Streptavidin-hrp Complex

The streptavidin-HRP complex is a detection reagent that combines streptavidin, a protein with exceptionally strong affinity for biotin, with horseradish peroxidase (HRP), an enzyme that generates measurable signals. In an immunoassay, biotinylated antibodies, antigens, or nucleic acid probes capture the complex through specific biotin-streptavidin binding, while HRP catalyzes the conversion of a substrate into a colored or chemiluminescent product. This signal amplification supports sensitive detection and measurement of immune responses, pathogen-associated molecules, and infection biomarkers in applications such as ELISA, immunoblotting, and tissue staining. The system helps researchers localize targets and quantify molecular interactions in diagnostic and experimental studies.

Streptavidin-hrp Complex - Related Videos

Research

JoVE EoE - Viral Growth and Techniques

Analyzing Influenza Virus Internalization Using a Streptavidin Blocking Assay

0 Views •

2026

Source: Pohl, M. O. & Stertz, S. Measuring Attachment and Internalization of Influenza A Virus in A549 Cells by Flow Cytometry. J. Vis. Exp. (2015)This video demonstrates the use of a streptavidin blocking assay to distinguish surface-bound from internalized influenza virus in human lung epithelial cells. Comparing fluorescence signals shows that a higher intensity after incubation indicates successful viral internalization.

Isolation of Proteins from Viral DNA-protein Complexes

0 Views •

2026

Source: Dembowski, J. A., et al. Purification of Viral DNA for the Identification of Associated Viral and Cellular Proteins. J. Vis. Exp. (2017).This video demonstrates the isolation of protein–viral DNA complexes from cell nuclei using click chemistry and magnetic bead purification. The protocol involves labeling viral genomes with alkyne-modified nucleotides, biotinylation via a click reaction, and binding to streptavidin-coated magnetic beads. Following washing and heat elution, the purified...

Analyzing DNA-Protein Interactions with Streptavidin-Based Biolayer Interferometry

0 Views •

2025

This article describes a protocol for studying DNA-protein interactions using a streptavidin-based biolayer interferometry (BLI) system. It outlines the essential steps and considerations for utilizing either basic or advanced binding kinetics to determine the equilibrium binding affinity (KD) of the interaction.

Education

JoVE Science Education - Chemistry

Coordination Chemistry Complexes

0 Views •

2023

Source: Laboratory of Dr. Neal Abrams — SUNY College of Environmental Science and Forestry Transition metals are found everywhere from vitamin supplements to electroplating baths. Transition metals also make up the pigments in many paints and compose all minerals. Typically, transition metals are found in the cationic form since they readily oxidize, or lose electrons, and are surrounded by electron donors called ligands. These ligands do not form ionic or covalent bonds with the metal center,...

Protein Complex Assembly

0 Views •

2020

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes. Many viruses self-assemble into a fully functional unit using the infected host cell to...

View All Results

FAQs

Related Topics