Reva Detergent Removal Resin
Detergents or surfactants are used extensively in protein chemistry to solubilize and stabilize proteins and to disaggregate protein complexes . However, the presence of excess unbound detergent interferes with many downstream applications like ELISA, enzyme assays, isoelectric focusing, and mass spectrometry. Orochem’s REVA detergent removal resin specifically binds and removes high concentrations of a wide variety of detergents used in protein research for the preparation of biological samples.
The resin is designed for the efficient removal of a wide variety of commonly used ionic, nonionic, and zwitterionic detergents from proteins and peptide samples with high sample recovery in a centrifuge format for 25 to 1000 μl samples. Detergent removal is based on the presence of a small hydrophobic cavity in the resin into which appropriately sized non-polar moieties such as detergents can enter to form an inclusion complex.
The easy-to-use spin format is fast (less than 15 min) and significantly improves results over the standard drip column and batch methodologies with >95% removal of detergents. The resin is available in bulk resin slurries, 96-well plate format for high-throughput applications as well as in spin column format.
- Efficient Detergent Removal – removes >95% of detergents
- Easy-to-use – no cumbersome column preparation or equilibration
- Fast – no waiting for protein to emerge by gravity-flow
- High protein recovery – low non-specific protein binding resin maximizes protein recovery
 Neugebauer, J. (1990). Methods Enzymol. 182, 239-282.
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|Overall Proteomics Flyer||File size: 6.3MB||Download|
|Proteomics General Brochure||File size: 4MB||Download|
|Reva Detergent Removal Resin||File size: 2.7MB||Download|
|Automated tryptic digestion procedure for HPLC/MS/MS peptide mapping of immunoglobulin gamma antibodies in pharmaceutics||Chelius, Dirk, Gang Xiao, Andrew C. Nichols, Alona Vizel, Bing He, Thomas M. Dillon, Douglas S. Rehder et al. Journal of pharmaceutical and biomedical analysis 47, no. 2 (2008): 285-294.||Amgen, CA|
|Immunoglobulin G (IgG) Fab glycosylation analysis using a new mass spectrometric high-throughput profiling method reveals pregnancy-associated changes||Bondt, Albert, Yoann Rombouts, Maurice HJ Selman, Paul J. Hensbergen, Karli R. Reiding, Johanna MW Hazes, Radboud JEM Dolhain, and Manfred Wuhrer. Molecular & Cellular Proteomics 13, no. 11 (2014): 3029-3039.||Erasmus University Medical center, UV University Amsterdam, The Netherlands,|