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Desthiobiotin reagents are vital tools in biochemical research and diagnostics, offering an alternative to traditional biotin reagents with unique reversible binding properties. Unlike biotin, which binds irreversibly to streptavidin or avidin, desthiobiotin allows for gentle elution, making it ideal for applications requiring reversible binding and recovery of biotinylated molecules.
Explore our complete catalog of desthiobiotin reagents to find the right solution for your research needs.
Desthiobiotin, a biotin analog lacking the ureido ring's sulfur atom, retains a high affinity for streptavidin and avidin, albeit slightly lower than biotin. This subtle difference enables efficient binding while permitting the elution of the biotinylated compound under mild conditions using biotin or other elution agents. Desthiobiotin's reduced binding strength (Kd ~10-11 M compared to biotin's Kd ~10-15 M) is a critical factor in its reversible interaction, allowing it to be utilized effectively in various biochemical processes.
Desthiobiotin reagents are employed in affinity purification protocols where the recovery of the target protein, nucleic acid, or other biomolecules is necessary. After binding the biotinylated molecule to streptavidin or avidin-conjugated beads, desthiobiotin allows for efficient elution without harsh conditions, preserving the functionality of the recovered molecule.
Desthiobiotinylation is particularly useful in studying protein-protein and protein-DNA interactions. The reversible binding characteristic is crucial for the sequential analysis of binding events, ensuring that the native state of proteins and nucleic acids is maintained throughout the experiment.
As a labeling agent, desthiobiotin offers flexibility in detecting biomolecules. Its reversible nature is advantageous in assays where the removal of the label is required post-detection, allowing for further downstream processing or reuse of the sample.
Figure 1. Synthesis of biotin and desthiobiotin probes by click chemistry with reporter tag azide[1].
A. Improved stability - Desthiobiotin is more resistant to enzymatic degradation than biotin, making it a better choice for long-term studies.
B. Reduced non-specific binding - Desthiobiotin can have lower non-specific binding than biotin, leading to cleaner and more reliable results.
C. Increased sensitivity - Desthiobiotin can be detected with higher sensitivity than biotin in some applications.
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※ It should be noted that our service is only used for research, not for clinical use.