RNF34 functions primarily as an E3 ubiquitin-protein ligase, which means it plays a crucial role in the ubiquitination process. Ubiquitination is a post-translational modification where ubiquitin proteins are attached to a substrate protein, marking it for degradation by the proteasome. This process is essential for maintaining cellular homeostasis by regulating the levels of various proteins.
One of the key roles of RNF34 is to regulate the levels of caspase-8 (CASP8) and caspase-10 (CASP10) by targeting them for proteasomal degradation . Caspases are a family of protease enzymes that play essential roles in programmed cell death (apoptosis). By controlling the degradation of these caspases, RNF34 helps protect cells against apoptosis induced by tumor necrosis factor (TNF).
Recombinant human RNF34 is produced using various expression systems, including Escherichia coli and baculovirus-insect cells . The recombinant protein is typically purified using chromatographic techniques to ensure high purity and biological activity. It is supplied in a sterile solution containing Tris-HCl buffer, glycerol, NaCl, and DTT to maintain stability and activity .
Recombinant RNF34 is used in various research applications, including studies on protein-protein interactions, apoptosis, and ubiquitination. It is also valuable for investigating the regulatory mechanisms of caspases and the role of phosphoinositides in cellular signaling.