UBL3 Human

UBL3 is not directly involved in protein degradation, unlike ubiquitin itself. However, it shares many mechanistic similarities with the ubiquitin pathway. Ubiquitin-like proteins, including UBL3, play crucial roles in various cellular processes such as protein localization, stability, and function. These proteins are often involved in post-translational modifications, which can alter the behavior and interactions of target proteins .

Recombinant human UBL3 protein is typically produced using Escherichia coli (E. coli) expression systems. The recombinant protein is often fused to a His-tag at the N-terminus to facilitate purification. The production process involves expressing the protein in E. coli, followed by purification using conventional chromatography techniques. The resulting recombinant UBL3 protein is highly pure, with a purity greater than 95% as determined by SDS-PAGE .

Recombinant UBL3 protein is primarily used for research purposes. It is utilized in various biochemical and cellular assays to study the function and interactions of UBL3. Researchers often use recombinant UBL3 to investigate its role in cellular processes and its potential involvement in disease mechanisms. The protein is also used to identify UBL3-interacting partners and to explore its post-translational modifications .

Recombinant UBL3 protein is typically supplied in a buffer containing Tris-HCl, glycerol, DTT, and NaCl. It should be stored at 4°C for short-term use and at -20°C for long-term storage. It is important to avoid repeated freeze-thaw cycles to maintain the protein’s stability and activity .