Recombinant Human TRIM14 Protein, N-His from ProteoGenix; catalogue ARO-P11684; research use only.
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Recombinant Human TRIM14 Protein, also known as Tripartite Motif Containing 14, is a protein that is encoded by the TRIM14 gene in humans. It belongs to the TRIM family of proteins, which are characterized by a tripartite motif consisting of a RING finger, B-box, and coiled-coil domain. TRIM14 is a multifunctional protein that plays a crucial role in various cellular processes, including immune response, cell signaling, and cancer development. In this article, we will discuss the structure, activity, and application of Recombinant Human TRIM14 Protein.
The human TRIM14 protein is composed of 486 amino acids and has a molecular weight of approximately 55 kDa. It consists of three distinct domains: a RING finger domain at the N-terminus, two B-box domains in the middle, and a coiled-coil domain at the C-terminus. The RING finger domain is responsible for E3 ubiquitin ligase activity, while the B-box domains are involved in protein-protein interactions. The coiled-coil domain is responsible for the oligomerization of TRIM14, which is crucial for its function.
Recombinant Human TRIM14 Protein is produced by cloning the TRIM14 gene into a suitable expression vector and expressing it in a host cell, typically E. coli or mammalian cells. The resulting recombinant protein is then purified using various chromatography techniques to obtain a highly pure and active protein.
Recombinant Human TRIM14 Protein has been shown to have multiple activities in various cellular processes. One of its main functions is its role as an E3 ubiquitin ligase, which is responsible for tagging proteins with ubiquitin for degradation by the proteasome. This function of TRIM14 is crucial for maintaining cellular homeostasis and regulating various signaling pathways.
In addition to its E3 ubiquitin ligase activity, TRIM14 also plays a role in innate immunity. It has been shown to interact with and regulate the activity of several immune-related proteins, such as NF-κB, IRF3, and STAT3. This activity of TRIM14 is important for the activation of immune responses and defense against pathogens.
Furthermore, Recombinant Human TRIM14 Protein has been implicated in cancer development and progression. It has been shown to interact with and regulate the activity of various oncogenes and tumor suppressor genes, leading to altered cell proliferation, survival, and migration. TRIM14 has also been found to be overexpressed in several types of cancer, making it a potential therapeutic target for cancer treatment.
The use of Recombinant Human TRIM14 Protein in research has been crucial in understanding its structure and function. Its recombinant form allows for easier purification and manipulation, making it an ideal protein for studying its role in various cellular processes. Additionally, recombinant TRIM14 can also be used in in vitro assays to study its E3 ubiquitin ligase activity and its interactions with other proteins.
Moreover, the potential therapeutic applications of Recombinant Human TRIM14 Protein are being explored. As mentioned earlier, TRIM14 has been implicated in cancer development and progression, making it a potential target for cancer treatment. Studies have shown that targeting TRIM14 can inhibit tumor growth and sensitize cancer cells to chemotherapy. Therefore, recombinant TRIM14 may have a future as a therapeutic agent for cancer treatment.
In summary, Recombinant Human TRIM14 Protein is a multifunctional protein with various activities in cellular processes such as immune response, cell signaling, and cancer development. Its
ProteoGenix catalogue number ARO-P11684. For research use only.
Host: Escherichia coli (E.coli); Expression system: Prokaryotic expression; Molecular weight: 23.77 kDa; Fragment: Ser254-Pro442; Buffer: Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol..
Available configurations: 50ug, 100ug, 1mg.
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