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Next stop: The industry's top trade shows
Agarose Bead Technologies (ABT) is excited to announce our participation in several important trade fairs this October.
Read moreAgarose Bead Technologies expands facility to meet rising global demand for novel therapies market
Agarose Bead Technologies has enhanced its Burgos facility by boosting its agarose resin production to 100,000 liters annually to position itself as a powerhouse in the novel therapies market.
Read moreSee you at Bioprocess International Conference and Exhibition 2024
ABT will be exhibiting at one of the most prestigious events in the bioprocessing industry, the Bioprocess International Conference. This prestigious event will be held...
Read moreUnveiling the role of TAOK3 and SHP-1 in T cell activation: Protein isolation and purification
Modulation of SHP-1 abundance by TAOK3 serves as a rheostat for TCR signaling and determines the activation threshold of T lymphocytes.
Read more"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).