UBD Human

Ubiquitin-D is composed of 165 amino acids and has a molecular weight of approximately 18 kDa. It shares structural similarities with ubiquitin, a highly conserved protein found in all eukaryotic organisms. Ubiquitin itself is a 76 amino acid protein that is involved in tagging proteins for degradation .

The primary function of Ubiquitin-D is to covalently modify target proteins, tagging them for destruction in the proteasome. This process is vital for maintaining cellular homeostasis by removing damaged, misfolded, or excess proteins. Ubiquitin-D is involved in various biological processes, including the regulation of the immune response, cell cycle, and apoptosis .

Recombinant Ubiquitin-D is typically produced using Escherichia coli (E. coli) expression systems. The gene encoding Ubiquitin-D is cloned into an expression vector, which is then introduced into E. coli cells. These cells are cultured under specific conditions to induce the expression of the recombinant protein. After expression, the protein is purified using techniques such as affinity chromatography and size-exclusion chromatography to achieve high purity levels .

Ubiquitin-D plays a significant role in the immune system by regulating the activity of various immune cells. It is involved in the positive regulation of I-kappaB kinase/NF-kappaB signaling, which is crucial for the immune response to infections and inflammation . Additionally, Ubiquitin-D is implicated in the response to tumor necrosis factor and interferon-gamma, highlighting its importance in immune regulation and inflammation .

Recombinant Ubiquitin-D is widely used in research to study protein degradation pathways, immune responses, and cell cycle regulation. It serves as a valuable tool for investigating the mechanisms of protein ubiquitination and the role of ubiquitin-like modifiers in cellular processes. Researchers utilize recombinant Ubiquitin-D to explore its interactions with other proteins and its impact on various signaling pathways .