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NUP62 antibody (Nucleoporin 62) (AA 24-178)

Details for Product anti-NUP62 Antibody No. ABIN968004, Supplier: Log in to see
  • CG6251
  • Dmel\\CG6251
  • p62
  • DDBDRAFT_0167902
  • DDBDRAFT_0237712
  • DDB_0167902
  • DDB_0237712
  • nup62
  • Nucleoporin 62
  • predicted protein
  • nuclear pore protein
  • Nup62 nuclear pore complex glycoprotein p62-related protein (IC)
  • Nuclear pore glycoprotein p62
  • Nup62
  • nup62
AA 24-178
Chicken, Human, Mouse (Murine), Rat (Rattus)
Clonality (Clone)
Monoclonal ()
Immunofluorescence (IF), Immunoprecipitation (IP), Immunohistochemistry (IHC), Western Blotting (WB)
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Immunogen Human Nucleoporin aa. 24-178
Clone 53-Nucleoporin p62
Isotype IgG2b
Cross-Reactivity Chicken, Mouse (Murine), Rat (Rattus)
Characteristics 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
Purification The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography.
Alternative Name Nucleoporin p62
Background The nuclear pore complex (NPC) acts as a gate to mediate active transport of proteins and RNA into and out of the nucleus. Proteins actively transported into the nucleus through the NPC require specific nuclear localization sequences. Many of these nucleoporins contain N-acetylglucosamine (GlcNAc) residues that are O-linked to serine or threonine. p62 is the best characterized member of a group of nucleoporins that line the central region of the NPC. A tightly associated complex is formed by p62 and two other nucleoporins, p54 and p58. p54 binds to a carboxy-terminal coiled-coil domain of p62 and p58 binds to a dimer of p54. The amino-terminal domain of p62 contains a series of XFXFX repeats and is joined to the coiled-coil domain by a threonine-rich linker segment. The major role of p62 is maintenance of the structural integrity of NPCs.
Molecular Weight 62 kDa
Research Area Chromatin and Nuclear Signaling, Apoptosis/Necrosis

Related Products: ABIN968535, ABIN967389

Restrictions For Research Use only
Format Liquid
Concentration 250 μg/mL
Buffer Aqueous buffered solution containing BSA, glycerol, and ≤0.09 % sodium azide.
Preservative Sodium azide
Precaution of Use This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Storage Comment Store undiluted at -20° C.
Supplier Images
Western Blotting (WB) image for anti-NUP62 antibody (Nucleoporin 62) (AA 24-178) (ABIN968004) Western blot analysis of Nucleoporin p62 on HeLa cell lysate. Lane 1: 1:1000, lane 2:...
Immunofluorescence (IF) image for anti-NUP62 antibody (Nucleoporin 62) (AA 24-178) (ABIN968004) Immunofluorescent staining on WI38 cells.
Product cited in: Paroni, Henderson, Schneider, Brancolini: "Caspase-2 can trigger cytochrome C release and apoptosis from the nucleus." in: The Journal of biological chemistry, Vol. 277, Issue 17, pp. 15147-61, 2002 (PubMed).

Shah, Patel, Fried, Sehgal: "Interactions of STAT3 with caveolin-1 and heat shock protein 90 in plasma membrane raft and cytosolic complexes. Preservation of cytokine signaling during fever." in: The Journal of biological chemistry, Vol. 277, Issue 47, pp. 45662-9, 2002 (PubMed).

Daigle, Beaudouin, Hartnell, Imreh, Hallberg, Lippincott-Schwartz, Ellenberg: "Nuclear pore complexes form immobile networks and have a very low turnover in live mammalian cells." in: The Journal of cell biology, Vol. 154, Issue 1, pp. 71-84, 2001 (PubMed).

Iborra, Jackson, Cook: "The path of RNA through nuclear pores: apparent entry from the sides into specialized pores." in: Journal of cell science, Vol. 113 Pt 2, pp. 291-302, 2000 (PubMed).

Background publications 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, Vol. 55, Issue 1, pp. 17-30, 1991 (PubMed).