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The protein encoded by TRIM25 is a member of the tripartite motif (TRIM) family. Additionally we are shipping TRIM25 Antibodies (149) and TRIM25 Kits (2) and many more products for this protein.
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The RNA-binding activity of TRIM25 is mediated by its PRY/SPRY domain, which we postulate to be a novel RNA-binding domain.
TRIM25 inhibits hepatocellular carcinoma progression by targeting MTA1 (show MTA1 Proteins).
TRIM25 is a key determinant of breast cancer metastasis.
V interaction with TRIM25 and RIG-I (show DDX58 Proteins) prevents TRIM25-mediated ubiquitination of RIG-I (show DDX58 Proteins) and disrupts downstream RIG-I (show DDX58 Proteins) signaling to the mitochondrial antiviral signaling protein (show MAVS Proteins).
HPV E6 oncoprotein antagonizes the activation of the cytoplasmic innate immune sensor RIG-I (show DDX58 Proteins) by targeting its upstream regulatory enzymes TRIM25 and USP15 (show USP15 Proteins). We further show that the RIG-I (show DDX58 Proteins) signaling cascade is important for an antiviral innate immune response to HPV16 infection
this study shows thatTRIM25 targets ERG (show ERG Proteins) for degradation in prostate cancer
TRIM25 actively participates in higher-order assembly of the RIG-I (show DDX58 Proteins) signalosome.
Our results indicate that TRIM25 is associated with cisplatin resistance and 14-3-3sigma-MDM2 (show MDM2 Proteins)-p53 (show TP53 Proteins) signaling pathway is involved in this process, suggesting targeting TRIM25 may be a potential strategy for the reversal of cisplatin resistance.
expression of TRIM25 might be critical for lung cancer cell migration, proliferation as well as doxorubicin resistance.
Disturbed p53 (show TP53 Proteins)-MDM2 (show MDM2 Proteins) feedback loop contributing to the pathogenesis of thoracic aortic dissection may be linked to TRIM25 overexpression.
TRIM25 as a key determinant of breast cancer metastasis.
Studies indicated that mice with disrupted Trim25 were viable and fertile, uterine response to oestrogen was greatly attenuated and the uteri were underdeveloped.
Two key residues (Asp (show C3 Proteins)(488) and Trp (show TYRP1 Proteins)(621)) in the TRIM25 B30.2 domain are critical for binding to the RIG-I (show DDX58 Proteins) CARDs.
Two well-known E3 ubiquitin ligases, Trim25 (also called Efp) and Trim71 (show TRIM71 Proteins) (also called Lin41 (show TRIM71 Proteins)), are validated as RNA-binding proteins, revealing a potential link between RNA biology and protein-modification pathways.
The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The protein localizes to the cytoplasm. The presence of potential DNA-binding and dimerization-transactivation domains suggests that this protein may act as a transcription factor, similar to several other members of the TRIM family. Expression of the gene is upregulated in response to estrogen, and it is thought to mediate estrogen actions in breast cancer as a primary response gene.
tripartite motif-containing 25
, E3 ubiquitin/ISG15 ligase TRIM25
, tripartite motif containing 25
, RING finger protein 147
, estrogen-responsive finger protein
, tripartite motif protein TRIM25
, tripartite motif-containing protein 25
, ubiquitin/ISG15-conjugating enzyme TRIM25
, zinc finger protein 147 (estrogen-responsive finger protein)
, zinc finger protein-147
, tripartite motif protein 25
, zinc finger protein 147