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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.
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Agarose 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...
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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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"This study highlights the importance of protein purification techniques to identify protein-protein interactions that are critical for cell biology"
The E3 ubiquitin ligase RNF2 protects polymerase ι from destabilization and represents a potential therapeutic target for diseases associated with DNA instability.
Polymerase ι (Polι) is a Y-family DNA polymerase involved in translesion synthesis (TLS), a critical mechanism for DNA damage tolerance. Its regulation is essential because its instability can compromise genome stability and lead to diseases such as cancer.
This study explores the role of RNF2, an E3 ubiquitin ligase, in protecting Polι from proteasomal degradation. For this purpose, co-immunoprecipitation (Co-IP) experiments were conducted using a glutathione agarose resin column from Agarose Beads Technologies (ABT) to purify the protein and evaluate the interaction between Polι and RNF2.
The stability of Polι was also analyzed in cells with and without RNF2, revealing that the loss of RNF2 resulted in a significant reduction of Polι due to proteasomal degradation.
Figure 1. Polɩ interacts with E3 ubiquitin ligase, RNF2. (B) Pull-down assay showing the interaction between GST-tagged RNF2 and His-tagged Polɩ. His-Polɩ was incubated with GST- or GST-RNF2. GST was captured on glutathione agarose beads, washed and separated by SDS-PAGE parallel to 5% of protein input, followed by immunoblotting with polyclonal antibodies raised to the C-terminus of Polɩ [37] and anti-GST antibodies (Covance and Santa Cruz, respectively)
The results indicate that RNF2 directly interacts with Polι and prevents its degradation, ensuring its function in translesion synthesis and reducing cellular susceptibility to DNA damage.
This study concludes that the regulation of Polι by RNF2 is critical for genome stability and suggests that it may represent a potential therapeutic target for diseases associated with DNA instability.
Furthermore, it highlights the importance of protein purification techniques using ABT agarose beads to identify protein-protein interactions that are critical for cell biology.
- Fedorowicz M. et al., IE3 ubiquitin ligase RNF2 protects polymerase ι from destabilization, Molecular Cell Research (2024).