Novel click chemistry probes for enrichment of azide-tagged biomolecules. This probe overcomes a major drawback of the streptavidin-biotin affinity purification associated with extraordinary strength of the streptavidin-biotin interaction. These probes contain a biotin moiety linked to an alkyne group through a spacer arm containing a Dde linker. Dde moiety is stable to rigorous, denaturing wash conditions, acidic or basic conditions including generally applied buffer systems to which the biological sample may be exposed. At the same time Dde linker can be quantitatively cleaved under mild aqueous buffered conditions with 2% hydrazine. Finally, the cleaved moiety that remains on the modified peptide minimally changes the peptide mass and generates an additional positive charge, which facilitates peptide sequencing by ETD.
|Molecular weight left behind||55.07|
|Solubility||DMSO, DMF, THF, DCM, Chloroform|
|Shipping conditions||Ambient temperature|
1. Yang Y., et al. (2013). Cleavable Trifunctional Biotin Reagents for Protein Labeling, Capture, and Release. Chem. Commun., 48: 5366-5386.
2. Matthew E. G., et al. (2017). Comprehensive Mapping of O-GlcNAc Modification Sites Using a Chemically Cleavable Tag. Mol. Biosyst, 12(6): 1756–1759.
3. Gertsik N., et al. (2017). Mapping the Binding Site of BMS-708163 on y-Secretase with Cleavable Photoprobes. Cell Chemical Biology, 32: 3-8.
|THTPA||A water-soluble ligand for copper-catalyzed azide-alkyne cycloadditions (CuAAC).|
|BTTAA||A newest generation, water-soluble accelerating ligand for CuAAC.|
|Click-&-Go™ Protein Reaction Buffer Kit||All-inclusive kit that provides everything required to perform CuAAC on azide or alkyne tagged proteins with the corresponding click detection reagent.|