The data presented in this paper is generated from SLS and DLS experiments that monitored the solution behavior of rAAV capsids with and without DNA. The comparison and superimposition of SLS and DLS scattering profiles provides insights into the differential colloidal stability of the full and empty species, as well as a dynamic quantification of...Read More
In this case study, ARGEN was used to determine the effect of protein concentration on the aggregation propensity of bovine serum albumin under stirring stress.Read More
These rAAV capsid stability experiments investigated and monitored the solution behavior of full and empty capsids under thermal stress using ARGEN. ARGEN is uniquely suitable for in situ and real-time characterization of solution stability of larger species such as rAAVs and LNP-RNA complexes. This case study demonstrates ARGEN's ability to elucidate differences in full and...Read More
The ARGEN eBook discusses the key indicators of biopolymer instability, the importance of accelerating development times, and how ARGEN expedites the development of stable biopolymers.Read More
The ARGEN Digital Booklet provides insight into various applications utilizing ARGEN’s patented simultaneous multiple sample light scattering (SMSLS) technology to accelerate and optimize the development of novel biotherapeutics. Biopharmaceutical companies are experiencing greater demand to develop novel biologic therapeutics in less time, and this requires a paradigm shift in the way teams approach formulation development...Read More
The successful development of biotherapeutics requires an in-depth understanding of the impacts associated with mechanical and physical stress. Instability and subsequent aggregation can render them biologically inactive or even induce an immunological response in patients. Stirring stress is one of the most notable factors which disrupts native biopolymer structure and promotes aggregation. However, contact stirring...Read More
On the limits of 90° static light scattering for determining weight average molar mass Mw A discussion with Chief Science Officer, Dr. Wayne Reed This Technical Note assesses the fractional error in Mw that results when θ=90° static light scattering detection is used, instead of a full angular extrapolation via MALS. Read More
Colloidal stability is determined by the balance of repulsive and attractive intermolecular interactions between protein molecules, like a monoclonal antibody, to conserve the native folded state. Simply stated, the propensity for aggregation is reduced by less intermolecular interaction. Therefore, determination of the second virial coefficient (B22) is a valuable screening tool to predict aggregation propensity....Read More
These experiments demonstrate the utility of ARGEN™ to define oligomeric states and transitions of Human Insulin under thermal stress. Time to dimerization and time to tetramerization measurements permitted the characterization of a stable dimer species, as well as insights into the mechanisms and kinetics of higher order oligomer formation. Whereas, SEC allows the characterization of...Read More
In these experiments, ARGEN was used to characterize the thermal and chemical stability of a monoclonal antibody and subsequently establish quantitative and qualitative properties such as pH and temperature dependence on aggregation kinetics. Additionally, SEC elution profiles were superimposed onto Mw/Mo output, providing a robust comparison and identification of the stability landscape for the mAb....Read More
