|Application ||WB, IHC-P, IF, E|
|Other Accession||Q13501, 74735628|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||47687 Da|
|Application Notes||SQSTM1 antibody can be used for detection of SQSTM1 by Western blot at 1 - 2 µg/mL. Antibody can also be used for immunohistochemistry starting at 5 µg/mL. For immunofluorescence start at 20 µg/mL.|
|Reconstitution & Storage||SQSTM1 antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.|
|Precautions||SQSTM1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Autophagy receptor that interacts directly 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.|
|Cellular Location||Cytoplasm. Late endosome. Lysosome. Cytoplasmic vesicle, autophagosome. Nucleus. Endoplasmic reticulum. Cytoplasm, P-body. Note=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.|
|Tissue Location||Ubiquitously expressed.|
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Provided below are standard protocols that you may find useful for product applications.
SQSTM1 Antibody: SQSTM1/p62 is an adapter protein which binds ubiquitin and regulates signaling cascades through ubiquitination. It may regulate the activation of NF-κB by TNF-α, nerve growth factor (NGF) and interleukin-1. SQSTM1/p62, a co-interacting protein of the atypical PKC isoforms, has a UBA domain at its C-terminal end, which binds non-covalently to polyubiquitin chain. SQSTM1's UBA domain is necessary for recruitment of polyubiquitin and aggresome formation. SQSTM1 may play a role in titin/TTN downstream signaling in muscle cells and may be involved in cell differentiation, apoptosis, immune response and regulation of K+ channels. Mutations in the ubiquitin-associated (UBA) domain of SQSTM1 commonly cause Paget's disease of bone since the UBA is necessary for aggregate sequestration and cell survival.
Seibenhener ML, Babu JR, Geeth T, et al. Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation. Mol. Cell. Biol.2004; 24:8055-68.
Hocking LJ, Lucas GJ, Daroszewska A, et al. Domain-specific mutations in sequestosome 1 (SQSTM1) cause familial and sporadic Paget’s disease. Hum. Mol. Genet.2002; 11:2735-9.
Rousiere M, Michou L, Cornelis F, et al. Paget’s disease of bone. Best Pract. Res. Clin. Rheumatol.2003; 17:1019-41.
Layfield R, Ciani B, Ralston SH, et al. Structural and functional studies of mutations affecting the UBA domain of SQSTM1 (p62) which cause Paget’s disease of bone. Biochem. Soc. Trans.2004; 32:728-30.
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