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Human Polyclonal NUP62 Primary Antibody for EIA, WB - ABIN453235
Stochaj, Ba?ski, Kodiha, Matusiewicz: The N-terminal domain of the mammalian nucleoporin p62 interacts with other nucleoporins of the FXFG family during interphase. in Experimental cell research 2006
Show all 3 references for ABIN453235
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
Show all 2 references for ABIN2452063
Human Polyclonal NUP62 Primary Antibody for ELISA - ABIN334450
Carmo-Fonseca, Kern, Hurt: Human nucleoporin p62 and the essential yeast nuclear pore protein NSP1 show sequence homology and a similar domain organization. in European journal of cell biology 1991
Role for NUP62 depletion and PYK2 (show PTK2B Antibodies) redistribution in dendritic retraction resulting from chronic stress
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.
ORP8 (show OSBPL8 Antibodies) was shown to compete with Exo70 (show EXOC7 Antibodies) for interaction with NUP62, and NUP62 knockdown abolished the migration enhancement of ORP8 (show OSBPL8 Antibodies)-silenced cells, suggesting that the endogenous ORP8 (show OSBPL8 Antibodies) 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.
Knockdown of Nup62 (and CaMKK2 (show CAMKK2 Antibodies)) reduced androgen receptor (show AR Antibodies) transcriptional activity in castrate resistant prostate cancer cells.
The data presented here suggest that BGLF4 interferes with the normal functions of Nup62 and Nup153 (show NUP153 Antibodies) and preferentially helps the nuclear import of viral proteins for viral DNA replication and assembly.
These data reveal an emergent Kap (show CDKN3 Antibodies)-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.
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 (show NUP153 Antibodies).
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 (show NUP214 Antibodies)) 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 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.
, nuclear pore glycoprotein p62
, 62 kDa nucleoporin
, nuclear pore glycoprotein 62
, nucleoporin Nup62
, nuclear pore complex 1