The Thermo Scientific Aspire RP30 Desalting Tip contains a bed of proprietary porous Styrene-divinylbenzene (SDVB) reversed-phase resin, which allows the removal of ion-suppressing contaminants from digested complex protein mixture prior to LC/MS or LC/MS/MS analysis, improving sensitivity and data quality (Table A). The Aspire tips offer superior overall peptide binding and recovery compared to the conventional C18 products (Figure 1). The Aspire tip employs a rapid purification protocol which streamlines low to medium-throughput sample clean-up.
Learn about a fast and effective way to facilitate MS sample cleanup that significantly improved sensitivity and MS data quality.
**Random Drawing Winner**
The winner of the Aspire Starter Kit Random Drawing is Liang Zhao from University of Pacific! The kit includes two Thermo Scientific Aspire RP30 Desalting Tip Kits and a Thermo Scientific Finnpipette Novus Electronic Multichannel Pipette.
**Special Offer**
For a limited time! Take advantage of our introductory Starter Kits offering. The starter kits include two Thermo Scientific Aspire™ RP30 Desalting Tip Kits and a Finnpipette® Novus Electronic Multichannel Pipette.”
Aspire RP30 Desalting Tips
Aspire RP30 Highlights:
Improve Sensitivity and MS Data Quality - Removes salt, detergents and other ion-suppressing contaminants. Increases signal-to-noise ratios and sequence coverage.
Effective Sample Clean-Up Prior to LC/MS and LC/MS/MS Analysis - Proprietary reversed-phase resin allows superior peptide binding and recovery of digested protein complex mixtures compared to conventional C18 products.
Fast and Easy - 20-minute purification protocol features color-coded parallel sample processing.
Table A
Processing Method
Number of Proteins Identified
Number of Unique Peptides Identified
C18 Trap Column
19
139
Aspire RP30 Desalting Tip + C18 Trap Column
27
212
Table A. Results from 1-hour LC/MS/MS runs of tryptic-digested protein complex samples (mixture of 48 proteins). The Aspire tip further removes salts, detergents and other ion-suppressing interference present in the samples. As a result, peptide fragments are more readily detected and the total number of protein identifications increases.
Figure 1
Figure 1 - The mass chromatograms of a single ion corresponding to the peptide with the m/z of 528 were extracted and traced. Due to the improved peptide binding and recovery of the Aspire tip, the ratio of the target peptide peak/contaminant peak is substantially higher compared to the unprocessed sample and the sample purified by competitor’s C18 product.
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