A three-step purification process for a Dab successfully developed and verified. The step yield ranged between 86% and 99%, giving a total process yield of approximately 81%. The ECP in the start sample was more than 200 000 ppm whereas the final sample contained only 5.5 ppm. The endotoxin content in the feed was approximately 2 million endotoxin units/mg of protein and the final sample was below the limit of quantification. Protein L leakage was undetectable in all samples. This…

Micro-flow imaging (MFI) is a sensitive, simple and automated method for the analysis of sub-visible particles and translucent protein aggregates that provides particle size, count and morphology. Because it quantifies particle shape, this technology can discriminate groups of particles from each other, and evaluate how these groups change over time. In this article, we provide an overview of how biopharma is using MFI to characterize and monitor their protein formulations in new and emerging applications.  

This application note describes a model system in which Enbrel® protein, a fusion protein consisting of TNF receptor and IgG1 Fc, is purified from a dilute sample matrix for further analytical characterization. The resulting purified protein was subjected to N-linked glycan structural analysis by mass spectrometry (MS) and its aggregation state was assessed by analytical ultracentrifugation (AUC). This data set serves as a model to demonstrate the capability of the POROS® CaptureSelect™ product line for the affinity purification of biomolecules…

Platform methods, high resolution and ease of use have made the iCE system the gold standard for protein charge heterogeneity characterization for biopharmaceuticals. At 15-18 minutes per sample, iCE methods are already fast and simple but now they are even better. In this white paper we describe a high throughput 10 minute charge heterogeneity analysis method and performance improvements that provide automated analysis of 100 samples at a time.