Human Recombinant Vitronectin

Human recombinant vitronectin is a laboratory-produced form of the human extracellular matrix glycoprotein vitronectin, used to provide a defined surface for cell attachment and growth. Its RGD sequence engages cell-surface integrins, promoting adhesion and activating signaling pathways that influence survival, proliferation, migration, and differentiation. In developmental biology, recombinant vitronectin supports the maintenance and directed differentiation of human pluripotent stem cells under xeno-free culture conditions, reducing variability associated with animal-derived matrices. By supplying a consistent matrix component, it helps researchers model early development, generate specialized cell types, and improve the reproducibility of stem cell-based studies.

Human Recombinant Vitronectin - Related Videos

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JoVE EoE - Immunopathology

Determining the Role of Vitronectin in Bacterial Resistance to Bactericidal Activity of Human Serum

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2025

This video demonstrates the role of vitronectin, a human serum glycoprotein, on bacterial resistance. Antibodies in the serum interact with bacterial surface proteins, activating complement proteins and forming the membrane attack complex, causing bacterial cell lysis. Vitronectin binding on bacterial membrane protein prevents the membrane attack complex formation, resulting in bacterial survival.

Detection of Vitronectin Binding to Bacterial Surfaces using Flow Cytometry

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2025

This video demonstrates the detection of vitronectin's interaction with bacterial surface proteins. The flow-cytometry analysis measures the fluorescence signal of fluorescently labeled antibodies bound to vitronectin, confirming its presence at the bacterial surface. This technique provides insights into host-pathogen interactions and potential bacterial infection therapies.

An Assay to Study the Role of Vitronectin in Bacterial Adherence to Host Epithelial Cells

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2025

In this video, we demonstrate an assay to study the role of vitronectin in Haemophilus influenzae adherence to the host epithelial cells.

Purification of Bacteria-Derived Recombinant P Domain Proteins of Human Norovirus

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2025

Source: Leuthold, M. M., et al. Production of Human Norovirus Protruding Domains in E. coli for X-ray Crystallography. J. Vis. Exp. (2016).This video demonstrates the purification of recombinant human norovirus P domain using size exclusion chromatography, highlighting the separation of the target protein from higher and lower molecular weight impurities based on differential pore accessibility. The process is monitored by UV absorbance and confirmed through SDS-PAGE analysis of eluted...

Recombineering Homologous Recombination Constructs in Drosophila

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Cited by 9 •

2013

Homologous recombination techniques greatly advance Drosophila genetics by enabling the creation of molecularly precise mutations. The recent adoption of recombineering allows one to manipulate large pieces of DNA and transform them into Drosophila6. The methods presented here combine these techniques to rapidly generate large homologous recombination vectors.

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