Welcome to Iris Biotech
For better service please confirm your country and language we detected.
Währung
EUR
Cleavable Bifunctional Biotin-Linkers
Cleavable Bifunctional Biotin-Linkers
Published on 11.11.2019
However, removal of captured proteins from Streptavidin can be problematic due to the strong nature of the binding. One possible solution to this problem are linkers that allow for a selective cleavage following purification.
We recently introduced three bifunctional clickable linkers that each bear a biotin moiety on one end as well as a clickable group (azide or alkyne) on the other. Those two ends are connected by a Dde-based linker. Dde [N-1-(4,4-dimethyl-2,6-dioxocyclohexylidene)ethyl] is stable to denaturing wash conditions as well as acidic and basic conditions, while allowing for a mild and selective cleavage with a buffered aqueous solution of 2% hydrazine. Consequently, our new bifunctional linkers can be selectively attached to appropriately modified biomolecules via Click-chemistry, allowing for subsequent purification on Streptavidin beads followed by mild release of the captured protein from the beads.
→ Order our catalogue Biotinylation Reagents, or download the E-Book, to get a comprehensive overview of our compounds for biotinylation.
Biotinylation of an azide-bearing glycoprotein using Click-chemistry, followed by purification of the labelled protein over Streptavidin beads, release of the protein by hydrazinolysis of the Dde-group, and analysis of the isolated glycoprotein (adapted from Griffin et al. Mol. Biosys. 2016).
We recently introduced three bifunctional clickable linkers that each bear a biotin moiety on one end as well as a clickable group (azide or alkyne) on the other. Those two ends are connected by a Dde-based linker. Dde [N-1-(4,4-dimethyl-2,6-dioxocyclohexylidene)ethyl] is stable to denaturing wash conditions as well as acidic and basic conditions, while allowing for a mild and selective cleavage with a buffered aqueous solution of 2% hydrazine. Consequently, our new bifunctional linkers can be selectively attached to appropriately modified biomolecules via Click-chemistry, allowing for subsequent purification on Streptavidin beads followed by mild release of the captured protein from the beads.
→ Order our catalogue Biotinylation Reagents, or download the E-Book, to get a comprehensive overview of our compounds for biotinylation.
References:
- Mapping the Binding Site of BMS-708163 on gamma-Secretase with Cleavable Photoprobes; N. Gertsik, C. W. Am Ende, K. F. Geoghegan, C. Nguyen, P. Mukherjee, S. Mente, U. Seneviratne, D. S. Johnson and Y. M. Li; Cell Chem Biol 2017; 24: 3-8. doi:10.1016/j.chembiol.2016.12.006
- Comprehensive mapping of O-GlcNAc modification sites using a chemically cleavable tag; M. E. Griffin, E. H. Jensen, D. E. Mason, C. L. Jenkins, S. E. Stone, E. C. Peters and L. C. Hsieh-Wilson; Mol Biosyst 2016; 12: 1756-9. doi:10.1039/c6mb00138f
- Cleavable trifunctional biotin reagents for protein labelling, capture and release; Y. Yang and S. H. Verhelst; Chem Commun 2013; 49: 5366-8. doi:10.1039/c3cc42076k
Verwandte Produkte
