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anti asc antibody  (Proteintech)


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    Structured Review

    Proteintech anti asc antibody
    Anti Asc Antibody, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 62 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/trip4/TRIP4+Antibody/pmc12781742-73-38-40
    Average 93 stars, based on 62 article reviews
    anti asc antibody - by Bioz Stars, 2026-10
    93/100 stars

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    Proximity Ligation Assay:

    Article Title: The Ski2 helicase ASCC3 unwinds DNA upon fork stalling to control replication stress responses
    Article Snippet: Drugs used were aphidicolin (Sigma); camptothecin (Sigma); hydroxyurea (BioShop Canada); RAD52 inhibitor (AICAR, Cayman Chemical); REV1 inhibitor JH-RE-06 (SML2993, Sigma); RO-3306 (Selleck Chemicals). .. Antibodies used include: ASCC2 (1:1000; A304-020A, Bethyl Laboratories); ASCC2 (1:5000; 1152-1-AP, Proteintech); ASCC3 (1:400; 17627-1-AP, Proteintech); ASCC3 (1:1000; PA5-56794, Invitrogen); Biotin (1:100000; A150-109A, Bethyl Laboratory); Biotin (1:100000; 200-002-211, Jackson ImmunoResearch); BrdU (1:100; 347580, BD Biosciences); BrdU (1:500; MAB3222, Millipore); BrdU (BU1/75 [ICR1]) (1:800; NB500-169, Novus Biologicals); 53BP1 (1:2000; 612522, BD Biosciences); BRCA1 (1:5000; 07-434, Millipore); BRCA2 (1:2000; 29450-1-AP, Proteintech); CHK1 (1:250; sc-7898, Santa cruz); CHK1-pS345 (1:1000; 2348S, Cell Signaling); CSB (1:200; ab66598, Abcam); FASN (1:20000; 10624-2-AP, Proteintech); GFP (1:1000; 50430-2-AP, Proteintech); HA (1:500; #2367, Cell Signaling); HLTF (1:1000; A300-229A, Bethyl Laboratory); Myc (1:1000; 9E10, Calbiochem); PCNA (1:2000; sc-56, Santa Cruz); PCNA (1:600 for PLA or 1:4000 for western blot; 10205-2-AP, Proteintech); Ubiquityl-PCNA (K164) (1:1000; 13439T, Cell Signaling); PRIMPOL (1:1000; 29824-1-AP, Proteintech); RAD51 (1:2000, ab63801, Abcam); RFWD3 (1:1000; 19893-1-AP, Proteintech); RPA32 (1:10000; NB100-332, Novus Biologicals); RPA32 (1:200; ab2175, Abcam); RPA32-pS33 (1:50000; A300-246A, Bethyl Laboratories); RPA70 (1:2000; 2267S, Cell Signaling); SHPRH (21995-1-AP, Proteintech); SMARCAL1 (1:100, sc-166209, Santa cruz); SMARCAL1 (1:2000; GTX109468, GenTex); TRIP4 (1:1000; 12324-1-AP, Proteintech); α-tubulin (1:20,000; T9026, Sigma); γ-tubulin (1:20,000; GTU88, Sigma). ..

    Western Blot:

    Article Title: The Ski2 helicase ASCC3 unwinds DNA upon fork stalling to control replication stress responses
    Article Snippet: Drugs used were aphidicolin (Sigma); camptothecin (Sigma); hydroxyurea (BioShop Canada); RAD52 inhibitor (AICAR, Cayman Chemical); REV1 inhibitor JH-RE-06 (SML2993, Sigma); RO-3306 (Selleck Chemicals). .. Antibodies used include: ASCC2 (1:1000; A304-020A, Bethyl Laboratories); ASCC2 (1:5000; 1152-1-AP, Proteintech); ASCC3 (1:400; 17627-1-AP, Proteintech); ASCC3 (1:1000; PA5-56794, Invitrogen); Biotin (1:100000; A150-109A, Bethyl Laboratory); Biotin (1:100000; 200-002-211, Jackson ImmunoResearch); BrdU (1:100; 347580, BD Biosciences); BrdU (1:500; MAB3222, Millipore); BrdU (BU1/75 [ICR1]) (1:800; NB500-169, Novus Biologicals); 53BP1 (1:2000; 612522, BD Biosciences); BRCA1 (1:5000; 07-434, Millipore); BRCA2 (1:2000; 29450-1-AP, Proteintech); CHK1 (1:250; sc-7898, Santa cruz); CHK1-pS345 (1:1000; 2348S, Cell Signaling); CSB (1:200; ab66598, Abcam); FASN (1:20000; 10624-2-AP, Proteintech); GFP (1:1000; 50430-2-AP, Proteintech); HA (1:500; #2367, Cell Signaling); HLTF (1:1000; A300-229A, Bethyl Laboratory); Myc (1:1000; 9E10, Calbiochem); PCNA (1:2000; sc-56, Santa Cruz); PCNA (1:600 for PLA or 1:4000 for western blot; 10205-2-AP, Proteintech); Ubiquityl-PCNA (K164) (1:1000; 13439T, Cell Signaling); PRIMPOL (1:1000; 29824-1-AP, Proteintech); RAD51 (1:2000, ab63801, Abcam); RFWD3 (1:1000; 19893-1-AP, Proteintech); RPA32 (1:10000; NB100-332, Novus Biologicals); RPA32 (1:200; ab2175, Abcam); RPA32-pS33 (1:50000; A300-246A, Bethyl Laboratories); RPA70 (1:2000; 2267S, Cell Signaling); SHPRH (21995-1-AP, Proteintech); SMARCAL1 (1:100, sc-166209, Santa cruz); SMARCAL1 (1:2000; GTX109468, GenTex); TRIP4 (1:1000; 12324-1-AP, Proteintech); α-tubulin (1:20,000; T9026, Sigma); γ-tubulin (1:20,000; GTU88, Sigma). ..



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    Anti Asc Antibody, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    MED8 regulates EMT through <t>TRIP4.</t> (A) MED8 interaction network from STRING website. (B) Mass spectrum showing unique peptides of TRIP4 identified by 2D-LC-MS/MS from protein lysates prepared from MHCC97H/SR cells after silencing MED8. (C–E) Representative western blot analysis of MED8 and TRIP4 protein expression in HCC and paired paracancerous tissues (n = 40, T, tumour; NT, non-tumour tissue). (F) Scatter plots showing a positive correlation between MED8 and TRIP4 protein expression levels in 40 HCC samples (n = 40, r = 0.3167, p = 0.0002, Pearson test). (G–I) Western blot analyses were used to detect MED8 and TRIP4 protein expression in cells stably transfected with the shMED8 or pcDNA-MED8 plasmid. (J, K) Western blot analysis confirming MED8 silencing and TRIP4 restoration and their effects on EMT-related biomarkers. (L) Western blot analysis showing the levels of MED8 overexpression and TRIP4 inhibition and their effects on EMT-related biomarkers.
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    MED8 regulates EMT through <t>TRIP4.</t> (A) MED8 interaction network from STRING website. (B) Mass spectrum showing unique peptides of TRIP4 identified by 2D-LC-MS/MS from protein lysates prepared from MHCC97H/SR cells after silencing MED8. (C–E) Representative western blot analysis of MED8 and TRIP4 protein expression in HCC and paired paracancerous tissues (n = 40, T, tumour; NT, non-tumour tissue). (F) Scatter plots showing a positive correlation between MED8 and TRIP4 protein expression levels in 40 HCC samples (n = 40, r = 0.3167, p = 0.0002, Pearson test). (G–I) Western blot analyses were used to detect MED8 and TRIP4 protein expression in cells stably transfected with the shMED8 or pcDNA-MED8 plasmid. (J, K) Western blot analysis confirming MED8 silencing and TRIP4 restoration and their effects on EMT-related biomarkers. (L) Western blot analysis showing the levels of MED8 overexpression and TRIP4 inhibition and their effects on EMT-related biomarkers.
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    anti apoptosis associated speck like protein  (Proteintech)
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    MED8 regulates EMT through <t>TRIP4.</t> (A) MED8 interaction network from STRING website. (B) Mass spectrum showing unique peptides of TRIP4 identified by 2D-LC-MS/MS from protein lysates prepared from MHCC97H/SR cells after silencing MED8. (C–E) Representative western blot analysis of MED8 and TRIP4 protein expression in HCC and paired paracancerous tissues (n = 40, T, tumour; NT, non-tumour tissue). (F) Scatter plots showing a positive correlation between MED8 and TRIP4 protein expression levels in 40 HCC samples (n = 40, r = 0.3167, p = 0.0002, Pearson test). (G–I) Western blot analyses were used to detect MED8 and TRIP4 protein expression in cells stably transfected with the shMED8 or pcDNA-MED8 plasmid. (J, K) Western blot analysis confirming MED8 silencing and TRIP4 restoration and their effects on EMT-related biomarkers. (L) Western blot analysis showing the levels of MED8 overexpression and TRIP4 inhibition and their effects on EMT-related biomarkers.
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    Image Search Results


    MED8 regulates EMT through TRIP4. (A) MED8 interaction network from STRING website. (B) Mass spectrum showing unique peptides of TRIP4 identified by 2D-LC-MS/MS from protein lysates prepared from MHCC97H/SR cells after silencing MED8. (C–E) Representative western blot analysis of MED8 and TRIP4 protein expression in HCC and paired paracancerous tissues (n = 40, T, tumour; NT, non-tumour tissue). (F) Scatter plots showing a positive correlation between MED8 and TRIP4 protein expression levels in 40 HCC samples (n = 40, r = 0.3167, p = 0.0002, Pearson test). (G–I) Western blot analyses were used to detect MED8 and TRIP4 protein expression in cells stably transfected with the shMED8 or pcDNA-MED8 plasmid. (J, K) Western blot analysis confirming MED8 silencing and TRIP4 restoration and their effects on EMT-related biomarkers. (L) Western blot analysis showing the levels of MED8 overexpression and TRIP4 inhibition and their effects on EMT-related biomarkers.

    Journal: Journal of Enzyme Inhibition and Medicinal Chemistry

    Article Title: Targeting MED8 enhances sorafenib sensitivity in hepatocellular carcinoma by disrupting epithelial–mesenchymal transition mechanisms

    doi: 10.1080/14756366.2025.2574988

    Figure Lengend Snippet: MED8 regulates EMT through TRIP4. (A) MED8 interaction network from STRING website. (B) Mass spectrum showing unique peptides of TRIP4 identified by 2D-LC-MS/MS from protein lysates prepared from MHCC97H/SR cells after silencing MED8. (C–E) Representative western blot analysis of MED8 and TRIP4 protein expression in HCC and paired paracancerous tissues (n = 40, T, tumour; NT, non-tumour tissue). (F) Scatter plots showing a positive correlation between MED8 and TRIP4 protein expression levels in 40 HCC samples (n = 40, r = 0.3167, p = 0.0002, Pearson test). (G–I) Western blot analyses were used to detect MED8 and TRIP4 protein expression in cells stably transfected with the shMED8 or pcDNA-MED8 plasmid. (J, K) Western blot analysis confirming MED8 silencing and TRIP4 restoration and their effects on EMT-related biomarkers. (L) Western blot analysis showing the levels of MED8 overexpression and TRIP4 inhibition and their effects on EMT-related biomarkers.

    Article Snippet: Sangon Biotech (Shanghai, China) synthesised shRNA-mediated RNA duplexes targeting MED8 and TRIP4.

    Techniques: Liquid Chromatography with Mass Spectroscopy, Western Blot, Expressing, Stable Transfection, Transfection, Plasmid Preparation, Over Expression, Inhibition

    MED8 interacts with TRIP4. (A) qRT-PCR analysis of MED8 and TRIP4 mRNA expression in HCC/SR. Left, HCCLM03/SR and MHCC97H/SR cells transfected with either shNC or shMED8. Right, HepG2/SR cells transfected with either vector or pcDNA-MED8. Data represent the mean ± SD of triplicate experiments and were statistically analysed with Student’s t-test; ns, not significant, **p < 0.01. (B) MHCC97H/SR and HCCLM03/SR cells were fixed and stained using TRIP4 (green) and MED8 (red) antibodies. Cell nuclei were stained using DAPI (blue). (C) Co-IP test was implemented to identify the protein binding of MED8 and TRIP4 in MHCC97H/SR cells. (D) Top ranked docking conformations and 3D structures of TRIP4 and MED8. TRIP4 and MED8 are displayed in cyan and green, respectively. (E) Diagram of TRIP4 truncated mutant constructs. (F) The N-terminal domain and the ASCH domain within the C-terminal region of TRIP4 interact with MED8. Mapping the TRIP4 domain that interacts with MED8. Constructs for MYC-tagged TRIP4 (full-length or truncated mutants) and FLAG-tagged MED8 were cotransfected into MHCC97H/SR cells. IP was performed using anti-MYC antibodies, and precipitates and input were analysed by western blotting with antibodies to FLAG and MYC.

    Journal: Journal of Enzyme Inhibition and Medicinal Chemistry

    Article Title: Targeting MED8 enhances sorafenib sensitivity in hepatocellular carcinoma by disrupting epithelial–mesenchymal transition mechanisms

    doi: 10.1080/14756366.2025.2574988

    Figure Lengend Snippet: MED8 interacts with TRIP4. (A) qRT-PCR analysis of MED8 and TRIP4 mRNA expression in HCC/SR. Left, HCCLM03/SR and MHCC97H/SR cells transfected with either shNC or shMED8. Right, HepG2/SR cells transfected with either vector or pcDNA-MED8. Data represent the mean ± SD of triplicate experiments and were statistically analysed with Student’s t-test; ns, not significant, **p < 0.01. (B) MHCC97H/SR and HCCLM03/SR cells were fixed and stained using TRIP4 (green) and MED8 (red) antibodies. Cell nuclei were stained using DAPI (blue). (C) Co-IP test was implemented to identify the protein binding of MED8 and TRIP4 in MHCC97H/SR cells. (D) Top ranked docking conformations and 3D structures of TRIP4 and MED8. TRIP4 and MED8 are displayed in cyan and green, respectively. (E) Diagram of TRIP4 truncated mutant constructs. (F) The N-terminal domain and the ASCH domain within the C-terminal region of TRIP4 interact with MED8. Mapping the TRIP4 domain that interacts with MED8. Constructs for MYC-tagged TRIP4 (full-length or truncated mutants) and FLAG-tagged MED8 were cotransfected into MHCC97H/SR cells. IP was performed using anti-MYC antibodies, and precipitates and input were analysed by western blotting with antibodies to FLAG and MYC.

    Article Snippet: Sangon Biotech (Shanghai, China) synthesised shRNA-mediated RNA duplexes targeting MED8 and TRIP4.

    Techniques: Quantitative RT-PCR, Expressing, Transfection, Plasmid Preparation, Staining, Co-Immunoprecipitation Assay, Protein Binding, Mutagenesis, Construct, Western Blot

    MED8 stabilises TRIP4 protein expression by suppressing its ubiquitination and degradation. (A–C) TRIP4 protein levels at various times were measured by western blotting after MG132 addition (10 µM) to MHCC97H/SR, HCCLM03/SR, and HepG2/SR cells. (D–F) Western blot analysis of TRIP4 and MED8 protein expression in MHCC97H/SR and HCCLM03/SR cells transfected with shMED8-1# or shNC and HepG2/SR cells transfected with pcDNA-MED8 or control vector, with or without treatment with 10 µM MG132. (G–I) MHCC97H/SR and HCCLM03/SR cells transfected with shMED8-1# or shNC and HepG2/SR cells transfected with pcDNA-MED8 or control vector were subjected to treatment with 20 µg/mL CHX, followed by assessment of TRIP4 protein levels using western blotting. n = 3, **p < 0.01. (J–L) MHCC97H/SR, HCCLM03/SR, and HepG2/SR cells were treated with either shMED8-1# or pcDNA-MED8 for 72 hours, and intracellular proteasome activity was assessed using a proteasome activity fluorometric assay kit. The relative proteolytic activities are presented as average percentages of the total fluorescence intensity of the control group at the end of the assay. Data are shown as mean ± SD, n = 5, with statistical analysis performed using a two-sided Student’s t-test; ns, not significant. (M–O) Lysates of MHCC97H/SR, HCCLM03/SR, and HepG2/SR cells transfected with sh-MED8-1#, FLAG-MED8, and MYC-ubiquitin (MYC-Ub) were analysed by immunoblotting and then immunoprecipitated using anti-TRIP4, followed by probing with anti-MYC.

    Journal: Journal of Enzyme Inhibition and Medicinal Chemistry

    Article Title: Targeting MED8 enhances sorafenib sensitivity in hepatocellular carcinoma by disrupting epithelial–mesenchymal transition mechanisms

    doi: 10.1080/14756366.2025.2574988

    Figure Lengend Snippet: MED8 stabilises TRIP4 protein expression by suppressing its ubiquitination and degradation. (A–C) TRIP4 protein levels at various times were measured by western blotting after MG132 addition (10 µM) to MHCC97H/SR, HCCLM03/SR, and HepG2/SR cells. (D–F) Western blot analysis of TRIP4 and MED8 protein expression in MHCC97H/SR and HCCLM03/SR cells transfected with shMED8-1# or shNC and HepG2/SR cells transfected with pcDNA-MED8 or control vector, with or without treatment with 10 µM MG132. (G–I) MHCC97H/SR and HCCLM03/SR cells transfected with shMED8-1# or shNC and HepG2/SR cells transfected with pcDNA-MED8 or control vector were subjected to treatment with 20 µg/mL CHX, followed by assessment of TRIP4 protein levels using western blotting. n = 3, **p < 0.01. (J–L) MHCC97H/SR, HCCLM03/SR, and HepG2/SR cells were treated with either shMED8-1# or pcDNA-MED8 for 72 hours, and intracellular proteasome activity was assessed using a proteasome activity fluorometric assay kit. The relative proteolytic activities are presented as average percentages of the total fluorescence intensity of the control group at the end of the assay. Data are shown as mean ± SD, n = 5, with statistical analysis performed using a two-sided Student’s t-test; ns, not significant. (M–O) Lysates of MHCC97H/SR, HCCLM03/SR, and HepG2/SR cells transfected with sh-MED8-1#, FLAG-MED8, and MYC-ubiquitin (MYC-Ub) were analysed by immunoblotting and then immunoprecipitated using anti-TRIP4, followed by probing with anti-MYC.

    Article Snippet: Sangon Biotech (Shanghai, China) synthesised shRNA-mediated RNA duplexes targeting MED8 and TRIP4.

    Techniques: Expressing, Ubiquitin Proteomics, Western Blot, Transfection, Control, Plasmid Preparation, Activity Assay, Fluorescence, Immunoprecipitation

    Diagram of the regulatory mechanism of MED8 promoting sorafenib resistance in HCC. This is a proposed model by which MED8 inhibits the ubiquitination and degradation of TRIP4, thereby regulating its protein abundance, promoting EMT, and ultimately leading to sorafenib resistance in HCC cells.

    Journal: Journal of Enzyme Inhibition and Medicinal Chemistry

    Article Title: Targeting MED8 enhances sorafenib sensitivity in hepatocellular carcinoma by disrupting epithelial–mesenchymal transition mechanisms

    doi: 10.1080/14756366.2025.2574988

    Figure Lengend Snippet: Diagram of the regulatory mechanism of MED8 promoting sorafenib resistance in HCC. This is a proposed model by which MED8 inhibits the ubiquitination and degradation of TRIP4, thereby regulating its protein abundance, promoting EMT, and ultimately leading to sorafenib resistance in HCC cells.

    Article Snippet: Sangon Biotech (Shanghai, China) synthesised shRNA-mediated RNA duplexes targeting MED8 and TRIP4.

    Techniques: Ubiquitin Proteomics, Quantitative Proteomics