Streptavidin Binding Peptide
Streptavidin Binding Peptide - Related Videos
07:59
A High Throughput MHC II Binding Assay for Quantitative Analysis of Peptide Epitopes
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Cited by 21 •
2014
Biochemical assays with recombinant human MHC II molecules can provide rapid, quantitative insights into immunogenic epitope identification, deletion, or design. Here, a peptide-MHC II binding assay scaled to 384-well plates is described. This cost effective format should prove useful in the fields of protein deimmunization and vaccine design and development.
14:28
Peptide-based Identification of Functional Motifs and their Binding Partners
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Cited by 2 •
2013
Techniques to dissect the mechanisms underlying the secretion of HIV-1 Nef in exosomes are described. Specific short peptides derived from Nef and protein transfection were exploited to determine the structure, function, and binding partners of Nef’s Secretion Modification Region. These procedures have general relevance in many mechanistic studies.
03:41
Analyzing Influenza Virus Internalization Using a Streptavidin Blocking Assay
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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.
04:54
Evaluation of Controlled T Cell Activation with a Photoactivatable Peptide MHC
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2025
This video demonstrates a method of decaging a photoactivatable peptide-major histocompatibility complex using UV irradiation. The decaging process exposes the native peptide sequence, enabling precise T cell activation.
09:34
Identification of Modified Histones as Binding Substrates of Human Spindlin Family Member 4 (SPIN4) by Peptide Arrays and Native Nucleosome Pulldown
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2026
Genetic variants in human Spindlin Family Member 4 (SPIN4) have recently been identified in patients with bone overgrowth, a novel developmental disorder. A protocol and new results describing the biochemical identification of modified histones in the context of nucleosomes as SPIN4 binding substrates are presented.
FAQs
Binding depends on specific, noncovalent interactions between residues in the engineered peptide and sites within streptavidin’s tetrameric structure. Because the interaction is selective, a tagged molecule can be distinguished from other molecules in a sample and captured through a streptavidin-coated surface or particle. This molecular recognition supports labeling and purification workflows.
Biotin can act as a competitive ligand that disrupts the interaction between the tagged peptide and streptavidin. Introducing biotin or a related ligand therefore provides a controlled way to release material after capture, rather than treating immobilization as irreversible. This feature is useful when purification or pull-down experiments require recovery of the tagged protein or associated complex.
When a tagged protein participates in a molecular complex, immobilizing that tagged component on streptavidin-coated surfaces or particles can support retention of the complex for a pull-down assay. The affinity pair therefore connects a defined peptide handle to analysis of larger biological assemblies, helping researchers examine associated material rather than focusing only on the purified tagged protein.
A typical workflow places the engineered peptide tag on the molecule of interest, brings that tagged molecule into contact with streptavidin-coated surfaces or particles, and uses the resulting selective immobilization for capture or detection. Researchers can then apply the format to purification, labeling, imaging, or pull-down analysis, with competitive biotin-based release available when recovery is needed.
The approach can be configured with streptavidin-coated surfaces or particles. Surfaces support immobilization in a fixed format, whereas particles provide a separate format for selective capture. The same peptide-streptavidin recognition can therefore be incorporated into purification, labeling, or pull-down workflows, with the selected format matching how researchers need to handle the tagged molecule.
The selective interaction provides a way to place a tagged molecule at a streptavidin-containing location, enabling detection or visualization. In imaging, the pair supports molecular labeling, while in biosensor development it supplies the recognition and immobilization step needed to position tagged material for measurement. These uses extend the method beyond purification into biological observation and sensing.