Recombinant Human TRIM28 Protein, N-His

Description of Recombinant Human TRIM28 Protein, N-His

Recombinant human TRIM28 protein, also known as tripartite motif-containing protein 28, is a highly conserved protein found in various species, including humans. It is encoded by the TRIM28 gene, located on chromosome 19 in humans. TRIM28 is a member of the tripartite motif (TRIM) family, which plays a crucial role in various cellular processes, including transcriptional regulation, DNA damage response, and innate immunity. In this article, we will explore the structure, activity, and applications of recombinant human TRIM28 protein.

Recombinant human TRIM28 protein is a 53 kDa protein consisting of 490 amino acids. It contains three domains: a RING domain, a B-box domain, and a coiled-coil domain. The RING domain is responsible for E3 ubiquitin ligase activity, while the B-box domain is involved in protein-protein interactions. The coiled-coil domain is responsible for the dimerization of TRIM28 and its interaction with other proteins.

TRIM28 also contains a nuclear localization signal (NLS) and a C-terminal plant homeodomain (PHD) finger. The NLS is responsible for the nuclear localization of TRIM28, where it exerts its functions. The PHD finger is involved in chromatin remodeling and transcriptional regulation.

Recombinant human TRIM28 protein has multiple activities, making it a crucial player in various cellular processes. One of its main functions is as a transcriptional co-repressor. TRIM28 interacts with various transcription factors, such as Kruppel-associated box (KRAB) domain-containing zinc finger proteins, and recruits histone deacetylases (HDACs) to repress gene expression.

TRIM28 also has E3 ubiquitin ligase activity, which is essential for protein degradation and regulation of cellular processes. It has been shown to regulate the stability of various proteins, including p53, p73, and c-Myc.

Moreover, TRIM28 plays a crucial role in the DNA damage response. It interacts with DNA damage sensors, such as p53 and ATM, and regulates their activity. TRIM28 also plays a role in the repair of DNA double-strand breaks.

Recombinant human TRIM28 protein has various applications in both basic research and clinical settings. Due to its role in transcriptional regulation, it has been widely used in studies investigating gene expression and regulation. Its interaction with transcription factors and HDACs makes it a valuable tool for studying epigenetic mechanisms.

TRIM28 has also been implicated in various diseases, including cancer and viral infections. Its function as a transcriptional co-repressor and E3 ubiquitin ligase makes it a potential therapeutic target for these diseases. Recombinant TRIM28 protein can be used to study its role in disease pathogenesis and to develop novel therapies.

Moreover, recombinant human TRIM28 protein has been used in the development of diagnostic tools. Its interaction with various proteins, such as p53 and c-Myc, can be exploited to detect their levels and activity in different diseases.

In conclusion, recombinant human TRIM28 protein is a multifunctional protein with various activities, including transcriptional co-repression, E3 ubiquitin ligase activity, and involvement in the DNA damage response. Its structure, consisting of a RING domain, B-box domain, coiled-coil domain, NLS, and PHD finger, allows it to interact with multiple proteins and play crucial roles in various cellular processes. Its applications in basic research, disease studies, and diagnostic tools make it a valuable protein in the field of molecular biology.