Recombinant Human TRIM31 Protein, N-His-SUMO & C-Strep

Description of Recombinant Human TRIM31 Protein, N-His-SUMO & C-Strep

Title: Introduction to Recombinant Human TRIM31 Protein: A Versatile Antigen for Research and Therapeutic Applications

Recombinant Human TRIM31 Protein: Structure and Function

The human TRIM31 (tripartite motif-containing 31) protein is a member of the tripartite motif (TRIM) family of proteins, characterized by the presence of a RING (Really Interesting New Gene) domain, a B-box domain, and a coiled-coil domain. TRIM31 is a 56 kDa protein consisting of 490 amino acids and is predominantly expressed in the cytoplasm of various tissues, including immune cells, brain, and heart.

TRIM31 has been shown to play a crucial role in regulating various cellular processes, such as protein degradation, cell proliferation, and immune response. It functions as an E3 ubiquitin ligase, which catalyzes the transfer of ubiquitin molecules onto target proteins, leading to their degradation via the proteasome pathway. Additionally, TRIM31 has been reported to interact with various signaling molecules and transcription factors, suggesting its involvement in multiple signaling pathways.

Recombinant Human TRIM31 Protein: Production and Purification

Recombinant proteins are artificially produced proteins that are derived from the genetic material of a different organism. Recombinant Human TRIM31 Protein is produced using recombinant DNA technology, where the gene encoding TRIM31 is cloned into an expression vector and introduced into a host cell, such as E. coli or yeast. The host cell then produces large quantities of the protein, which can be easily purified using chromatography techniques.

Recombinant Human TRIM31 Protein: Applications in Research

Due to its diverse functions and interactions, TRIM31 has been implicated in various diseases, including cancer, autoimmune disorders, and viral infections. Recombinant Human TRIM31 Protein has been widely used as a research tool to study the role of TRIM31 in these diseases. It has been shown to regulate the activity of key signaling molecules, such as NF-κB and STAT3, which are involved in cancer progression and immune response.

Moreover, recombinant TRIM31 protein has been used to investigate the role of TRIM31 in viral infections, particularly in HIV and influenza. Studies have shown that TRIM31 can inhibit the replication of these viruses by targeting viral proteins for degradation. This highlights the potential of TRIM31 as a therapeutic target for antiviral therapy.

Recombinant Human TRIM31 Protein: Therapeutic Applications

The unique structure and function of TRIM31 make it a promising candidate for therapeutic applications. Its E3 ubiquitin ligase activity and ability to regulate immune response make it an attractive target for the development of novel immunotherapies. For instance, recombinant TRIM31 protein has been used to stimulate the immune response against cancer cells, leading to their destruction.

Furthermore, TRIM31 has been shown to play a role in the development of autoimmune disorders, such as rheumatoid arthritis and systemic lupus erythematosus. Recombinant Human TRIM31 Protein has been used in preclinical studies to inhibit the activity of TRIM31, leading to a reduction in disease symptoms. This highlights the potential of TRIM31 as a therapeutic target for autoimmune diseases.

In conclusion, Recombinant Human TRIM31 Protein is a versatile antigen that has been extensively studied for its role in various cellular processes and diseases. Its structure, function, and potential therapeutic applications make it a valuable tool for both research and therapeutic purposes. With ongoing studies and advancements in recombinant protein technology, the potential of TRIM31 as a therapeutic target continues to grow, offering hope for the development of novel treatments for various diseases.