Bovine Vitronectin Protein, CF
Bovine Vitronectin Protein, CF Summary
Optimal concentration depends on cell type as well as the application or research objectives.
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.
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.
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.
- Schvartz, I. et al. (1999) Int. J. Biochem. Cell Biol. 31:539.
- Nakashima, N. et al. (1992) Biochem. Biophys. Acta 1120:1.
Citation 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.
1 Citation: Showing 1 - 1
Endothelin-3 stimulates cell adhesion and cooperates with ?1-integrins during enteric nervous system ontogenesis
Sci Rep, 2016;6(0):37877.
Sample Types: Whole Cells
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