokinase receptor, an Agr-Gly-ASP (RGD) sequence (aa 45 - 47) that provides a binding site for alpha v beta 3, alpha v beta 5, alpha v beta 1, alpha IIb beta 3, alpha v beta 6, and alpha v beta 8 integrins, a stretch of acidic amino acids including two sulfated tyrosine residues (aa 56 and 59) that provide a binding site for thrombin-anti-thrombin III complexes, and a collagen binding site. The major part of the vitronecitn molecule (aa 132 - 459) accommodate six hemopexin repeats. The carboxyl-terminal end of vitronectin containing a stretch of basic amino acids (aa 348 - 379) that binds the acidic stretch of acidic amino acids in the amino-terminal section and stabilized vitronectin’s three dimensional structure. The carboxyl-terminal end of vitronectin also contains a plaminogen binding site (aa 332 ‑ 348), a heparin binding site that can be bound by complement factor C7, C8 or C9 (aa 348 ‑ 376), a glycosaminoglycan binding site (aa 348 ‑ 361), and a second PAI-1 binding site (aa 348 ‑ 370). Vitronectin also contains an endogenous cleavage site, two elastase cleavage sites, two thrombin cleavage sites, and a plasmin cleavage site. Vitronectin also has been shown to bind insulin growth factor II (IGF‑II) and TGF-beta. The apparent molecular weight of bovine vitronectin is 70 kDa, with ~15% of its molecular mass being contributed to by glycosylation. In blood and plasma, vitronectin is found predominantly as a single chain monomer. It can also be found as a dimer after endogenous cleavage. The dimer is comprised of a 65 kDa and 10 kDa component held together by a disulfide bond. Binding of thrombin-anti-thrombin II complex or complement lead to an unfolding of vitronectin. Unfolding of vitronectin leads to the formation of disulfide-linked multimers that are found in platelet releasate and in the extracellular matrix. Vitronectin is produced at high levels by the liver and many tumors. Vitronectin is involved in a number of biological functions including cell adhesion, cell spreading and migration, cell proliferation, extracellular anchoring, fibrinolysis, hemostasis, and complement immune defense.

  1. Schvartz, I. et al. (1999) Int. J. Biochem. Cell Biol. 31:539.
  3. Nakashima, N. et al. (1992) Biochem. Biophys. Acta 1120:1.
Entrez Gene IDs
7448 (Human); 22370 (Mouse); 507525 (Bovine)
Alternate Names
Complement S-protein; epibolin; Serum Spreading Factor; Serum-spreading factor; Somatomedin B; S-protein; V75; vitronectin (serum spreading factor, somatomedin B, complement S-protein); Vitronectin; VN; VNT; VTN

Citations for Bovine Vitronectin Protein, CF

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.

2 Citations: Showing 1 - 2
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  1. Nanostructure of bioactive glass affects bone cell attachment via protein restructuring upon adsorption
    Authors: U Thamma, TJ Kowal, MM Falk, H Jain
    Scientific Reports, 2021;11(1):5763.
    Species: Mouse
    Sample Types: Cell Lysates
    Applications: Western Blot Control
  2. Endothelin-3 stimulates cell adhesion and cooperates with ?1-integrins during enteric nervous system ontogenesis
    Sci Rep, 2016;6(0):37877.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay


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