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- Table of Contents
Facts about E3 ubiquitin/ISG15 ligase TRIM25.
Functions as a ubiquitin E3 ligase as Well as an ISG15 E3 ligase.
Involved in innate immune defense against viruses by mediating ubiquitination of DDX58.Mediates'Lys-63'-linked polyubiquitination of the DDX58 N-terminal CARD-like area that's crucial for triggering the cytosolic signal transduction that leads to the production of interferons in response to viral infection. Promotes ISGylation of 14-3-3 sigma (SFN), an adapter protein implicated in the regulation of a large spectrum signaling pathway.
Human | |
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Gene Name: | TRIM25 |
Uniprot: | Q14258 |
Entrez: | 7706 |
Belongs to: |
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No superfamily |
EC 6.3.2.19; EC 6.3.2.n3; EFPZ147; Estrogen-responsive finger protein; RING finger protein 147; RNF147E3 ubiquitin/ISG15 ligase TRIM25; tripartite motif containing 25; tripartite motif-containing 25; Tripartite motif-containing protein 25; Ubiquitin/ISG15-conjugating enzyme TRIM25; zinc finger protein 147 (estrogen-responsive finger protein); Zinc finger protein 147; zinc finger protein-147; ZNF147tripartite motif protein TRIM25
Mass (kDA):
70.973 kDA
Human | |
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Location: | 17q22 |
Sequence: | 17; NC_000017.11 (56887909..56914049, complement) |
Expressed in breast tumors (at protein level). Ubiquitous.
Cytoplasm. Cytoplasm, Stress granule.
This article will provide more details about the Anti-TRIM25 Antibody from Boster Bio. This article will focus on the TRIM25 marker as well as the Boster Bio Anti-TRIM25 Antibody. We will also discuss other TRIM25 markers, including the pGEX Grb2 SH2-SH3 as well as the pGE.
TRIM25 is an epitope the TRIM25 antibody recognizes. This polyclonal antibody was generated by immunizing animals with an artificial peptide. These antibodies are then purified using a method known as protein A affinity chromatography (PACh).
TRIM25, also known by Estrogen-responsive Finger Protein, is part of the tripartite motif family. It is composed of a RING domain, one or two B-box motif, and a coiled-coil region. In a search for genes related to breast cancer, TRIM25 was identified as an estrogen-responsive protein. Breast cancer tumors typically overexpress this protein and its knockdown can be seen in infected MCF7 cells in vitro as well in mouse xenograft models. Recent functional studies have shown that TRIM25 could be a ubiquitin-E3 Ligase.
TRIM25 is a multidomain RNA binding protein with a multidomain RNA-binding. The SPRY domain is essential for binding to RNA. The 28-bp dsRNA fluorescently tagged with fluorescent tags was incubated with purified TRIM25 proteins. The native polyacrylamide gel separated the bound fraction from the free fraction. The amount of TRIM25-bound RNA quantified by densitometry. Full-length TRIM25 gel scans revealed a highly co-operative binding mechanism.
TRIM25 interacts with RNA through its central CC domain and influences RNA replication and intracellular signaling. It could use the RNA structure to alter its targets, like RIG-I or viral ribonucleoproteins. TRIM25 is a potential target for certain RNA viruses to block their function. The best uses of TRIM25 are described below.
TRIM25 is multifunctional protein, with its role in transcription. It binds both double-stranded DNA and RNA. Additionally its ubiquitin and ligase activity regulates transcriptional targets. This connection between TRIM25 and target transcripts , and RNA is shown in Figure 1D. Both proteins play crucial roles in the regulation of cells. TRIM25 is vital for a variety of cell functions and has the potential to control a range of cell phenotypes.
In cancer research in cancer research, the TRIM25 gene is an important regulator of metastasis and low overall survival. By targeting TRIM25 scientists hope to develop an innovative new intervention strategy. Its high-expression levels in cancer cells can provide a new avenue to target this mRNA. This marker may be useful for treatment, but the next step is to determine whether it is associated with the progression of the tumor.
TRIM25 is involved in many immune systems that are inherently immune. Its function is controlled by viral and cellular proteins. The following article explains the various processes. The RING domain is able to bind E2-conjugating enzymes. The RING domain is catalytically efficient in vitro, but does not interact with the full-length TRIM25 dimer. It is therefore necessary in the creation of an oligomer of higher order.
TRIM25 is a molecular marker that may be detected in the human body. Boster Bio has developed a polyclonal antibody for identifying TRIM25. The antibody recognizes amino acid 557-557 of human-derived TRIM25. This antibody is compatible with both mouse and human tissues and is specifically designed to recognize this protein. This antibody against TRIM25 is made against A03232-2, a synthetic peptide produced by Boster Bio.
The Anti-TRIM25 antibody is a monoclonal antibody for humans that reacts with the TRIM25 peptide. It can be stored at -20°C or 4°C up to one year. It is packaged in PBS that contains 0.022% sodium azide. It recognizes amino acids 520-570 from human TRIM25. To identify specific lengths of the immunogen, you can also buy blocking peptides.
PMID: 8248217 by Inoue S., et al. Genomic binding-site cloning reveals an estrogen-responsive gene that encodes a RING finger protein.
PMID: 15130519 by Shimada N., et al. Systemic distribution of estrogen-responsive finger protein (Efp) in human tissues.