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NDSB 221

(NDSB Reagents)


SB221   3-(1-Methylpiperidinium)-1-propane sulfonate
[ 160788-56-7 ]   f.w.: 221.3 daltons

NDSB 221 is a non detergent sulfobetaine that prevents protein aggregation and facilitates the renaturation of chemically and thermally denatured proteins. Most enzymes remain active in the presence of these reagents. The applications are wide ranging in protein biochemistry useful to enhance extraction, solubilization and crystalization. The non detergent sulfobetaine reagents are zwitterionic, very soluble in water ( greater than 2.0 molar), do not alter significantly the pH or viscosity of biological buffers and can easily be removed by dialysis.



Quantity Price  
5gm $34.20
10gm $70.00
25gm $161.50


NDSB 221 is a non detergent sulfobetaine that prevents protein aggregation and facilitates the renaturation of chemically and thermally denatured proteins. Most enzymes remain active in the presence of these reagents. The applications are wide ranging in protein biochemistry useful to enhance extraction, solubilization and crystalization. The non detergent sulfobetaine reagents are zwitterionic, very soluble in water ( greater than 2.0 molar), do not alter significantly the pH or viscosity of biological buffers and can easily be removed by dialysis. NDSBs contain a hydrophilic sulfobetaine group and a short hydrophobic group. Hence, NDSBs cannot form micelles and are not considered detergents. Despite this, NDSBs have been used successfully to increase the yields of membrane, nuclear, and cytoskeletal associated proteins.It has been suggested that the NDSBs short hydrophobic group interacts with the hydrophobic regions on proteins to prevent aggregation. An analogy for using NDSB non detergent sulfobetaines with proteins and detergents would be to look at these reagents as fabric softeners. Examples: NDSB 221 at 1.8 molar yields about 15% native hen egg white lysozyme, which is about 10 fold higher than in the absence of NDSB221.

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  • Prevents protein aggregation
  • Facilitates the renaturation of chemically and thermally denaturated proteins
  • Zwitterionic over a wide pH range •Easily removed by dialysis