NUP62 Antibody

Code CSB-PA255769
Size US$166
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Image
  • The image on the left is immunohistochemistry of paraffin-embedded Human prostate cancer tissue using CSB-PA255769(NUP62 Antibody) at dilution 1/50, on the right is treated with fusion protein. (Original magnification: ×200)
  • Gel: 8%SDS-PAGE, Lysate: 40 μg, Lane 1-5: Hela cells, human brain malignant glioma tissue, NIH/3T3 cells, PC3 cells, A549 cells, Primary antibody: CSB-PA255769(NUP62 Antibody) at dilution 1/300, Secondary antibody: Goat anti rabbit IgG at 1/8000 dilution, Exposure time: 5 seconds
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Product Details

Uniprot No.
Target Names
NUP62
Alternative Names
NUP62 antibody; Nuclear pore glycoprotein p62 antibody; 62 kDa nucleoporin antibody; Nucleoporin Nup62 antibody
Raised in
Rabbit
Species Reactivity
Human,Mouse,Rat
Immunogen
Fusion protein of Human NUP62
Immunogen Species
Homo sapiens (Human)
Conjugate
Non-conjugated
Isotype
IgG
Purification Method
Antigen affinity purification
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
-20°C, pH7.4 PBS, 0.05% NaN3, 40% Glycerol
Form
Liquid
Tested Applications
ELISA,WB,IHC
Recommended Dilution
Application Recommended Dilution
ELISA 1:2000-1:5000
WB 1:500-1:2000
IHC 1:50-1:200
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

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Target Background

Function
Essential component of the nuclear pore complex. The N-terminal is probably involved in nucleocytoplasmic transport. The C-terminal is involved in protein-protein interaction probably via coiled-coil formation, promotes its association with centrosomes and may function in anchorage of p62 to the pore complex. Plays a role in mitotic cell cycle progression by regulating centrosome segregation, centriole maturation and spindle orientation. It might be involved in protein recruitment to the centrosome after nuclear breakdown.
Gene References into Functions
  1. 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 PMID: 27298184
  2. Knockdown of Nup62 (and CaMKK2) reduced androgen receptor transcriptional activity in castrate resistant prostate cancer cells. PMID: 26552607
  3. Loss of presenilin (PS)1 function propagates tau accumulation through impairment of cargo-receptor protein p62-dependent tau degradation. PMID: 23794287
  4. 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. PMID: 24107630
  5. Nup62 and Nup88 protein levels were significantly decreased upon knockdown of O-GlcNAc transferase. PMID: 23777819
  6. 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. PMID: 24074597
  7. Nucleoporin p62 (NUP62) and nucleoporin 214 (NUP214) are differentially distributed between nuclear pore complexes. PMID: 22558357
  8. 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. PMID: 22334672
  9. the cellular Nup62 is specifically recruited by HIV-1 IN and contribute to an efficient viral DNA integration. PMID: 22308026
  10. impact of overexpressed ORP8 on nSREBPs and their target mRNAs was inhibited in cells depleted of Nup62 PMID: 21698267
  11. 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 PMID: 20622012
  12. 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. PMID: 19828735
  13. Relocation of cellular proteins and inhibition of nuclear import in HeLa cells during rhinovirus type 14 infections correlated with the degradation of p62 PMID: 12163599
  14. 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. PMID: 16730000
  15. p62 has a cell type-specific role and is important in the degeneration of the basal ganglia in humans PMID: 16786527
  16. autoantibodies reacting with the 60 kDa component of NPCs target p62 nucleoporin PMID: 17960595
  17. Nuclear envelope permeabilization was accompanied by hyperphosphorylation of Nup62 in cells infected with wild-type mengovirus, whereas both of these alterations were suppressed in L-deficient virus mutants. PMID: 19144712

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Involvement in disease
Infantile striatonigral degeneration (SNDI)
Subcellular Location
Nucleus, nuclear pore complex. Cytoplasm, cytoskeleton, spindle pole. Nucleus envelope. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
Protein Families
Nucleoporin NSP1/NUP62 family
Database Links

HGNC: 8066

OMIM: 271930

KEGG: hsa:23636

STRING: 9606.ENSP00000305503

UniGene: Hs.574492

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