Hi all,
I am currently setting up a protocol to biotinylate the extracellular part of membrane proteins on cells (and in particular yeasts cells). I found 2 reagents that seems both suitable but I would like to know which one could be more appropriate. Did anyone test both of them (or even only one of them) and in which context ? Does the sulfo group have an importance for the reaction ?
In advance, thank you very much for your answers and your help !
Lucile
The sulfo-group makes the molecule less hydrophobic "Activation with NHS, however, decreases water- solubility of the modified carboxylate molecule, while activation with Sulfo-NHS preserves or increases water-solubility of the modified molecule, by virtue of the charged sulfonate group" http://tools.thermofisher.com/content/sfs/manuals/MAN0011309_NHS_SulfoNHS_UG.pdf. The SS in Sulfo-NHS-SS-biotin allows to cleave the linker by reducing the disulfide bond, e.g. if you use biotin to pull down your protein with streptavidin beads and want to elute it from the beads after pull-down. NHS-PEG4-Biotin has a somewhat longer linker between the NHS and the biotin.
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