Nanotrap® Blue Protein Capture Kit
The Ceres Nanosciences Nanotrap® Protein particles utilize affinity capture and size exclusion to attract and bind low abundance proteins, while excluding unwanted high abundance and high molecular weight interfering molecules.
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Plasma proteomics
The Blue Nanotrap product exceeded my expectations for enrichment of low level proteins as measured by LC-MS/MS analysis. Over the years we have used multiple vendors' affinity depletion and enrichment products and the nanotraps outperformed all hands-down. The team at Ceres were very helpful and interested in our experience - great product support.
Review Date: 25 Mar 2020 | Ceres Nanosciences, Inc.
Nanotrap particles offer a simple and effective approach to protein biomarker discovery from complex human or animal samples such as plasma, serum, urine, and cell cultures.
Unlike other sample prep solutions, Nanotrap particles utilize affinity capture and enrichment to attract and bind low abundance proteins, while excluding unwanted high abundance proteins, resulting in improved proteome coverage. Nanotrap particles do not utilize antibodies or other biomolecules as affinity molecules.
There are three types of Nanotrap particles for protein enrichment for mass spectrometry. Each uses a different affinity capture molecule and each will have a slightly different capture profile. Nanotrap particles can increase the enrichment of proteins below 60 kilodaltons from plasma by at least 2-3 fold as compared to the same volume of neat sample.
Easy-to-follow sample processing protocol for enrichment of low abundance proteins from serum, plasma, saliva, and urine prior to analysis by mass spectrometry. A simplified "on particle" digestion method which reduces processing time by performing protein digestion and clean up while the proteins are still bound to the Nanotrap particles.
Each 100 µl unit of Nanotrap protein particles can be used to process up to 10 mg of protein per sample. Nanotrap particles perform better in enrichment of low molecular weight proteins than other methods.