Vitronectin can be used with cells with integrin receptors that bind vitronectin, including platelets, endothelial cells, melanoma cells, and osteosarcoma. It is recommended as a cell culture substratum at 0.1 μg/cm2. Optimal conditions for attachment depend on cell line and application.
Biochem./physiol. Wirkung
Vitronectin binds to glycosaminoglycans, is incorporated as an inhibitor to the membrane cytolytic attack complex of the complement system, has interaction with thrombin and antithrombin III during coagulation, and may play a role in the coagulation pathway.
Komponenten
Vitronectin is a glycoprotein present in plasma and tissues, and is one of the major cell adhesion proteins, along with fibronectin, in plasma. The N-terminal residues of vitronectin are identical to somatomedin B and are followed by an R-G-D sequence that interacts with a specific cell-surface receptor. The central domain of vitronectin is enriched with hydrophobic residues. Closer to the C-terminus, it has an arginine rich region that allows for heparin binding activity.
Vorsicht
The lyophilized product should be stored desiccated at 2-8°C. Under these conditions it is stable for at least 2 years. Aliquots should be stored at -20°C or -70°C, but repeated freezing and thawing should be avoided.
Angaben zur Herstellung
This product is supplied as a cell culture tested lyophilized powder from buffered saline. It is recommended to use polypropylene vessels during handling, due to the strong affinity of vitronectin for hydrophilic surfaces. Reconstitution of this product can be done with 1 mL of water per vial. The stock solution should then be filter-sterilized using a 0.2μm membrane and aliquoted and frozen for long term storage.
We examined the effect of surface chemistry on adsorption of fibronectin (Fn) and vitronectin (Vn) and subsequent cell adhesion, employing self-assembled monolayers (SAMs) of alkanethiols carrying terminal methyl (CH3), hydroxyl groups (OH), carboxylic acid (COOH), and amine (NH2). More Fn
The Journal of cell biology, 198(4), 657-676 (2012-08-22)
Mena is an Ena/VASP family actin regulator with roles in cell migration, chemotaxis, cell-cell adhesion, tumor cell invasion, and metastasis. Although enriched in focal adhesions, Mena has no established function within these structures. We find that Mena forms an adhesion-regulated
Glycosylphosphatidylinositol-anchored proteins (GPI-APs) are a major class of lipid-anchored plasma membrane proteins. GPI-APs form nanoclusters generated by cortical acto-myosin activity. While our understanding of the physical principles governing this process is emerging, the molecular machinery and functional relevance of GPI-AP
Cancer stem cell media, spheroid plates and cancer stem cell markers to culture and characterize CSC populations.
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