Monoclonal antibodies (mAbs) represent a rapidly growing class of therapeutics designed to target and bind to specific proteins to treat a variety of diseases, including cancer, autoimmune disorders, and infectious diseases. They can be custom engineered to have specific properties that suit specific therapeutic needs, such as increased potency, longer half-life in the body, or reduced immunogenicity.
As the field continues to advance, the molecular diversity of mAbs is increasing rapidly, where non-traditional mAb formats such as bispecific antibodies, fragments, and antibody-drug conjugates now account for up to a quarter of projects in the clinical pipeline. Conventional purification protocols relying on protein A may not always be suitable for these novel antibody variants since they may require new ligands or base matrices for effective capture of target molecule and separation of impurities. Therefore, the development of chromatography resins that can accommodate these variants is crucial for manufacturing and process development in the evolving landscape of mAb therapeutics.
Cytiva has released a new protein L resin—the MabSelect™ VL resin—designed to more effectively capture antibody Fabs, bispecific antibodies, and other molecules containing kappa variants of the variable light (VL) chain. Compared to its predecessor, the Capto™ L resin, a two-fold increase in binding capacity of MabSelect™ VL resin is observed. The MabSelect™ VL resin provides highly effective purification and separation of product-related impurities for capturing antibody variants that do not bind to protein A or when protein A does provide separation of impurities. The resin is available in a wide range of formats suitable for research to clinical and commercial scale chromatography purification.
Key features of MabSelect™ VL resin include:
High dynamic binding capacity (DBC) for bispecific antibodies and antibody fragments containing a kappa light chain subclasses 1, 3, and 4
Stable when cleaned with 0.1 M NaOH, reducing risk for bioburden incidents
Provides good resolution for product-related impurities in the capture of bispecific antibodies