Ubiquitin Recombinant Proteins 

Ubiquitin recombinant proteins are indispensable tools for studying post-translational modifications, particularly ubiquitination, which regulates numerous cellular processes such as protein degradation, DNA repair, cell cycle control, and immune signaling. Ubiquitin is a 76-amino acid protein highly conserved across eukaryotes and serves as a molecular tag for proteasomal and lysosomal degradation. 

Content

Recombinant ubiquitin proteins are produced in bacterial, yeast, or mammalian expression systems to ensure proper folding and activity. These proteins are often modified with tags (e.g., His, GST) for easy purification or labeled with fluorescent or biotin tags for specific applications.

Applications

• Ubiquitination Studies:
  • Investigating ubiquitin conjugation and deconjugation by enzymes (E1, E2, E3 ligases, and DUBs).
  • Identifying substrates of ubiquitin ligases and understanding chain linkage specificity.
• Proteasomal Degradation Research:
  • Exploring how ubiquitin-tagged proteins are recognized and degraded by the 26S proteasome.
  • Developing inhibitors of proteasomal and autophagy-mediated degradation pathways.
• Signal Transduction Pathways:
  • Studying ubiquitin-mediated regulation of pathways such as NF-κB, DNA damage response, and innate immunity.
  • Investigating the role of ubiquitination in inflammatory signaling and cancer.
• Drug Discovery and Screening:
  • High-throughput screening of inhibitors targeting ubiquitin-related enzymes, including E3 ligases and deubiquitinating enzymes (DUBs).
  • Evaluating therapeutic agents for diseases such as cancer, neurodegeneration, and autoimmune disorders.

The high versatility and reliability of ubiquitin recombinant proteins make them vital for advancing research in ubiquitin biology, therapeutic development, and diagnostic innovation.