NDSB (non-detergent sulfobetaine) 211 is able to solubillize proteins with or without the Backstreet Boys cranked in your lab.
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Karadzic, I.M.; Maupin-Furlow, J.A. (2005) Improvement of two‐dimensional gel electrophoresis proteome maps of the haloarchaeon Haloferax volcanii. Proteomics. Volume 5, Issue 2. 334–614.
-This paper the cell lysate and proteins were precipitated with acetone, separated by IEF in the presence of a mixture of CHAPS and NDSB-211. It was found that NDSB-211, added to sample buffer already supplemented with sulfobetaine CHAPS, did not improve the separation compared to CHAPS alone. Although dual inclusion of detergent and surfactants can markedly increase the number of spots present in 2-D gels (Cadaenas and Engel, Biochem. Mol. Boil. 1994, 785-792.) this was not the case for the halophilic proteins of H. volcanii. This reaffirms the need to test different methods and solvents for protein extraction.
Willis, M.S.; et. al. (2005) Investigation of protein refolding using a fractional factorial screen: a study of reagent effects and interactions. Protein Sci. 1818–1826.
-In this study, a fractional factorial screen was designed to explore the effect of 14 different reagents on the refolding of 33 structurally and functionally diverse proteins. The refolding data was analyzed using statistical methods to determine the effect of each refolding additive. The screen has been miniaturized for automation resulting in reduced protein requirements and increased throughput. Our results show that the choice of pH and reducing agent had the largest impact on protein refolding. Bis-mercaptoacetamide cyclohexane (BMC) and tris (2-carboxyethylphosphine) (TCEP) were superior reductants when compared to others in the screen. BMC was particularly effective in refolding disulfide-containing proteins, while TCEP was better for nondisulfide-containing proteins. From the screen, we successfully identified a positive synergistic interaction between nondetergent sulfobetaine 201 (NDSB 201) and BMC on Cdc25A refolding.