Recombinant Human Vitronectin Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human 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
Mouse myeloma cell line, NS0-derived human Vitronectin protein
Asp20-Leu478
Accession #
N-terminal Sequence
Asp20
Protein/Peptide Type
Recombinant Proteins
Gene
VTN
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
52.3 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
70-80 kDa, reducing conditions
Publications
Read Publications using
2308-VN in the following applications:

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 Tris and NaCl.
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
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 Recombinant Human 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 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.
  2. http://www.copewithcytokines.de/cope.cgi

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Publications for Vitronectin (2308-VN)(8)

We have publications tested in 2 confirmed species: Human, Mouse.

We have publications tested in 1 application: Bioassay.


Filter By Application
Bioassay
(7)
All Applications
Filter By Species
Human
(5)
Mouse
(1)
All Species
Showing Publications 1 - 8 of 8.
Publications using 2308-VN Applications Species
A Rajan, BD Persson, L Frängsmyr, A Olofsson, L Sandblad, J Heino, Y Takada, AP Mould, LM Schnapp, J Gall, N Arnberg Enteric Species F Human Adenoviruses use Laminin-Binding Integrins as Co-Receptors for Infection of Ht-29 Cells Sci Rep, 2018;8(1):10019. 2018 [PMID: 29968781] (Bioassay, Human) Bioassay Human
T Tougan, JR Edula, E Takashima, M Morita, M Shinohara, A Shinohara, T Tsuboi, T Horii Molecular Camouflage of Plasmodium falciparum Merozoites by Binding of Host Vitronectin to P47 Fragment of SERA5 Sci Rep, 2018;8(1):5052. 2018 [PMID: 29567995] (Bioassay) Bioassay
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 A ligand-specific blockade of the integrin Mac-1 selectively targets pathologic inflammation while maintaining protective host-defense Nat Commun, 2018;9(1):525. 2018 [PMID: 29410422] (Bioassay, Human) Bioassay Human
Levi L, Toyooka T, Patarroyo M, Frisan T Bacterial genotoxins promote inside-out integrin beta1 activation, formation of focal adhesion complexes and cell spreading. PLoS ONE, 2015;10(4):e0124119. 2015 [PMID: 25874996] (Bioassay, Human) Bioassay Human
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 c-FOS suppresses ovarian cancer progression by changing adhesion. Br J Cancer, 2014;110(3):753-63. 2014 [PMID: 24322891]
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 Epoxy metabolites of docosahexaenoic acid (DHA) inhibit angiogenesis, tumor growth, and metastasis. Proc Natl Acad Sci U S A, 2013;110(16):6530-5. 2013 [PMID: 23553837] (Bioassay, Human) Bioassay Human
Chang, Mei-Ying, Huang, Duen-Yi, Ho, Feng-Min, Huang, Kuo-Chin, Lin, Wan-Wan PKC-dependent human monocyte adhesion requires AMPK and Syk activation. PLoS ONE, 2012;7(7):e40999. 2012 [PMID: 22848421] (Bioassay, Human) Bioassay Human
Franco M, Roswall P, Cortez E, Hanahan D, Pietras K Pericytes promote endothelial cell survival through induction of autocrine VEGF-A signaling and Bcl-w expression. Blood, 2011;118(10):2906-17. 2011 [PMID: 21778339] (Bioassay, Mouse) Bioassay Mouse

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Bioinformatics

Gene Symbol VTN
Uniprot