Desthiobiotin Streptavidin
Desthiobiotin Streptavidin - Related Videos
11:11
Desthiobiotin-Streptavidin-Affinity Mediated Purification of RNA-Interacting Proteins in Mesothelioma Cells
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Cited by 6 •
2018
Desthiobiotin labeling of a synthetic 25-nucleotide RNA oligo, which contains an adenine-rich element (ARE) motif, allows specific binding of cytosolic ARE-binding protein.
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.
08:07
Analyzing DNA-Protein Interactions with Streptavidin-Based Biolayer Interferometry
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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.
04:51
Streptavidin-Affinity Grid Fabrication for Cryo-Electron Microscopy Sample Preparation
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Cited by 15 •
2023
A step-by-step protocol for fabricating streptavidin affinity grids is provided for use in structural studies of challenging macromolecular samples by cryo-electron microscopy.
05:07
RNA-Protein Pull-Down Assay to Isolate RNA-Binding Proteins via Affinity Extraction
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2025
This video demonstrates an in vitro RNA pull-down assay to identify RNA-binding proteins (RBPs), which interact with the adenylate-uridylate-rich element (ARE) sequences in mRNA. The target RBPs from a cell lysate are mixed with an RNA probe to form RNA-protein complexes. The complexes are isolated via affinity purification utilizing the affinity of the desthiobiotin label of the RNA probe to a streptavidin-labeled magnetic bead.
FAQs
Free biotin has a higher affinity for streptavidin than desthiobiotin does. When introduced after capture, it competes for the same binding pockets and displaces desthiobiotin through an affinity-driven exchange. Because this process can occur under mild conditions, researchers can recover labeled targets while reducing the need for harsh treatments that may interfere with downstream analysis.
Streptavidin provides binding pockets that recognize biotin-related molecules through strong noncovalent interactions. Desthiobiotin occupies these pockets firmly enough to immobilize a labeled target, yet remains replaceable by free biotin. This balance between strong capture and controlled competition distinguishes the system from an irreversible attachment and supports temporary handling of biomolecules or cells.
Reversible affinity binding allows a captured molecule to be released without relying on harsh elution treatments. Gentle recovery can help preserve the usefulness of proteins, nucleic acids, antibodies, or cells for subsequent analysis. The exchange-based design also supports workflows in which targets must be captured, processed, and recovered more than once.
A typical workflow begins with a target that has been biotinylated, followed by contact with desthiobiotin-streptavidin so the labeled material becomes temporarily captured. The bound material can then support enrichment or purification, after which free biotin is introduced to promote release. This sequence separates capture from recovery under controlled, mild conditions.
The approach can be applied to biotinylated proteins, nucleic acids, antibodies, and cells. Its value lies in combining selective temporary capture with later recovery, rather than permanently retaining the labeled material. Consequently, it can support biomedical analysis workflows that require enrichment or purification before examining the recovered target.
In cancer research, reversible capture can help process tumor-associated biomolecules and support molecular assays. Researchers may use the system when labeled proteins, nucleic acids, antibodies, or cells need temporary immobilization followed by gentle recovery. This can improve workflows that depend on enrichment, purification, or repeated handling of cancer-related analytical materials.