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anti-Rat (Rattus) NUP153 Antikörper:
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Rat (Rattus) Monoclonal NUP153 Primary Antibody für ICC, IF - ABIN2452062
Lim, Fahrenkrog, Köser, Schwarz-Herion, Deng, Aebi: Nanomechanical basis of selective gating by the nuclear pore complex. in Science (New York, N.Y.) 2007
Show all 2 Pubmed References
Human Polyclonal NUP153 Primary Antibody für ICC, IF - ABIN408608
Wan, Zhang, Langley, Liu, Hu, Han, Peng, Ellis, Jones, Lu: DNA-damage-induced nuclear export of precursor microRNAs is regulated by the ATM-AKT pathway. in Cell reports 2013
Human Polyclonal NUP153 Primary Antibody für IP, WB - ABIN408609
Watters, Palmenberg: Differential processing of nuclear pore complex proteins by rhinovirus 2A proteases from different species and serotypes. in Journal of virology 2011
Nup153 and Megator (Mtor) bind to 25% of the genome in continuous domains extending 10 kb to 500 kb.
The FG repeats of Nup153 are necessary for its function in transport, whereas the remainder of the protein maintains pore integrity.
Nucleoporins 107, 62 and 153 mediate Kcnq1ot1 imprinted domain regulation in extraembryonic endoderm stem cells.
Nup153 and Sox2 bind and co-regulate hundreds of genes.
Nup50 dynamics are independent of importin alpha, Nup153, and Nup98, even though the latter two proteins also exhibit transcription-dependent mobility.
results demonstrate a chromatin-associated role of Nup153 in maintaining stem cell pluripotency by functioning in mammalian epigenetic gene silencing
Nup153 is essential for the HIV-1 nuclear import in nondividing cells, and CPSF6 is important for HIV-1 integration.
Despite the requirement of all three nucleoporins for accurate NHEJ, only Nup153 is needed for proper nuclear import of 53BP1 and SENP1-dependent sumoylation of 53BP1. Our data support the role of Nup153 as an important regulator of 53BP1 activity and efficient NHEJ.
results further highlight the antagonistic relationship between 53BP1 and BRCA1, and place Nup153 and Nup50 in a molecular pathway that regulates 53BP1 function by counteracting BRCA1-mediated events.
Nup153 is an epigenetic regulator which, upon altered NO signalling, mediates the activation of genes potentially associated with early dystrophic cardiac remodelling.
NUP153 and CPSF6 have overlapping binding sites, but each makes unique capsid monomers (CA) interactions. Multiple ligands share an overlapping interface in HIV-1 capsid that is lost upon viral disassembly.
Study assessed the extent of collapse of a Nup153 fragment in molecular dynamics simulations and compared the results to single molecule FRET and small-angle X-ray scattering experiments of this peptide
Our data indicate a central function of Nup153 in the organization of the nucleus, not only at the periphery, but throughout the entire nuclear interior.
Nucleoporin Nup153 is required for NPC assembly during interphase but not during mitotic exit. It functions in interphasic NPC formation by binding directly to the inner nuclear membrane via an N-terminal amphipathic helix.
The data presented here suggest that BGLF4 interferes with the normal functions of Nup62 and Nup153 and preferentially helps the nuclear import of viral proteins for viral DNA replication and assembly.
These data reveal an emergent Kap-centric barrier mechanism that may underlie mechanistic and kinetic control in the nuclear pore complex.
a subset of lentiviral CA proteins directly engage FG-motifs present on NUP153 to affect viral nuclear import.
The Nup153 binds to both SENP1 and SENP2 and does so by interacting with the unique N-terminal domain of Nup153 as well as a specific region within the C-terminal FG-rich region.
A hydrophobic patch 65LRLFV69 within the zinc-binding domain is essential for the nuclear import and localization of HPV8 E7 via hydrophobic interactions with Nup62 and Nup153.
The roles of NUP153 and nup98 in the integration and replication of HIV-1 in human Jurkat lymphocytes are reported.
analysis of the Nup153-Nup50 protein interface and its role in nuclear import
human nucleoporin 153 (NUP153) has a role in repair of DSBs and in the activation of DNA damage checkpoints.
Nup153 binds to importin alpha
Data show that the C-terminal part of NUP153 is required for effective 53BP1 nuclear import, and that 53BP1 is imported to the nucleus through the NUP153-importin-beta interplay.
Nup153 levels regulate the localization of Mad1 during the metaphase/anaphase transition thereby affecting its phoshorylation status and in turn spindle checkpoint activity and mitotic exit.
The N-terminal domain of Nup153 and its C terminus associate with the Ig-fold domain of A- and B-type lamins.
analysis of RNA recognition sequence preference by the nucleoporin Nup153
Nuclear pore complexes are extremely elaborate structures that mediate the regulated movement of macromolecules between the nucleus and cytoplasm. These complexes are composed of at least 100 different polypeptide subunits, many of which belong to the nucleoporin family. Nucleoporins are pore complex-specific glycoproteins characterized by cytoplasmically oriented O-linked N-acetylglucosamine residues and numerous repeats of the pentapeptide sequence XFXFG. The protein encoded by this gene has three distinct domains: a N-terminal region within which a pore targeting domain has been identified, a central region containing multiple zinc finger motifs, and a C-terminal region containing multiple XFXFG repeats.
, nucleoporin 153
, nuclear pore complex protein Nup153
, nucleoporin 153kDa
, nuclear pore complex protein Nup153-like
, 153 kDa nucleoporin
, nucleoporin 153kD
, nucleoporin Nup153
, nuclear pore complex protein hnup153