Online hyphenation of capillary electrophoresis and mass spectrometry is nearly 30 years old, but has been ignored in certain camps. It’s time to give CE-MS a chance.

We ask an impossible question as 2015 comes to a close: which piece of literature stood out from the crowd

To formulate successfully with HA it is essential to understand the impact of factors such as molecular weight, molecular structure, concentration and degree of cross-linking on rheological characteristics such as viscoelasticity which are directly linked to aspects of product performance. Linking structural characteristics to product performance, via rheological properties, supports smart, fast, and effective formulation. The following study shows how rheology and particle size measurements can be used to characterize the physical properties of HA dermal fillers.

A new DNA-based sensor shows promise for indirect detection of thallium

Nanoporous gold helps ‘sieve out’ biological debris for fuss-free nucleic acid detection

Polyol-induced increases in thermal stability of antibodies. See how Differential scanning calorimetry can be used to assess the effects of polyol excipients on antibodies. DSC was used to monitor polyol-induced increases in thermal stability across seven monoclonal antibodies. The increases in thermal stability were measured as a function of polyol concentration and orientation of hydroxyl groups. It was found that increases in thermal stability were linear with respect to alcohol concentration.

In this report, we illustrate the utility of calorimetry in making better laboratory decisions. Examples will include improved protein construct selection for scale-up; direct measurement of the effects of mutations and post-translational modifications on protein stability; rapid optimization of solvent formulation; direct measurement of substrate and inhibitor binding affinity; determination of the mode of inhibitor binding; characterization of protein-protein interactions; and improved structural biology efficiency, when used in conjunction of other biophysical methods.

Contribution of variable domains to the stability of humanized IgG1 monoclonal antibodies Choosing the best antibody to progress in your biologic pipeline. Temperature-induced unfolding of three humanized IgG1 monoclonal antibodies and their Fab and Fc fragments was monitored by differential scanning calorimetry at neutral pH. With some exceptions, the thermogram of the intact antibody presents two peaks and the transition with the larger experimental enthalpy contains the contribution from the Fab fragments. Although the measured enthalpy was similar for all three Fab fragments studied, the apparent melting temperatures were found to vary significantly, even for Fab fragments originating from the same human germline.

Kickstarter technology is nothing new – but Clear Labs is making in-roads into something less common: kickstarter analytical science

Using total reflection X-ray fluorescence for the non-destructive analysis of nuclear fuel oxides