SQSTM1 polyclonal antibody
- Known as:
- SQSTM1 pab (anti-)
- Catalog number:
- PAB1750
- Product Quantity:
- 100 ug
- Category:
- -
- Supplier:
- Abno
- Gene target:
- SQSTM1 polyclonal antibody
Related genes to: SQSTM1 polyclonal antibody
- Gene:
- SQSTM1 NIH gene
- Name:
- sequestosome 1
- Previous symbol:
- PDB3, OSIL
- Synonyms:
- p62, p60, p62B, A170
- Chromosome:
- 5q35.3
- Locus Type:
- gene with protein product
- Date approved:
- 2000-06-13
- Date modifiied:
- 2019-03-07
Related products to: SQSTM1 polyclonal antibody
Related articles to: SQSTM1 polyclonal antibody
- Mcl1 is a major driver of therapeutic resistance across hematologic malignancies, but direct Mcl1 inhibition has been limited by on-target cardiotoxicity. Here, building on our development of an Mcl1-targeting autophagy-targeting chimera (AUTAC), we show that AUTAC-mediated degradation creates a tumor-selective therapeutic window that spares the heart. AUTAC induced robust cytotoxicity and Mcl1 degradation in multiple myeloma models, while showing minimal toxicity in cardiac cell lines, primary cardiomyocytes, and murine heart tissue. , AUTAC reduced tumor Mcl1 without measurably affecting cardiac Mcl1. Mechanistically, this selectivity was associated with lower expression of the p62/SQSTM1, TRAF6, and UBC13 machinery required for AUTAC activity in cardiac cells, together with lower intracellular AUTAC accumulation relative to tumor cells. AUTAC also enhanced the antitumor activity of carfilzomib and venetoclax, including in resistant models, without worsening cardiotoxicity or promoting cardiac Mcl1 loss. Compared with classical Mcl1 inhibitors, AUTAC caused markedly less cardiomyocyte death, mitochondrial depolarization, and apoptotic signaling. These findings identify AUTAC-mediated Mcl1 degradation as a cardiac-sparing strategy to target an otherwise clinically constrained vulnerability and support tumor-selective lysosomal degradation as a path to safer Mcl1-directed therapy. - Source: PubMed
Publication date: 2026/06/24
Elshazly Ahmed MVangala Janakiram RMauro Adolfo GSalloum Fadi NRadhakrishnan Senthil K - Herpes simplex virus 1 (HSV-1) is a globally prevalent pathogen that poses a significant health threat due to its lifelong latency. This persistence is driven by intricate immune evasion mechanisms, the deciphering of which remains a challenge. Here, we identified the HSV-1 tegument protein UL16 as a novel viral immunosuppressive factor, which significantly suppresses the RIGI-like receptor (RLR)-mediated antiviral immunity. We found that UL16 can interact with MAVS (mitochondrial antiviral signaling protein) and induce its degradation, thereby inhibiting type I interferon (IFN-I) production. Further investigation revealed that UL16-induced MAVS degradation was facilitated via mitophagy involving the mitochondrial cargo receptor FUNDC1 (FUN14 domain containing 1). Knockout of expression completely disrupted UL16-induced MAVS degradation and restricted HSV-1 replication. In contrast, overexpression of FUNDC1 augmented the suppressive effect of UL16 on MAVS-triggered IFN-I signaling and consequently benefited viral replication. Notably, the C-terminal domain (CTD) of UL16 primarily accounted for its immunosuppressive function, which was also demonstrated to be essential for UL16 engagement with MAVS, FUNDC1 and MAP1LC3/LC3 (microtubule associated protein 1 light chain 3). A conserved LC3-interacting region (LIR) motif within the UL16 CTD was identified to play a critical role in LC3 recruitment enhancement. Furthermore, the UL16-deficient HSV-1 exhibited markedly attenuated viral infectivity and pathogenicity . In summary, our findings uncover a previously uncharacterized pathway through which HSV-1 UL16 subverts host immunity by inducing mitophagy. This study provides critical insights into host-pathogen interactions and establishes a rational foundation for developing novel therapeutics against HSV-1 infection.:3-MA: 3-methyladenine; BNIP3L/NIX: BCL2 interacting protein 3 like; BSA: bovine serum albumin; CALCOCO2/NDP52: calcium binding and coiled-coil domain 2; CARD: caspase recruitment domain; Cas9: CRISPR-associated system 9; CGAS: cyclic GMP-AMP synthase; co-IP: co-immunoprecipitation; COX8: cytochrome c oxidase subunit 8; CQ: chloroquine; CRISPR: clustered regulatory interspaced short palindromic repeat; CTD: C-terminal domain; Ctrl: control; CXCL10: C-X-C motif chemokine ligand 10; DAPI: 4,'6-diamidino-2-phenylindole; DMEM: Dulbecco's modified Eagle's medium; DMSO: dimethyl sulfoxide; ds: double-stranded; FBS: fetal bovine serum; FUNDC1: FUN14 domain containing 1; GAPDH: glyceraldehyde-3-phosphate dehydrogenase; GFP: green fluorescent protein; HEK: human embryonic kidney; HSV-1: herpes simplex virus 1; IAV: influenza A virus; IFIH1/MDA5: interferon induced with helicase C domain 1; IFIT1/ISG56: interferon induced protein with tetratricopeptide repeats 1; IFN-I: type I interferon; IgG: Immunoglobulin G; IRF3: interferon regulatory factor 3; ISGs: IFN-stimulated genes; kDa: kilodalton; KO: knockout; KSHV: Kaposi sarcoma-associated herpesvirus; LIR: LC3-interacting region; MAP1LC3/LC3: microtubule associated protein 1 light chain 3; MAVS: mitochondrial antiviral signaling protein; Mdivi-1: mitochondrial division inhibitor 1; MG132: cbz-leu-leu-leucinal; MOI: multiplicity of infection; NanoBiT: NanoLuc Binary Technology; NC: negative control; NTD: N-terminal domain; OPTN: optineurin; p-: phosphorylated; PFU: plaque-forming unit; PINK1: PTEN induced kinase 1; poly(I:C): polyinosinic-polycytidylic acid; PRKN/parkin: parkin RBR E3 ubiquitin protein ligase; qPCR: quantitative polymerase chain reaction; RIGI/RIG-I: RNA sensor RIG-I; RLR: RIGI-like receptor; SARS-CoV-2: severe acute respiratory syndrome coronavirus 2; SeV: Sendai virus; sgRNA: single guide RNA; shRNA: short hairpin RNA; SQSTM1/p62: sequestosome 1; STING1: stimulator of interferon response cGAMP interactor 1; TBK1: TANK binding kinase 1; TM: transmembrane; TOMM20: translocase of outer mitochondrial membrane 20; TRAF: TNF receptor associated factor; TUFM: Tu translation elongation factor, mitochondrial; UL16: unique long region 16; VSV: vesicular stomatitis virus; VZV: varicella zoster virus; WCL: whole-cell lysate; WT: wild-type; Z-VAD-FMK: carbobenzoxy-valyl-alanyl-aspartyl-[O-methyl]-fluoromethylketone. - Source: PubMed
Publication date: 2026/07/02
Wang JingwenZhu RongliYi PingGan MengyaoLong Feng - The incidence of inflammatory bowel disease (IBD) has been demonstrated to be increased over recent decades. Butyrate derived from the gut microbiota is known to be beneficial in alleviating inflammation, yet the underlying mechanisms remain undefined. - Source: PubMed
Publication date: 2026/06/17
Mao QingyiLin BeibeiZhang WenluoZhang YuLei YueZhang ZhouXu Mengque - To investigate the mechanism by which SHP2 influences ferroptosis through the regulation of signaling pathways, thereby impacting hepatocellular carcinoma. Integrate bulk RNA-seq and single-cell transcriptomic data to identify differentially expressed genes and analyze cellular heterogeneity, pseudotemporal trajectories, and cell-cell communication networks. In vitro experiments involved treating HepG2, Huh7, and Hep3B cells with the SHP2 inhibitor (PHPS1), the CREB agonist (AE-18), the EZH2 inhibitor (IN-14), and the FOXO1 inhibitor (AS1842856). Western blot analysis was performed for P-SHP2, P-PI3K, nuclear P-CREB, nuclear EZH2, nuclear FOXO1, GPX4, Nur77, NCOA4, LC-3B, and SQSTM1; immunofluorescence was used to detect the localization and intensity of nuclear FOXO1 and nuclear CREB; biochemical colorimetric assays were used to measure Fe⁺, ROS, and oxidative stress markers; flow cytometry was used to detect apoptosis; CCK-8 assay for proliferation; Scratch and Transwell assays for migration and invasion. SHP2 resists ferroptosis in hepatocellular carcinoma by regulating the CREB/EZH2/FOXO1 signaling pathway, thereby modulating the protein expression of autophagy/NCOA4/GPX4. Integrated bulk RNA-seq and single-cell transcriptomic analyses further revealed that SHP2-mediated transcriptional reprogramming and altered cellular communication within the HCC microenvironment jointly promote resistance to ferroptosis. - Source: PubMed
Publication date: 2026/07/01
Yu GuodongHan JijingKang RanYang JihongCui Yong - SQSTM1 is one of the causative genes of neurodegenerative disorders, amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). The SQSTM1 protein regulates the degradation of polyubiquitinated proteins and autophagosome formation through its interaction with microtubule-associated protein light chain 3 (MAP1LC3/LC3). However, the molecular mechanisms by which SQSTM1-LC3 binding regulates the autophagy-endolysosomal system (APELS) remain unclear. To elucidate the spatiotemporal role of SQSTM1, we transiently expressed wild-type SQSTM1 or missense mutants carrying mutations in the LC3-interacting region (LIR), fused with the photoconvertible fluorescent protein Dendra2. Live-cell fluorescence imaging and co-localization analyses with markers of the APELS were then performed. Particle analysis of photoconverted or non-photoconverted SQSTM1-positive structures in live cells revealed that the pathogenic L341V variant formed larger structures than the wild-type. Co-localization analyses further showed that both the L341V and artificial LIR3A mutants accumulated in large ubiquitin-positive structures, likely due to impaired localization to autophagosomes. These results suggest that mutations within the LIR differentially affect autophagosome formation and cargo degradation within APELS-related compartments, highlighting the importance of SQSTM1 structural integrity in ALS/FTD pathogenesis. - Source: PubMed
Shimakura KentoOka AkiraYudahira HarukaHama YutaroOtomo AsakoHadano Shinji