Unique Intact Proteins Insight

Intact proteins and antibodies, whether naturally occurring or manufactured, exist as a population of variants. These complex populations are the result of post translational modifications and degradation that can occur during expression, processing and storage. These modifications may include disulfide bond scrambling, glycosylation, deamidation, pyroglutamate formation, C-terminal lysine truncation, oxidation, and amino acid substitutions among others. In order to be used as a therapeutic agent the biomolecule must be fully characterized to ensure safety, efficacy and potency. Mass Spectrometry is ideal for unique identification but requires pre-separation to simplify the data for analysis. Historical separation techniques for proteins and antibodies are incompatible with MS as they require high salt content.

Full Characterization. Fast.

ZipChip is the only directly MS-compatible technique that separates protein and antibody variants. ZipChips integrate both separation and electrospray ionization on a single device – near native-state protein variants with a full mass spectrum behind every peak! With ZipChip HR, proteins require no sample prep and analysis is complete in 3 minutes.

Empowering Traditional Mass Spec

ZipChip™ uses integrated microfluidic technology to prepare, separate and electrospray biological samples directly into traditional mass spectrometers (MS).

In less than 3 minutes per sample, the cost-effective ZipChip analyzes a broad range of matrices from growth media to cell lysates, blood, plasma, urine and biopharma products. ZipChip delivers answers on analytes from small molecules and peptides up to intact proteins, antibodies and antibody drug conjugates; providing better separation quality than most liquid chromatography instruments — in a fraction of the time — all with full MS identification behind every separations peak. The ZipChip interface simply mounts onto your mass spectrometer for seamless integration with existing data collection and processing.

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