Recombinant Human UBE2L3, N-His

Description of Recombinant Human UBE2L3, N-His

Introduction

Recombinant Human UBE2L3, also known as Ubiquitin-conjugating enzyme E2L3, is a protein that plays a crucial role in the ubiquitin-proteasome system. This system is responsible for regulating protein degradation and maintaining cellular homeostasis. UBE2L3 is highly conserved across species and has been shown to have diverse cellular functions. In this article, we will explore the structure, activity, and applications of this important recombinant protein.

Structure of Recombinant Human UBE2L3

UBE2L3 is a small protein consisting of 153 amino acids with a molecular weight of 17 kDa. It is composed of a highly conserved catalytic core domain and a C-terminal extension. The catalytic core domain contains a catalytic cysteine residue that is essential for the enzymatic activity of UBE2L3. The C-terminal extension, on the other hand, is responsible for binding to other proteins and regulating the activity of UBE2L3.

Recombinant Human UBE2L3 is produced through genetic engineering techniques, where the gene encoding UBE2L3 is cloned into an expression vector and then expressed in a host organism, such as bacteria or yeast. This allows for the production of large quantities of pure and active UBE2L3 protein for research and therapeutic purposes.

Activity of Recombinant Human UBE2L3

As a member of the E2 family of ubiquitin-conjugating enzymes, UBE2L3 plays a crucial role in the ubiquitination process. Ubiquitination is a post-translational modification where ubiquitin molecules are attached to target proteins, marking them for degradation by the proteasome. UBE2L3 specifically catalyzes the transfer of ubiquitin from an E1 activating enzyme to a target protein, thereby initiating the ubiquitination process.

In addition to its role in protein degradation, UBE2L3 has also been shown to have non-proteolytic functions. It has been reported to be involved in DNA damage repair, cell cycle regulation, and immune response. These diverse functions of UBE2L3 are thought to be mediated by its ability to interact with a variety of proteins and regulate their activity.

Applications of Recombinant Human UBE2L3

Recombinant Human UBE2L3 has a wide range of applications in both basic research and drug development. Its role in the ubiquitin-proteasome system makes it a valuable tool for studying protein degradation and cellular homeostasis. Researchers can use recombinant UBE2L3 to investigate the mechanisms of ubiquitination and its role in various cellular processes.

Furthermore, UBE2L3 has been identified as a potential therapeutic target for various diseases. It has been shown to play a role in cancer, neurodegenerative disorders, and viral infections. Inhibitors of UBE2L3 have been developed and are being studied for their potential use in treating these diseases.

Recombinant Human UBE2L3 is also used in the development of diagnostic assays. Its high specificity and activity make it a useful tool for detecting and quantifying ubiquitinated proteins in biological samples. This can aid in the diagnosis and monitoring of diseases where ubiquitination is dysregulated.

Conclusion

In summary, Recombinant Human UBE2L3 is a crucial protein involved in the ubiquitin-proteasome system with diverse cellular functions. Its structure, activity, and applications make it a valuable tool for research and drug development. Further studies on UBE2L3 and its role in various diseases may lead to the development of new therapeutic strategies for these conditions.