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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.
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Human TRIM24 Protein expressed in Wheat germ - ABIN1323631
Fujimoto, Hamaguchi, Kaji, Matsushita, Ichimura, Kodera, Ishiguro, Ueda-Hayakawa, Asano, Ogawa, Fujikawa, Miyagi, Mabuchi, Hirose, Akimoto, Hatta, Tsutsui, Higashi, Igarashi, Seishima, Hasegawa et al.: Myositis-specific anti-155/140 autoantibodies target transcription intermediary factor 1 family proteins. ... in Arthritis and rheumatism 2012
Show all 2 Pubmed References
Study showed that TRIM24 was upregulated during gastric carcinogenesis and demonstrated that TRIM24 was a functional target gene of miR (show MLXIP Proteins)-511, and miR (show MLXIP Proteins)-511 inactivated PI3K (show PIK3CA Proteins)/AKT (show AKT1 Proteins) and Wnt (show WNT2 Proteins)/beta-catenin (show CTNNB1 Proteins) pathways by suppressing TRIM24.
Overexpression of KAT6A or TRIM24 promoted PIK3CA (show PIK3CA Proteins) expression, AKT (show AKT1 Proteins) phosphorylation, and cell proliferation.
we identified altered glucose metabolism in the progression of head and neck squamous cell carcinoma and showed that it could be partially attributed to the novel link between GLUT4 (show SLC2A4 Proteins) and TRIM24
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 Proteins) 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 Proteins) 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 Proteins) and AKT (show AKT1 Proteins) signaling pathways.
Maintenance of pluripotency is regulated by a network of transcription factors coordinated by Oct4 (show POU5F1 Proteins), Sox2 (show SOX2 Proteins), and Nanog (show NANOG Proteins); 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 Proteins) pathway and suggest that this repression through Rara (show RARA Proteins) inhibition may prevent liver cancer.
Somatic hepatocyte-specific inactivation of TRIM24, TRIM28 (show TRIM28 Proteins), or TRIM33 (show TRIM33 Proteins) all promote hepatocellular carcinoma in a cell-autonomous manner in mice.
TRIM24 regulates AR-mediated transcription in collaboration with TIP60 (show KAT5 Proteins) and BRD7 (show BRD7 Proteins).
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 Proteins) co-regulate hepatocarcinogenesis in an antagonistic manner but also suggest that aberrant activation of Rara (show RARA Proteins) 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