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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
Authors identify a viral mechanism for the counteraction of KAP1 (zeige CDKN3 Proteine) in which interference with the KAP1 (zeige CDKN3 Proteine) phosphatase protein phosphatase 1 (zeige PPP1CB Proteine) (PP1 (zeige PPA1 Proteine)) by the AAV2 Rep proteins mediates enhanced phosphorylation of KAP1 (zeige CDKN3 Proteine)-S824 and thus relief from KAP1 (zeige CDKN3 Proteine) repression.
Evaluation of the potential mechanism demonstrated that TRIM28 promoted cervical cancer cell growth by activating the mammalian target of rapamycin (mTOR (zeige FRAP1 Proteine)) signaling pathway. In support of this finding, TRIM28-induced cell proliferation was abolished by treatment with everolimus, a specific mTOR (zeige FRAP1 Proteine) inhibitor
TRIM28 employs KRAB-ZNFs to evoke epigenetic silencing of its target differentiation genes via H3K9me3 and DNA methylation (zeige HELLS Proteine).
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 (zeige CTNND2 Proteine) expression.
Data indicate a mechanism in breast cancer cells that tripartite motif-containing 28 protein (TRIM28) enhances metastasis by stabilizing TWIST1 (zeige TWIST1 Proteine), suggesting that targeting TRIM28 could be an efficacious strategy in breast cancer treatment.
Gamma-H2AX (zeige H2AFX Proteine), phosphorylated KAP-1 (zeige CDKN3 Proteine) and 53BP1 (zeige TP53BP1 Proteine) 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 (zeige E2F1 Proteine). 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.
regulation of epigenetic modifications coordinated by TRIM28 plays a crucial role in reprogramming process.
The interaction of repressor proteins Trim28 and YY1 (zeige YY1 Proteine) 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 (zeige SOX9 Proteine); TRIM28 is a new SOX9 (zeige SOX9 Proteine) 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 (zeige ZNF223 Proteine) 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 (zeige HELLS Proteine)
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