Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all synonyms
Human TRIM28 Protein expressed in Wheat germ - ABIN1323643
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 describes germline mutations and loss of function of TRIM28 in familial Wilms tumours, along with somatic loss of function in a non-familial Wilms tumour. Inactivation of TRIM28 provides the molecular basis for defining a previously described subtype of Wilms tumour, that has early age of onset and excellent prognosis.
Study identified TRIM28 among REST-interacting proteins, and suggested functional links between REST and TRIM28 during neuronal development and differentiation via induction of CTNND2 (show CTNND2 Proteins) expression.
Data indicate a mechanism in breast cancer cells that tripartite motif-containing 28 protein (TRIM28) enhances metastasis by stabilizing TWIST1 (show TWIST1 Proteins), suggesting that targeting TRIM28 could be an efficacious strategy in breast cancer treatment.
Gamma-H2AX (show H2AFX Proteins), phosphorylated KAP-1 (show CDKN3 Proteins) and 53BP1 (show TP53BP1 Proteins) play an important role in the repair of heterochromatic radon-induced DNA double-strand breaks.
Our data demonstrate that the downregulation of TRIM28 gene expression reduced the ability of CSCs to self-renew that resulted in significant reduction of tumor growth. Loss of function of TRIM28 leads to dysregulation of cell cycle, cellular response to stress, cancer cell metabolism, and inhibition of oxidative phosphorylation.
Cell proliferation and apoptosis were almost completely abolished in the PAa cells cotreated with TRIM28 siRNA and etoposide following knockdown of E2F1 (show E2F1 Proteins). The results of our study demonstrated that the combination of TRIM28 siRNA and etoposide may be effective against nonsmall cell lung cancer (NSCLC)and has the potential of being a new therapeutic tool for future treatment.
The authors found that TRIM28 regulates alpha-Synuclein and tau nuclear levels and that its reduction rescues toxicity in animal models of tau- and alpha-Synuclein-mediated degeneration.
TRIM28 represses Endogenous retroviruses and consequently regulates the expression of neighboring genes.
it is primarily peroxide-induced p38 MAPK (show MAPK14 Proteins) that mediates Ser473 phosphorylation and activation of TIF1beta to enable more efficient DNA repair to assist in tumor cell survival against exogenous ROS (show ROS1 Proteins)
TRIM28 acts as a central factor in controlling endothelial inflammatory responses and angiogenic activities by retaining expression of TNFR-1 (show TNFRSF1A Proteins) and -2 and VEGF receptor 2 in endothelial cells
regulation of epigenetic modifications coordinated by TRIM28 plays a crucial role in reprogramming process.
The interaction of repressor proteins Trim28 and YY1 (show YY1 Proteins) are involved in the silencing of Moloney murine leukemia virus.
an important role for TRIM28 in cells resisting transition between somatic and pluripotent states, is reported.
Nuclear factors that bind to genomic regions with "Sertoli Cell Signature" could functionally interact with SOX9 (show SOX9 Proteins); TRIM28 is a new SOX9 (show SOX9 Proteins) partner in fetal testes.
TRIM28 safeguards germline-to-soma inheritance of epigenetic features at other genomic regions in an exquisitely stage-dependent manner.
Data suggest that TRIM28 regulates the expression of a subset of lncRNAs.
Zygotic TRIM28 is essential for genomic imprinting. Secondary imprints were hypomethylated in TRIM28 mutants.
Trim28(+/D9) mutant mice exhibit a bi-modal body-weight distribution, with isogenic animals randomly emerging as either normal or obese and few intermediates.
Data suggest that interaction between KAP1 and the KRAB A (show ZNF223 Proteins) box of zinc finger protein 809 (ZFP809) is critical in KAP1-dependent control of gene silencing for ZFP809 targets.
We find that NPCs use TRIM28-mediated histone modifications to dynamically regulate transcription and silencing of ERVs, which is in contrast to other somatic cell types using DNA methylation (show HELLS Proteins)
The protein encoded by this gene mediates transcriptional control by interaction with the Kruppel-associated box repression domain found in many transcription factors. The protein localizes to the nucleus and is thought to associate with specific chromatin regions. The protein is a member of the tripartite motif family. This tripartite motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region.
E3 SUMO-protein ligase TRIM28
, KRAB-associated protein 1
, KRAB-interacting protein 1
, RING finger protein 96
, nuclear corepressor KAP-1
, transcription intermediary factor 1-beta
, transcriptional intermediary factor 1-beta
, tripartite motif-containing 28
, tripartite motif-containing protein 28
, transcription intermediary factor 1-beta-like
, KRAB-A-interacting protein
, transcriptional intermediary factor 1, beta
, tripartite motif protein 28
, TIF1beta transcription factor