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See 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...

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The significance of protein purification in the fight against cancer

Discover how ABT's Nickel NTA Agarose Resin is paving the way for new immunotherapy breakthroughs that could transform treatments for immune-related diseases...

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We’re celebrating: Our brand-NEW Website is live!

Our new website is more than just a visual upgrade. It represents our commitment to providing the best possible resources and information to our clients and partners in the bioprocessing and biopharmaceutical industries...

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Unveiling 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.

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Purifying HIV proteins to discover new therapeutic targets

ABT Antibody Purification Chromatography Resins have demonstrated that the instability of the HIV HLA-E peptidome may be a significant barrier...

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Advancing bacteriophage research with Nickel NTA agarose resins

Our technology offers a unique advantage in studying bacteriophages, particularly in the purification and analysis of phage components like...

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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.

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