Anti-p62 (SQSTM1) (Human) pAb (Polyclonal Antibody)

  • Applications
    • ICC
    • IHC
    • IP
    • WB
  • Target p62
  • Host Species Rabbit
  • Species Reactivities Hamster, Human, Mouse, Rat
  • Code # PM045
  • Size 100 µl
  • Price

Alternative Names

sequestosome 1, p60, p62, A170, OSIL, PDB3, ZIP3, p62B, Osi, A170, STAP, OSF-6, Osi, ZIP


p62/SQSTM1 interacts with various molecular groups such as RIP, TRAF6, ERK, aPKCs, and poly-ubiquitin through PB1 domain, Zn finger domain, and UBA domain. This protein direct interacts with LC3, which is localized on autophagosome membrane, and is degradated by autophagic-lysosome pathway. p62 regulates ubiquitin-positive protein aggregates caused by autophagy deficiency.
  • Antibody Type:
  • Application:
    ICC, IHC, IP, WB
  • Conjugate:
  • Description:
    This LC3 antibody is validated for multiple applications (WB, IHC, ICC and IP) and is widely cited, including in research papers with more than 200 citations (Waguri S, Komatsu M. Biochemical and morphological detection of inclusion bodies in autophagy-deficient mice. Methods Enzymol. 453, 181-96 (2009)). This is a polyclonal antibody of 100 ul that is raised in rabbit and is reactive with human, hamster, mouse, rat.
  • Formulation:
    100 μl volume of PBS containing 50% glycerol, pH 7.2. No preservative is contained.
  • Gene ID (Human):
  • Gene ID (Mouse):
  • Gene ID (Rat):
  • Host Species:
  • Immunogen:
    Recombinant human p62 (120-440 a.a.)
  • Isotype:
    Affinity Purified Ig
  • Product Type:
  • Reactivity:
    This antibody reacts with p62 on Western blotting, Immunoprecipitation, Immunohistochemistry and Immunocytochemistry.
  • Research Area:
  • Short Description:

    p62 Polyclonal Antibody.

  • Size:
    100 µl
  • Species Reactivity:
    Hamster, Human, Mouse, Rat
  • Storage Temperature:
  • Target:
  1. Berliocchi L et al. Autophagy impairment in a mouse model of neuropathic pain. Mol Pain 7, 83 (2011),
  2. Dupont N et al. Shigella phagocytic vacuolar membrane remnants participate in the cellular response to pathogen invasion and are regulated by autophagy. Cell Host Microbe. 6, 137-49 (2009),
  3. Frankel LB et al. microRNA-101 is a potent inhibitor of autophagy. EMBO J. 30, 4628-41 (2011),
  4. Higaki K et al. Chemical chaperone therapy: chaperone effect on mutant enzyme and cellular pathophysiology in β-galactosidase deficiency. Hum Mutat. 32, 843-52 (2011),
  5. Huang C et al. Preconditioning involves selective mitophagy mediated by Parkin and p62/SQSTM1. PLoS One 6, e20975 (2011),
  6. Huang Y et al. PML-RARα enhances constitutive autophagic activity through inhibiting the Akt/mTOR pathway. Autophagy 7, 1132-44 (2011),
  7. Itakura E, Mizushima N. p62 Targeting to the autophagosome formation site requires self-oligomerization but not LC3 binding. J Cell Biol. 192, 17-27 (2011),
  8. Lee EJ, Tournier C. The requirement of uncoordinated 51-like kinase 1 (ULK1) and ULK2 in the regulation of autophagy. Autophagy 7 689-95  (2011),
  9. Myeku N, Figueiredo-Pereira ME. Dynamics of the degradation of ubiquitinated proteins by proteasomes and autophagy: association with sequestosome 1/p62. J Biol Chem. 286, 22426-40 (2011),
  10. Ogata T et al. Fasting-related autophagic response in slow- and fast-twitch skeletal muscle. Biochem Biophys Res Commun. 394, 136-40 (2010),
  11. Osawa Y et al. L-tryptophan-mediated enhancement of susceptibility to nonalcoholic fatty liver disease is dependent on the mammalian target of rapamycin. J Biol Chem. 286, 34800-8 (2011),
  12. Otomo T et al. Inhibition of autophagosome formation restores mitochondrial function in mucolipidosis II and III skin fibroblasts. Mol Genet Metab. 98, 393-9 (2009),
  13. Rovetta F et al. ER signaling regulation drives the switch between autophagy and apoptosis in NRK-52E cells exposed to cisplatin. Exp Cell Res. 318, 238-50 (2012),
  14. Seto S et al. Coronin-1a inhibits autophagosome formation around Mycobacterium tuberculosis-containing phagosomes and assists mycobacterial survival in macrophages. Cell Microbiol. 14, 710-27 (2012),
  15. Takaesu G et al. TGFβ-activated kinase 1 (TAK1)-binding proteins (TAB) 2 and 3 negatively regulate autophagy. J Biochem. 151, 157-66 (2012),
  16. Takamura A et al. Lysosomal accumulation of Trk protein in brain of GM1 -gangliosidosis mouse and its restoration by chemical chaperone. J Neurochem. 118, 399-406 (2011),
  17. Urbanczyk A et al. PKCζ-interacting protein ZIP3 is generated by intronic polyadenylation, and is expressed in the brain and retina of the rat. Biochem J. 433, 43-50 (2011),
  18. Velikkakath AK et al. Mammalian Atg2 proteins are essential for autophagosome formation and important for regulation of size and distribution of lipid droplets. Mol Biol Cell 23, 896-909 (2012),
  19. Waguri S, Komatsu M. Biochemical and morphological detection of inclusion bodies in autophagy-deficient mice. Methods Enzymol. 453, 181-96 (2009),
  20. Wu SY et al. Ras-related tumorigenesis is suppressed by BNIP3-mediated autophagy through inhibition of cell proliferation. Neoplasia 13, 1171-82 (2011)
  21. Homma, T., et al., Sci. Rep. (2014) In press. [WB, IC]
  22. Waguri, S. and Komatsu, M., Methods Enzymol. 453, 181-196 (2009) [WB, IHC]
  1. Komatsu, M., et al., Cell 131, 1149-1163 (2007)
  2. Moscat, J., et al., Mol. Cell 23, 631-640 (2006)
  3. Seibenhener, M. L., et al., Mol. Cell Biol. 24, 8055-8068 (2004)