Bovine Vitronectin Protein, CF

• Reactivity: Bv
• Applications: Bioactivity
• Format: Carrier-Free

Bovine Vitronectin Protein, CF Summary

• Details of Functionality: 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.
• Source: Bovine plasma-derived Vitronectin protein
• N-terminal Sequence: DQESCKGRCT
• Protein/Peptide Type: Natural Proteins
• Gene: VTN
• Purity: >90%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• SDS-PAGE: 58 kDa, 68 kDa and 80 kDa, reducing conditions

Packaging, Storage & Formulations

• 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.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS and Urea.
• Purity: >90%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Reconstitution Instructions: Reconstitute at 100 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Bovine Vitronectin Protein, CF

• 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

Background

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.
2. http://www.copewithcytokines.de/cope.cgi
3. Nakashima, N. et al. (1992) Biochem. Biophys. Acta 1120:1.

Publications for Vitronectin (2348-VN)(2)

Publications using 2348-VN

• U Thamma, TJ Kowal, MM Falk, H Jain Nanostructure of bioactive glass affects bone cell attachment via protein restructuring upon adsorption Scientific Reports, 2021-03-11;11(1):5763. 2021-03-11 [PMID: 33707489] (Western Blot Control, Mouse)
• Endothelin-3 stimulates cell adhesion and cooperates with ?1-integrins during enteric nervous system ontogenesis Sci Rep, 2016-12-01;6(0):37877. 2016-12-01 [PMID: 27905407] (Bioassay, Mouse)

Bioinformatics

• Gene Symbol: VTN