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Ion Exchange Chromatography with Agarose Beads in Antibody Purification
ABT agarose beads provide reliable performance in ion exchange chromatography, ensuring high protein binding, precise separation of charge variants, and reproducible results from lab-scale analysis to industrial antibody purification.
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ABT at Analytica 2026: Advancing Bioprocessing Innovation in Munich
From March 24–27, ABT will be showcasing its expertise in agarose-based resins and custom chromatography solutions at Analytica 2026 in Munich, Germany. Visit us to explore how our advanced purification technologies can support scalable and high-quality bioprocess workflows. Our team will be on-site to discuss tailored solutions designed for pharmaceutical and biotech leaders seeking robust, reproducible, and high-performance results.
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ABT to Attend Bioprocessing Summit Europe 2026: High-Performance Agarose Resins for Downstream Processing
ABT will attend Bioprocessing Summit Europe 2026 in Barcelona. Discover how our agarose chromatography resins support scalable, robust downstream processing from early development to GMP manufacturing.
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Next Stop: BPI Boston 2025!
ABT returns to Bioprocess International Boston, where the future of bioprocessing from cell line and cell culture to downstream and next generation manufacturing, is showcased.
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"ABT Antibody Purification resins have demonstrated that the instability of the HIV HLA-E peptidome may be a significant barrier to therapeutic targeting of these antigens"
Naturally occurring T cells may play a crucial role in universal immunotherapy by recognizing antigens through nonpolymorphic human leukocyte class Ib (HLA-E).
However, uncertainties remain regarding the biological relevance of these ligands due to poorly understood mechanisms of pathogen-derived peptide access to the HLA-E pathway.
Therefore, studying these HLA-E ligands is essential for addressing diseases as significant as HIV (1,2).
In this paper, among other informatic and cellular assays, researchers proceed with an immunopurification of peptide-HLA complexes from HIV infected cells using high-performance Agarose Bead Technologies (ABT) resins (Fig 1).
The ABT resins used were Protein L Agarose Resin linked to 3D12 antibody and Protein A Agarose Resin.
Figure 1. Schematic representation of performed cellular and biochemical assays followed by immunopurification (Adapted from 1).
The study highlights the potential contribution of ABT resins in pharmacological research and treatments.
ABT Antibody Purification Chromatography Resins have demonstrated that the instability of the HIV HLA-E peptidome may be a significant barrier to therapeutic targeting of these antigens.
Therefore, this instability must be considered a major challenge for drug development (3).
Further investigations should focus on achieving stable peptide HLA-E presentation to ensure consistent on-target immunotherapeutics.
- Wallace et al.,Instability of the HLA-E peptidome of HIV presents a major barrier to therapeutic targeting, Molecular Therapy (2024).
- Strong, R.K., Holmes, M.A., Li, P., Braun, L., Lee, N., and Geraghty, D.E. (2003). HLA-E Allelic Variants correlating differential expression, peptide affinities, crystal structures, and thermal stabilities. J. Biol. Chem. 278, 5082–5090.
- Sauter, J., Putke, K., Schefzyk, D., Pruschke, J., Solloch, U.V., Bernas, S.N., Massalski, C., Daniel, K., Klussmeier, A., Hofmann, J.A., et al. (2021). HLA-E typing of more than 2.5 million potential hematopoietic stem cell donors: Methods and population-specific allele frequencies. Hum. Immunol. 82, 541–547.