Source	Mouse myeloma cell line, NS0-derived human Vitronectin protein Asp20-Leu478
Purity	>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.
N-terminal sequence Analysis	Asp20
Predicted Molecular Mass	52.3 kDa
SDS-PAGE	70-80 kDa, reducing conditions
Activity	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.

Formulation, Preparation and Storage

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.

2308-VN

Formulation	Lyophilized from a 0.2 μm filtered solution in Tris and NaCl.
Reconstitution	Reconstitute at 100 μg/mL in sterile PBS. Reconstitution Buffer Available: Size / Price Qty Loading... RB01:
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.

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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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.

Item	Value
References	Schvartz, I. Seger, D. and S. Shaltiel (1999) Int. J. Biochem. Cell Biol. 31:539. http://www.copewithcytokines.de/cope.cgi
Entrez Gene IDs	7448 (Human); 22370 (Mouse); 507525 (Bovine)
Alternate Names	Complement S-protein, S-protein, Serum Spreading Factor, Serum-spreading factor, Somatomedin B, V75, VN, VNT, VTN, Vitronectin, epibolin, vitronectin (serum spreading factor, somatomedin B, complement S-protein)

Citations for Recombinant Human Vitronectin Protein, CF (11)

Showing 1 - 10 of 11 citations Showing All

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Citations are publications that use Bio-Techne products. Selected citations for Recombinant Human Vitronectin Protein, CF include:

Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay

IS Kang et al. (2020), Opposing roles of hematopoietic-specific small GTPase Rac2 and the guanine nucleotide exchange factor Vav1 in osteoclast differentiation Sci Rep, 10(1):7024.
PMID: 32341385
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

M Gruet et al. (2020), &beta2-Adrenergic Signalling Promotes Cell Migration by Upregulating Expression of the Metastasis-Associated Molecule LYPD3 Biology (Basel), 9(2).
PMID: 32098331
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

A Rajan et al. (2018), Enteric Species F Human Adenoviruses use Laminin-Binding Integrins as Co-Receptors for Infection of Ht-29 Cells Sci Rep, 8(1):10019.
PMID: 29968781
Sample Types: Protein
Applications: Bioassay

T Tougan et al. (2018), Molecular Camouflage of Plasmodium falciparum Merozoites by Binding of Host Vitronectin to P47 Fragment of SERA5 Sci Rep, 8(1):5052.
PMID: 29567995
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

D Wolf et al. (2018), A ligand-specific blockade of the integrin Mac-1 selectively targets pathologic inflammation while maintaining protective host-defense Nat Commun, 9(1):525.
PMID: 29410422
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

JV Lee et al. (2018), Acetyl-CoA promotes glioblastoma cell adhesion and migration through Ca2+-NFAT signaling Genes Dev., 32(7):497-511.
PMID: 29674394
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

Levi L et al. (2015), Bacterial genotoxins promote inside-out integrin beta1 activation, formation of focal adhesion complexes and cell spreading. PLoS ONE, 10(4):e0124119.
PMID: 25874996
Oliveira-Ferrer L et al. (2014), c-FOS suppresses ovarian cancer progression by changing adhesion. Br J Cancer, 110(3):753-63.
PMID: 24322891
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

Zhang G et al. (2013), Epoxy metabolites of docosahexaenoic acid (DHA) inhibit angiogenesis, tumor growth, and metastasis. Proc Natl Acad Sci U S A, 110(16):6530-5.
PMID: 23553837
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

Chang et al. (2012), PKC-dependent human monocyte adhesion requires AMPK and Syk activation. PLoS ONE, 7(7):e40999.
PMID: 22848421
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay

Franco M et al. (2011), Pericytes promote endothelial cell survival through induction of autocrine VEGF-A signaling and Bcl-w expression. Blood, 118(10):2906-17.
PMID: 21778339

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