Recombinant Human TRIM28 Protein, N-His

Description of Recombinant Human TRIM28 Protein, N-His

Introduction Recombinant Human TRIM28 Protein, also known as Tripartite Motif Containing 28, is a protein that plays a crucial role in various cellular processes such as gene regulation, DNA damage response, and immune response. It is a member of the tripartite motif (TRIM) protein family, which is characterized by the presence of a RING finger, B-box, and coiled-coil domains. In this article, we will explore the structure, activity, and applications of Recombinant Human TRIM28 Protein. Structure of Recombinant Human TRIM28 Protein The human TRIM28 gene is located on chromosome 19 and consists of 10 exons. The encoded protein is 740 amino acids long and has a molecular weight of approximately 83 kDa. It is composed of several functional domains, including a RING finger domain, two B-box domains, a coiled-coil domain, and a PHD domain. The RING finger domain is responsible for the E3 ubiquitin ligase activity of TRIM28, which is essential for its role in protein degradation and regulation of cellular processes. The B-box domains are involved in protein-protein interactions, while the coiled-coil domain is responsible for the dimerization of TRIM28. The PHD domain is involved in chromatin binding and transcriptional regulation. Activity of Recombinant Human TRIM28 Protein TRIM28 is a multifunctional protein with diverse roles in cellular processes. It acts as a transcriptional co-repressor by binding to specific DNA sequences and recruiting other proteins to regulate gene expression. It also plays a crucial role in DNA damage response by promoting DNA repair and suppressing cell death. Moreover, TRIM28 is involved in the regulation of immune response by interacting with various signaling molecules and transcription factors. It acts as a negative regulator of the NF-κB pathway, which is essential for the activation of immune cells. It also plays a role in the development and function of T cells and B cells. Another important activity of TRIM28 is its involvement in the maintenance of genomic stability. It has been shown to interact with several proteins involved in DNA repair and regulate their activity. Additionally, TRIM28 is essential for the proper formation of heterochromatin, which is crucial for the organization and stability of the genome. Applications of Recombinant Human TRIM28 Protein The diverse functions of TRIM28 make it an attractive target for research and potential therapeutic applications. Recombinant Human TRIM28 Protein can be used in various studies to understand its role in different cellular processes. It can also be used to investigate its interactions with other proteins and its role in protein degradation and gene regulation. Moreover, TRIM28 has been implicated in various diseases, including cancer, autoimmune disorders, and neurodegenerative diseases. Therefore, recombinant TRIM28 protein can be used in drug discovery and development for these diseases. It can also be used as a potential biomarker for disease diagnosis and prognosis. Furthermore, the E3 ubiquitin ligase activity of TRIM28 makes it a potential target for cancer therapy. Inhibition of this activity can lead to the accumulation of tumor suppressor proteins, which can inhibit the growth of cancer cells. Recombinant Human TRIM28 Protein can be used to study and develop inhibitors of its E3 ubiquitin ligase activity for potential cancer treatment. Conclusion In summary, Recombinant Human TRIM28 Protein is a multifunctional protein with diverse roles in cellular processes such as gene regulation, DNA damage response, and immune response. Its structure, activity, and applications make it an important target for research and potential therapeutic interventions. Further studies on TRIM28 will provide a better understanding of its function and potential clinical applications.