Anti-SQSTM1/p62 Antibody Picoband®, APC Conjugate

SQSTM1 (Sequestosome-1), also known as Ubiquitin-Binding Protein P62 or P62, is a protein that in humans is encoded by the SQSTM1 gene. The Src homology type 2 (SH2) domain is a highly conserved motif of about 100 amino acids which mediates protein-protein interactions by binding to phosphotyrosine.p56-lck, a T-cell-specific src family tyrosine kinase with an SH2 domain, is involved in T-cell signal transduction. The International Radiation Hybrid Mapping Consortium mapped the p62 gene to chromosome 5q35. Park et al. (1995) found that the p56-lck SH2 domain binds to p62 at the ser59 of p62 only when that serine is phosphorylated. Joung et al. (1996) expressed epitope-tagged p62 in Hela cells and showed that the expressed protein bound to the lck SH2 domain and that this binding was dependent on the N-terminal 50 amino acids of p62 but not on the tyrosine residue in this region.

Sequestosome-1;EBI3-associated protein of 60 kDa;EBIAP;p60;Phosphotyrosine-independent ligand for the Lck SH2 domain of 62 kDa;Ubiquitin-binding protein p62;SQSTM1;ORCA, OSIL;

A synthetic peptide corresponding to a sequence at the N-terminus of human SQSTM1, different from the related rat and mouse sequences by one amino acid.

Autophagy receptor that interacts ly with both the cargo to become degraded and an autophagy modifier of the MAP1 LC3 family. Required both for the formation and autophagic degradation of polyubiquitin-containing bodies, called ALIS (aggresome-like induced structures) and links ALIS to the autophagic machinery. Involved in midbody ring degradation. May regulate the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF) and interleukin- 1. May play a role in titin/TTN downstream signaling in muscle cells. May regulate signaling cascades through ubiquitination. Adapter that mediates the interaction between TRAF6 and CYLD (By similarity). May be involved in cell differentiation, apoptosis, immune response and regulation of K (+) channels. .

1. Hocking, L. J., Lucas, G. J. A., Daroszewska, A., Mangion, J., Olavesen, M., Cundy, T., Nicholson, G. C., Ward, L., Bennett, S. T., Wuyts, W., Van Hul, W., Ralston, S. H. Domain-specific mutations in sequestosome 1 (SQSTM1) cause familial and sporadic Paget's disease. Hum. Molec. Genet. 11: 2735-2739, 2002. 2. Joung, I., Strominger, J. L., Shin, J. Molecular cloning of a phosphotyrosine-independent ligand of the p56-lck SH2 domain. Proc. Nat. Acad. Sci. 93: 5991-5995, 1996. 3. Park, I., Chung, J., Walsh, C. T., Yun, Y., Strominger, J. L., Shin, J. Phosphotyrosine-independent binding of a 62-kDa protein to the src homology 2 (SH2) domain of p56-lck and its regulation by phosphorylation of ser-59 in the lck unique N-terminal region. Proc. Nat. Acad. Sci. 92: 12338-12342, 1995.

Store at -20℃ for one year from date of receipt. After reconstitution, at 4℃ for one month. It can also be aliquotted and stored frozen at -20℃ for six months. Avoid repeated freeze-thaw cycles.

Western blot, 0.1-0.5μg/ml, Human<br> Immunohistochemistry (Paraffin-embedded Section), 0.5-1μg/ml, Human, Mouse, Rat, By Heat<br> Immunocytochemistry/Immunofluorescence, 2μg/ml, Human<br> Flow Cytometry (Fixed), 1-3μg/1x10⁶ cells, Human<br>

Cytoplasm. Late endosome. Lysosome. Cytoplasmic vesicle, autophagosome. Nucleus. Endoplasmic reticulum. Cytoplasm, P-body. Sarcomere (By similarity). In cardiac muscles localizes to the sarcomeric band (By similarity). Commonly found in inclusion bodies containing polyubiquitinated protein aggregates. In neurodegenerative diseases, detected in Lewy bodies in Parkinson disease, neurofibrillary tangles in Alzheimer disease, and HTT aggregates in Huntington disease. In protein aggregate diseases of the liver, found in large amounts in Mallory bodies of alcoholic and nonalcoholic steatohepatitis, hyaline bodies in hepatocellular carcinoma, and in SERPINA1 aggregates. Enriched in Rosenthal fibers of pilocytic astrocytoma. In the cytoplasm, observed in both membrane-free ubiquitin- containing protein aggregates (sequestosomes) and membrane- surrounded autophagosomes. Colocalizes with TRIM13 in the perinuclear endoplasmic reticulum. Co-localizes with TRIM5 in the cytoplasmic bodies. .