DetergentOUT™ GBS10 (10 Citations)
Detergents are essential for protein solubility during protein extraction and sample preparation, especially when working with hydrophobic proteins. The presence of high concentrations of detergents in protein samples can impair ELISA, IEF, protease digestion of proteins, and suppress peptide ionization when analyzed by mass spectrometry.
DetergentOUT™ GBS10 features a research grade detergent binding resin that has a high affinity for most detergents and a low affinity for proteins and peptides. DetergentOUT™ GBS10 is ideal for detergent removal prior to ELISA, IEF, protease digestion of proteins, and peptide ionization when analyzed by mass spectrometry.
DetergentOUT™ GBS10 is available in four spin format column sizes or as resin alone. The column specifications are:
Cat. # | Description | Sample Size (µl) | Resin Volume (µl) |
786-154 | DetergentOUT™ GBS-10-125 | 10-30 | 125 |
786-155 | DetergentOUT™ GBS-10-800 | 30-200 | 800 |
786-156 | DetergentOUT™ GBS-10-3000 | 200-750 | 3,000 |
786-157 | DetergentOUT™ GBS-10-5000 | 500-1,250 | 5,000 |
Our DetergentOUT™ GBS10 resin removes free, unbound anionic, nonionic or zwitterionic detergents (e.g. SDS, Triton® X-100 or CHAPS) from aqueous protein and peptide samples with minimal sample loss (Table below) for downstream analysis by mass spectrometry (Figure 1 & 2) and other techniques.
Also available in 96-well spin plate formats for processing up to 96 samples.
The DetergentOUT™ GBS10 columns were shown in independent studies to be fully compatible with DI-QTOF and LC-MS/MS (see references). The use of the DetergentOUT™ GBS10 columns significantly increased the number of peptide spectra detected (Figure 1 & 2).
In addition, the DetergentOUT™ GBS10 columns have a high binding capacity for detergents, with 6 milligrams SDS (Figure 3) and 14 milligrams Triton® X-100 for every milliliter of settled resin.
Detergent | % Removed | BSA | Phosphorylase B | Cytochrome C | E.coli Lysate |
---|---|---|---|---|---|
Triton X-100, 2% | >99 | >90 | >91 | >92 | >93 |
Triton X-114, 2% | >96 | >99 | >98 | >97 | >91 |
Nonidet P-40, 1% | >96 | >93 | >95 | >91 | >91 |
Brij 35, 1% | >99 | >98 | >99 | >97 | >91 |
SDS, 2.5% | >99 | >96 | >97 | >92 | >90 |
Sodium deoxycholare, 5% | >99 | >99 | >99 | >98 | >95 |
CHAPS, 3% | >99 | >92 | >95 | >92 | >91 |
Octyl glucoside, 5% | >99 | >93 | >95 | >96 | >91 |
Lauryl maltoside, 1% | >97 | >99 | >99 | >99 | >91 |
Tween 20*, 0.25% | >98 | >86 | >85 | >89 | >85 |
Tween 80*, 0.13% | >85 | >83 | >81 | >80 | >81 |
Detergent removal rates and percentage protein recovery with DetergentOUT™ GBS10
- For removal of polysorbate detergents (commercially known as Tween®), we recommend using our DetergentOUT™ Tween® columns.
- For removal of detergents from protein solutions, including hydrophobic protein solutions, try our highly flexible and compatible OrgoSol DetergentOUT™ columns.
- Click here to request bulk or custom sizes.
Features
- Easy-to-use, spin-format columns
- Rapid removal of free detergents
- Suitable for anionic, non-ionic and zwitterionic detergents
- Minimal sample loss
- Available for sample volumes ranging from 10µl to 1,250µl
Applications
- Detergent removal from protein and peptide solutions
- Detection of peptide fragments by Mass spectrometry
- Enhances Mass spectrometry Spectra
- Ideal for Mass spectrometry sample preparation and prior to downstream analysis and applications
Protocol | |
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Material Safety Data Sheet | |
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Technical Literature | |
ASMS Poster, May 2010 | Alvarez, S. et al. Efficiency assay of detergent removal columns on protein and peptide samples for mass spectrometric analysis. Poster presented as part of the 58th ASMS Conference on Mass Spectrometry and Allied Topics, May 23-27, 2010, Salt Lake City, Utah |
Detergent Handbook & Selection Guide | A Comprehensive Guide to the Properties and Uses of Detergents in Research. Also features information on detergent removal systems. |
Detergent Handbook & Selection Guide | A Comprehensive Guide to the Properties and Uses of Detergents in Research. Also features information on detergent removal systems. |
Highly efficient detergent removal for improved mass spectrometry analysis | Detergents are essential for protein solubility during protein extraction and sample preparation, especially when working with hydrophobic proteins. The presence of high concentrations of detergents in protein samples can impair ELISA, IEF, protease digestion of proteins and suppress peptide ionization when analyzed by mass spectrometry. Our DetergentOUT™ GBS10 resin removes free, unbound anionic, nonionic or zwitterionic detergents (e.g. SDS, Triton® X-100 or CHAPS) from aqueous protein and peptide samples with minimal sample loss for downstream analysis by mass spectrometry and other techniques. Remove Free Aqueous Detergents Prevent Interference of Downstream Applications Improve Mass Spec. Detection The application note shows how DetergentOUT™ GBS10 improves mass spec detection of peptides after detergent removal. Download the free application note to find the key to improved mass spectrometry analysis! |
Mass Spectrometry Sample Prep Handbook | A guide to the preparation of protein samples for Mass Spectrometry, including protein extraction, clean-up and peptide generation. |
Plant Proteomics Handbook | |
Protein Electrophoresis Handbook | A guide to 1D and 2D protein electrophoresis products, including protein markers, electrophoresis buffers, 2D electrophoresis reagents, clean-up reagents and stains. The guide also offers protein sample preparation products. |
Protein Purification Handbook | |
Sample Preparation Handbook | For Lysis Buffers, Fractionation, Dialysis, Protein Concentration and Enrichment |
Certificate Of Analysis | |
786-156 |
- Ito-Kureha, T et al (2020) Nat. Comm. doi.org/10.1038/s41467-020-19975-4
- Haddock, E. and Feldmann, F. (2017) Validating the Inactivation Effectiveness of Chemicals on Ebola Virus. Methods Mol Biol. 1628:251
- Srivastasva, O.P. et al (2017) Post-Translationally Modified Human Lens Crystallin Fragments Show Aggregation in vitro. Biochemistry and Biophysics Report. http://dx.doi.org/10.1016/j.bbrep.2017.01.011
- Chiu, J. et al (2016) Knockout of a difficult-to-remove CHO host cell protein, lipoprotein lipase, for improved polysorbate stability in monoclonal antibody formulations.Biotechnol Bioeng. DOI: 10.1002/bit.26237
- Haddock, E. et al (2016) Effective Chemical Inactivation of Ebola Virus. Emerg Infect Dis. Vol 22:7.
- Min, L. et al (2015) Electrophoresis. DOI: 10.1002/elps.201400579
- Valente, K. N. et al (2014) Biotechnol Bioeng. DOI: 10.1002/bit.25515
- Hou, S. et al (2013) Methods. 61:269
- Hashii, N. et al (2005) Proteomics. 5:4665
- Higgins, D. et al (2005) Anitmicrob. Agents Chemother. 49:1127