Analysis of proteins by SEC-MALS with UHPLC provides the same results as with HPLC, while requiring less protein, mobile phase and time per measurement. Learn more by reading our application note.
This application note shows how the combination of column chromatography (SEC/GPC) with multi-angle light scattering (MALS) can be applied as a powerful tool to identify monomers, dimers, hexamers and higher aggregates of insulin.
Drug-Antibody Ratio (DAR) is a critical attribute of antibody-drug conjugates (ADCs). DAR may often be determined quickly and effectively by combining SEC with three online detectors: MALS, UV and dRI.
Transient self-association may be evaluated by SEC-MALS to obtain binding affinity of a protein in monomer-dimer dynamic equilibrium.
Intrinsically-disordered proteins cannot be analyzed by SEC columns calibration. SEC-MALS provides accurate molecular masses of these proteins and of their complexes with other proteins. Learn more.
Quality and consistency in reagents is critical to successful drug discovery and development. When targeting a particular protein of interest, in vitro experiments should be performed with proteins of biological properties similar to those for in vivo tests. It is important that molecularity, purity, shape and degree of heterogeneity remain the same when any alterations are made.
Reversed-phase chromatography (RPC) represents one of the most popular applications of HPLC, with particular importance for protein characterization. Adding a DAWN or miniDAWN multi-angle light scattering (MALS) detector to one’s HPLC system, however, simplifies protein identification significantly. It allows one to measure absolute molar masses directly, irrespective of retention time, and to observe the properties of the protein in solution.
This note shows that the concomitant use of a DAWN multi-angle light scattering (MALS) detector and RPC constitutes a powerfully effective means to determine both molar mass and size for the wheat protein, TAM 105.
In this application note we demonstrate the information that can be obtained on the results of a PEGylation process by combining size-exclusion chromatography with multi-angle light scattering (SEC-MALS) to analyze conjugation.
SEC-MALS is not just for large proteins - it can even be used for small peptides below 1 kDa. In fact, a DAWN® or miniDAWN® multi-angle light scattering (MALS) detector is instrumental in obtaining on-line molar mass determinations for peptides of fewer than a thousand Daltons. Learn more by reading our application note.
In this application note we demonstrate the use of multi-angle light scattering (MALS) detection in combination with UV absorption and differential refractive index (DRI) detection to determine the molar masses (MM) of both the core protein and the entire protein-lipid complex.
Kinase fragments lacking the purported oligomerization domain are shown by SEC-MALS to dimerize. Reliance on column calibration by globular proteins would have lead to the deduction of kinase trimers or tetramers.