The characterization of complex polyclonal anti-HCP antibodies has traditionally been accomplished by 2 dimensional Western blot as correlated to a non-specific silver stain. We discuss the limitations of this method and suggest 2D HPLC fractionation of HCPs followed by ELISA detection as a much more sensitive, specific, and quantitative method to detect individual HCPs. This paper shows data comparing the 2 methods on both an upstream and final drug substance sample.

The biotechnology industry has mushroomed over the past decade, with revenues increasing from $8 billion in 1992 to $39 billion in 2003,1 and it shows no signs of slowing down. New therapeutics are entering and pressing through clinical trials. Treatments are emerging from clinical trials ready for marketing and scaling up for commercial production, leading to a growing need for new facilities.

Surface analysis using grazing-angle FTIR spectroscopy provides an in-situ, real-time method for cleaning validation. Recent trials at three manufacturing facilities show that the method works well under real-life conditions.

In-situ FTIR spectroscopy provides a direct view of the "vital signs" inside a fermenter. Tracking dissolved carbon dioxide is an important part of this monitoring method.

The Waters Synapt HDMS System combines high-efficiency ion mobility with high-performance tandem mass spectrometry. This enables the analysis of samples differentiated by size, shape, and charge, as well as mass, to deliver increased specificity and sample definition. In this study, we describe the use of HDMS to quickly obtain a partial amino acid sequence of a monoclonal antibody (MAb) via a top-down approach.

Biopharmaceutical companies are requiring their analysts to screen increasingly larger quantities of monoclonal antibody samples to support clone selection, stability, and product formulation studies. In this study, we have combined a quadrupole-based LC/MS system, the ACQUITY SQD, with robust methodology, using the MassPREP Micro Desalting Column, for rapid sample desalting and efficient variant profiling of reduced monoclonal antibodies.

Within the human body many circulating proteins are glycosylated, and therefore the most promising candidate drugs for biopharmaceutical use have glycan chains. The oligosaccharide components can directly affect the efficacy and safety of these drugs by influencing binding, immunogenicity, and turnover. It is, therefore, critical to characterize oligosaccharide structure in biopharmaceutical development.

Cell culture techniques are routinely used to produce proteins intended for use as biopharmaceuticals. The culture conditions must be optimized to ensure that the protein is produced without structural modification and in the highest possible yield. These preferred conditions will often be different for each clone investigated, so a large number of optimization experiments may be required.

Transforming Technology Transfer and Process Definition Management: From Spreadsheets to Standardized Practices