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Human Monoclonal TRF2 Primary Antibody für IHC, ELISA - ABIN1724941
Diehl, Idowu, Kimmelshue, York, Jackson-Cook, Turner, Holt, Elmore: Elevated TRF2 in advanced breast cancers with short telomeres. in Breast cancer research and treatment 2011
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Both TRF1 (zeige TERF1 Antikörper) and TRF2 were overexpressed in prostate cancer. There was no specificity of TRF2 in prostate cancer, while TRF1 (zeige TERF1 Antikörper) may be associated with prostate cancer progression.
the excessive HULC plus MALAT1 reduced the methylation of the TERC promoter dependent on TRF2, increasing the TERC expression that causes the increase of interplay between TRET and TERC.
TERF2 knockdown by RNA interference had no effect on cell proliferation, migration, senescence and apoptosis. Instead, TERF2 knockdown increased the expression of cytokines implicated in inflammation and angiogenesis, except for vascular endothelial growth factor (zeige VEGF Antikörper).
the telomere stability is under direct control of one of the major pro-oncogenic signaling pathways (RAS/RAF (zeige RAF1 Antikörper)/MEK (zeige MAP2K1 Antikörper)/ERK (zeige EPHB2 Antikörper)) via TRF2 phosphorylation.
the B-domain improves TRF2's interaction with DNA via enhanced long-range electrostatic interactions.
our findings describe TRF2 as a novel SIRT6 (zeige SIRT6 Antikörper) substrate and demonstrate that acetylation of TRF2 plays a crucial role in the regulation of TRF2 protein stability, thus providing a new route for modulating its expression level during oncogenesis and damage response.
The results suggest that dimerized TRF2 recruits origin recognition complex and stimulates pre-replication complex formation at telomeres through the TRFH domain.
Studied the disruption pattern of of 3D telomere-TRF2 interaction in the progression from mononuclear Hodgkin cells (H) to multinucleated Reed-Sternberg cells (RS).
TRF2, a component of shelterin, binds to core histones to protect chromosome ends from inappropriate DNA damage response and loss of telomeric DNA. The N-terminal Gly/Arg-rich domain (GAR domain) of TRF2 directly binds to the globular domain of core histones.
TRF2 deficiency led to a 1,5-2 fold increase in the radiosensitivity of hMSC-telo1 (zeige ATM Antikörper) cells through telomere destabilization.
It plays a role in hematopoietic stem cell regulation and in the maintenance of the HSC (zeige FUT1 Antikörper) pool and the development of hematological disorders.
Selective inactivation of Terf2 in neural progenitors induced apoptosis, resulting in a complete loss of the brain structure.
The authors propose that TRF2 masks and stabilizes the t-loop three-way junction, thereby protecting telomeres from detrimental deletions and PARP1 (zeige PARP1 Antikörper) activation.
Overexpressing TRF2-S and silencing FMRP (zeige FMR1 Antikörper) promotes mRNA entry to axons and enhances axonal outgrowth and neurotransmitter release from presynaptic terminals.
TRF2 binds and transactivates the promoter of the angiogenic tyrosine kinase (zeige TYRO3 Antikörper) platelet-derived growth factor receptor beta (zeige PDGFRB Antikörper) (PDGFRbeta).
role of TRF2 in skin homeostasis, is reported.
shelterin protein TIN2 (zeige TINF2 Antikörper) can protect chromosome ends as a TRF2-tethered TIN2 (zeige TINF2 Antikörper)/TPP1 (zeige TPP1 Antikörper)/POT1 (zeige POT1 Antikörper) complex that lacks a physical connection to TRF1 (zeige TERF1 Antikörper)
We concluded that genomic instability resulting from loss of TRF2 expression provides biological advantages to the cancer stem cell population
Conditional deletion of individual components of shelterin showed that TRF2 was required for the formation and/or maintenance of t-loops, whereas deletion of TRF1 (zeige TERF1 Antikörper), Rap1 (zeige TERF2IP Antikörper), or the POT1 (zeige POT1 Antikörper) proteins (POT1a (zeige POT1 Antikörper) and POT1b) had no effect on the frequency of t-loop occurrence.
This gene encodes a telomere specific protein, TERF2, which is a component of the telomere nucleoprotein complex. This protein is present at telomeres in metaphase of the cell cycle, is a second negative regulator of telomere length and plays a key role in the protective activity of telomeres. While having similar telomere binding activity and domain organization, TERF2 differs from TERF1 in that its N terminus is basic rather than acidic.
telomeric repeat binding factor 2
, TTAGGG repeat-binding factor 2
, telomeric DNA-binding protein
, telomeric repeat binding protein 2
, telomeric repeat-binding factor 2
, TTAGGG-repeat binding factor 2 TRF2
, telomeric repeat binding factor a
, TTAGGG repeat binding factor 2