Golga2 monoclonal antibody, clone NN 2C10/1
- Known as:
- Golga2 mab (anti-), clonality NN 2C10/1
- Catalog number:
- MAB7085
- Product Quantity:
- 100 ug
- Category:
- -
- Supplier:
- Abno
- Gene target:
- Golga2 monoclonal antibody clone 2C10/1
Related genes to: Golga2 monoclonal antibody, clone NN 2C10/1
- Gene:
- GOLGA2 NIH gene
- Name:
- golgin A2
- Previous symbol:
- -
- Synonyms:
- GM130, golgin-95
- Chromosome:
- 9q34.11
- Locus Type:
- gene with protein product
- Date approved:
- 1997-11-05
- Date modifiied:
- 2016-10-05
Related products to: Golga2 monoclonal antibody, clone NN 2C10/1
Related articles to: Golga2 monoclonal antibody, clone NN 2C10/1
- The term CASM describes a process in which MAP1LC3B/LC3B and other Atg8-family proteins are covalently ligated to lipids in damaged endomembranes. While CASM is commonly described as a cytoprotective response to multiple types of membrane damage, how CASM helps cells maintain homeostasis is still unclear. Here, we show that CASM maintains Golgi apparatus architecture following the loss of TRIM46, a ubiquitin ligase with roles in microtubule organization. TRIM46 deficient cells were notable for enhanced TFEB-driven lysosomal biogenesis and Golgi ribbon fragmentation, with colocalization of the -Golgi marker TGOLN2 and the Atg8-family proteins LC3B and GABARAP. Further studies revealed that the Golgi Atg8ylation seen in knockout cells was not degradative and mechanistically resembled CASM. Genetic inhibition of CASM in TRIM46 deficient cells reduced TFEB activation and exacerbated the Golgi morphology defects, suggesting that CASM contributes to Golgi repair. Accordingly, Golgi reformation after drug-induced fragmentation was impaired upon knockdown of CASM genes. Together, these studies identify lysosomal biogenesis and CASM as coordinated features of a Golgi damage response, with CASM acting to preserve Golgi integrity. AMPK (AMP-activated protein kinase); ATG3 (autophagy related 3); ATG5 (autophagy related 5); ATG7 (autophagy related 7); ATG12 (autophagy related 12); ATG13 (autophagy related 13); ATG16L1 (autophagy related 16 like 1); BECN1 (beclin 1); CASM, conjugation of Atg8 to single membranes; GABARAP (GABA type A receptor-associated protein); GABARAPL1 (GABA type A receptor associated protein like 1); GABARAPL2 (GABA type A receptor associated protein like 2); GOLGA2 (golgin A2); HT (HaloTag); HL (HaloTag ligand); MAP1LC3A/LC3A (microtubule associated protein 1 light chain 3 alpha); MAP1LC3B/LC3B (microtubule associated protein 1 light chain 3 beta); MAP1LC3C/LC3C (microtubule associated protein 1 light chain 3 gamma); MTORC1 (mechanistic target of rapamycin kinase complex 1); PE (phosphatidylethanolamine); PIK3C3/VPS34 (phosphatidylinositol 3-kinase catalytic subunit type 3); PS (phosphatidylserine); TECPR1 (tectonin beta-propellor repeat containing 1); SQSTM1/p62 (sequestosome 1); TFEB (transcription factor EB); TFE3 (transcription factor binding to IGHM enhancer 3); TGOLN2 (trans-golgi network protein 2); TRIM46 (tripartite motif containing 46); ULK1 (unc-51 like autophagy activating kinase 1); ULK2 (unc-51 like autophagy activating kinase 2): VAIL (V-ATPase-ATG16L1 induced LC3 lipidation). - Source: PubMed
Publication date: 2026/05/18
Oh SeeunUllah SaifSaha BhaskarMandell Michael A - Colorectal cancer still causes many cancer deaths, and patient outcomes differ a lot. The tumor microenvironment can shape tumor growth and treatment response. Autophagy is a cell recycling process linked to tumor survival and immune control, but its cell-type pattern in colorectal cancer tissue and its clinical meaning are not clear. We mapped autophagy activity across cell types, defined autophagy-based subtypes, and tested their value for risk stratification. - Source: PubMed
Publication date: 2026/04/21
Wu YuemingTeng LanZhou LihuaLiu SideGuo Yubin - Ferroptosis, characterized by iron-dependent lipid peroxidation, has emerged as a pivotal cell death pathway in various diseases, yet its regulation during viral infection remains elusive. Here, we reveal that Newcastle disease virus (NDV) exploits the Golgi apparatus as a central hub to orchestrate ferroptotic cell death in tumor cells. NDV infection provokes robust Golgi stress and Golgiphagy, leading to the selective degradation of ARF1 (ARF GTPase 1), a GA-resident regulator of redox homeostasis, which in turn triggers a cascade of reactive oxygen species accumulation, lipid peroxidation, and ferroptosis. Mechanistically, we show that this process is dependent on the activation of the Golgi stress response and macroautophagy/autophagy-lysosome pathway. Importantly, inhibition of Golgi stress by exogenous spermine not only alleviates NDV-induced ferroptosis, but also demonstrates antiviral and cytoprotective effects, underscoring the translational potential of targeting the Golgi stress axis. Our findings uncover a previously unappreciated axis of virus-host interaction centering on Golgi stress and ferroptosis and suggest that modulation of organelle-specific stress responses represents a promising therapeutic strategy in both antiviral and cancer contexts.: AMPK: AMP-activated protein kinase; ARF1: ARF GTPase 1; ARF4: ARF GTPase 4; ATG7: autophagy related 7; BFA: brefeldin A; CGAS: cyclic GMP-AMP synthase; CHX: cycloheximide; CQ: chloroquine; CREB3: cAMP responsive element binding protein 3; DFO: deferoxamine; ER: endoplasmic reticulum; Fe: ferrous ions, GA: Golgi apparatus; GOLGA2/GM130: golgin A2; GPX4: glutathione peroxidase 4; GSH: glutathione; GSR: Golgi stress response; HCMV: human cytomegalovirus; HSV-1: herpes simplex virus 1; Lip-1: Liproxstatin-1; MAP1LC3/LC3: microtubule associated protein 1 light chain 3; MDA: malondialdehyde; mtDNA: mitochondrial DNA; MTOR: mechanistic target of rapamycin kinase; NDV: Newcastle disease virus; NCOA4: nuclear receptor coactivator 4; PUFA: polyunsaturated fatty acid; ROS: reactive oxygen species; Rot: rotenone; SLC7A11: solute carrier family 7 member 11; SERPINH1/HSP47: serpin family H member 1; TFE3: transcription factor binding to IGHM enhancer 3; WT: wild-type. - Source: PubMed
Publication date: 2026/04/10
Kan XianjinYang MengqingXie GuangleiYin YuncongJiang HuiYuan YanmeiSun YingjieDing Chan - During the development of sepsis, aberrant dendritic cell (DC) pyroptosis results in a significant decrease in the numbers of DCs and immune dysfunction. However, the molecular mechanisms regulating DC pyroptosis in sepsis remain unclear. Emerging evidence indicates that RETREG1/FAM134B (reticulophagy regulator 1) is involved in the regulation of programmed cell death to maintain cell viability. Therefore, this study aimed to investigate the potential role and regulatory pathways of RETREG1 in DC death during sepsis. We found that the upregulation of RETREG1 upon septic challenge was intimately associated with the maintenance of immune function. Depletion of RETREG1 in DC significantly aggravated DC pyroptosis and sepsis-induced immune dysfunction by activating the CASP3 (caspase 3)-GSDME (gasdermin E) signaling pathway. Mechanistically, defective RETREG1 expression inhibited autophagic degradation of the endoplasmic reticulum-Golgi intermediate compartment (ERGIC), resulting in abnormal activation of STING1 (stimulator of interferon response cGAMP interactor 1), which further induced CASP3-GSDME-dependent pyroptosis. Genetic downregulation of prevented the activation of STING1 and GSDME-mediated pyroptosis by disturbing ERGIC structure. These results suggest a novel RETREG1-based protective mechanism against DC-mediated immune impairment during sepsis. Genetic or pharmacological modulation of RETREG1 May represent a promising therapeutic strategy for treating sepsis-induced immune suppression.Abbreviations: 7-AAD: 7-aminoactinomycin D; ANXA5/annexin V: annexin A5; ARF1: ARF GTPase 1; ATP: adenosine triphosphate; CALCOCO1: calcium binding and coiled-coil domain 1; CASP1: caspase 1; cC3: cleaved CASP3; CCDC50: coiled-coil domain containing 50; CD274/PD-L1: CD274 molecule; CFSE: carboxyfluorescein diacetate succinimidyl ester; CGAS: cyclic GMP-AMP synthase; CLP: cecal ligation and puncture; DC: dendritic cell; DEGs: differentially expressed genes; DEPs: differently expressed proteins; ER: endoplasmic reticulum; ERGIC: endoplasmic reticulum-Golgi intermediate compartment; GO: Gene Ontology; GOLGA2/GM130: golgin A2; GSDMD: gasdermin D; GSDME: gasdermin E; GSEA: Gene set enrichment analysis; IFN-I: type I interferon; IKK: IκB kinase; IL2: interleukin 2; IRF3: interferon regulatory factor 3; ITGAX/Cd11c: integrin subunit alpha X; KEGG: Kyoto Encyclopedia of Genes and Genomes; LMAN1/ERGIC53: lectin, mannose binding 1; LPS: lipopolysaccharide; MAP1LC3B/LC3B: microtubule associated protein 1 light chain 3 beta; MAP3K7/TAK1: mitogen-activated protein kinase kinase kinase 7; NFKB/NFκB: nuclear factor kappa B; NLRP3: NLR family pyrin domain containing 3; PBMCs: peripheral blood mononuclear cells; PBS: phosphate-buffered saline; PCD: programmed cell death; PINK1: PTEN induced kinase 1; PRKN: parkin RBR E3 ubiquitin protein ligase; PRRs: pattern recognition receptors; PYCARD/ASC: PYD and CARD domain containing; RETREG1/FAM134B: reticulophagy regulator 1; SAMHD1: SAM and HD domain containing deoxynucleoside triphosphate triphosphohydrolase 1; SEC62: SEC62 preprotein translocation factor; SQSTM1/p62: sequestosome 1; STEEP1: STING1 ER exit protein 1; STING1: stimulator of interferon response cGAMP interactor 1; TBK1: TANK binding kinase 1; TGFB/TGFβ: transforming growth factor beta; TMED9: transmembrane p24 trafficking protein 9; TLR4: toll like receptor 4; TNF: tumor necrosis factor; T: regulatory T cells; VAP: VAMP associated protein. - Source: PubMed
Publication date: 2026/03/20
Duan YuHe Peng-YiZhu Cheng-LongLi Jin-RuChen YuZheng Li-YuFan QiLing HuaWang LuWu Meng-YaoHan Ze-XinLi TaoYao Yong-MingDai Xin-GuiYao Ren-Qi - Cellular uptake and intracellular distribution of phosphorothioate-modified antisense oligonucleotides (PS-ASOs) are mediated by protein interactions. While several PS-ASOs-binding proteins have been identified, mainly using gapmer designs with 2'-O-methoxyethyl (2'MOE) modifications, less is known about protein partners of splice-switching oligonucleotides (SSOs) with alternative ribose modifications. Here, using affinity purification mass spectrometry (AP-MS), we identified the intracellular protein partners of PS-SSOs of the same sequence with three distinct ribose modifications: tricyclo-DNA (tcDNA), locked nucleic acid (LNA), and 2'MOE. Interestingly, we found previously reported PS interactors, such as GRSF1, NONO, and NCL, as well as uncharacterized protein partners. Four shared interactors identified in this study, ERC1, SPIRE1, THRAP3, and GOLGA2, were selected based on functional relevance and tested for their impact on exon skipping efficacy using PS-SSOs targeting the human Duchenne muscular dystrophy (DMD) transcript. RNA interference-mediated knockdown of each protein led to a reduction of exon skipping efficiency, suggesting that these proteins may contribute to PS-ASOs activity regardless of their sugar modifications. Overall, our results provide a set of intracellular protein interactors of different PS-ASOs, representing a valuable resource to explore mechanisms underlying their activity and offering potential leads for the optimization of oligonucleotide therapeutics. - Source: PubMed
Publication date: 2026/01/12
Gaci ArisMenchon GrégoryBruce JohannaSalnot VirginiePedeux RémyGoyenvalle Aurélie