Description
Antigen
C-terminal domain (20 amino acids: C-NYD IGA ALD TIQ YSK HPP PL) of human p62 protein, coupled to KLH. This peptide sequence is identical in human, monkey, bovine, mouse, and rat.
Reactive Polypeptide (Specificity)
Human 62 kD (p62) protein, is present in intracytoplasmic inclusions (e.g. hyaline bodies) of hepatocellular carcinoma. p62 protein (also described as ubiqutin-binding protein; sequestosome 1; SQSTM1) has been found in many tissues and cells, including lymphoid cells, serving probably a common cellular signal transduction mechanism (e.g. ubiquitin-associated degradation and autophagy). The antiserum stains also neurofibrillary tangles in the brain of patients suffering from Alzheimer’s disease.
Suitable for
- immunohistochemistry on frozen and paraffin* sections (*enhanced after microwave treatment)
- cytological material - immunoblotting
Working Dilution
1: 100 – 1:200 for immunohistochemistry
1:1,000 – 1:2000 for Western blotting (ECL)
Incubation Time
1 h at RT; extended with paraffin sections
Volume
100 μl; contains 0.09% sodium azide
Reference
Stumptner C, Heid H, Fuchsbichler A, Hauser H, Mischinger H-J, Zatloukal K and Denk H: Analysis of intracytoplasmic hyaline
bodies in a hepatocellular carcinoma. Demonstration of p62 as major constituent. Am J Pathol 154, 1701-1710 (1999).
Zatloukal K, Stumptner C, Fuchsbichler A, Heid H, Schnoelzer M, Kenner L, Kleinert R, Prinz M, Aguzzi A and Denk H: p62 is a common component of cytoplasmic inclusions in protein aggregation diseases. Am J Pathol 160, 255-263 (2002)
Stumptner C, Fuchsbichler A, Heid H, Zatloukal K, Denk H: Mallory Body - a disease-associated type of sequestosome. Hepatology 35, 1053-1062 (2002)
Kuusisto E, Salminen A and Alafuzoff I: Early accumulation of p62 in neurofibrillary tangles in Alzheimer’s disease: possible role in tangle formation. Neuropathology & Applied Neurobiology 28, 228-237 (2002)
Arai T, Nonaka T, Hasegawa M, Akiyama H, Yoshida M, Hashizume Y, Tsuchiya K, Oda T, Ikeda K: Neuronal and glial inclusions in frontotemporal dementia with or without motor neuron disease are immunopositive for p62. Neuroscience Letters 342, 41-44 (2003)
Furukawa Y, Iseki E, Hino H, Kanai A, Odawara T, Kosaka K: Ubiqitin and ubiquitin-related proteins in neurons and dendrites of brains of atypical Pick’s disease without Pick bodies. Neuropathology 24, 38-45 (2004)
Müller T, Langner C, Fuchsbichler A, Heinz-Erian P, Ellemunter H, Schlenck B, Bavdekar AR, Pradhan AM, Pandit A, Müller-Höcker J, Melter M, Kobayashi K, Nagasaka H, Kikuta H, Müller W, Tanner MS, Sternlieb I, Zatloukal K, Denk H: Immunohistochemical analysis of Mallory Bodies in Wilsonian and Non-Wilsonian hepatic copper toxicosis. Hepatology 39, 963-969 (2004)
Janig E, Stumptner C, Fuchsbichler A, Denk H, Zatloukal K: Interaction of stress proteins with misfolded keratins. Eur J Cell Biol 84, 329-339 (2005)
Kuusisto E, Kauppinen T, Alafuzoff I: Use of p62/SQSTM1 antibodies for neuropathological diagnosis. Neuropathology & Applied Neurobiology pp 1-12 (2007)
BjørkøyG, Lamark T, Pankiv S, Øvervatn A, Brech A, Johansen T: Monitoring autophagic degradation of p62/SQSTM1. Methods Enzymol 452, 181-197 (2009)
Aishima S, Fujita N, Mano Y, Iguchi T, Taketomi A, Maehara Y, Oda Y, Tsuneyoshi M: p62+ hyaline inclusions in intrahepatic cholangiocarcinoma associated with viral hepatitis or alcoholic liver disease. Am j Clin Pathol 134,457-465 (2010)
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)
