DBCO-PEG4-Desthiobiotin
An azide-reactive desthiobiotin reagent that allows easy eluion from streptavidin.
Highlights:
- Biocompatible – click reaction occurs efficiently under mild buffer conditions; requires no accessory reagents such as a copper catalyst or reducing agents (e.g. DTT)
- Chemoselective – azide and DBCO groups do not react or interfere with other functional groups found in biological samples, but conjugate to one another with high efficiency
- Desthiobiotin – allows easy elution from streptavidin, an ideal feature for affinity purification applications
- Extended PEG4 spacer – reduces aggregation, minimizes steric hindrance for affinity-binding to avidin or streptavidin
Desthiobiotin is a single-ring, sulfur-free analog of biotin that binds to streptavidin with nearly equal specificity but less affinity than biotin (Kd = 1011 vs. 1015M, respectively). Consequently, desthiobiotinylated proteins can be eluted readily and specifically from streptavidin affinity resin using mild conditions based on competitive displacement with free biotin. For pull-down experiments with biological samples, this soft-release characteristic of desthiobiotin also helps to minimize co-purification of endogenous biotinylated molecules, which remain bound to streptavidin upon elution of the target protein complexes with free biotin.
An azide-reactive desthiobiotin reagent that allows easy eluion from streptavidin.
Highlights:
- Biocompatible – click reaction occurs efficiently under mild buffer conditions; requires no accessory reagents such as a copper catalyst or reducing agents (e.g. DTT)
- Chemoselective – azide and DBCO groups do not react or interfere with other functional groups found in biological samples, but conjugate to one another with high efficiency
- Desthiobiotin – allows easy elution from streptavidin, an ideal feature for affinity purification applications
- Extended PEG4 spacer – reduces aggregation, minimizes steric hindrance for affinity-binding to avidin or streptavidin
Desthiobiotin is a single-ring, sulfur-free analog of biotin that binds to streptavidin with nearly equal specificity but less affinity than biotin (Kd = 1011 vs. 1015M, respectively). Consequently, desthiobiotinylated proteins can be eluted readily and specifically from streptavidin affinity resin using mild conditions based on competitive displacement with free biotin. For pull-down experiments with biological samples, this soft-release characteristic of desthiobiotin also helps to minimize co-purification of endogenous biotinylated molecules, which remain bound to streptavidin upon elution of the target protein complexes with free biotin.
| Catalog Number | Product | DataSheet | Size | AVAILABILITY | Price | Qty |
|---|
| Product Type: | Small Molecule |
| Name: | DBCO-PEG4-Desthiobiotin |
| Chemical Formula: | C39H51N5O8 |
| Molecular Weight: | 719.87 |
| Variant MPN: | 1108 |
| Format: | Colorless to slightly yellow oil |
| Solubility: | DMSO, DMF, MeOH, DCM, THF |
| Storage: | -20C. Desiccate |
| Shipped: | Frozen overnight - Ambient |
- Mortison JD, Schenone M, Myers JA, Zhang Z, Chen L, Ciarlo C, Comer E, Natchiar SK, Carr SA, Klaholz BP, Myers AG. Tetracyclines Modify Translation by Targeting Key Human rRNA Substructures. Cell Chem Biol. 2018 Dec 20;25(12):1506-1518.e13. View Article
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