rupintrivir ag7088 Search Results


ag7088 rupintrivir  (MedChemExpress)
92
MedChemExpress ag7088 rupintrivir
Ag7088 Rupintrivir, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/ag7088 rupintrivir/product/MedChemExpress
Average 92 stars, based on 1 article reviews
ag7088 rupintrivir - by Bioz Stars, 2026-02
92/100 stars
  Buy from Supplier
rupintrivir  (TargetMol)
94
TargetMol rupintrivir
(A) Wild-type or mutant 3C or 3CD protease was expressed in HEK293T cells. The expression of each 3C protease was detected with fluorescent microscopy using a FLAG antibody. (B) Wild-type or mutant 3C or 3CD protease was transfected along with flipGFP (3B/3C). The fluorescent signals were detected using microscopy at 24 h post-transfection. (C) Wilde-type or mutant 3C or 3CD protease was transfected along with flipGFP (3B/3C). The fluorescent intensity was calculated 24 h post-transfection. (D) Wild-type or mutant 3C or 3CD protease was transfected along with flipGFP (VP2/VP3). The fluorescent signals were detected using microscopy at 24 h post-transfection. (E) Wild-type or mutant 3C or 3CD protease was transfected along with flipGFP (VP2/VP3). The fluorescent intensity was calculated 24 h post-transfection. (F) HEK293T cells transfected with the expression vector of 3C protease and flipGFP (3B/3C) were treated with <t>rupintrivir</t> at concentrations of 0.01, 0.03, 0.1, or 0.3 µM. The fluorescent signals were detected using microscopy at 24 h post-transfection. (G) HEK293T cells transfected with the expression vector of 3C protease and flipGFP (3B/3C) were treated with rupintrivir at concentrations of 0.01, 0.03, 0.1, or 0.3 µM. The fluorescent intensity was calculated 24 h post-transfection. (H) HEK293T cells transfected with the expression vector of 3C protease and flipGFP (VP2/VP3) were treated with rupintrivir at concentrations of 0.01, 0.03, 0.1, or 0.3 µM. The fluorescent signals were detected using microscopy at 24 h post-transfection. (I) HEK293T cells transfected with the expression vector of 3C protease and flipGFP (VP2/VP3) were treated with rupintrivir at concentrations of 0.01, 0.03, 0.1, or 0.3 µM. The fluorescent intensity was calculated 24 h post-transfection. The data presented in A-I are representative of two independent experiments. For the experiments presented in C, E, G, and I, significance was determined using a one-way ANOVA test (n = 3) (**P ≤ 0.01; ****P ≤ 0.00001; n.s., not significant).
Rupintrivir, supplied by TargetMol, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/rupintrivir/product/TargetMol
Average 94 stars, based on 1 article reviews
rupintrivir - by Bioz Stars, 2026-02
94/100 stars
  Buy from Supplier

Image Search Results


(A) Wild-type or mutant 3C or 3CD protease was expressed in HEK293T cells. The expression of each 3C protease was detected with fluorescent microscopy using a FLAG antibody. (B) Wild-type or mutant 3C or 3CD protease was transfected along with flipGFP (3B/3C). The fluorescent signals were detected using microscopy at 24 h post-transfection. (C) Wilde-type or mutant 3C or 3CD protease was transfected along with flipGFP (3B/3C). The fluorescent intensity was calculated 24 h post-transfection. (D) Wild-type or mutant 3C or 3CD protease was transfected along with flipGFP (VP2/VP3). The fluorescent signals were detected using microscopy at 24 h post-transfection. (E) Wild-type or mutant 3C or 3CD protease was transfected along with flipGFP (VP2/VP3). The fluorescent intensity was calculated 24 h post-transfection. (F) HEK293T cells transfected with the expression vector of 3C protease and flipGFP (3B/3C) were treated with rupintrivir at concentrations of 0.01, 0.03, 0.1, or 0.3 µM. The fluorescent signals were detected using microscopy at 24 h post-transfection. (G) HEK293T cells transfected with the expression vector of 3C protease and flipGFP (3B/3C) were treated with rupintrivir at concentrations of 0.01, 0.03, 0.1, or 0.3 µM. The fluorescent intensity was calculated 24 h post-transfection. (H) HEK293T cells transfected with the expression vector of 3C protease and flipGFP (VP2/VP3) were treated with rupintrivir at concentrations of 0.01, 0.03, 0.1, or 0.3 µM. The fluorescent signals were detected using microscopy at 24 h post-transfection. (I) HEK293T cells transfected with the expression vector of 3C protease and flipGFP (VP2/VP3) were treated with rupintrivir at concentrations of 0.01, 0.03, 0.1, or 0.3 µM. The fluorescent intensity was calculated 24 h post-transfection. The data presented in A-I are representative of two independent experiments. For the experiments presented in C, E, G, and I, significance was determined using a one-way ANOVA test (n = 3) (**P ≤ 0.01; ****P ≤ 0.00001; n.s., not significant).

Journal: bioRxiv

Article Title: Establishment of a green fluorescent protein (GFP)-based reporter for picornaviral 3C proteases

doi: 10.1101/2025.07.31.667855

Figure Lengend Snippet: (A) Wild-type or mutant 3C or 3CD protease was expressed in HEK293T cells. The expression of each 3C protease was detected with fluorescent microscopy using a FLAG antibody. (B) Wild-type or mutant 3C or 3CD protease was transfected along with flipGFP (3B/3C). The fluorescent signals were detected using microscopy at 24 h post-transfection. (C) Wilde-type or mutant 3C or 3CD protease was transfected along with flipGFP (3B/3C). The fluorescent intensity was calculated 24 h post-transfection. (D) Wild-type or mutant 3C or 3CD protease was transfected along with flipGFP (VP2/VP3). The fluorescent signals were detected using microscopy at 24 h post-transfection. (E) Wild-type or mutant 3C or 3CD protease was transfected along with flipGFP (VP2/VP3). The fluorescent intensity was calculated 24 h post-transfection. (F) HEK293T cells transfected with the expression vector of 3C protease and flipGFP (3B/3C) were treated with rupintrivir at concentrations of 0.01, 0.03, 0.1, or 0.3 µM. The fluorescent signals were detected using microscopy at 24 h post-transfection. (G) HEK293T cells transfected with the expression vector of 3C protease and flipGFP (3B/3C) were treated with rupintrivir at concentrations of 0.01, 0.03, 0.1, or 0.3 µM. The fluorescent intensity was calculated 24 h post-transfection. (H) HEK293T cells transfected with the expression vector of 3C protease and flipGFP (VP2/VP3) were treated with rupintrivir at concentrations of 0.01, 0.03, 0.1, or 0.3 µM. The fluorescent signals were detected using microscopy at 24 h post-transfection. (I) HEK293T cells transfected with the expression vector of 3C protease and flipGFP (VP2/VP3) were treated with rupintrivir at concentrations of 0.01, 0.03, 0.1, or 0.3 µM. The fluorescent intensity was calculated 24 h post-transfection. The data presented in A-I are representative of two independent experiments. For the experiments presented in C, E, G, and I, significance was determined using a one-way ANOVA test (n = 3) (**P ≤ 0.01; ****P ≤ 0.00001; n.s., not significant).

Article Snippet: The following antibodies and reagents were used in this study: Enterovirus 71 3C antibody (GTX132357; GeneTex), anti-FLAG M2-Peroxidase (HRP) monoclonal antibody produced in mouse (A8592; Merck), Anti-Strep-tag II mAb (M211-3; MBL), Anti-DDDDK-tag mAb-Alexa FluorTM 594 (M185-A59, MBL), anti-β-Actin monoclonal antibody produced in mouse (A2228; Merck), Peroxidase AffiniPure Goat anti-mouse IgG (H+L) (115-035-003; Jackson Immuno Research Laboratories, Inc.), Peroxidase AffiniPure Goat anti-Rabbit IgG (H+L) (111-035-003; Jackson Immuno Research Laboratories, Inc.), and Rupintrivir (T16809; TargetMol).

Techniques: Mutagenesis, Expressing, Microscopy, Transfection, Plasmid Preparation

(A) Phylogenetic tree of 3C protease derived from human and animal picornaviruses (i.e., human (EV- A71, CVB3, PV1, or EV-D68), bats (BatPicoV1, BatPicoV2, or BatPicoV3), primates (EVJ1 or EV125), or rodents (NX2015 or Tibet2015). The amino acid sequence of each picornaviral 3C protease was aligned by Clustal Omega (EMBL-EBI) and indicated using Jalview software version 2.11.4.1 . (B) The accession number of the picornavirus used in this study, the information on the reservoir, and the corresponding amino acid sequence between the 3B and 3C regions. (C) The protease cleavage sequence presented in (animal picornaviruses) was analyzed and visualized using WebLogo Version 2.8.2. (D) The protease cleavage sequence presented in (human picornaviruses) was analyzed and visualized using WebLogo Version 2.8.2. (E) The FLAG-tagged picornaviral 3C proteases were expressed in HEK293T cells. The expression of each 3C protease was detected with fluorescent microscopy using a FLAG antibody. (F) HEK293T cells were transfected with the plasmid encoding 3C protease and the flipGFP optimized for each 3C protease. The fluorescent signal of flipGFP was monitored with fluorescent microscopy. (G) HEK293T cells were transfected with the plasmid encoding 3C protease derived from bats, primates, or rodents, and the flipGFP optimized for each 3C protease. The fluorescent intensity was calculated 24 h post-transfection. (H) HEK293T cells transfected with the expression vector of 3C protease and flipGFP were treated with rupintrivir at concentrations of 0.01, 0.03, 0.1, or 0.3 µM. The fluorescent intensity was calculated 24 h post- transfection. The data presented in E-H are representative of two independent experiments. For the experiment presented in G, significance was determined using Student’s t -test (n = 3) (**P ≤ 0.01; ***P ≤ 0.001; ****P ≤ 0.00001). For the experiment presented in H, significance was determined using one-way ANOVA test (n = 3) (*P ≤ 0.05; **P ≤ 0.01; ****P ≤ 0.00001; n.s., not significant).

Journal: bioRxiv

Article Title: Establishment of a green fluorescent protein (GFP)-based reporter for picornaviral 3C proteases

doi: 10.1101/2025.07.31.667855

Figure Lengend Snippet: (A) Phylogenetic tree of 3C protease derived from human and animal picornaviruses (i.e., human (EV- A71, CVB3, PV1, or EV-D68), bats (BatPicoV1, BatPicoV2, or BatPicoV3), primates (EVJ1 or EV125), or rodents (NX2015 or Tibet2015). The amino acid sequence of each picornaviral 3C protease was aligned by Clustal Omega (EMBL-EBI) and indicated using Jalview software version 2.11.4.1 . (B) The accession number of the picornavirus used in this study, the information on the reservoir, and the corresponding amino acid sequence between the 3B and 3C regions. (C) The protease cleavage sequence presented in (animal picornaviruses) was analyzed and visualized using WebLogo Version 2.8.2. (D) The protease cleavage sequence presented in (human picornaviruses) was analyzed and visualized using WebLogo Version 2.8.2. (E) The FLAG-tagged picornaviral 3C proteases were expressed in HEK293T cells. The expression of each 3C protease was detected with fluorescent microscopy using a FLAG antibody. (F) HEK293T cells were transfected with the plasmid encoding 3C protease and the flipGFP optimized for each 3C protease. The fluorescent signal of flipGFP was monitored with fluorescent microscopy. (G) HEK293T cells were transfected with the plasmid encoding 3C protease derived from bats, primates, or rodents, and the flipGFP optimized for each 3C protease. The fluorescent intensity was calculated 24 h post-transfection. (H) HEK293T cells transfected with the expression vector of 3C protease and flipGFP were treated with rupintrivir at concentrations of 0.01, 0.03, 0.1, or 0.3 µM. The fluorescent intensity was calculated 24 h post- transfection. The data presented in E-H are representative of two independent experiments. For the experiment presented in G, significance was determined using Student’s t -test (n = 3) (**P ≤ 0.01; ***P ≤ 0.001; ****P ≤ 0.00001). For the experiment presented in H, significance was determined using one-way ANOVA test (n = 3) (*P ≤ 0.05; **P ≤ 0.01; ****P ≤ 0.00001; n.s., not significant).

Article Snippet: The following antibodies and reagents were used in this study: Enterovirus 71 3C antibody (GTX132357; GeneTex), anti-FLAG M2-Peroxidase (HRP) monoclonal antibody produced in mouse (A8592; Merck), Anti-Strep-tag II mAb (M211-3; MBL), Anti-DDDDK-tag mAb-Alexa FluorTM 594 (M185-A59, MBL), anti-β-Actin monoclonal antibody produced in mouse (A2228; Merck), Peroxidase AffiniPure Goat anti-mouse IgG (H+L) (115-035-003; Jackson Immuno Research Laboratories, Inc.), Peroxidase AffiniPure Goat anti-Rabbit IgG (H+L) (111-035-003; Jackson Immuno Research Laboratories, Inc.), and Rupintrivir (T16809; TargetMol).

Techniques: Derivative Assay, Sequencing, Software, Expressing, Microscopy, Transfection, Plasmid Preparation