Sample Preparation

Learn how Isothermal titration calorimetry can be used to guide protein (RNA)/ligand crystallization and to resolve common issues with crystallization of complexes.

Determining the components, and their proportion, in a protein sample is essential for the improvement of candidate formulations and characterization of final formulations.

In what should be our constant endeavor to improve sample preparation, we must look to new materials – and focus on bending them to our own needs.

The techniques of laser diffraction and automated particle imaging support the fast, cost-effective development of nasal spray products, simultaneously providing the data required for regulatory compliance. This paper examines their application.

GPC/SEC is mainly used for the characterization of macromolecules including synthetic and natural polymers (including polysaccharides) as well as proteins or RNA/DNA. This white paper provides an introduction to the technique in 30 minutes.

In this application note, we show that Malvern’s OmniSEC software can now communicate with Waters Empower® for the seamless exchange of sample sequences. This allows OmniSEC to follow the injections performed by a Waters SEC system and to synchronize data collection. A selection of proteins was used to demonstrate the measurement of protein molecular weight, oligomeric and aggregation state.

Four different polymers are analyzed by GPC/SEC to investigate the effect of molecular weight, dispersity and molecular structure on the final properties of the polymer.

This paper shows how using a solvent trap can be used to prevent sample drying/solvent loss during extended testing, helping to ensure that only rheological changes are being measured and not artifacts resulting from drying of the sample at the air/sample interface.

The top 10 reasons to consider an advanced multi-detector SEC system, which incorporates light scattering detectors for the measurement of absolute molecular weight and molecular weight distribution with excellent accuracy.

The stability of a protein sample and its tendency to aggregate is explored using a combination of SEC-MALS and DLS