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Boston, Here We Come: ABT at BPI 2026
From September 22–25, the ABT team will be in Boston for one of the leading events in the bioprocessing industry, bringing together experts and companies working across cell line development, upstream and downstream processing, CMC, digital biomanufacturing, and next-generation therapies.
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What Is Chromatography? A Practical Guide for Life-Science Labs
Chromatography is a key technique for separating, analyzing, and purifying biomolecules in life science laboratories. Discover the main chromatography methods, their applications, and how agarose resins support efficient protein, antibody, and nucleic acid purification workflows.
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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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"Developing a CEACAM1 variant with higher binding affinity to the TIM-3 receptor could have promising implications for immunotherapy"
TIM-3 is an inhibitory receptor expressed on various cells, including dendritic cells, T-helper 1 lymphocytes, and natural killer cells.
The binding of this protein to its ligand CEACAM1 causes T-cell exhaustion, a condition in which effector T cells lose their ability to proliferate and produce cytokines. Blocking this inhibitory receptor is considered an effective strategy for the treatment of cancer and related diseases. In this study, a recombinant protein with increased binding affinity to TIM-3 was developed and produced through protein engineering to block the inhibitory TIM-3 receptor.
Evidence has revealed that only the extracellular domain of CEACAM1 is sufficient for binding to TIM-3. By introducing mutations in the IgV domain of CEACAM1 at these positions, the aim was to increase the binding affinity to TIM-3 by selecting amino acids capable of forming hydrogen or ionic bonds. Mutant 39 was identified as the most appropriate CEACAM1 variant.
Figure 1. Protein analysis using 12% SDS gel electrophoresis. M, the molecular weight marker; lanes 1 and 2, proteins extracted from SHuffle T7 strain before and after purification by Ni+2-NTA chromatography, respectively.
ABT's Nickel NTA Agarose Resin is used in this article for recombinant protein purification. In this process, the agarose beads are conjugated with nickel ions, which have a high affinity for the histidine residues of the protein of interest.
With this ABT product, they can isolate or immobilize the recombinant CEACAM-1 variant 39 protein, obtaining a purified and homogeneous sample.
The study concludes that developing a CEACAM1 variant with higher binding affinity to the TIM-3 receptor could have promising implications for immunotherapy and the treatment of diseases associated with immune inhibition.
This highlights the potential of purifying proteins to modulate specific immune responses, opening new avenues for developing more effective therapies against cancer and other immune-related diseases.
- Hajihassan et al., Engineering a CEACAM1 Variant with the Increased Binding Affinity to TIM-3 Receptor, Iranian Biomedical Journal (2023).