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SQSTM1 (p62) Antibody (C-term)
Purified Rabbit Polyclonal Antibody (Pab)
_(C-term)_-_U251_CQ.jpg)
- SPECIFICATION
- CITATIONS: 30
- PROTOCOLS
- BACKGROUND
Application 
| WB, IF, IHC-P, E |
|---|---|
| Primary Accession | Q13501 |
| Other Accession | O08623, Q64337 |
| Reactivity | Human, Mouse |
| Predicted | Rat |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 47687 Da |
| Antigen Region | 317-346 aa |
| Gene ID | 8878 |
|---|---|
| Other Names | 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 |
| Target/Specificity | This SQSTM1 (p62) antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 317-346 amino acids of human SQSTM1 (p62). |
| Dilution | IF~~1:50~100 WB~~1:2000 IHC-P~~1:50~100 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | SQSTM1 (p62) Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | SQSTM1 {ECO:0000303|PubMed:16286508, ECO:0000312|HGNC:HGNC:11280} |
|---|---|
| Function | Molecular adapter required for selective macroautophagy (aggrephagy) by acting as a a bridge between polyubiquitinated proteins and autophagosomes (PubMed:16286508, PubMed:20168092, PubMed:24128730, PubMed:34471133, PubMed:22622177, PubMed:22017874, PubMed:15340068, PubMed:17580304, PubMed:28404643, PubMed:15953362, PubMed:29507397, PubMed:29343546, PubMed:31857589, PubMed:33509017, PubMed:37306101, PubMed:37802024). Promotes the recruitment of ubiquitinated cargo proteins to autophagosomes via multiple domains that bridge proteins and organelles in different steps (PubMed:16286508, PubMed:20168092, PubMed:24128730, PubMed:22622177, PubMed:29507397, PubMed:29343546, PubMed:28404643, PubMed:37802024). SQSTM1 first mediates the assembly and removal of ubiquitinated proteins by undergoing liquid-liquid phase separation upon binding to ubiquitinated proteins via its UBA domain, leading to the formation of insoluble cytoplasmic inclusions, known as p62 bodies (PubMed:15911346, PubMed:20168092, PubMed:24128730, PubMed:22017874, PubMed:29507397, PubMed:29343546, PubMed:31857589, PubMed:37802024). SQSTM1 then interacts with ATG8 family proteins on autophagosomes via its LIR motif, leading to p62 body recruitment to autophagosomes, followed by autophagic clearance of ubiquitinated proteins (PubMed:16286508, PubMed:20168092, PubMed:24128730, PubMed:22622177, PubMed:28404643, PubMed:17580304, PubMed:37802024). SQSTM1 is itself degraded along with its ubiquitinated cargos (PubMed:16286508, PubMed:17580304, PubMed:37802024). Also required to recruit ubiquitinated proteins to PML bodies in the nucleus (PubMed:20168092). Also involved in autophagy of peroxisomes (pexophagy) in response to reactive oxygen species (ROS) by acting as a bridge between ubiquitinated PEX5 receptor and autophagosomes (PubMed:26344566). Acts as an activator of the NFE2L2/NRF2 pathway via interaction with KEAP1: interaction inactivates the BCR(KEAP1) complex by sequestering the complex in inclusion bodies, promoting nuclear accumulation of NFE2L2/NRF2 and subsequent expression of cytoprotective genes (PubMed:20452972, PubMed:28380357, PubMed:33393215, PubMed:37306101). Promotes relocalization of 'Lys-63'-linked ubiquitinated STING1 to autophagosomes (PubMed:29496741). Involved in endosome organization by retaining vesicles in the perinuclear cloud: following ubiquitination by RNF26, attracts specific vesicle-associated adapters, forming a molecular bridge that restrains cognate vesicles in the perinuclear region and organizes the endosomal pathway for efficient cargo transport (PubMed:27368102, PubMed:33472082). Sequesters tensin TNS2 into cytoplasmic puncta, promoting TNS2 ubiquitination and proteasomal degradation (PubMed:25101860). May regulate the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF) and interleukin-1 (PubMed:16079148, PubMed:10747026, PubMed:10356400, PubMed:11244088, PubMed:19931284, PubMed:12471037). May play a role in titin/TTN downstream signaling in muscle cells (PubMed:15802564). Adapter that mediates the interaction between TRAF6 and CYLD (By similarity). |
| Cellular Location | Cytoplasmic vesicle, autophagosome. Preautophagosomal structure. Cytoplasm, cytosol. Nucleus, PML body. Late endosome. Lysosome. Nucleus Endoplasmic reticulum. Cytoplasm, myofibril, sarcomere {ECO:0000250|UniProtKB:O08623}. Note=In cardiac muscle, localizes to the sarcomeric band (By similarity). Localizes to cytoplasmic membraneless inclusion bodies, known as p62 bodies, containing polyubiquitinated protein aggregates (PubMed:11786419, PubMed:20357094, PubMed:22017874, PubMed:29507397, PubMed:29343546, PubMed:37802024, PubMed:31857589, PubMed:37306101). In neurodegenerative diseases, detected in Lewy bodies in Parkinson disease, neurofibrillary tangles in Alzheimer disease, and HTT aggregates in Huntington disease (PubMed:15158159). 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 (PubMed:11981755) Enriched in Rosenthal fibers of pilocytic astrocytoma (PubMed:11786419). In the cytoplasm, observed in both membrane-free ubiquitin-containing protein aggregates (sequestosomes) and membrane- surrounded autophagosomes (PubMed:15953362, PubMed:17580304) Colocalizes with TRIM13 in the perinuclear endoplasmic reticulum (PubMed:22178386). Co-localizes with TRIM5 in cytoplasmic bodies (PubMed:20357094). When nuclear export is blocked by treatment with leptomycin B, accumulates in PML bodies (PubMed:20168092) {ECO:0000250|UniProtKB:O08623, ECO:0000269|PubMed:11786419, ECO:0000269|PubMed:11981755, ECO:0000269|PubMed:15158159, ECO:0000269|PubMed:15953362, ECO:0000269|PubMed:17580304, ECO:0000269|PubMed:20168092, ECO:0000269|PubMed:20357094, ECO:0000269|PubMed:22017874, ECO:0000269|PubMed:22178386, ECO:0000269|PubMed:29343546, ECO:0000269|PubMed:29507397, ECO:0000269|PubMed:31857589, ECO:0000269|PubMed:37306101, ECO:0000269|PubMed:37802024} |
| Tissue Location | Ubiquitously expressed. |
Provided below are standard protocols that you may find useful for product applications.
Background
SQSTM1/p62 is an adapter protein which binds ubiquitin and may regulate the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF) and interleukin-1. This protein may play a role in titin/TTN downstream signaling in muscle cells, and may also regulate signaling cascades through ubiquitination. This protein is involved in cell differentiation, apoptosis, immune response and regulation of K(+) channels. SQSTM1/p62 also appears to play a role in macroautophagic removal of intracellular protein aggregates. Cellular depletion studies of SQSTM1/p62 have indicated a role for association with LC3 and aggregate proteins in order to facilitate normal formation of the autophagosome.
References
References for protein:
1.Seibenhener, M.L., et al., Mol. Cell. Biol. 24(18):8055-8068 (2004).
2.Eekhoff, E.W., et al., Arthritis Rheum. 50(5):1650-1654 (2004).
3.Brajenovic, M., et al., J. Biol. Chem. 279(13):12804-12811 (2004).
4.Kuusisto, E., et al., J. Neuropathol. Exp. Neurol. 62(12):1241-1253 (2003).
5. Johnson-Pais, T.L., et al., J. Bone Miner. Res. 18(10):1748-1753 (2003).
References for U251 cell line:
1. Westermark B.; Pontén J.; Hugosson R. (1973).” Determinants for the establishment of permanent tissue culture lines from human gliomas”. Acta Pathol Microbiol Scand A. 81:791-805. [PMID: 4359449].
2. Pontén, J.,Westermark B. (1978).” Properties of Human Malignant Glioma Cells in Vitro”. Medical Biology 56: 184-193.[PMID: 359950].
3. Geng Y.;Kohli L.; Klocke B.J.; Roth K.A.(2010). “Chloroquine-induced autophagic vacuole accumulation and cell death in glioma cells is p53 independent”. Neuro Oncol. 12(5): 473–481.[ PMID: 20406898].
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