Freeze-thaw stability studies are a requirement for the successful development, distribution, and storage of a wide range of biopharmaceutical products.
Learn how to optimize the analysis of your viral vectors by reading our E-book.
Biopharmaceuticals, comprising monoclonal antibodies, antibody-drug conjugates, recombinant or fusion proteins, and bispecifics, among others, have recently gained commercial success and are rapidly changing the therapeutic landscape. Due to their large size and complex structures, characterizing these biotherapeutics requires robust and demanding analytical techniques. Often, traditional methods used to characterize proteins fail to deliver on either the sensitivity required or the speed desired to accelerate the drug development pipeline.
This note demonstrates the use of batch dynamic light scattering (DLS) and online multi-angle light scattering and dynamic light scattering in combination with field-flow fractionation (FFF-MALS-DLS) for characterizing large viral vectors such as lentivirus and gammaretrovirus. DLS in batch mode rapidly screens particle size distribution, concentration/titer and stability.
In this E-book, we present how light scattering can be used to characterize lipid nanoparticles (LNPs) in the product and process development stages.
In this white paper, we describe a validated FFFMALS method in line with technical specification ISO/TS 21362 for the analysis of lipid-based nanoparticles (LNPs) encapsulating siRNA and mRNA.
Thermostability screening by means of a temperature ramp is a common approach to assessing the aggregation propensity of different candidate molecules and formulation conditions. In this application note, we discuss how to screen by SEC-MALS and DLS.
Composition-gradient multi-angle light scattering (CG-MALS) provides easily interpreted data for complicated macromolecular interactions. Here we show how a simple protocol provides information-rich data with a completion time of a few hours.
AAV characterization and stability screening are achieved with multi-angle light scattering coupled to separation methods and high-throughput dynamic light scattering.
This white paper describes the technical innovations of the new Eclipse field-flow fractionation system and how they help the FFF-MALS user achieve new levels of performance, with less effort, in characterizing macromolecules, nanoparticles, nano-emulsions and other analytes in solution/suspension with sizes from 1 to 1000 nm.
While conventional calibration for gel permeation (GPC) or size-exclusion chromatography (SEC) is useful, there are inherent disadvantages in this type of analysis that introduce experimental error. This uncertainty may cast serious aspersions on the rigour and utility of the results. Multi-angle light scattering (MALS) detection is quite simple to add to an existing chromatography system and can help overcome the challenges faced with single detector chromatography and conventional calibration-based methods. An alternative separation technique called asymmetric flow field-flow fractionation (AF4) offers tunable, column-free fractionation.
Biopharmaceuticals, comprising monoclonal antibodies, antibody-drug conjugates, recombinant or fusion proteins, and bispecifics, among others, have recently gained commercial success and are rapidly changing the therapeutic landscape. Due to their large size and complex structures, characterizing these biotherapeutics requires robust and demanding analytical techniques. Often, traditional methods used to characterize proteins fail to deliver on either the sensitivity required or the speed desired to accelerate the drug development pipeline.