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Western blot analysis of Nucleoporin p62 on HeLa cell lysate. Lane 1: 1:1000, lane 2: 1:2000, lane 3: 1:4000 dilution of anti-Nucleoporin p62.
Immunofluorescent staining on WI38 cells.
BD Transduction Laboratories™ Purified Mouse Anti-Nucleoporin p62
BD Transduction Laboratories™ Purified Mouse Anti-Nucleoporin p62
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Preparation And Storage
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- 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.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
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.
Development References (5)
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Carmo-Fonseca M, Kern H, Hurt EC. Human nucleoporin p62 and the essential yeast nuclear pore protein NSP1 show sequence homology and a similar domain organization. Eur J Cell Biol. 1991; 55(1):17-30. (Biology). View Reference
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Daigle N, Beaudouin J, Hartnell L, et al. Nuclear pore complexes form immobile networks and have a very low turnover in live mammalian cells. J Cell Biol. 2001; 154(1):71-84. (Clone-specific: Immunohistochemistry). View Reference
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Iborra FJ, Jackson DA, Cook PR. The path of RNA through nuclear pores: apparent entry from the sides into specialized pores. J Cell Sci. 2000; 113(2):291-302. (Clone-specific: Electron microscopy). View Reference
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Paroni G, Henderson C, Schneider C, Brancolini C. Caspase-2 can trigger cytochrome C release and apoptosis from the nucleus. J Biol Chem. 2002; 277(17):15147-15161. (Clone-specific: Immunofluorescence). View Reference
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Shah M, Patel K, Fried VA, Sehgal PB. Interactions of STAT3 with caveolin-1 and heat shock protein 90 in plasma membrane raft and cytosolic complexes. Preservation of cytokine signaling during fever. J Biol Chem. 2002; 277(47):45662-45669. (Clone-specific: Western blot). View Reference
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