Recombinant Human Vitronectin Protein, CF

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R&D Systems Recombinant Proteins and Enzymes
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Citations (11)
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Recombinant Human Vitronectin Protein, CF Summary

Product Specifications

>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
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.
Mouse myeloma cell line, NS0-derived human Vitronectin protein
Accession #
N-terminal Sequence
Predicted Molecular Mass
52.3 kDa
70-80 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 Tris and NaCl.
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 large glycoprotein found in blood and the extracellular matrix (ECM). The gene for Vitronectin encodes a 19 amino acid (aa) signal peptide and a 459 aa protein. The amino terminal 130 aa residues of Vitronectin contain multiple binding sites for a variety of structures. Included is a site for binding to plasminogen activator inhibitor-1 (PAI‑1) and urokinase receptor, an (RGD) sequence that binds 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 that includes two sulfated tyrosine residues that bind thrombin-anti-thrombin III complexes, and a collagen binding site. The major part of the Vitronectin molecule
(aa 132-459) contains six hemopexin-like repeats. The carboxyl-terminal end of Vitronectin also has multiple sites and functions. It contains a stretch of basic amino acids that binds the acidic amino acids of the amino-terminal region, thereby stabilizing Vitronectin’s three dimensional structure. The carboxyl-terminal end also contains a plasminogen binding site, a heparin binding site that binds complement factor C7, C8 or C9, a glycosaminoglycan binding site, and a second PAI-1 binding site (aa 348-370). Vitronectin also contains an endogenous cleavage site, plus cleavage sites for elastase, thrombin and plasmin. Vitronectin has also been shown to bind IGF-2 and TGF-beta. The apparent molecular weight of human Vitronectin is 75 kDa, with ~30% of its molecular mass being attributed to glycosylation at 3 different sites. 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 composed of a 65 kDa and 10 kDa component held together by a disulfide bond. Binding of thrombin-anti-thrombin II complex or complement leads to an unfolding of Vitronectin. Unfolding of Vitronectin generates disulfide-linked multimers that are found in platelet secretions and extracellular matrix. Vitronectin is produced at high levels by the liver and many tumors. As might be expected by its structure, Vitronectin is involved in a number of biological activities including cell adhesion, cell spreading and migration, cell proliferation, extracellular anchoring, fibrinolysis, hemostasis, and complement mediated immune defense.

  1. Schvartz, I. Seger, D. and S. Shaltiel (1999) Int. J. Biochem. Cell Biol. 31:539.
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 Recombinant Human 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.

11 Citations: Showing 1 - 10
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  1. Opposing roles of hematopoietic-specific small GTPase Rac2 and the guanine nucleotide exchange factor Vav1 in osteoclast differentiation
    Authors: IS Kang, JS Jang, C Kim
    Sci Rep, 2020;10(1):7024.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  2. &beta2-Adrenergic Signalling Promotes Cell Migration by Upregulating Expression of the Metastasis-Associated Molecule LYPD3
    Authors: M Gruet, D Cotton, C Coveney, DJ Boocock, S Wagner, L Komorowski, RC Rees, AG Pockley, AC Garner, JD Wallis, AK Miles, DG Powe
    Biology (Basel), 2020;9(2):.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  3. Enteric Species F Human Adenoviruses use Laminin-Binding Integrins as Co-Receptors for Infection of Ht-29 Cells
    Authors: A Rajan, BD Persson, L Frängsmyr, A Olofsson, L Sandblad, J Heino, Y Takada, AP Mould, LM Schnapp, J Gall, N Arnberg
    Sci Rep, 2018;8(1):10019.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  4. Molecular Camouflage of Plasmodium falciparum Merozoites by Binding of Host Vitronectin to P47 Fragment of SERA5
    Authors: T Tougan, JR Edula, E Takashima, M Morita, M Shinohara, A Shinohara, T Tsuboi, T Horii
    Sci Rep, 2018;8(1):5052.
    Applications: Bioassay
  5. A ligand-specific blockade of the integrin Mac-1 selectively targets pathologic inflammation while maintaining protective host-defense
    Authors: D Wolf, N Anto-Miche, H Blankenbac, A Wiedemann, K Buscher, JD Hohmann, B Lim, M Bäuml, A Marki, M Mauler, D Duerschmie, Z Fan, H Winkels, D Sidler, P Diehl, DM Zajonc, I Hilgendorf, P Stachon, T Marchini, F Willecke, M Schell, B Sommer, C von Zur Mu, J Reinöhl, T Gerhardt, EF Plow, V Yakubenko, P Libby, C Bode, K Ley, K Peter, A Zirlik
    Nat Commun, 2018;9(1):525.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  6. Acetyl-CoA promotes glioblastoma cell adhesion and migration through Ca2+-NFAT signaling
    Authors: JV Lee, CT Berry, K Kim, P Sen, T Kim, A Carrer, S Trefely, S Zhao, S Fernandez, LE Barney, AD Schwartz, SR Peyton, NW Snyder, SL Berger, BD Freedman, KE Wellen
    Genes Dev., 2018;32(7):497-511.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  7. Bacterial genotoxins promote inside-out integrin beta1 activation, formation of focal adhesion complexes and cell spreading.
    Authors: Levi L, Toyooka T, Patarroyo M, Frisan T
    PLoS ONE, 2015;10(4):e0124119.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  8. c-FOS suppresses ovarian cancer progression by changing adhesion.
    Authors: Oliveira-Ferrer L, Rossler K, Haustein V, Schroder C, Wicklein D, Maltseva D, Khaustova N, Samatov T, Tonevitsky A, Mahner S, Janicke F, Schumacher U, Milde-Langosch K
    Br J Cancer, 2014;110(3):753-63.
  9. Epoxy metabolites of docosahexaenoic acid (DHA) inhibit angiogenesis, tumor growth, and metastasis.
    Authors: Zhang G, Panigrahy D, Mahakian L, Yang J, Liu J, Stephen Lee K, Wettersten H, Ulu A, Hu X, Tam S, Hwang S, Ingham E, Kieran M, Weiss R, Ferrara K, Hammock B
    Proc Natl Acad Sci U S A, 2013;110(16):6530-5.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  10. PKC-dependent human monocyte adhesion requires AMPK and Syk activation.
    Authors: Chang, Mei-Ying, Huang, Duen-Yi, Ho, Feng-Min, Huang, Kuo-Chin, Lin, Wan-Wan
    PLoS ONE, 2012;7(7):e40999.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  11. Pericytes promote endothelial cell survival through induction of autocrine VEGF-A signaling and Bcl-w expression.
    Authors: Franco M, Roswall P, Cortez E, Hanahan D, Pietras K
    Blood, 2011;118(10):2906-17.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay


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