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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 741 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/ahp500/pmc13128109-306-19-22?v=Bio-Rad
Average 96 stars, based on 741 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

(A) mKate2-FM4-HA transport from the ER to the PM via the Golgi complex in HA-HeLa cells. A high magnification of the boxed area is shown in the inset where brightness/contrast enhancement was applied. (B) Colocalization of mKate2-FM4-HA with the ER maker calnexin (0 min) and the TGN maker TGN46 (25 min) in permeabilized HA-HeLa cells and visualization of extracellularly located mKate2 (50 min) by labelling of non-permeabilized HA-HeLa cells with anti-mKate2 antibody. (C) Distribution of HA carriers, clathrin-coated vesicles (labeled with anti-clathrin HC and anti – ψ-adaptin antibodies), COPI-coated vesicles (labeled with an anti – β-COP antibody), and COPII-coated vesicles (labeled with an anti-Sec31 antibody) in HA-HeLa cells. (D and E) Colocalization of HA carriers and EQ-SM in HA-HeLa cells. (E) Quantification of the mKate-FM4-HA–positive HA carriers containing EQ-SM (magenta) and EQ-SM–positive carriers containing mKate-FM4-HA (green). Boxes delimit the first and third quartiles, and the central line is the median. The whiskers represent the minimum and maximum values (mKate-FM4-HA positive: n = 1,631 puncta; EQ-SM positive: n = 4,055 puncta in 20 cells; ****, P < 0.0001; paired two-tailed Student’s t test). (F and G) Colocalization of HA carriers with GFP-Rab6a and GFP-Rab8a, but not with GFP-Rab11a, in HeLa cells. (G) Quantification of the mKate-FM4-HA–positive HA carriers containing Rab6a-GFP, Rab8a-GFP, or Rab11a-GFP. Data are means ± SEM (Rab6a, mKate-FM4-HA positive: n = 1,574 puncta and Rab6a-GFP positive: n = 2,756 puncta in 15 cells; Rab8a, mKate-FM4-HA positive: n = 2,144 puncta and Rab8a-GFP positive: n = 6,340 puncta in 15 cells; Rab11a, mKate-FM4-HA positive: n = 1,974 puncta and Rab11a-GFP positive: n = 5,740 puncta in 15 cells; ****, P < 0.0001; one-way ANOVA multiple comparison test). (H and I) Distribution of HA carriers and CARTS in HeLa cells stably expressing PAUF-MycHis. (I) Quantification of the mKate-FM4-HA–positive HA carriers containing PAUF-MycHis (blue) and mKate-FM4-PAUF–positive CARTS containing PAUF-MycHis (red). Boxes delimit the first and third quartiles, and the central line is the median. The whiskers represent the minimum and maximum values (blue, mKate-FM4-HA positive: n = 829 puncta and PAUF-MycHis positive: n = 870 puncta in 15 cells; red, mKate-FM4-PAUF positive: n = 461 puncta and PAUF-MycHis positive: n = 603 puncta in 15 cells; ****, P < 0.0001; paired two-tailed Student’s t test). High magnifications of the boxed areas are shown in the insets. Scale bars, 10 μm (large panels), 5 μm (insets).

Journal: bioRxiv

Article Title: A PKD-caveolin axis drives secretory carrier biogenesis at the TGN

doi: 10.64898/2026.01.13.699385

Figure Lengend Snippet: (A) mKate2-FM4-HA transport from the ER to the PM via the Golgi complex in HA-HeLa cells. A high magnification of the boxed area is shown in the inset where brightness/contrast enhancement was applied. (B) Colocalization of mKate2-FM4-HA with the ER maker calnexin (0 min) and the TGN maker TGN46 (25 min) in permeabilized HA-HeLa cells and visualization of extracellularly located mKate2 (50 min) by labelling of non-permeabilized HA-HeLa cells with anti-mKate2 antibody. (C) Distribution of HA carriers, clathrin-coated vesicles (labeled with anti-clathrin HC and anti – ψ-adaptin antibodies), COPI-coated vesicles (labeled with an anti – β-COP antibody), and COPII-coated vesicles (labeled with an anti-Sec31 antibody) in HA-HeLa cells. (D and E) Colocalization of HA carriers and EQ-SM in HA-HeLa cells. (E) Quantification of the mKate-FM4-HA–positive HA carriers containing EQ-SM (magenta) and EQ-SM–positive carriers containing mKate-FM4-HA (green). Boxes delimit the first and third quartiles, and the central line is the median. The whiskers represent the minimum and maximum values (mKate-FM4-HA positive: n = 1,631 puncta; EQ-SM positive: n = 4,055 puncta in 20 cells; ****, P < 0.0001; paired two-tailed Student’s t test). (F and G) Colocalization of HA carriers with GFP-Rab6a and GFP-Rab8a, but not with GFP-Rab11a, in HeLa cells. (G) Quantification of the mKate-FM4-HA–positive HA carriers containing Rab6a-GFP, Rab8a-GFP, or Rab11a-GFP. Data are means ± SEM (Rab6a, mKate-FM4-HA positive: n = 1,574 puncta and Rab6a-GFP positive: n = 2,756 puncta in 15 cells; Rab8a, mKate-FM4-HA positive: n = 2,144 puncta and Rab8a-GFP positive: n = 6,340 puncta in 15 cells; Rab11a, mKate-FM4-HA positive: n = 1,974 puncta and Rab11a-GFP positive: n = 5,740 puncta in 15 cells; ****, P < 0.0001; one-way ANOVA multiple comparison test). (H and I) Distribution of HA carriers and CARTS in HeLa cells stably expressing PAUF-MycHis. (I) Quantification of the mKate-FM4-HA–positive HA carriers containing PAUF-MycHis (blue) and mKate-FM4-PAUF–positive CARTS containing PAUF-MycHis (red). Boxes delimit the first and third quartiles, and the central line is the median. The whiskers represent the minimum and maximum values (blue, mKate-FM4-HA positive: n = 829 puncta and PAUF-MycHis positive: n = 870 puncta in 15 cells; red, mKate-FM4-PAUF positive: n = 461 puncta and PAUF-MycHis positive: n = 603 puncta in 15 cells; ****, P < 0.0001; paired two-tailed Student’s t test). High magnifications of the boxed areas are shown in the insets. Scale bars, 10 μm (large panels), 5 μm (insets).

Article Snippet: Polyclonal antibodies were procured as follows: Clathrin HC (sc-6579) and GST (sc-459) from Santa Cruz Biotechnology; ZO-1 (21773-1-AP) and CAV1 (16447-1-AP) from Proteintech; TGN46 (AHP500GT) from AbD Serotec; tRFP (mKate2; AB233) from evrogen; CAV2 (GTX108294) from GeneTex.

Techniques: Labeling, Two Tailed Test, Comparison, Stable Transfection, Expressing

(A and B) Accumulation of HA-mEGFP at the Golgi complex upon PKD2 knockdown in HeLa Tet-On HA-mEGFP cells. Merged images of HA-mEGFP (green) and the TGN maker TGN46 (magenta) in the boxed areas are shown in the insets. Scale bars, 10 μm (large panels), 5 μm (insets). (B) Quantification of the HA-mEGFP distribution between the PM and the Golgi complex. The ratio of fluorescence intensity of HA-mEGFP in the PM and the Golgi complex, normalized as the values in control cells, is shown. Boxes delimit the first and third quartiles, and the central line is the median, whereas the cross represents the mean value. The whiskers represent the minimum and maximum values (control [Cont] siRNA: n = 95 cells; PKD2 siRNA [882]: n = 90 cells; PKD2 siRNA [1303]: n = 78 cells; ****, P < 0.0001; one-way ANOVA multiple comparison test).

Journal: bioRxiv

Article Title: A PKD-caveolin axis drives secretory carrier biogenesis at the TGN

doi: 10.64898/2026.01.13.699385

Figure Lengend Snippet: (A and B) Accumulation of HA-mEGFP at the Golgi complex upon PKD2 knockdown in HeLa Tet-On HA-mEGFP cells. Merged images of HA-mEGFP (green) and the TGN maker TGN46 (magenta) in the boxed areas are shown in the insets. Scale bars, 10 μm (large panels), 5 μm (insets). (B) Quantification of the HA-mEGFP distribution between the PM and the Golgi complex. The ratio of fluorescence intensity of HA-mEGFP in the PM and the Golgi complex, normalized as the values in control cells, is shown. Boxes delimit the first and third quartiles, and the central line is the median, whereas the cross represents the mean value. The whiskers represent the minimum and maximum values (control [Cont] siRNA: n = 95 cells; PKD2 siRNA [882]: n = 90 cells; PKD2 siRNA [1303]: n = 78 cells; ****, P < 0.0001; one-way ANOVA multiple comparison test).

Techniques: Knockdown, Fluorescence, Control, Comparison

(A) 3D super-resolution microscopic images of HA-HeLa cells expressing GST-PKD2 KD at 30 min after transport initiation. (B) 3D super-resolution microscopic images of HeLa cells expressing GST-PKD2 KD alone. Maximum intensity merges of z-stack images are shown. High magnifications of the boxed areas are shown in the right of each panels. Arrows indicate GST-PKD2 KD- and TGN46-containing long tubules extended from the TGN. N, nucleus. Scale bars, 10 μm (left panels), 5 μm (right panels).

Journal: bioRxiv

Article Title: A PKD-caveolin axis drives secretory carrier biogenesis at the TGN

doi: 10.64898/2026.01.13.699385

Figure Lengend Snippet: (A) 3D super-resolution microscopic images of HA-HeLa cells expressing GST-PKD2 KD at 30 min after transport initiation. (B) 3D super-resolution microscopic images of HeLa cells expressing GST-PKD2 KD alone. Maximum intensity merges of z-stack images are shown. High magnifications of the boxed areas are shown in the right of each panels. Arrows indicate GST-PKD2 KD- and TGN46-containing long tubules extended from the TGN. N, nucleus. Scale bars, 10 μm (left panels), 5 μm (right panels).

Techniques: Expressing

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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"

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