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anti-Human NUP62 Antibodies:
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Human Monoclonal NUP62 Primary Antibody for ICC, IF - ABIN2452063
Fukuhara, Sakaguchi, Katahira, Yoneda, Ogino, Tachibana: Functional analysis of nuclear pore complex protein Nup62/p62 using monoclonal antibodies. in Hybridoma (2005) 2006
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Human Polyclonal NUP62 Primary Antibody for ICC, IF - ABIN4341192
Stadler, Hjelmare, Neumann, Jonasson, Pepperkok, Uhlén, Lundberg: Systematic validation of antibody binding and protein subcellular localization using siRNA and confocal microscopy. in Journal of proteomics 2012
Show all 2 Pubmed References
XIAP enhanced cancer cell proliferation, viability, and colony formation in vitro via suppression of p62. In addition, we demonstrated that XIAP-enhanced tumor growth is dependent on depletion of p62 in vivo. Herein, we have therefore delineated a novel mechanism by which XIAP contributes to development and progression of breast and colon carcinoma
ROCK-dependent phosphorylation of NUP62 regulates p63 nuclear transport and squamous cell carcinoma proliferation.
it was revealed that a fraction of Nup62 was associated with mitotic spindle microtubule instead of spindle matrix, and the localization of Nup62 in the mitotic spindle depended on its three coiled-coil domains rather than Crm1, although Nup62 strongly interacted with Crm1 during mitosis. Moreover, depletion of Nup62 by small interference of RNA seriously induced the defects of chromosome alignment and spindle assembly
Knockdown of Nup62 (and CaMKK2) reduced androgen receptor transcriptional activity in castrate resistant prostate cancer cells.
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.
Loss of presenilin (PS)1 function propagates tau accumulation through impairment of cargo-receptor protein p62-dependent tau degradation.
Nup62 depletion leads to the appearance of multinucleated cells and induces the formation of multipolar centrosomes, centriole synthesis defects, dramatic spindle orientation defects, and centrosome component rearrangements that impair cell bi-polarity.
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.
Nup62 and Nup88 protein levels were significantly decreased upon knockdown of O-GlcNAc transferase.
that a patch of hydrophobic residues, 65LRLCV69, within the zinc-binding domain of HPV16 E7 mediates its nuclear import via hydrophobic interactions with the FG domain of the central channel nucleoporin Nup62.
Nucleoporin p62 (NUP62) and nucleoporin 214 (NUP214) are differentially distributed between nuclear pore complexes.
Nup62 protein intact and properly localized in HSV-1-infected cells, and an ICP27 mutant deficient for Nup62 binding failed to inhibit cellular nucleocytoplasmic transport pathways.
the cellular Nup62 is specifically recruited by HIV-1 IN and contribute to an efficient viral DNA integration.
impact of overexpressed ORP8 on nSREBPs and their target mRNAs was inhibited in cells depleted of Nup62
Site-directed mutagenesis of putative cleavage sites in Nup62 identified six different positions that are cleaved by 2A(pro) in vitro. This analysis revealed that 2A(pro) cleavage sites were located between amino acids 103 and 298 in Nup62
Oxidative stress up-regulated the binding of Crm1 to Ran and affected multiple repeat-containing nucleoporins by changing their localization, phosphorylation, O-glycosylation, or interaction with other transport components.
Relocation of cellular proteins and inhibition of nuclear import in HeLa cells during rhinovirus type 14 infections correlated with the degradation of p62
The formation of Nup358/p62 and p62/Nup153 complexes was restricted to interphase cells, whereas Nup214/p62 binding was detected in interphase as well as during mitosis.
p62 has a cell type-specific role and is important in the degeneration of the basal ganglia in humans
Nucleoporins 107, 62 and 153 mediate Kcnq1ot1 imprinted domain regulation in extraembryonic endoderm stem cells.
Role for NUP62 depletion and PYK2 redistribution in dendritic retraction resulting from chronic stress
ORP8 was shown to compete with Exo70 for interaction with NUP62, and NUP62 knockdown abolished the migration enhancement of ORP8-silenced cells, suggesting that the endogenous ORP8 suppresses migration via binding to NUP62.
Dtaa show that importin beta and the integral nuclear pore glycoprotein Nup62 interact with hsp90, hsp70, p23, and the TPR domain proteins FKBP52 and PP5 during nuclear transport.
Study analyzed genomic interactions of full-length nucleoporins Nup98, Nup50, and Nup62 and found that they predominantly interacted with active genes inside the nucleoplasm, particularly those involved in developmental regulation and the cell cycle.
The nuclear pore complex is a massive structure that extends across the nuclear envelope, forming a gateway that regulates the flow of macromolecules between the nucleus and the cytoplasm. Nucleoporins are the main components of the nuclear pore complex in eukaryotic cells. The protein encoded by this gene is a member of the FG-repeat containing nucleoporins and is localized to the nuclear pore central plug. This protein associates with the importin alpha/beta complex which is involved in the import of proteins containing nuclear localization signals. Multiple transcript variants of this gene encode a single protein isoform.
62 kDa nucleoporin
, nuclear pore glycoprotein p62
, nucleoporin Nup62
, nucleoporin 62kDa
, nuclear pore complex 1
, nucleoporin 62
, predicted protein
, Nup62 nuclear pore complex glycoprotein p62-related protein (IC)
, Nuclear pore glycoprotein p62
, nuclear pore glycoprotein 62