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anti-Human TRF1 Antikörper:
anti-Rat (Rattus) TRF1 Antikörper:
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Human Polyclonal TRF1 Primary Antibody für WB - ABIN537315
Nikitina, Woodcock: Closed chromatin loops at the ends of chromosomes. in The Journal of cell biology 2004
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Human Polyclonal TRF1 Primary Antibody für WB - ABIN4249337
Nyborg, Jansen, Ladd, Fauq, Golde et al.: A signal peptide peptidase (SPP) reporter activity assay based on the cleavage of type II membrane protein substrates provides further evidence for an inverted orientation of the SPP active site ... in The Journal of biological chemistry 2004
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Human Monoclonal TRF1 Primary Antibody für MA, ELISA - ABIN151222
Zhu, Yasumoto, Tsai: Nucleostemin delays cellular senescence and negatively regulates TRF1 protein stability. in Molecular and cellular biology 2006
Human Polyclonal TRF1 Primary Antibody für ELISA, WB - ABIN257852
Chong, van Steensel, Broccoli, Erdjument-Bromage, Hanish, Tempst, de Lange: A human telomeric protein. in Science (New York, N.Y.) 1996
Human Monoclonal TRF1 Primary Antibody für ELISA, FACS - ABIN259053
Jullien, Mestre, Roux, Gire: Eroded human telomeres are more prone to remain uncapped and to trigger a G2 checkpoint response. in Nucleic acids research 2013
Human Monoclonal TRF1 Primary Antibody für IHC (fro), IHC (p) - ABIN2476942
Perez Alvarez, Gurbindo, Hernandez-Sampelayo, Casada, Leon, Garcia Saiz, De Andres, Najera: Mother-to-infant transmission of HIV and hepatitis C infections in children born to HIV-seropositive mothers. in AIDS 1992
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TERF1 is a multifunctional ERF protein that can integrate different stress signal pathways
Data indicate that neither the naturally occurring auxins indole-3-acetic acid and indole-3-butyric acid, nor the synthetic auxin analogs were able to inhibit endocytosis of the putative auxin transporter PIN (zeige DYNLL1 Antikörper)-FORMED2 (PIN2) in root epidermis cells.
AUX1 and PIN2 protect lateral root (LR) formation in Arabidopsis during the early stages of iron (Fe) stress.
Data show that ROTUNDA3 (RON3; At4g24500) protein as a regulator of the protein phosphatase 2A-driven PIN (zeige DYNLL1 Antikörper)-FORMED (PIN (zeige DYNLL1 Antikörper)) auxin transport recycling and its importance in auxin transport-related plant developmental programs.
Brief treatment with indole-3-carbinol led to a reduction in the amount of PIN1 and to mislocalization of PIN2.
PIN2 auxin efflux carriers are differentially controlled in tricho- and atrichoblast cells. PIN2 proteins show lower abundance at the plasma membrane of trichoblast cells, despite showing higher rates of intracellular trafficking in these cells.
under low-B conditions PIN1 is down-regulated and PIN2 plays an important role in root meristem maintenance.
Reduction in PIN2 intensity, polarization, and endocytosis under low phosphate conditions is MAX2 dependent.
Functional interplay between protein kinase CK2 (zeige CSNK2A1 Antikörper) and salicylic acid sustains PIN2 transcriptional expression.
High temperature selectively promotes the retrieval of PIN2 from late endosomes and sorts them to the plasma membrane through an endosomal trafficking pathway dependent on SORTING NEXIN1.
By using solubilized membrane protein immunoprecipitation assays, we established quantitative approaches, suitable for analysis of PIN2 ubiquitylation and variations therein
Data show that TRF1 expression is increased in both human and mouse glioblastoma multiforme (GBM).
our results suggest that RhoGDIalpha regulate TRF1 and telomere length and may be novel prognostic biomarkers in colorectal cancer
TRF1 phosphorylation by Nek7 (zeige NEK7 Antikörper) favors the binding of shelterin protein TIN2 (zeige TINF2 Antikörper) and disfavors E3 ligase Fbx4 (zeige FBXO4 Antikörper) interaction, thus preventing TRF1 ubiquitination and proteasome degradation to maintain telomere integrity.
Cdk-dependent phosphorylation of TRF1 on threonine 371 promotes TRF1 to interact with APBs in S and G2 phases independently of its binding to telomeric DNA. We have demonstrated that the interaction of (pT371)TRF1 with APBs is dependent upon ATM and homologous-recombination-promoting factors such as Mre11 and BRCA1.
TRF1 tethers SA1 (zeige STAG1 Antikörper) within telomeric regions that SA1 (zeige STAG1 Antikörper) transiently interacts with. SA1 (zeige STAG1 Antikörper) and TRF1 together form longer DNA-DNA pairing tracts than with TRF1 alone, as revealed by atomic force microscopy imaging
data suggest that NUB1 participates in telomere maintenance by regulating the levels of TRF1 at telomeres through both NEDD8 (zeige NEDD8 Antikörper)-dependent and NEDD8 (zeige NEDD8 Antikörper)-independent pathways.
Data indicate that overexpression of telomeric repeat binding factor 1 (TRF1) in aging endothelial cells (EC) reduced telomere-associated DNA damage foci.
we provide mechanistic insight into the role of TRF1 in liver regeneration and provide a mouse model recapitulating the clinical features of LLCC.
TRF1 links TopoIIalpha and SAC (zeige ADCY10 Antikörper) proteins in a pathway that ensures correct telomere replication and mitotic segregation, unveiling how TRF1 protects from telomere fragility and mitotic defects.
ZSCAN4 (zeige ZSCAN4 Antikörper) indirectly interacts with TRF1 in cancer cells. We show that ZSCAN4 (zeige ZSCAN4 Antikörper) plays an important role independent of telomere maintenance pathways (telomerase positive and alternative pathway) or cell lineage.
Loss of AURKB (zeige AURKB Antikörper) function affects TERF1 telomere binding and results in aberrant telomere structure.
loss of telomere structure mediated by the TERB1-TRF1 interaction significantly affects homologous pairing of the telomere-adjacent pseudoautosomal region (PAR (zeige AFG3L2 Antikörper)) of the X and Y chromosomes in mouse spermatocytes.
full-length TRF1 presents a molecular architecture that assists its interaction with telometic DNA and at the same time makes TRFH domains accessible to other TRF1 binding partners.
Gene dosage reductions of Trf1 and/or Tin2 (zeige TINF2 Antikörper) induce telomere DNA damage and lymphoma formation in aging mice.
TRF1 is exclusively located at telomeres under normal conditions and under extreme telomere shortening.
Telomeric repeat-binding factor 1, a core component of the telomere protein complex, is a mediator of telomere associations in mammalian cells.
TRF1 binds BLM (zeige BLM Antikörper) to facilitate lagging but not leading strand telomeric DNA synthesis
TRF1 is necessary for both induction and maintenance of pluripotency.
Loss of TRF1 leads to bone marrow failure and recapitulates clinical features of dyskeratosis congenita.
This gene encodes a telomere specific protein which is a component of the telomere nucleoprotein complex. This protein is present at telomeres throughout the cell cycle and functions as an inhibitor of telomerase, acting in cis to limit the elongation of individual chromosome ends. The protein structure contains a C-terminal Myb motif, a dimerization domain near its N-terminus and an acidic N-terminus. Two transcripts of this gene are alternatively spliced products.
telomeric repeat binding factor 1
, telomeric repeat binding factor (NIMA-interacting) 1
, telomeric repeat-binding factor 1
, ethylene-responsive factor 1
, ethylene response factor
, telomeric repeat-binding factor 1-like
, NIMA-interacting protein 2
, TTAGGG repeat-binding factor 1
, telomeric protein Pin2/TRF1
, Telomeric repeat-binding factor 1