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The protein encoded by TRIM24 mediates transcriptional control by interaction with the activation function 2 (AF2) region of several nuclear receptors, including the estrogen, retinoic acid, and vitamin D3 receptors. Additionally we are shipping TRIM24 Antibodies (118) and TRIM24 Proteins (14) and many more products for this protein.
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This study concluded that reduced TRIM24 protein is associated with poor survival in esophageal squamous cell cancer (ESCC) patients, suggesting TRIM24 protein is a potential prognostic biomarker for ESCC.
Data suggest that, in cardiomyocytes, TRIM32 attenuates activation of SRF signaling and hypertrophy due to dysbindin; TRIM24 promotes these effects. TRIM32 promotes dysbindin degradation; TRIM24 protects dysbindin from degradation. (TRIM = tripartite motif-containing protein; SRF = serum response factor)
hypothesis of "synergistic modification induced recognition" is then proposed to link histone modification and TRIM24 binding
Report provides evidence for an oncogenic role for TRIM24 as a transcriptional activator and mediator of hormone-refractory prostate cancer cell growth in SPOP (show SPOP ELISA Kits) mutant and castration-resistant prostate cells.
TRIM24 expression is positively correlated with Acetylated H3 lysine 23 levels, and high levels of both TRIM24 and Acetylated H3 lysine 23 predict shorter overall survival of breast cancer patients.
TRIM24 regulate resistance to Gefitinib via Akt (show AKT1 ELISA Kits) pathway in non-small cell lung cancer cells.
TRIM24 is overexpressed in human bladder cancer and facilitates bladder cancer growth and invasion, possibly through NF-kappaB (show NFKB1 ELISA Kits) and AKT (show AKT1 ELISA Kits) signaling pathways.
functions as an oncogene (show RAB1A ELISA Kits) in colorectal carcinogenesis
A role for TRIM24 in breast tumorigenesis through reprogramming of glucose metabolism in human mammary epithelial cells, further supporting TRIM24 as a viable therapeutic target in breast cancer.
our study shows that TRIM24 is overexpressed in human gastric cancer and accelerates cell growth as well as induce chemoresistance
Maintenance of pluripotency is regulated by a network of transcription factors coordinated by Oct4 (show POU5F1 ELISA Kits), Sox2 (show SOX2 ELISA Kits), and Nanog (show NANOG ELISA Kits); Trim24 significantly improved efficiency of cellular reprogramming, demonstrating its direct functionality in establishing pluripotency.
data identify a previously unappreciated Trim24-dependent requirement for IL-1R expression on TH2 cells and an important nonredundant role for T-cell-intrinsic Trim24 in TH2-mediated allergy and antihelminth immunity
Trim24 repressed VL30-class endogenous retroviruses retrotransposons
These results identify Trim24 as a novel negative regulator of the IFN/STAT (show STAT1 ELISA Kits) pathway and suggest that this repression through Rara (show RARA ELISA Kits) inhibition may prevent liver cancer.
Somatic hepatocyte-specific inactivation of TRIM24, TRIM28 (show TRIM28 ELISA Kits), or TRIM33 (show TRIM33 ELISA Kits) all promote hepatocellular carcinoma in a cell-autonomous manner in mice.
TRIM24 regulates AR-mediated transcription in collaboration with TIP60 (show KAT5 ELISA Kits) and BRD7 (show BRD7 ELISA Kits).
TIF1alpha-chromatin association is direct and involves DNA and nucleosome interactions mediated by the bromodomain
These studies indicate that TIF1alpha is a factor that modulates the expression of a set of genes during the first wave of genome activation in the mouse embryo.
The results not only provide genetic evidence that Trim24 and Rara (show RARA ELISA Kits) co-regulate hepatocarcinogenesis in an antagonistic manner but also suggest that aberrant activation of Rara (show RARA ELISA Kits) is deleterious to liver homeostasis.
TIF1alpha-null mutant pathological phenotype supports the hypothesis that aging is promoted by increased activity of the vitamin D signaling pathway
The protein encoded by this gene mediates transcriptional control by interaction with the activation function 2 (AF2) region of several nuclear receptors, including the estrogen, retinoic acid, and vitamin D3 receptors. The protein localizes to nuclear bodies and is thought to associate with chromatin and heterochromatin-associated factors. The protein 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. Two alternatively spliced transcript variants encoding different isoforms have been described for this gene.
tripartite motif-containing 24
, transcriptional intermediary factor 1 alpha
, tripartite motif containing 24
, E3 ubiquitin-protein ligase TRIM24
, RING finger protein 82
, transcription intermediary factor 1-alpha
, transcriptional intermediary factor 1
, E3 ubiquitin-protein ligase Trim24
, transcriptional intermediary factor 1, alpha
, tripartite motif-containing protein 24