Recombinant Human Nuclear pore glycoprotein p62 (NUP62)

Code CSB-YP016204HU
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Source Yeast
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Code CSB-EP016204HU
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Source E.coli
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Code CSB-EP016204HU-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP016204HU
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Source Baculovirus
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Code CSB-MP016204HU
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
NUP62
Uniprot No.
Alternative Names
NUP62; Nuclear pore glycoprotein p62; 62 kDa nucleoporin; Nucleoporin Nup62
Species
Homo sapiens (Human)
Expression Region
2-522
Target Protein Sequence
SGFNFGGTG APTGGFTFGT AKTATTTPAT GFSFSTSGTG GFNFGAPFQP ATSTPSTGLF SLATQTPATQ TTGFTFGTAT LASGGTGFSL GIGASKLNLS NTAATPAMAN PSGFGLGSSN LTNAISSTVT SSQGTAPTGF VFGPSTTSVA PATTSGGFSF TGGSTAQPSG FNIGSAGNSA QPTAPATLPF TPATPAATTA GATQPAAPTP TATITSTGPS LFASIATAPT SSATTGLSLC TPVTTAGAPT AGTQGFSLKA PGAASGTSTT TSTAATATAT TTSSSSTTGF ALNLKPLAPA GIPSNTAAAV TAPPGPGAAA GAAASSAMTY AQLESLINKW SLELEDQERH FLQQATQVNA WDRTLIENGE KITSLHREVE KVKLDQKRLD QELDFILSQQ KELEDLLSPL EELVKEQSGT IYLQHADEER EKTYKLAENI DAQLKRMAQD LKDIIEHLNT SGAPADTSDP LQQICKILNA HMDSLQWIDQ NSALLQRKVE EVTKVCEGRR KEQERSFRIT FD
Protein Length
Full Length of Mature Protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

Customer Reviews and Q&A

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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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