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- Table of Contents
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Facts about Sequestosome-1.
Interacts directly with both the freight to become degraded and an autophagy modifier of the MAP1 LC3 family (PubMed:16286508, PubMed:20168092, PubMed:24128730, PubMed:28404643, PubMed:22622177). Together with WDFY3, involved with the formation and autophagic degradation of cytoplasmic ubiquitin- containing inclusions (p62 bodies, ALIS/aggresome-like induced structures).
Human | |
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Gene Name: | SQSTM1 |
Uniprot: | Q13501 |
Entrez: | 8878 |
Belongs to: |
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No superfamily |
A170; Autophagy Receptor P62; DMRV; EBI3-associated protein of 60 kDa; EBI3-associated protein p60; EBIAP; FTDALS3; NADGP; ORCA; OSIL; oxidative stress induced like; p60PDB3; p62; p62B; Paget disease of bone 3; PDB3; phosphotyrosine independent ligand for the Lck SH2 domain p62; Phosphotyrosine-independent ligand for the Lck SH2 domain of 62 kDa; Sequestosome 1; sequestosome-1; SQSTM1; Ubiquitin-binding protein p62; ZIP3
Mass (kDA):
47.687 kDA
Human | |
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Location: | 5q35.3 |
Sequence: | 5; NC_000005.10 (179806393..179838078) |
Ubiquitously expressed.
Cytoplasm, cytosol. Late endosome. Lysosome. Cytoplasmic vesicle, autophagosome. Nucleus. Endoplasmic reticulum. Nucleus, PML body. Cytoplasm, myofibril, sarcomere. In cardiac muscle, 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 st
The SQSTM1 protein is expressed in E.coli and contains a His-Tag. It is a substrate of autophagy, and interacts with HDAC6 in order to regulate its activity. It is useful in analysis of proteins by SDS/PAGE. Continue reading to find out more. This article will provide additional details about the SQSTM1 Protein. You can purchase this protein at Boster Bio.
The autophagy pathway is dominated by the p62/SQSTM1 proteins. It is responsible to deliver cargo ubiquitinated from autophagosomes to the lysosomes. But, when autophagy fails, p62 accumulates as an accumulation marker. Autophagy causes Oligomers that build up in the cytosol as inclusion bodies in the cytosol, which contain K63-linked polyubiquitinated substrates.
The conserved domains of p62 interact with other proteins and perform various roles. The protein is thought to perform a variety of functions that include participation in selective autophagy and UPS, programmed cell death, and signaling pathways. Mutations in p62 can cause diminished autophagy, cellular function, or p62 expression may lead to its accumulation.
During allergic inflammation, p62 levels are greatly increased. It is involved in the regulation of cell interactions as well as mediating the interactions during allergic inflammation. It has also been proven to be negatively affected by 3-MA. However, it's not clear whether autophagy has a role in anaphylaxis. However it is important to note that p62 plays a role in the regulation of a variety of the hallmarks of allergic inflammation.
In the course of allergic inflammation, the hormone p62 can also encourage tumor cell growth and metastasis. PSA increased the activity of b-hexosaminidase in B16F1 cells in a manner that is p62 dependent. Additionally, down-regulation of the p62 gene inhibited PSA-induced interactions with HDAC3. These results suggest that the p62/SQSTM1 is a critical element in the increased metastatic potential of cancerous cells.
The multifunctional scaffolding protein, p62/SQSTM1, is involved in regulating various processes including autophagy. It also serves as an essential adaptor in delivering specific organelles to autophagosomes. These processes are crucial to cell metabolism and are associated with cardiometabolic disorders. To better understand the role of SQSTM1, Boster Bio has developed antibodies that recognize its target.
The protein p62/SQSTM1 is composed of multiple distinct domains. The most prominent domains are the N-terminal PB1 (Phox/Bem1p), ZZ-type zinc finger (ZF) domain, TNF receptor-associated factor 6 (TRAF6)-binding sequence, microtubule-associated protein light chain 3 interacting region, and ubiquitin-associated domain.
Dual regulation of protein localization via acetylation/oxidation has important implications on the regulation of autophagy. Increased oxidation and reduced NAD cause impaired autophagy, which ultimately helps to maintain cellular homeostasis as well as healthy ageing. SQSTM1 may play a role in regulating oxidative stress within cells.
SQSTM1 and CCL2 are related in chemoresistance. CCL2 and SQSTM1 expression levels were associated in primary stomach carcinoma tissues, and higher levels of these proteins was associated to shorter overall survival and the rate of relapse-free survival. These results suggest that CCL2 and SQSTM1 contribute to the development and progression of drug resistance.
Boster Bio has created a variety of biological assays using antibodies against Sequestosome-1. The antibodies can be monoclonal or polyclonal and they cross-react with animal specimens. The SQSTM1 marker has been found to react with WDFY3, a receptor for the autophagy pathway that is involved in cytoplasmic ubiquitin-containing inclusions.
The SQSTM1 marker can be utilized in a variety of fields of science and biomedicine. It can be used to study particles or cells. Boster provides primary antibodies that can be used to determine SQSTM1 and are highly specific for residues 360 - 38 of the human SQSTM/p62. The SQSTM1 marker is highly regarded as a marker of sensitivity, selectivity, and sensitivity, and Boster continues to improve their SQSTM1 immunoassay kit.
The HDAC6 enzyme is a type II histone deacetylase with tubulin deacetylase activities. It is localized at subcellular structures that are dynamic and its activity is not linked to the polarity of lymphocytes. Overexpression of HDAC6 increased the rate of lymphocyte migration, mediated by chemokines as well as transendothelial mobility in shear flow. Likewise, knockdown decreased chemotaxis in T cells.
AKT is expressed in high levels in cancer cells. Class III lysine -deacetylases that belong to the sirtuin gene families are able to remove the reversible modifications. In other types of cells however, the activity of AKT is controlled by the extent of its acetylation. HDAC6 is one of the members of this family and regulates AKT Kinase activity.
HDAC1 suppresses AR activity in the PSA promoter. It also regulates AR activity indirectly. Its activity is in turn regulated by the presence of HDAC1 and HDAC2.
Carbocisteine is a natural substance that is present in the human body, is just one example. It has a significant influence on the HDAC2 activity. It improves HDAC2 deacetylase in human epithelial cells. The mechanism that carbocisteine works is not understood. In the meantime, it is possible to reverse the downregulation of HDAC2 in COPD. In addition, it increases the susceptibility of human alveolar epithelial cells towards glucocorticoid treatment.
SQSTM1 is an elongation protein that interacts with various proteins which include RIP1 PCK lambda/octa and PCK kinase. The protein is believed to be involved in autophagy, the process of destroying unwanted molecules within cells. A lot of these diseases are also associated with the SQSTM1 gene.
SQSTM1 is located on chromosomes 5q35 and has 8 exons that code. The entire codon was sequenced in 546 patients with ALS as well as 340 patients with FALS and 206 patients suffering from SALS. Researchers identified a mutation in SQSTM1 that was not present in 724 healthy controls. The SQSTM1 gene is widely multimorphic, and mutations are linked to a number of disease states.
There are many diseases and aging issues that are linked to the SQSTM1 gene. SQSTM1 is a major regulator of the cytosolic response. It creates aggresome-like structures that contain ubiquitinated proteins and heat shock proteins. UFM1 knockout cells also produce other ubiquitin-binding cargo receptors. SQSTM1 could also inhibit autophagy , reducing the efficiency of the other autophagy cargo receivers.
SQSTM1 is a protein from the human body that plays an important role in the autophagy pathway. The protein is found in the cytoplasm as well as the nucleus but also in autophagosomes as well as Lysosomes. It has multiple domains and forms oligomers together with the PB1domain. SQSTM1 is a part of cell biology and may regulate the signaling pathways.
Numerous studies have shown that neurodegeneration as well as cancer, metabolic disorders, and abnormal Sequestosome-1 function are all linked to Sequestosome-1 dysfunction. Genetic mutations in this protein are also linked to frontotemporal lobar degeneration, Paget's Disease of the bone, and autophagy. This protein also plays a role in autophagy through binding to ubiquitin-containing proteins.
To determine SQSTM1 Antibodies against PA1955 that recognize human SQSTM1 were employed. These antibodies were used to perform immunocytochemical staining on cells of A549. The primary antibody (PA1955) was used to do immunocytochemistry. The secondary antibody, DyLight!AE488-conjugated goat anti-rabbit IgG, was incubated with the sample for 30 minutes at 37!C. The image was examined under an optical microscope that was fluorescence, and then visualized using appropriate filters.
PMID: 8551575 by Devergne O., et al. A novel interleukin-12 p40-related protein induced by latent Epstein- Barr virus infection in B lymphocytes.
PMID: 8650207 by Joung I., et al. Molecular cloning of a phosphotyrosine-independent ligand of the p56lck SH2 domain.
*More publications can be found for each product on its corresponding product page