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  • 85
    Santa Cruz Biotechnology α rab pab
    α Rab Pab, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 85/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology rabbit polyclonal antibody
    Dtnbp1 mRNA is smaller and dysbindin is undetectable in tissues of sdy mutant mice. ( a ) Genomic PCR. We amplified genomic DNA from control DBA/2J, sdy /+, sdy/sdy and various inbred strains by a duplex PCR method targeting exon 7 of Dtnbp1 and designed to produce PCR products of 472 bp from wild-type DNA and 274 bp from sdy/sdy DNA. sdy arose in the DBA/2J strain. ( b ) Northern-blot analysis. We hybridized total RNA (20 μg) from kidney, brain and heart of wild-type (DBA/2J), heterozygous ( sdy /+) and homozygous ( sdy/sdy ) mice with Dtnbp1 (upper panels) and Gapd (lower panels) cDNA probes. Dtnbp1 mRNA in sdy tissues was 1.5 kb in size compared with 1.65 kb in control DBA/2J; mRNA of heterozygous sdy /+ mice contains both ∼1.5-kb and 1.65-kb Dtnbp1 mRNAs. ( c ) Western-blot analysis. We resolved kidney extracts of control DBA/2J, sdy /+ and sdy/sdy mutant mice together with transgenic progeny containing (+) or lacking (−) BAC54F9, which contains the entire Dtnbp1 genomic region, in denaturing gels, blotted gels and incubated them with <t>polyclonal</t> antibody to dysbindin 3111A (top). The blots were reprobed with antibody to Rab4 as a loading control (bottom). Immunoblot analyses of brain, heart, liver and skeletal muscle (data not shown) also showed lack of expression of dysbindin in sdy/sdy mutants.
    Rabbit Polyclonal Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 8151 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc p65 rb pab
    Dtnbp1 mRNA is smaller and dysbindin is undetectable in tissues of sdy mutant mice. ( a ) Genomic PCR. We amplified genomic DNA from control DBA/2J, sdy /+, sdy/sdy and various inbred strains by a duplex PCR method targeting exon 7 of Dtnbp1 and designed to produce PCR products of 472 bp from wild-type DNA and 274 bp from sdy/sdy DNA. sdy arose in the DBA/2J strain. ( b ) Northern-blot analysis. We hybridized total RNA (20 μg) from kidney, brain and heart of wild-type (DBA/2J), heterozygous ( sdy /+) and homozygous ( sdy/sdy ) mice with Dtnbp1 (upper panels) and Gapd (lower panels) cDNA probes. Dtnbp1 mRNA in sdy tissues was 1.5 kb in size compared with 1.65 kb in control DBA/2J; mRNA of heterozygous sdy /+ mice contains both ∼1.5-kb and 1.65-kb Dtnbp1 mRNAs. ( c ) Western-blot analysis. We resolved kidney extracts of control DBA/2J, sdy /+ and sdy/sdy mutant mice together with transgenic progeny containing (+) or lacking (−) BAC54F9, which contains the entire Dtnbp1 genomic region, in denaturing gels, blotted gels and incubated them with <t>polyclonal</t> antibody to dysbindin 3111A (top). The blots were reprobed with antibody to Rab4 as a loading control (bottom). Immunoblot analyses of brain, heart, liver and skeletal muscle (data not shown) also showed lack of expression of dysbindin in sdy/sdy mutants.
    P65 Rb Pab, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 90/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher cul 2 rb pab
    Visualization of the expression of WNV E glycoprotein in cells treated with PKC inhibitors. ( a ) Cells were infected with an MOI of 0.5 PFU/cell, treated with 200 nM calphostin C or 8 µM chelerythrine, fixed at 24 h p.i., and processed for immunofluorescence using a monoclonal antibody against WNV-E protein and a secondary antibody coupled to Alexa Fluor 488. Nuclei were stained with TO-PRO 3. Mock-infected cells were processed in parallel and included as control. Scale bars: 25 µm; ( b ) Quantification of the fluorescence intensity of anti-E antibody in cells infected and treated or not with drugs; ( c ) Vero cells were infected with a MOI of 0.5 PFU/cell and treated with calphostin C or chelerythrine as in ( a ). Cells were lysed and WNV E glycoprotein was detected by Western blotting using a <t>polyclonal</t> specific antibody. Membrane was reincubated with an anti-β-actin antibody as a control for protein loading; ( d ) Reduction of WNV RNA in the supernatants from cells treated with the PKC inhibitors. Vero cells were infected with an MOI of 0.5 PFU/cell and treated with the drugs, as in ( a ). Culture supernatants were collected at 24 h p.i., and the amount of viral RNA was determined by quantitative RT-PCR. Statistically significant differences are denoted as * p
    Cul 2 Rb Pab, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 86/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GeneTex rb pab against lc3b
    Visualization of the expression of WNV E glycoprotein in cells treated with PKC inhibitors. ( a ) Cells were infected with an MOI of 0.5 PFU/cell, treated with 200 nM calphostin C or 8 µM chelerythrine, fixed at 24 h p.i., and processed for immunofluorescence using a monoclonal antibody against WNV-E protein and a secondary antibody coupled to Alexa Fluor 488. Nuclei were stained with TO-PRO 3. Mock-infected cells were processed in parallel and included as control. Scale bars: 25 µm; ( b ) Quantification of the fluorescence intensity of anti-E antibody in cells infected and treated or not with drugs; ( c ) Vero cells were infected with a MOI of 0.5 PFU/cell and treated with calphostin C or chelerythrine as in ( a ). Cells were lysed and WNV E glycoprotein was detected by Western blotting using a <t>polyclonal</t> specific antibody. Membrane was reincubated with an anti-β-actin antibody as a control for protein loading; ( d ) Reduction of WNV RNA in the supernatants from cells treated with the PKC inhibitors. Vero cells were infected with an MOI of 0.5 PFU/cell and treated with the drugs, as in ( a ). Culture supernatants were collected at 24 h p.i., and the amount of viral RNA was determined by quantitative RT-PCR. Statistically significant differences are denoted as * p
    Rb Pab Against Lc3b, supplied by GeneTex, used in various techniques. Bioz Stars score: 91/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology rbab k 19
    Visualization of the expression of WNV E glycoprotein in cells treated with PKC inhibitors. ( a ) Cells were infected with an MOI of 0.5 PFU/cell, treated with 200 nM calphostin C or 8 µM chelerythrine, fixed at 24 h p.i., and processed for immunofluorescence using a monoclonal antibody against WNV-E protein and a secondary antibody coupled to Alexa Fluor 488. Nuclei were stained with TO-PRO 3. Mock-infected cells were processed in parallel and included as control. Scale bars: 25 µm; ( b ) Quantification of the fluorescence intensity of anti-E antibody in cells infected and treated or not with drugs; ( c ) Vero cells were infected with a MOI of 0.5 PFU/cell and treated with calphostin C or chelerythrine as in ( a ). Cells were lysed and WNV E glycoprotein was detected by Western blotting using a <t>polyclonal</t> specific antibody. Membrane was reincubated with an anti-β-actin antibody as a control for protein loading; ( d ) Reduction of WNV RNA in the supernatants from cells treated with the PKC inhibitors. Vero cells were infected with an MOI of 0.5 PFU/cell and treated with the drugs, as in ( a ). Culture supernatants were collected at 24 h p.i., and the amount of viral RNA was determined by quantitative RT-PCR. Statistically significant differences are denoted as * p
    Rbab K 19, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 85/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology rbab c 16
    Visualization of the expression of WNV E glycoprotein in cells treated with PKC inhibitors. ( a ) Cells were infected with an MOI of 0.5 PFU/cell, treated with 200 nM calphostin C or 8 µM chelerythrine, fixed at 24 h p.i., and processed for immunofluorescence using a monoclonal antibody against WNV-E protein and a secondary antibody coupled to Alexa Fluor 488. Nuclei were stained with TO-PRO 3. Mock-infected cells were processed in parallel and included as control. Scale bars: 25 µm; ( b ) Quantification of the fluorescence intensity of anti-E antibody in cells infected and treated or not with drugs; ( c ) Vero cells were infected with a MOI of 0.5 PFU/cell and treated with calphostin C or chelerythrine as in ( a ). Cells were lysed and WNV E glycoprotein was detected by Western blotting using a <t>polyclonal</t> specific antibody. Membrane was reincubated with an anti-β-actin antibody as a control for protein loading; ( d ) Reduction of WNV RNA in the supernatants from cells treated with the PKC inhibitors. Vero cells were infected with an MOI of 0.5 PFU/cell and treated with the drugs, as in ( a ). Culture supernatants were collected at 24 h p.i., and the amount of viral RNA was determined by quantitative RT-PCR. Statistically significant differences are denoted as * p
    Rbab C 16, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 85/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher rbab anti mbp
    Immunoblot analysis of the two <t>anti-MBP</t> mAbs, 2A1 and 3D7, using native and denatured MBP recombinant proteins. (A) Dot blot analysis of anti-MBP mAbs against native MBP recombinant proteins. Detection with rabbit polyclonal anti-MBP antibody <t>(RbAb</t> anti-MBP)
    Rbab Anti Mbp, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Active Motif rabbit polyclonal antibody
    Immunostaining of human adult liver for 5mC and 5hmC . Representative stainings of 40 µM adult liver sections are shown. (a) Negative control without the primary antibody. (b) Staining with the monoclonal antibody to 5mC (green) and DAPI (blue). (c) Staining with a <t>polyclonal</t> antibody against 5hmC (red) and DAPI (blue). (d) Merge of 5mC and 5hmC staining and DAPI. As evident from (d), 5mC and 5hmC show similar patterns of intranuclear distribution, indicating that 5hmC, when present, tends to co-localize with 5mC in the hepatocyte nucleus.
    Rabbit Polyclonal Antibody, supplied by Active Motif, used in various techniques. Bioz Stars score: 92/100, based on 70 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Promega rabbit polyclonal antibody
    A to F : WNV antigens in different regions of the mouse CNS. Mice were inoculated with 10 3 FFU of IS-98-ST1 WNV upon different routes (i.c., i.p., i.n., i.d.); at Day 7 of infection, mice were euthanazied, brains were cut in 14 μm thick cryostat sections, and processed for immunofluorescence using anti-WNV serum (obtained from i.p.-inoculated resistant mice) as primary antibody. A : hippocampus (pyramidal layer), i.c. inoculation. B : frontal cortex, i.c. inoculation. C : spinal cord, i.p. inoculation. D : olfactory bulb, i.n. inoculation. Magnification: × 350. E : Average levels of infection of the different brain structures was estimated on 10 different sections for each of the 3 animals per group (I.C.: intracerebral, I.P.: intraperitoneal, I.D.: intradermal; I.N.: intranasal) according to the scale: +++: more than 10 positive cells per microscopic field; ++: between 3 and 9 positive cells; +: 1 or 2 positive cells; -: no positive cell. F : Immunodetection of WNV antigens (green) and Glial Fibrillary Acidic Protein (red) in cryostat section of WNV-infected mouse brain, day 7 of infection, i.c Magnification: × 700. G, H : WNV infection in primary neural cultures from C57BL/6 mouse brain cortex. Primary cultures were performed as described in text and infected with IS-98-ST1 WNV. G : Detection of WNV antigens (using anti-WNV mouse immune serum and a FITC-conjugated secondary antibody, green staining) and neuronal specific enolase (using a rabbit <t>polyclonal</t> antiserum and an anti-rabbit polyclonal antibody made in goat conjugated with Texas Red, red staining) by immunofluorescence at 24 h p.i. (m.o.i. 12.5). Magnification: × 700. H : Kinetics of infection and variation of cell number at various times post-infection for different m.o.i; three cultures for each m.o.i. were fixed and processed for WNV antigen detection by immunofluorescence, whereas cell nuclei were visualized with DAPI. Cell nuclei of adherent cells were counted in 8 different different fields for the three cultures (histogram) whereas the percentage of infected cell was estimated by counting WNV antigen positive cells and cell nuclei; the percentage of infected cells is indicated as values (%) in white squares.
    Rabbit Polyclonal Antibody, supplied by Promega, used in various techniques. Bioz Stars score: 92/100, based on 71 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    BioLegend biolegend rb pab
    Reactivity of rNanogP8 and rNanog proteins towards 8 anti-Nanog Abs. WB analysis using 8 anti-Nanog Abs (A-H). Cell types from which the initial cDNAs were cloned are indicated on top. Individual Abs are indicated on the right and M.W on the left. For some Abs, both a long (LE) and short (SE) exposures were shown. N: non-induced; I: induced by IPTG (see Methods ). The red arrowheads in each panel indicate the 42 kD major Nanog protein and green arrows point to minor upper bands. In panel F, the two arrows point to the ∼48/54 kD doublets recognized by the <t>BioLegend</t> Rb <t>pAb.</t>
    Biolegend Rb Pab, supplied by BioLegend, used in various techniques. Bioz Stars score: 86/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Aviva Systems rabbit polyclonal antibody
    Reactivity of rNanogP8 and rNanog proteins towards 8 anti-Nanog Abs. WB analysis using 8 anti-Nanog Abs (A-H). Cell types from which the initial cDNAs were cloned are indicated on top. Individual Abs are indicated on the right and M.W on the left. For some Abs, both a long (LE) and short (SE) exposures were shown. N: non-induced; I: induced by IPTG (see Methods ). The red arrowheads in each panel indicate the 42 kD major Nanog protein and green arrows point to minor upper bands. In panel F, the two arrows point to the ∼48/54 kD doublets recognized by the <t>BioLegend</t> Rb <t>pAb.</t>
    Rabbit Polyclonal Antibody, supplied by Aviva Systems, used in various techniques. Bioz Stars score: 93/100, based on 77 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Novocastra rabbit polyclonal antibody
    Reactivity of rNanogP8 and rNanog proteins towards 8 anti-Nanog Abs. WB analysis using 8 anti-Nanog Abs (A-H). Cell types from which the initial cDNAs were cloned are indicated on top. Individual Abs are indicated on the right and M.W on the left. For some Abs, both a long (LE) and short (SE) exposures were shown. N: non-induced; I: induced by IPTG (see Methods ). The red arrowheads in each panel indicate the 42 kD major Nanog protein and green arrows point to minor upper bands. In panel F, the two arrows point to the ∼48/54 kD doublets recognized by the <t>BioLegend</t> Rb <t>pAb.</t>
    Rabbit Polyclonal Antibody, supplied by Novocastra, used in various techniques. Bioz Stars score: 92/100, based on 101 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Agilent technologies rabbit polyclonal antibody
    Western blot of S100A6, using the <t>polyclonal</t> anti-S100A6 antibody (Dako) on lysates from prostate cancer cell lines. Lane 1. Du145; lane 2, LNCaP; lane 3, PC3. Note the protein expression in Du145 and PC3 cells, seen as an ∼10 kDa band, but its absence in the LNCaP cell line.
    Rabbit Polyclonal Antibody, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 92/100, based on 1282 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Covance rabbit polyclonal antibody
    Lactosylceramide is associated with HCV NS4B protein. (A) Parental Huh7.5 and HCV Con1 (genotype 1b) replicon cells were grown for 48 h and processed for confocal microscopy with mouse monoclonal αLacCer antibody (1:500; green) and rabbit <t>polyclonal</t> αNS4B antibody (1:150; red). Huh7.5 cells also were infected with HCV Jc1 (MOI of 1) and processed for confocal microscopy as described above. The boxed areas represent a magnified view for colocalization (yellow) of lactosylceramide and HCV NS4B protein. (B) Huh7.5 cells were infected with HCV Jc1 (MOI of 1) as described for panel A and processed for confocal microscopy 24 h, 48 h, and 72 h postinfection. For each infection time point, confocal images were taken of 20 representative cells. The intensity of lactosylceramide pixels was calculated with the JACoP plugin in ImageJ software. Each filled circle or square (24 h; mock or Jc1 infected), upper or lower triangle (48 h; mock or Jc1 infected), diamond (72 h; mock), or open circle (72 h; Jc1 infected) represents one cell.
    Rabbit Polyclonal Antibody, supplied by Covance, used in various techniques. Bioz Stars score: 92/100, based on 261 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ChinaPeptides rabbit polyclonal antibody
    Lactosylceramide is associated with HCV NS4B protein. (A) Parental Huh7.5 and HCV Con1 (genotype 1b) replicon cells were grown for 48 h and processed for confocal microscopy with mouse monoclonal αLacCer antibody (1:500; green) and rabbit <t>polyclonal</t> αNS4B antibody (1:150; red). Huh7.5 cells also were infected with HCV Jc1 (MOI of 1) and processed for confocal microscopy as described above. The boxed areas represent a magnified view for colocalization (yellow) of lactosylceramide and HCV NS4B protein. (B) Huh7.5 cells were infected with HCV Jc1 (MOI of 1) as described for panel A and processed for confocal microscopy 24 h, 48 h, and 72 h postinfection. For each infection time point, confocal images were taken of 20 representative cells. The intensity of lactosylceramide pixels was calculated with the JACoP plugin in ImageJ software. Each filled circle or square (24 h; mock or Jc1 infected), upper or lower triangle (48 h; mock or Jc1 infected), diamond (72 h; mock), or open circle (72 h; Jc1 infected) represents one cell.
    Rabbit Polyclonal Antibody, supplied by ChinaPeptides, used in various techniques. Bioz Stars score: 92/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Swant rabbit polyclonal antibody
    Cultured cortical interneurons represent a nonoverlapping population with respect to the expression of calcium-binding proteins. Dissociated cortical neurons were grown for 21 d in vitro and fixed in 4% paraformaldehyde. Double immunocytochemistry was performed using a rabbit <t>polyclonal</t> antibody against PV (red) and a mouse monoclonal antibody (green) against calretinin (top), calbindin (middle), or αCaMKII (bottom) and AlexaFluor-conjugated secondary antibodies. Scale bar, 15 μm.
    Rabbit Polyclonal Antibody, supplied by Swant, used in various techniques. Bioz Stars score: 92/100, based on 196 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Merck & Co rabbit polyclonal antibody
    Cultured cortical interneurons represent a nonoverlapping population with respect to the expression of calcium-binding proteins. Dissociated cortical neurons were grown for 21 d in vitro and fixed in 4% paraformaldehyde. Double immunocytochemistry was performed using a rabbit <t>polyclonal</t> antibody against PV (red) and a mouse monoclonal antibody (green) against calretinin (top), calbindin (middle), or αCaMKII (bottom) and AlexaFluor-conjugated secondary antibodies. Scale bar, 15 μm.
    Rabbit Polyclonal Antibody, supplied by Merck & Co, used in various techniques. Bioz Stars score: 93/100, based on 32 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Agrisera rabbit polyclonal antibody
    Cultured cortical interneurons represent a nonoverlapping population with respect to the expression of calcium-binding proteins. Dissociated cortical neurons were grown for 21 d in vitro and fixed in 4% paraformaldehyde. Double immunocytochemistry was performed using a rabbit <t>polyclonal</t> antibody against PV (red) and a mouse monoclonal antibody (green) against calretinin (top), calbindin (middle), or αCaMKII (bottom) and AlexaFluor-conjugated secondary antibodies. Scale bar, 15 μm.
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    Immunex Corporation rabbit polyclonal antibody
    Cultured cortical interneurons represent a nonoverlapping population with respect to the expression of calcium-binding proteins. Dissociated cortical neurons were grown for 21 d in vitro and fixed in 4% paraformaldehyde. Double immunocytochemistry was performed using a rabbit <t>polyclonal</t> antibody against PV (red) and a mouse monoclonal antibody (green) against calretinin (top), calbindin (middle), or αCaMKII (bottom) and AlexaFluor-conjugated secondary antibodies. Scale bar, 15 μm.
    Rabbit Polyclonal Antibody, supplied by Immunex Corporation, used in various techniques. Bioz Stars score: 92/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Pharmingen rabbit polyclonal antibody
    Immunofluorescent dopaminergic neurons in primary cultures of rat mesencephalic neurons fixed after 12 hr of 1-μM MPP + treatment stained with a TH monoclonal mouse antibody revealed by FITC ( A ) and a rabbit <t>polyclonal</t> antibody recognizing activated caspase-3 (CM1) revealed by tetramethylrhodamine B isothiocyanate ( B ). Hoechst 33258 staining reveals an intact nucleus in this neuron ( C , arrow). (Bar = 20 μm.) In contrast, in a TH-positive neuron ( D ) with CM1 staining ( E ), DNA condensation assessed by Hoechst 33258 can be detected after 72 hr of MPP + treatment ( F , arrow). Note that a higher magnification was used to show DNA condensation. (Bar = 10 μm.)
    Rabbit Polyclonal Antibody, supplied by Pharmingen, used in various techniques. Bioz Stars score: 92/100, based on 87 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc rabbit polyclonal antibody
    Lactosylceramide is associated with HCV NS4B protein. (A) Parental Huh7.5 and HCV Con1 (genotype 1b) replicon cells were grown for 48 h and processed for confocal microscopy with mouse monoclonal αLacCer antibody (1:500; green) and rabbit <t>polyclonal</t> αNS4B antibody (1:150; red). Huh7.5 cells also were infected with HCV Jc1 (MOI of 1) and processed for confocal microscopy as described above. The boxed areas represent a magnified view for colocalization (yellow) of lactosylceramide and HCV NS4B protein. (B) Huh7.5 cells were infected with HCV Jc1 (MOI of 1) as described for panel A and processed for confocal microscopy 24 h, 48 h, and 72 h postinfection. For each infection time point, confocal images were taken of 20 representative cells. The intensity of lactosylceramide pixels was calculated with the JACoP plugin in ImageJ software. Each filled circle or square (24 h; mock or Jc1 infected), upper or lower triangle (48 h; mock or Jc1 infected), diamond (72 h; mock), or open circle (72 h; Jc1 infected) represents one cell.
    Rabbit Polyclonal Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 92/100, based on 4326 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Synaptic Systems rabbit polyclonal antibody
    Complexin 3/4 concentrates in retinal photoreceptor terminals concomitant with RIBEYE b . (A) The zpr 1/FRet 43 monoclonal antibody (red) and the pan-complexin 3/4 <t>polyclonal</t> (green) were also used to localize these complexins in developing retinal photoreceptors. At 2.5 dpf, retinal photoreceptors are most prominent in the ventronasal patch, where complexin 3/4 immunoreactivity appears in some photoreceptor terminals. (B) RIBEYE b (green) has also started to cluster in photoreceptor terminals (red) in the outer plexiform layer at 2.5 dpf. (C) At 3 dpf, complexin 3/4 (red) is highly expressed in zpr 1/FRet 43-positive (red) and zpr 1/FRet 43-negative photoreceptor terminals in the ventronasal patch. (D) Pleiomorphic RIBEYE b (green) expression is found at 3 dpf in zpr 1/FRet 43-positive (red) and zpr 1/FRet 43-negative photoreceptor terminals in the ventronasal patch. The inset shows a zpr 1/FRet 43-positive terminal containing curvilinear RIBEYE b immunoreactivity that may correspond to a ribbon. Scale bar = 5 μm.
    Rabbit Polyclonal Antibody, supplied by Synaptic Systems, used in various techniques. Bioz Stars score: 92/100, based on 105 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Spring Bioscience rabbit polyclonal antibody
    Complexin 3/4 concentrates in retinal photoreceptor terminals concomitant with RIBEYE b . (A) The zpr 1/FRet 43 monoclonal antibody (red) and the pan-complexin 3/4 <t>polyclonal</t> (green) were also used to localize these complexins in developing retinal photoreceptors. At 2.5 dpf, retinal photoreceptors are most prominent in the ventronasal patch, where complexin 3/4 immunoreactivity appears in some photoreceptor terminals. (B) RIBEYE b (green) has also started to cluster in photoreceptor terminals (red) in the outer plexiform layer at 2.5 dpf. (C) At 3 dpf, complexin 3/4 (red) is highly expressed in zpr 1/FRet 43-positive (red) and zpr 1/FRet 43-negative photoreceptor terminals in the ventronasal patch. (D) Pleiomorphic RIBEYE b (green) expression is found at 3 dpf in zpr 1/FRet 43-positive (red) and zpr 1/FRet 43-negative photoreceptor terminals in the ventronasal patch. The inset shows a zpr 1/FRet 43-positive terminal containing curvilinear RIBEYE b immunoreactivity that may correspond to a ribbon. Scale bar = 5 μm.
    Rabbit Polyclonal Antibody, supplied by Spring Bioscience, used in various techniques. Bioz Stars score: 92/100, based on 30 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal antibody/product/Spring Bioscience
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    rabbit polyclonal antibody - by Bioz Stars, 2020-05
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    Image Search Results


    Dtnbp1 mRNA is smaller and dysbindin is undetectable in tissues of sdy mutant mice. ( a ) Genomic PCR. We amplified genomic DNA from control DBA/2J, sdy /+, sdy/sdy and various inbred strains by a duplex PCR method targeting exon 7 of Dtnbp1 and designed to produce PCR products of 472 bp from wild-type DNA and 274 bp from sdy/sdy DNA. sdy arose in the DBA/2J strain. ( b ) Northern-blot analysis. We hybridized total RNA (20 μg) from kidney, brain and heart of wild-type (DBA/2J), heterozygous ( sdy /+) and homozygous ( sdy/sdy ) mice with Dtnbp1 (upper panels) and Gapd (lower panels) cDNA probes. Dtnbp1 mRNA in sdy tissues was 1.5 kb in size compared with 1.65 kb in control DBA/2J; mRNA of heterozygous sdy /+ mice contains both ∼1.5-kb and 1.65-kb Dtnbp1 mRNAs. ( c ) Western-blot analysis. We resolved kidney extracts of control DBA/2J, sdy /+ and sdy/sdy mutant mice together with transgenic progeny containing (+) or lacking (−) BAC54F9, which contains the entire Dtnbp1 genomic region, in denaturing gels, blotted gels and incubated them with polyclonal antibody to dysbindin 3111A (top). The blots were reprobed with antibody to Rab4 as a loading control (bottom). Immunoblot analyses of brain, heart, liver and skeletal muscle (data not shown) also showed lack of expression of dysbindin in sdy/sdy mutants.

    Journal: Nature genetics

    Article Title: Hermansky-Pudlak syndrome type 7 (HPS-7) results from mutant dysbindin, a member of the biogenesis of lysosome-related organelles complex 1 (BLOC-1)

    doi: 10.1038/ng1229

    Figure Lengend Snippet: Dtnbp1 mRNA is smaller and dysbindin is undetectable in tissues of sdy mutant mice. ( a ) Genomic PCR. We amplified genomic DNA from control DBA/2J, sdy /+, sdy/sdy and various inbred strains by a duplex PCR method targeting exon 7 of Dtnbp1 and designed to produce PCR products of 472 bp from wild-type DNA and 274 bp from sdy/sdy DNA. sdy arose in the DBA/2J strain. ( b ) Northern-blot analysis. We hybridized total RNA (20 μg) from kidney, brain and heart of wild-type (DBA/2J), heterozygous ( sdy /+) and homozygous ( sdy/sdy ) mice with Dtnbp1 (upper panels) and Gapd (lower panels) cDNA probes. Dtnbp1 mRNA in sdy tissues was 1.5 kb in size compared with 1.65 kb in control DBA/2J; mRNA of heterozygous sdy /+ mice contains both ∼1.5-kb and 1.65-kb Dtnbp1 mRNAs. ( c ) Western-blot analysis. We resolved kidney extracts of control DBA/2J, sdy /+ and sdy/sdy mutant mice together with transgenic progeny containing (+) or lacking (−) BAC54F9, which contains the entire Dtnbp1 genomic region, in denaturing gels, blotted gels and incubated them with polyclonal antibody to dysbindin 3111A (top). The blots were reprobed with antibody to Rab4 as a loading control (bottom). Immunoblot analyses of brain, heart, liver and skeletal muscle (data not shown) also showed lack of expression of dysbindin in sdy/sdy mutants.

    Article Snippet: We purchased rabbit polyclonal antibody to Rab4 (D-20) from Santa Cruz Biotechnology and mouse monoclonal antibody to α-tubulin (Clone B512) from Sigma.

    Techniques: Mutagenesis, Mouse Assay, Polymerase Chain Reaction, Amplification, Northern Blot, Western Blot, Transgenic Assay, Incubation, Expressing

    Visualization of the expression of WNV E glycoprotein in cells treated with PKC inhibitors. ( a ) Cells were infected with an MOI of 0.5 PFU/cell, treated with 200 nM calphostin C or 8 µM chelerythrine, fixed at 24 h p.i., and processed for immunofluorescence using a monoclonal antibody against WNV-E protein and a secondary antibody coupled to Alexa Fluor 488. Nuclei were stained with TO-PRO 3. Mock-infected cells were processed in parallel and included as control. Scale bars: 25 µm; ( b ) Quantification of the fluorescence intensity of anti-E antibody in cells infected and treated or not with drugs; ( c ) Vero cells were infected with a MOI of 0.5 PFU/cell and treated with calphostin C or chelerythrine as in ( a ). Cells were lysed and WNV E glycoprotein was detected by Western blotting using a polyclonal specific antibody. Membrane was reincubated with an anti-β-actin antibody as a control for protein loading; ( d ) Reduction of WNV RNA in the supernatants from cells treated with the PKC inhibitors. Vero cells were infected with an MOI of 0.5 PFU/cell and treated with the drugs, as in ( a ). Culture supernatants were collected at 24 h p.i., and the amount of viral RNA was determined by quantitative RT-PCR. Statistically significant differences are denoted as * p

    Journal: Viruses

    Article Title: Pharmacological Inhibition of Protein Kinase C Reduces West Nile Virus Replication

    doi: 10.3390/v10020091

    Figure Lengend Snippet: Visualization of the expression of WNV E glycoprotein in cells treated with PKC inhibitors. ( a ) Cells were infected with an MOI of 0.5 PFU/cell, treated with 200 nM calphostin C or 8 µM chelerythrine, fixed at 24 h p.i., and processed for immunofluorescence using a monoclonal antibody against WNV-E protein and a secondary antibody coupled to Alexa Fluor 488. Nuclei were stained with TO-PRO 3. Mock-infected cells were processed in parallel and included as control. Scale bars: 25 µm; ( b ) Quantification of the fluorescence intensity of anti-E antibody in cells infected and treated or not with drugs; ( c ) Vero cells were infected with a MOI of 0.5 PFU/cell and treated with calphostin C or chelerythrine as in ( a ). Cells were lysed and WNV E glycoprotein was detected by Western blotting using a polyclonal specific antibody. Membrane was reincubated with an anti-β-actin antibody as a control for protein loading; ( d ) Reduction of WNV RNA in the supernatants from cells treated with the PKC inhibitors. Vero cells were infected with an MOI of 0.5 PFU/cell and treated with the drugs, as in ( a ). Culture supernatants were collected at 24 h p.i., and the amount of viral RNA was determined by quantitative RT-PCR. Statistically significant differences are denoted as * p

    Article Snippet: Antibodies Mouse monoclonal antibody J2 against double-stranded RNA (dsRNA) (Scicons, Budapest, Hungary), rabbit polyclonal antibody (Thermo Scientific, Waltham, MA, USA), and mouse monoclonal antibody 3.67G (Millipore, Temecula, CA, USA), both directed against the E glycoprotein of WNV, and mouse monoclonal anti-β-actin (Sigma, St. Louis, MI, USA) were used as primary antibodies.

    Techniques: Expressing, Infection, Immunofluorescence, Staining, Fluorescence, Western Blot, Quantitative RT-PCR

    Immunoblot analysis of the two anti-MBP mAbs, 2A1 and 3D7, using native and denatured MBP recombinant proteins. (A) Dot blot analysis of anti-MBP mAbs against native MBP recombinant proteins. Detection with rabbit polyclonal anti-MBP antibody (RbAb anti-MBP)

    Journal: Monoclonal Antibodies in Immunodiagnosis and Immunotherapy

    Article Title: Generation and Validation of Monoclonal Antibodies Against the Maltose Binding Protein

    doi: 10.1089/mab.2015.0072

    Figure Lengend Snippet: Immunoblot analysis of the two anti-MBP mAbs, 2A1 and 3D7, using native and denatured MBP recombinant proteins. (A) Dot blot analysis of anti-MBP mAbs against native MBP recombinant proteins. Detection with rabbit polyclonal anti-MBP antibody (RbAb anti-MBP)

    Article Snippet: The capacity of the two generated anti-MBP mAbs, 2A1 and 3D7, to identify native MBP was tested by an immunoblot assay using the native recombinant MBP proteins 6xHis-MBP and MBP-Ror2 (MBP fused to a portion of the mouse Ror2 receptor). The results were compared to those obtained with a commercially available rabbit polyclonal antibody, RbAb anti-MBP (Thermo Fisher Scientific).

    Techniques: Recombinant, Dot Blot

    Immunostaining of human adult liver for 5mC and 5hmC . Representative stainings of 40 µM adult liver sections are shown. (a) Negative control without the primary antibody. (b) Staining with the monoclonal antibody to 5mC (green) and DAPI (blue). (c) Staining with a polyclonal antibody against 5hmC (red) and DAPI (blue). (d) Merge of 5mC and 5hmC staining and DAPI. As evident from (d), 5mC and 5hmC show similar patterns of intranuclear distribution, indicating that 5hmC, when present, tends to co-localize with 5mC in the hepatocyte nucleus.

    Journal: Genome Biology

    Article Title: Ontogeny, distribution and potential roles of 5-hydroxymethylcytosine in human liver function

    doi: 10.1186/gb-2013-14-8-r83

    Figure Lengend Snippet: Immunostaining of human adult liver for 5mC and 5hmC . Representative stainings of 40 µM adult liver sections are shown. (a) Negative control without the primary antibody. (b) Staining with the monoclonal antibody to 5mC (green) and DAPI (blue). (c) Staining with a polyclonal antibody against 5hmC (red) and DAPI (blue). (d) Merge of 5mC and 5hmC staining and DAPI. As evident from (d), 5mC and 5hmC show similar patterns of intranuclear distribution, indicating that 5hmC, when present, tends to co-localize with 5mC in the hepatocyte nucleus.

    Article Snippet: As primary antibodies, a rabbit polyclonal antibody to 5hmC (1:5,000; ActiveMotif, Carlsbad, CA, USA; catalogue number 39769) and a mouse monoclonal antibody to 5mC (1:500; ActiveMotif, catalogue number 39649) were used.

    Techniques: Immunostaining, Negative Control, Staining

    A to F : WNV antigens in different regions of the mouse CNS. Mice were inoculated with 10 3 FFU of IS-98-ST1 WNV upon different routes (i.c., i.p., i.n., i.d.); at Day 7 of infection, mice were euthanazied, brains were cut in 14 μm thick cryostat sections, and processed for immunofluorescence using anti-WNV serum (obtained from i.p.-inoculated resistant mice) as primary antibody. A : hippocampus (pyramidal layer), i.c. inoculation. B : frontal cortex, i.c. inoculation. C : spinal cord, i.p. inoculation. D : olfactory bulb, i.n. inoculation. Magnification: × 350. E : Average levels of infection of the different brain structures was estimated on 10 different sections for each of the 3 animals per group (I.C.: intracerebral, I.P.: intraperitoneal, I.D.: intradermal; I.N.: intranasal) according to the scale: +++: more than 10 positive cells per microscopic field; ++: between 3 and 9 positive cells; +: 1 or 2 positive cells; -: no positive cell. F : Immunodetection of WNV antigens (green) and Glial Fibrillary Acidic Protein (red) in cryostat section of WNV-infected mouse brain, day 7 of infection, i.c Magnification: × 700. G, H : WNV infection in primary neural cultures from C57BL/6 mouse brain cortex. Primary cultures were performed as described in text and infected with IS-98-ST1 WNV. G : Detection of WNV antigens (using anti-WNV mouse immune serum and a FITC-conjugated secondary antibody, green staining) and neuronal specific enolase (using a rabbit polyclonal antiserum and an anti-rabbit polyclonal antibody made in goat conjugated with Texas Red, red staining) by immunofluorescence at 24 h p.i. (m.o.i. 12.5). Magnification: × 700. H : Kinetics of infection and variation of cell number at various times post-infection for different m.o.i; three cultures for each m.o.i. were fixed and processed for WNV antigen detection by immunofluorescence, whereas cell nuclei were visualized with DAPI. Cell nuclei of adherent cells were counted in 8 different different fields for the three cultures (histogram) whereas the percentage of infected cell was estimated by counting WNV antigen positive cells and cell nuclei; the percentage of infected cells is indicated as values (%) in white squares.

    Journal: Virology Journal

    Article Title: The Israeli strain IS-98-ST1 of West Nile virus as viral model for West Nile encephalitis in the Old World

    doi: 10.1186/1743-422X-1-9

    Figure Lengend Snippet: A to F : WNV antigens in different regions of the mouse CNS. Mice were inoculated with 10 3 FFU of IS-98-ST1 WNV upon different routes (i.c., i.p., i.n., i.d.); at Day 7 of infection, mice were euthanazied, brains were cut in 14 μm thick cryostat sections, and processed for immunofluorescence using anti-WNV serum (obtained from i.p.-inoculated resistant mice) as primary antibody. A : hippocampus (pyramidal layer), i.c. inoculation. B : frontal cortex, i.c. inoculation. C : spinal cord, i.p. inoculation. D : olfactory bulb, i.n. inoculation. Magnification: × 350. E : Average levels of infection of the different brain structures was estimated on 10 different sections for each of the 3 animals per group (I.C.: intracerebral, I.P.: intraperitoneal, I.D.: intradermal; I.N.: intranasal) according to the scale: +++: more than 10 positive cells per microscopic field; ++: between 3 and 9 positive cells; +: 1 or 2 positive cells; -: no positive cell. F : Immunodetection of WNV antigens (green) and Glial Fibrillary Acidic Protein (red) in cryostat section of WNV-infected mouse brain, day 7 of infection, i.c Magnification: × 700. G, H : WNV infection in primary neural cultures from C57BL/6 mouse brain cortex. Primary cultures were performed as described in text and infected with IS-98-ST1 WNV. G : Detection of WNV antigens (using anti-WNV mouse immune serum and a FITC-conjugated secondary antibody, green staining) and neuronal specific enolase (using a rabbit polyclonal antiserum and an anti-rabbit polyclonal antibody made in goat conjugated with Texas Red, red staining) by immunofluorescence at 24 h p.i. (m.o.i. 12.5). Magnification: × 700. H : Kinetics of infection and variation of cell number at various times post-infection for different m.o.i; three cultures for each m.o.i. were fixed and processed for WNV antigen detection by immunofluorescence, whereas cell nuclei were visualized with DAPI. Cell nuclei of adherent cells were counted in 8 different different fields for the three cultures (histogram) whereas the percentage of infected cell was estimated by counting WNV antigen positive cells and cell nuclei; the percentage of infected cells is indicated as values (%) in white squares.

    Article Snippet: Some sections were also processed for Glial Fibrillary Acidic Protein (GFAP) using a rabbit polyclonal antibody (Promega).

    Techniques: Mouse Assay, Infection, Immunofluorescence, Immunodetection, Staining

    Reactivity of rNanogP8 and rNanog proteins towards 8 anti-Nanog Abs. WB analysis using 8 anti-Nanog Abs (A-H). Cell types from which the initial cDNAs were cloned are indicated on top. Individual Abs are indicated on the right and M.W on the left. For some Abs, both a long (LE) and short (SE) exposures were shown. N: non-induced; I: induced by IPTG (see Methods ). The red arrowheads in each panel indicate the 42 kD major Nanog protein and green arrows point to minor upper bands. In panel F, the two arrows point to the ∼48/54 kD doublets recognized by the BioLegend Rb pAb.

    Journal: PLoS ONE

    Article Title: Nanog1 in NTERA-2 and Recombinant NanogP8 from Somatic Cancer Cells Adopt Multiple Protein Conformations and Migrate at Multiple M.W Species

    doi: 10.1371/journal.pone.0090615

    Figure Lengend Snippet: Reactivity of rNanogP8 and rNanog proteins towards 8 anti-Nanog Abs. WB analysis using 8 anti-Nanog Abs (A-H). Cell types from which the initial cDNAs were cloned are indicated on top. Individual Abs are indicated on the right and M.W on the left. For some Abs, both a long (LE) and short (SE) exposures were shown. N: non-induced; I: induced by IPTG (see Methods ). The red arrowheads in each panel indicate the 42 kD major Nanog protein and green arrows point to minor upper bands. In panel F, the two arrows point to the ∼48/54 kD doublets recognized by the BioLegend Rb pAb.

    Article Snippet: Among the 8 anti-Nanog Abs, four [Kamiya Rb pAb, SC (Santa Cruz) goat pAb N17, Cell Signaling (CS) Rb pAb and Rb mAb] are directed to the ND, two (SC Rb pAb H-155 and R & D goat pAb) to the C-terminus, and one (BioLegend Rb pAb) to the HD (homeodomain) whereas another (eBioscience mAb) is raised against the full-length human Nanog1 protein ( ).

    Techniques: Western Blot, Clone Assay

    Western blot of S100A6, using the polyclonal anti-S100A6 antibody (Dako) on lysates from prostate cancer cell lines. Lane 1. Du145; lane 2, LNCaP; lane 3, PC3. Note the protein expression in Du145 and PC3 cells, seen as an ∼10 kDa band, but its absence in the LNCaP cell line.

    Journal: British Journal of Cancer

    Article Title: S100A6 (Calcyclin) is a prostate basal cell marker absent in prostate cancer and its precursors

    doi: 10.1038/sj.bjc.6602034

    Figure Lengend Snippet: Western blot of S100A6, using the polyclonal anti-S100A6 antibody (Dako) on lysates from prostate cancer cell lines. Lane 1. Du145; lane 2, LNCaP; lane 3, PC3. Note the protein expression in Du145 and PC3 cells, seen as an ∼10 kDa band, but its absence in the LNCaP cell line.

    Article Snippet: The loss of expression seen in the malignant cells was confirmed using two commercially available antibodies, that is, a mouse monoclonal antibody (Sigma) and rabbit polyclonal antibody (Dako).

    Techniques: Western Blot, Expressing

    Lactosylceramide is associated with HCV NS4B protein. (A) Parental Huh7.5 and HCV Con1 (genotype 1b) replicon cells were grown for 48 h and processed for confocal microscopy with mouse monoclonal αLacCer antibody (1:500; green) and rabbit polyclonal αNS4B antibody (1:150; red). Huh7.5 cells also were infected with HCV Jc1 (MOI of 1) and processed for confocal microscopy as described above. The boxed areas represent a magnified view for colocalization (yellow) of lactosylceramide and HCV NS4B protein. (B) Huh7.5 cells were infected with HCV Jc1 (MOI of 1) as described for panel A and processed for confocal microscopy 24 h, 48 h, and 72 h postinfection. For each infection time point, confocal images were taken of 20 representative cells. The intensity of lactosylceramide pixels was calculated with the JACoP plugin in ImageJ software. Each filled circle or square (24 h; mock or Jc1 infected), upper or lower triangle (48 h; mock or Jc1 infected), diamond (72 h; mock), or open circle (72 h; Jc1 infected) represents one cell.

    Journal: Journal of Virology

    Article Title: Modulation of Hepatitis C Virus Genome Replication by Glycosphingolipids and Four-Phosphate Adaptor Protein 2

    doi: 10.1128/JVI.00970-14

    Figure Lengend Snippet: Lactosylceramide is associated with HCV NS4B protein. (A) Parental Huh7.5 and HCV Con1 (genotype 1b) replicon cells were grown for 48 h and processed for confocal microscopy with mouse monoclonal αLacCer antibody (1:500; green) and rabbit polyclonal αNS4B antibody (1:150; red). Huh7.5 cells also were infected with HCV Jc1 (MOI of 1) and processed for confocal microscopy as described above. The boxed areas represent a magnified view for colocalization (yellow) of lactosylceramide and HCV NS4B protein. (B) Huh7.5 cells were infected with HCV Jc1 (MOI of 1) as described for panel A and processed for confocal microscopy 24 h, 48 h, and 72 h postinfection. For each infection time point, confocal images were taken of 20 representative cells. The intensity of lactosylceramide pixels was calculated with the JACoP plugin in ImageJ software. Each filled circle or square (24 h; mock or Jc1 infected), upper or lower triangle (48 h; mock or Jc1 infected), diamond (72 h; mock), or open circle (72 h; Jc1 infected) represents one cell.

    Article Snippet: Rabbit polyclonal antibody to HCV NS4B was produced by Covance (Denver, CO).

    Techniques: Confocal Microscopy, Infection, Software

    ). At 48 h postinfection, the cells were processed for confocal microscopy with mouse monoclonal αPI4P antibody (green). NS5A was detected via mCherry fluorescence. Alternatively, HCV Con1 replicon cells were grown for 48 h and stained with mouse monoclonal α-PI4P antibody (red) and rabbit polyclonal antibody against NS4B (green). The boxed areas are a magnified view for colocalization (yellow) of HCV NS5A or NS4B protein with PI4P. (C) Diagram of the de novo ) are two pharmacological inhibitors of UGCGC. FAPP2 is highlighted in gray and carries glucosylceramide from the cis -Golgi to the trans -Golgi network for conversion into lactosylceramide and other glycosphingolipids. CoA, coenzyme A.

    Journal: Journal of Virology

    Article Title: Modulation of Hepatitis C Virus Genome Replication by Glycosphingolipids and Four-Phosphate Adaptor Protein 2

    doi: 10.1128/JVI.00970-14

    Figure Lengend Snippet: ). At 48 h postinfection, the cells were processed for confocal microscopy with mouse monoclonal αPI4P antibody (green). NS5A was detected via mCherry fluorescence. Alternatively, HCV Con1 replicon cells were grown for 48 h and stained with mouse monoclonal α-PI4P antibody (red) and rabbit polyclonal antibody against NS4B (green). The boxed areas are a magnified view for colocalization (yellow) of HCV NS5A or NS4B protein with PI4P. (C) Diagram of the de novo ) are two pharmacological inhibitors of UGCGC. FAPP2 is highlighted in gray and carries glucosylceramide from the cis -Golgi to the trans -Golgi network for conversion into lactosylceramide and other glycosphingolipids. CoA, coenzyme A.

    Article Snippet: Rabbit polyclonal antibody to HCV NS4B was produced by Covance (Denver, CO).

    Techniques: Confocal Microscopy, Fluorescence, Staining

    ) virus-infected cells were grown as described for panel A and processed for confocal microscopy with mouse monoclonal antibody against dsRNA (1: 200; red) and rabbit polyclonal αFAPP2 antibody (1:100; green). The boxed areas indicate the magnified view for colocalization (yellow color) of HCV NS5A (A) or dsRNA (B) with FAPP2 protein. (C) FAPP2 cofractionates with HCV replicase NS5A protein in the detergent-resistant membrane fraction. Con1 replicon cell lysates were left untreated or were treated with 1% NP-40 on ice and subjected to membrane floatation. Proteins from pooled fractions (1 to 4 and 5 to 9) were separated by SDS-PAGE, followed by immunoblotting with antibodies against FAPP2, SPTLC1, NS5A, calnexin, or GAPDH. Numbers 1 to 4 refer to membrane (M) fractions, and numbers 5 to 8 refer to soluble (S) fractions.

    Journal: Journal of Virology

    Article Title: Modulation of Hepatitis C Virus Genome Replication by Glycosphingolipids and Four-Phosphate Adaptor Protein 2

    doi: 10.1128/JVI.00970-14

    Figure Lengend Snippet: ) virus-infected cells were grown as described for panel A and processed for confocal microscopy with mouse monoclonal antibody against dsRNA (1: 200; red) and rabbit polyclonal αFAPP2 antibody (1:100; green). The boxed areas indicate the magnified view for colocalization (yellow color) of HCV NS5A (A) or dsRNA (B) with FAPP2 protein. (C) FAPP2 cofractionates with HCV replicase NS5A protein in the detergent-resistant membrane fraction. Con1 replicon cell lysates were left untreated or were treated with 1% NP-40 on ice and subjected to membrane floatation. Proteins from pooled fractions (1 to 4 and 5 to 9) were separated by SDS-PAGE, followed by immunoblotting with antibodies against FAPP2, SPTLC1, NS5A, calnexin, or GAPDH. Numbers 1 to 4 refer to membrane (M) fractions, and numbers 5 to 8 refer to soluble (S) fractions.

    Article Snippet: Rabbit polyclonal antibody to HCV NS4B was produced by Covance (Denver, CO).

    Techniques: Infection, Confocal Microscopy, SDS Page

    Cultured cortical interneurons represent a nonoverlapping population with respect to the expression of calcium-binding proteins. Dissociated cortical neurons were grown for 21 d in vitro and fixed in 4% paraformaldehyde. Double immunocytochemistry was performed using a rabbit polyclonal antibody against PV (red) and a mouse monoclonal antibody (green) against calretinin (top), calbindin (middle), or αCaMKII (bottom) and AlexaFluor-conjugated secondary antibodies. Scale bar, 15 μm.

    Journal: The Journal of Neuroscience

    Article Title: A Specific Role for NR2A-Containing NMDA Receptors in the Maintenance of Parvalbumin and GAD67 Immunoreactivity in Cultured Interneurons

    doi: 10.1523/JNEUROSCI.4722-05.2006

    Figure Lengend Snippet: Cultured cortical interneurons represent a nonoverlapping population with respect to the expression of calcium-binding proteins. Dissociated cortical neurons were grown for 21 d in vitro and fixed in 4% paraformaldehyde. Double immunocytochemistry was performed using a rabbit polyclonal antibody against PV (red) and a mouse monoclonal antibody (green) against calretinin (top), calbindin (middle), or αCaMKII (bottom) and AlexaFluor-conjugated secondary antibodies. Scale bar, 15 μm.

    Article Snippet: For double immunostaining, the coverslips were incubated in 2% normal goat serum containing a dilution of either a mouse monoclonal antibody against parvalbumin (1:4000; Sigma, St. Louis, MO) or a dilution of a rabbit polyclonal antibody against the same protein (1:7000; Swant, Bellinzona, Switzerland), and a dilution of a rabbit polyclonal or mouse monoclonal antibodies against α calcium calmodulin-dependent protein kinase II (αCaMKII) (ABR), against calbindin or calretinin (Sigma), against GAD67, glutamate receptor 1 (GluR1), GluR2,3, metabotropic GluR1 (mGluR1), or mGluR5 (Chemicon, Temecula, CA) or against NR2A and NR2B (Invitrogen; Upstate Biotechnology, Lake Placid, NY; Santa Cruz Biotechnology, Santa Cruz, CA) for 1–2 h at 37°C.

    Techniques: Cell Culture, Expressing, Binding Assay, In Vitro, Immunocytochemistry

    Immunofluorescent dopaminergic neurons in primary cultures of rat mesencephalic neurons fixed after 12 hr of 1-μM MPP + treatment stained with a TH monoclonal mouse antibody revealed by FITC ( A ) and a rabbit polyclonal antibody recognizing activated caspase-3 (CM1) revealed by tetramethylrhodamine B isothiocyanate ( B ). Hoechst 33258 staining reveals an intact nucleus in this neuron ( C , arrow). (Bar = 20 μm.) In contrast, in a TH-positive neuron ( D ) with CM1 staining ( E ), DNA condensation assessed by Hoechst 33258 can be detected after 72 hr of MPP + treatment ( F , arrow). Note that a higher magnification was used to show DNA condensation. (Bar = 10 μm.)

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Caspase-3: A vulnerability factor and final effector in apoptotic death of dopaminergic neurons in Parkinson's disease

    doi:

    Figure Lengend Snippet: Immunofluorescent dopaminergic neurons in primary cultures of rat mesencephalic neurons fixed after 12 hr of 1-μM MPP + treatment stained with a TH monoclonal mouse antibody revealed by FITC ( A ) and a rabbit polyclonal antibody recognizing activated caspase-3 (CM1) revealed by tetramethylrhodamine B isothiocyanate ( B ). Hoechst 33258 staining reveals an intact nucleus in this neuron ( C , arrow). (Bar = 20 μm.) In contrast, in a TH-positive neuron ( D ) with CM1 staining ( E ), DNA condensation assessed by Hoechst 33258 can be detected after 72 hr of MPP + treatment ( F , arrow). Note that a higher magnification was used to show DNA condensation. (Bar = 10 μm.)

    Article Snippet: In addition, trial experiments were conducted by using a rabbit polyclonal antibody (65906E; PharMingen; 1:250, 48 hr at 4°C) raised against recombinant human caspase-3-His6 as immunogen ( ) (1:250, 48 hr at 4°C) or the CM1 antibody raised against the C terminus of the human p17 caspase-3 fragment,163 CRGTELDCGIETD175 , specifically recognizing activated (cleaved) caspase-3 ( ) (1:2,500, 48 hr at 4°C).

    Techniques: Staining

    Characterization of caspase-3 staining. ( A ) Specificity of the anti-caspase-3 p20 polyclonal rabbit antibody. Western immunoblot of caspase-3 from 50 μg of SNpc protein extracted from three control and three parkinsonian mesencephalons after SDS/PAGE. Molecular mass markers in the first lane are given in kDa and allow identification of caspase-3 protein at molecular masses of 32 kDa (including prodomain) and 30 kDa (without prodomain). ( B ) High-power photomicrograph showing cytosolic caspase-3 immunostaining of SNpc neuromelanin-containing neurons in transverse sections of control SNpc. ( C and D ) Immunofluorescent dopaminergic neurons in transverse SNpc sections of a control subject stained with a caspase-3 polyclonal rabbit antibody revealed by fluorescein ( C ) and a TH monoclonal mouse antibody revealed by rhodamine 600 ( D ). Whereas caspase-3 immunoreactivity is confined to the cytosol, TH staining can be observed in the perikarya and dendrites. The middle portion of the neuron is occupied by neuromelanin. (Bars = 30 μm.)

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Caspase-3: A vulnerability factor and final effector in apoptotic death of dopaminergic neurons in Parkinson's disease

    doi:

    Figure Lengend Snippet: Characterization of caspase-3 staining. ( A ) Specificity of the anti-caspase-3 p20 polyclonal rabbit antibody. Western immunoblot of caspase-3 from 50 μg of SNpc protein extracted from three control and three parkinsonian mesencephalons after SDS/PAGE. Molecular mass markers in the first lane are given in kDa and allow identification of caspase-3 protein at molecular masses of 32 kDa (including prodomain) and 30 kDa (without prodomain). ( B ) High-power photomicrograph showing cytosolic caspase-3 immunostaining of SNpc neuromelanin-containing neurons in transverse sections of control SNpc. ( C and D ) Immunofluorescent dopaminergic neurons in transverse SNpc sections of a control subject stained with a caspase-3 polyclonal rabbit antibody revealed by fluorescein ( C ) and a TH monoclonal mouse antibody revealed by rhodamine 600 ( D ). Whereas caspase-3 immunoreactivity is confined to the cytosol, TH staining can be observed in the perikarya and dendrites. The middle portion of the neuron is occupied by neuromelanin. (Bars = 30 μm.)

    Article Snippet: In addition, trial experiments were conducted by using a rabbit polyclonal antibody (65906E; PharMingen; 1:250, 48 hr at 4°C) raised against recombinant human caspase-3-His6 as immunogen ( ) (1:250, 48 hr at 4°C) or the CM1 antibody raised against the C terminus of the human p17 caspase-3 fragment,163 CRGTELDCGIETD175 , specifically recognizing activated (cleaved) caspase-3 ( ) (1:2,500, 48 hr at 4°C).

    Techniques: Staining, Western Blot, SDS Page, Immunostaining

    Lactosylceramide is associated with HCV NS4B protein. (A) Parental Huh7.5 and HCV Con1 (genotype 1b) replicon cells were grown for 48 h and processed for confocal microscopy with mouse monoclonal αLacCer antibody (1:500; green) and rabbit polyclonal αNS4B antibody (1:150; red). Huh7.5 cells also were infected with HCV Jc1 (MOI of 1) and processed for confocal microscopy as described above. The boxed areas represent a magnified view for colocalization (yellow) of lactosylceramide and HCV NS4B protein. (B) Huh7.5 cells were infected with HCV Jc1 (MOI of 1) as described for panel A and processed for confocal microscopy 24 h, 48 h, and 72 h postinfection. For each infection time point, confocal images were taken of 20 representative cells. The intensity of lactosylceramide pixels was calculated with the JACoP plugin in ImageJ software. Each filled circle or square (24 h; mock or Jc1 infected), upper or lower triangle (48 h; mock or Jc1 infected), diamond (72 h; mock), or open circle (72 h; Jc1 infected) represents one cell.

    Journal: Journal of Virology

    Article Title: Modulation of Hepatitis C Virus Genome Replication by Glycosphingolipids and Four-Phosphate Adaptor Protein 2

    doi: 10.1128/JVI.00970-14

    Figure Lengend Snippet: Lactosylceramide is associated with HCV NS4B protein. (A) Parental Huh7.5 and HCV Con1 (genotype 1b) replicon cells were grown for 48 h and processed for confocal microscopy with mouse monoclonal αLacCer antibody (1:500; green) and rabbit polyclonal αNS4B antibody (1:150; red). Huh7.5 cells also were infected with HCV Jc1 (MOI of 1) and processed for confocal microscopy as described above. The boxed areas represent a magnified view for colocalization (yellow) of lactosylceramide and HCV NS4B protein. (B) Huh7.5 cells were infected with HCV Jc1 (MOI of 1) as described for panel A and processed for confocal microscopy 24 h, 48 h, and 72 h postinfection. For each infection time point, confocal images were taken of 20 representative cells. The intensity of lactosylceramide pixels was calculated with the JACoP plugin in ImageJ software. Each filled circle or square (24 h; mock or Jc1 infected), upper or lower triangle (48 h; mock or Jc1 infected), diamond (72 h; mock), or open circle (72 h; Jc1 infected) represents one cell.

    Article Snippet: Rabbit polyclonal antibody to calnexin was purchased from Cell Signaling (Danvers, MA).

    Techniques: Confocal Microscopy, Infection, Software

    ). At 48 h postinfection, the cells were processed for confocal microscopy with mouse monoclonal αPI4P antibody (green). NS5A was detected via mCherry fluorescence. Alternatively, HCV Con1 replicon cells were grown for 48 h and stained with mouse monoclonal α-PI4P antibody (red) and rabbit polyclonal antibody against NS4B (green). The boxed areas are a magnified view for colocalization (yellow) of HCV NS5A or NS4B protein with PI4P. (C) Diagram of the de novo ) are two pharmacological inhibitors of UGCGC. FAPP2 is highlighted in gray and carries glucosylceramide from the cis -Golgi to the trans -Golgi network for conversion into lactosylceramide and other glycosphingolipids. CoA, coenzyme A.

    Journal: Journal of Virology

    Article Title: Modulation of Hepatitis C Virus Genome Replication by Glycosphingolipids and Four-Phosphate Adaptor Protein 2

    doi: 10.1128/JVI.00970-14

    Figure Lengend Snippet: ). At 48 h postinfection, the cells were processed for confocal microscopy with mouse monoclonal αPI4P antibody (green). NS5A was detected via mCherry fluorescence. Alternatively, HCV Con1 replicon cells were grown for 48 h and stained with mouse monoclonal α-PI4P antibody (red) and rabbit polyclonal antibody against NS4B (green). The boxed areas are a magnified view for colocalization (yellow) of HCV NS5A or NS4B protein with PI4P. (C) Diagram of the de novo ) are two pharmacological inhibitors of UGCGC. FAPP2 is highlighted in gray and carries glucosylceramide from the cis -Golgi to the trans -Golgi network for conversion into lactosylceramide and other glycosphingolipids. CoA, coenzyme A.

    Article Snippet: Rabbit polyclonal antibody to calnexin was purchased from Cell Signaling (Danvers, MA).

    Techniques: Confocal Microscopy, Fluorescence, Staining

    ) virus-infected cells were grown as described for panel A and processed for confocal microscopy with mouse monoclonal antibody against dsRNA (1: 200; red) and rabbit polyclonal αFAPP2 antibody (1:100; green). The boxed areas indicate the magnified view for colocalization (yellow color) of HCV NS5A (A) or dsRNA (B) with FAPP2 protein. (C) FAPP2 cofractionates with HCV replicase NS5A protein in the detergent-resistant membrane fraction. Con1 replicon cell lysates were left untreated or were treated with 1% NP-40 on ice and subjected to membrane floatation. Proteins from pooled fractions (1 to 4 and 5 to 9) were separated by SDS-PAGE, followed by immunoblotting with antibodies against FAPP2, SPTLC1, NS5A, calnexin, or GAPDH. Numbers 1 to 4 refer to membrane (M) fractions, and numbers 5 to 8 refer to soluble (S) fractions.

    Journal: Journal of Virology

    Article Title: Modulation of Hepatitis C Virus Genome Replication by Glycosphingolipids and Four-Phosphate Adaptor Protein 2

    doi: 10.1128/JVI.00970-14

    Figure Lengend Snippet: ) virus-infected cells were grown as described for panel A and processed for confocal microscopy with mouse monoclonal antibody against dsRNA (1: 200; red) and rabbit polyclonal αFAPP2 antibody (1:100; green). The boxed areas indicate the magnified view for colocalization (yellow color) of HCV NS5A (A) or dsRNA (B) with FAPP2 protein. (C) FAPP2 cofractionates with HCV replicase NS5A protein in the detergent-resistant membrane fraction. Con1 replicon cell lysates were left untreated or were treated with 1% NP-40 on ice and subjected to membrane floatation. Proteins from pooled fractions (1 to 4 and 5 to 9) were separated by SDS-PAGE, followed by immunoblotting with antibodies against FAPP2, SPTLC1, NS5A, calnexin, or GAPDH. Numbers 1 to 4 refer to membrane (M) fractions, and numbers 5 to 8 refer to soluble (S) fractions.

    Article Snippet: Rabbit polyclonal antibody to calnexin was purchased from Cell Signaling (Danvers, MA).

    Techniques: Infection, Confocal Microscopy, SDS Page

    Complexin 3/4 concentrates in retinal photoreceptor terminals concomitant with RIBEYE b . (A) The zpr 1/FRet 43 monoclonal antibody (red) and the pan-complexin 3/4 polyclonal (green) were also used to localize these complexins in developing retinal photoreceptors. At 2.5 dpf, retinal photoreceptors are most prominent in the ventronasal patch, where complexin 3/4 immunoreactivity appears in some photoreceptor terminals. (B) RIBEYE b (green) has also started to cluster in photoreceptor terminals (red) in the outer plexiform layer at 2.5 dpf. (C) At 3 dpf, complexin 3/4 (red) is highly expressed in zpr 1/FRet 43-positive (red) and zpr 1/FRet 43-negative photoreceptor terminals in the ventronasal patch. (D) Pleiomorphic RIBEYE b (green) expression is found at 3 dpf in zpr 1/FRet 43-positive (red) and zpr 1/FRet 43-negative photoreceptor terminals in the ventronasal patch. The inset shows a zpr 1/FRet 43-positive terminal containing curvilinear RIBEYE b immunoreactivity that may correspond to a ribbon. Scale bar = 5 μm.

    Journal: Neural Development

    Article Title: Enrichment and differential targeting of complexins 3 and 4 in ribbon-containing sensory neurons during zebrafish development

    doi: 10.1186/1749-8104-5-24

    Figure Lengend Snippet: Complexin 3/4 concentrates in retinal photoreceptor terminals concomitant with RIBEYE b . (A) The zpr 1/FRet 43 monoclonal antibody (red) and the pan-complexin 3/4 polyclonal (green) were also used to localize these complexins in developing retinal photoreceptors. At 2.5 dpf, retinal photoreceptors are most prominent in the ventronasal patch, where complexin 3/4 immunoreactivity appears in some photoreceptor terminals. (B) RIBEYE b (green) has also started to cluster in photoreceptor terminals (red) in the outer plexiform layer at 2.5 dpf. (C) At 3 dpf, complexin 3/4 (red) is highly expressed in zpr 1/FRet 43-positive (red) and zpr 1/FRet 43-negative photoreceptor terminals in the ventronasal patch. (D) Pleiomorphic RIBEYE b (green) expression is found at 3 dpf in zpr 1/FRet 43-positive (red) and zpr 1/FRet 43-negative photoreceptor terminals in the ventronasal patch. The inset shows a zpr 1/FRet 43-positive terminal containing curvilinear RIBEYE b immunoreactivity that may correspond to a ribbon. Scale bar = 5 μm.

    Article Snippet: These transiently transfected cells were stained with the mouse monoclonal anti-myc antibody (B, D, F, H, J) and a rabbit polyclonal antibody directed against mammalian complexin 4 (Synaptic Systems antibody 122402) (A, C, E, G, I). (E, F) Complexin and myc immunoreactivity, respectively, in a representative cell transfected with zf cplx4a-myc.

    Techniques: Expressing