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Bio-Rad sheep anti tgn46

TZM-bl cells were transfected with a plasmid coding for indicated HA-GBP5 species proteins: 10 bat orthologs, and 2 human GBP5s: wt and mutant C583A. Two days post-transfection, GBP5 localization was analyzed by confocal fluorescence microscopy with the indicated marker. Nuclei and trans- Golgi-network (TGN) were stained with DAPI and <t>anti-TGN46,</t> respectively. A, All the channels and a zoom are shown for Homo sapiens , the mutant Homo sapiens-C583A, Myotis yumanensis and Eptesicus fuscus . B, Only the merge is shown for the remaining bat species. The complete panel is shown in . The pictures present representative results observed in 3 independent experiments. Scale bar indicates 15 μm.

Sheep Anti Tgn46, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 746 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/anti+tgn46/pmc13128109-306-19-22?v=Bio-Rad
Average 96 stars, based on 746 article reviews

sheep anti tgn46 - by Bioz Stars, 2026-07

96/100 stars

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1) Product Images from "Genomic and functional adaptations in the guanylate-binding protein GBP5 highlight specificities of bat antiviral innate immunity"

Article Title: Genomic and functional adaptations in the guanylate-binding protein GBP5 highlight specificities of bat antiviral innate immunity

Journal: PLOS Biology

doi: 10.1371/journal.pbio.3003760

Figure Legend Snippet: TZM-bl cells were transfected with a plasmid coding for indicated HA-GBP5 species proteins: 10 bat orthologs, and 2 human GBP5s: wt and mutant C583A. Two days post-transfection, GBP5 localization was analyzed by confocal fluorescence microscopy with the indicated marker. Nuclei and trans- Golgi-network (TGN) were stained with DAPI and anti-TGN46, respectively. A, All the channels and a zoom are shown for Homo sapiens , the mutant Homo sapiens-C583A, Myotis yumanensis and Eptesicus fuscus . B, Only the merge is shown for the remaining bat species. The complete panel is shown in . The pictures present representative results observed in 3 independent experiments. Scale bar indicates 15 μm.

Techniques Used: Transfection, Plasmid Preparation, Mutagenesis, Fluorescence, Microscopy, Marker, Staining

A, Ancestral state sequence reconstruction upstream of the Eptesicus fuscus- CaaX prenylation motif. C-terminal end of the protein alignment of the 10 bat GBP5s tested in functional assays (asterisk, stop codon). Phylogenetic tree was used to infer the ancestral sequence of the C-terminal region, the branch where the prenylation motif was lost by a premature stop codon is annotated on the tree. The site of mutagenesis for reconstruction is indicated by the blue arrow. B, Reconstruction of the C-ter relocalizes Eptesicus fuscus GBP5-CaaX to the trans- Golgi network (TGN). Briefly, TZM-bl cells were transfected with plasmids encoding HA-GBP5s and, 48 hour later, were analyzed by confocal fluorescence microscopy. GBP5, nuclei and TGN were stained with anti-HA, DAPI and anti-TGN46 antibodies, respectively. Scale bar indicates 15 μm. C, GBP5 mean intensity at the Golgi vs. the total cell was quantified for the wild-type eptFus and the mutant eptFus-CaaX . Each dot corresponds to one cell. Two independent replicates are identified by different dot colors. D, Pearson coefficient correlation per cell calculated between GBP5 and TGN signals for the wild-type eptFus and the mutant eptFus-CaaX. Data are represented as a mean ± SD. Statistics vs. the corresponding control condition, Nested t test: **, p -value < 0.01 ( n = 2). E–G, Ancestral reconstruction of the prenylation CaaX did not increase Eptesicus fuscus GBP5 restriction of intrinsic viral infectivity. E, Infectivity of RT-normalized HIV-1 pseudotyped-viruses in the presence of GBP5, normalized to the condition without GBP5 (EV control) at 100%. Dose of GBP5 plasmids: 1, 2, and 4 µg with constant total DNA transfected across conditions. Experimental setup as in . RLU, Relative light units. Viral titers (RT activity) are shown in . F, Corresponding western blot showing the expression of HA-GBP5, HIV-1 Env and Gag in the viral producer Tzm-bl cells with beta-actin as loading control (kDa, on the right). Quantification of three independent experiments is shown in . G, Intrinsic infectivity of (RT-normalized) VSVg or EBLV-1g pseudotyped retroviruses in the presence of GBP5s, normalized to EV control at 100%. Experimental setup as in .**, p -value < 0.01 (versus control). The data underlying this Figure can be found in .

Figure Legend Snippet: A, Ancestral state sequence reconstruction upstream of the Eptesicus fuscus- CaaX prenylation motif. C-terminal end of the protein alignment of the 10 bat GBP5s tested in functional assays (asterisk, stop codon). Phylogenetic tree was used to infer the ancestral sequence of the C-terminal region, the branch where the prenylation motif was lost by a premature stop codon is annotated on the tree. The site of mutagenesis for reconstruction is indicated by the blue arrow. B, Reconstruction of the C-ter relocalizes Eptesicus fuscus GBP5-CaaX to the trans- Golgi network (TGN). Briefly, TZM-bl cells were transfected with plasmids encoding HA-GBP5s and, 48 hour later, were analyzed by confocal fluorescence microscopy. GBP5, nuclei and TGN were stained with anti-HA, DAPI and anti-TGN46 antibodies, respectively. Scale bar indicates 15 μm. C, GBP5 mean intensity at the Golgi vs. the total cell was quantified for the wild-type eptFus and the mutant eptFus-CaaX . Each dot corresponds to one cell. Two independent replicates are identified by different dot colors. D, Pearson coefficient correlation per cell calculated between GBP5 and TGN signals for the wild-type eptFus and the mutant eptFus-CaaX. Data are represented as a mean ± SD. Statistics vs. the corresponding control condition, Nested t test: **, p -value < 0.01 ( n = 2). E–G, Ancestral reconstruction of the prenylation CaaX did not increase Eptesicus fuscus GBP5 restriction of intrinsic viral infectivity. E, Infectivity of RT-normalized HIV-1 pseudotyped-viruses in the presence of GBP5, normalized to the condition without GBP5 (EV control) at 100%. Dose of GBP5 plasmids: 1, 2, and 4 µg with constant total DNA transfected across conditions. Experimental setup as in . RLU, Relative light units. Viral titers (RT activity) are shown in . F, Corresponding western blot showing the expression of HA-GBP5, HIV-1 Env and Gag in the viral producer Tzm-bl cells with beta-actin as loading control (kDa, on the right). Quantification of three independent experiments is shown in . G, Intrinsic infectivity of (RT-normalized) VSVg or EBLV-1g pseudotyped retroviruses in the presence of GBP5s, normalized to EV control at 100%. Experimental setup as in .**, p -value < 0.01 (versus control). The data underlying this Figure can be found in .

Techniques Used: Sequencing, Functional Assay, Mutagenesis, Transfection, Fluorescence, Microscopy, Staining, Control, Infection, Activity Assay, Western Blot, Expressing

A, Eptesicus fuscus cells were transfected with plasmids encoding HA-GBP5s and, 48 hours later, were analyzed by confocal fluorescence microscopy with anti-HA antibody. Nuclei were stained with DAPI. Of note, anti-TGN46 antibody did not cross-react in bat cells. MyoYum GBP5 was also transfected as a control of TGN subcellular localization. B and C, VSV-GFP infections of eptFus bat cells expressing or not GBP5s: total % of cell death (B) and % of VSV-GFP infected live cells as measured by flow-cytometry. Each point corresponds to an independent replicate. D, 3D protein structure prediction (AlphaFold) of the reconstructed Eptesicus fuscus - CaaX GBP5 dimer. Colored and gray chains each correspond to a monomer. Blue, GTPase domain. Green, hinge domain. Yellow, middle domain. Orange, catalytic domain. Red, residues different from Myotis yumanensis . Credit: https://www.phylopic.org/ . The data underlying this Figure can be found in .

Figure Legend Snippet: A, Eptesicus fuscus cells were transfected with plasmids encoding HA-GBP5s and, 48 hours later, were analyzed by confocal fluorescence microscopy with anti-HA antibody. Nuclei were stained with DAPI. Of note, anti-TGN46 antibody did not cross-react in bat cells. MyoYum GBP5 was also transfected as a control of TGN subcellular localization. B and C, VSV-GFP infections of eptFus bat cells expressing or not GBP5s: total % of cell death (B) and % of VSV-GFP infected live cells as measured by flow-cytometry. Each point corresponds to an independent replicate. D, 3D protein structure prediction (AlphaFold) of the reconstructed Eptesicus fuscus - CaaX GBP5 dimer. Colored and gray chains each correspond to a monomer. Blue, GTPase domain. Green, hinge domain. Yellow, middle domain. Orange, catalytic domain. Red, residues different from Myotis yumanensis . Credit: https://www.phylopic.org/ . The data underlying this Figure can be found in .

Techniques Used: Transfection, Fluorescence, Microscopy, Staining, Control, Expressing, Infection, Flow Cytometry

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Journal: PLOS Biology

Article Title: Genomic and functional adaptations in the guanylate-binding protein GBP5 highlight specificities of bat antiviral innate immunity

doi: 10.1371/journal.pbio.3003760

Figure Lengend Snippet: TZM-bl cells were transfected with a plasmid coding for indicated HA-GBP5 species proteins: 10 bat orthologs, and 2 human GBP5s: wt and mutant C583A. Two days post-transfection, GBP5 localization was analyzed by confocal fluorescence microscopy with the indicated marker. Nuclei and trans- Golgi-network (TGN) were stained with DAPI and anti-TGN46, respectively. A, All the channels and a zoom are shown for Homo sapiens , the mutant Homo sapiens-C583A, Myotis yumanensis and Eptesicus fuscus . B, Only the merge is shown for the remaining bat species. The complete panel is shown in . The pictures present representative results observed in 3 independent experiments. Scale bar indicates 15 μm.

Article Snippet: Primary antibody incubation was carried out for 1 hour at RT with rabbit anti-HA (1:500, Sigma, cat. H6908) and sheep anti-TGN46 (1:500, Biorad, cat.AHP500GT; not cross-reacting in bat cells) to label respectively HA-GBP5 proteins and the TGN.

Techniques: Transfection, Plasmid Preparation, Mutagenesis, Fluorescence, Microscopy, Marker, Staining

Journal: PLOS Biology

Article Title: Genomic and functional adaptations in the guanylate-binding protein GBP5 highlight specificities of bat antiviral innate immunity

doi: 10.1371/journal.pbio.3003760

Figure Lengend Snippet: A, Ancestral state sequence reconstruction upstream of the Eptesicus fuscus- CaaX prenylation motif. C-terminal end of the protein alignment of the 10 bat GBP5s tested in functional assays (asterisk, stop codon). Phylogenetic tree was used to infer the ancestral sequence of the C-terminal region, the branch where the prenylation motif was lost by a premature stop codon is annotated on the tree. The site of mutagenesis for reconstruction is indicated by the blue arrow. B, Reconstruction of the C-ter relocalizes Eptesicus fuscus GBP5-CaaX to the trans- Golgi network (TGN). Briefly, TZM-bl cells were transfected with plasmids encoding HA-GBP5s and, 48 hour later, were analyzed by confocal fluorescence microscopy. GBP5, nuclei and TGN were stained with anti-HA, DAPI and anti-TGN46 antibodies, respectively. Scale bar indicates 15 μm. C, GBP5 mean intensity at the Golgi vs. the total cell was quantified for the wild-type eptFus and the mutant eptFus-CaaX . Each dot corresponds to one cell. Two independent replicates are identified by different dot colors. D, Pearson coefficient correlation per cell calculated between GBP5 and TGN signals for the wild-type eptFus and the mutant eptFus-CaaX. Data are represented as a mean ± SD. Statistics vs. the corresponding control condition, Nested t test: **, p -value < 0.01 ( n = 2). E–G, Ancestral reconstruction of the prenylation CaaX did not increase Eptesicus fuscus GBP5 restriction of intrinsic viral infectivity. E, Infectivity of RT-normalized HIV-1 pseudotyped-viruses in the presence of GBP5, normalized to the condition without GBP5 (EV control) at 100%. Dose of GBP5 plasmids: 1, 2, and 4 µg with constant total DNA transfected across conditions. Experimental setup as in . RLU, Relative light units. Viral titers (RT activity) are shown in . F, Corresponding western blot showing the expression of HA-GBP5, HIV-1 Env and Gag in the viral producer Tzm-bl cells with beta-actin as loading control (kDa, on the right). Quantification of three independent experiments is shown in . G, Intrinsic infectivity of (RT-normalized) VSVg or EBLV-1g pseudotyped retroviruses in the presence of GBP5s, normalized to EV control at 100%. Experimental setup as in .**, p -value < 0.01 (versus control). The data underlying this Figure can be found in .

Techniques: Sequencing, Functional Assay, Mutagenesis, Transfection, Fluorescence, Microscopy, Staining, Control, Infection, Activity Assay, Western Blot, Expressing

Journal: PLOS Biology

Article Title: Genomic and functional adaptations in the guanylate-binding protein GBP5 highlight specificities of bat antiviral innate immunity

doi: 10.1371/journal.pbio.3003760

Figure Lengend Snippet: A, Eptesicus fuscus cells were transfected with plasmids encoding HA-GBP5s and, 48 hours later, were analyzed by confocal fluorescence microscopy with anti-HA antibody. Nuclei were stained with DAPI. Of note, anti-TGN46 antibody did not cross-react in bat cells. MyoYum GBP5 was also transfected as a control of TGN subcellular localization. B and C, VSV-GFP infections of eptFus bat cells expressing or not GBP5s: total % of cell death (B) and % of VSV-GFP infected live cells as measured by flow-cytometry. Each point corresponds to an independent replicate. D, 3D protein structure prediction (AlphaFold) of the reconstructed Eptesicus fuscus - CaaX GBP5 dimer. Colored and gray chains each correspond to a monomer. Blue, GTPase domain. Green, hinge domain. Yellow, middle domain. Orange, catalytic domain. Red, residues different from Myotis yumanensis . Credit: https://www.phylopic.org/ . The data underlying this Figure can be found in .

Techniques: Transfection, Fluorescence, Microscopy, Staining, Control, Expressing, Infection, Flow Cytometry

ELAPOR1 was required for recruitment of clathrin onto the pro-AVs. ( A ) Schematic diagrams of flag tagged recombinant ELAPOR1. ( B ) Representative co-immunoprecipitation of recombinant ELAPOR1 with clathrin, AP1, AP2 and AP3 in HEK-293T cells. Western blot analysis showed the interaction between ELAPOR1 and clathrin as well as APs, while the relative targets detected on cell lyses were performed as loading control. ( C ) Immunofluorescent co-staining of clathrin (red) and TGN46 (green, trans-TGN marker) in spermatids. The Elapor1 cKO spermatids displayed rare co-localization of clathrin and TGN46. The arrow indicates the acrosome. Scale bar = 10 μm. ( D ) The localization of clathrin on pro-AVs analyzed by IEM showed that clathrin localized on the surface of most pro-AVs situated between the Golgi apparatus and the acrosome in normal spermatids, whereas clathrin on the pro-AVs disappeared when Elapor1 deficiency. G, Golgi apparatus; A, Acrosome; pre-A, Preacrosomal granules; red arrows, immunogold labelled clathrin. Scale bars in low-magnification = 200 nm, in high-magnification = 100 nm

Journal: Cellular and Molecular Life Sciences: CMLS

Article Title: ELAPOR1 mediated vesicle traffic is required for acrosome biogenesis and male fertility in mice

doi: 10.1007/s00018-026-06125-0

Figure Lengend Snippet: ELAPOR1 was required for recruitment of clathrin onto the pro-AVs. ( A ) Schematic diagrams of flag tagged recombinant ELAPOR1. ( B ) Representative co-immunoprecipitation of recombinant ELAPOR1 with clathrin, AP1, AP2 and AP3 in HEK-293T cells. Western blot analysis showed the interaction between ELAPOR1 and clathrin as well as APs, while the relative targets detected on cell lyses were performed as loading control. ( C ) Immunofluorescent co-staining of clathrin (red) and TGN46 (green, trans-TGN marker) in spermatids. The Elapor1 cKO spermatids displayed rare co-localization of clathrin and TGN46. The arrow indicates the acrosome. Scale bar = 10 μm. ( D ) The localization of clathrin on pro-AVs analyzed by IEM showed that clathrin localized on the surface of most pro-AVs situated between the Golgi apparatus and the acrosome in normal spermatids, whereas clathrin on the pro-AVs disappeared when Elapor1 deficiency. G, Golgi apparatus; A, Acrosome; pre-A, Preacrosomal granules; red arrows, immunogold labelled clathrin. Scale bars in low-magnification = 200 nm, in high-magnification = 100 nm

Article Snippet: The unspecific binding sites were blocked with 5% goat serum in PBS and then incubated overnight at 4 °C with the primary antibodies against Elapor1 (1:200 dilution), ACRV1 (1:200 dilution, #14040-1-AP, Proteintech), GM130 (1:1000 dilution, #610822, BD Biosciences), Clathrin (1:200 dilution, #26523-1-AP, Proteintech), and TGN46 (1:200 dilution, #66477-1-Ig, Proteintech), respectively.

Techniques: Recombinant, Immunoprecipitation, Western Blot, Control, Staining, Marker

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