rabbit anti β galactosidase Search Results


93
Rockland Immunochemicals anti β galactosidase
Anti β Galactosidase, supplied by Rockland Immunochemicals, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Bio-Rad rabbit anti β galactosidase antibody
Immunohistochemical detection of vector-mediated transgene <t>expression</t> <t>(β-galactosidase</t> or luciferase; a1 to a6 and d1 to d6), macrophage activation (ED1; b1 to b6 and e1 to e6), and vector diffusion (hexon; c1 to c6) in 40-μm brain sections 3 days after injection into the brain of 1 × 109 (a to c) or 5 × 107 (d to e) particles of vector. Scale bars: panels a6, b6, and d6, 1 mm; c6, 250 μm; e6, 500 μm.
Rabbit Anti β Galactosidase Antibody, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 93 stars, based on 1 article reviews
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88
Rockland Immunochemicals rabbit polyclonal anti β galactosidase
Immunohistochemical detection of vector-mediated transgene <t>expression</t> <t>(β-galactosidase</t> or luciferase; a1 to a6 and d1 to d6), macrophage activation (ED1; b1 to b6 and e1 to e6), and vector diffusion (hexon; c1 to c6) in 40-μm brain sections 3 days after injection into the brain of 1 × 109 (a to c) or 5 × 107 (d to e) particles of vector. Scale bars: panels a6, b6, and d6, 1 mm; c6, 250 μm; e6, 500 μm.
Rabbit Polyclonal Anti β Galactosidase, supplied by Rockland Immunochemicals, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/rabbit+anti+%CE%B2+galactosidase/Beta+Galactosidase+Antibody+Biotin+Conjugated/pmc05533775-206-43-47
Average 88 stars, based on 1 article reviews
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Organon Teknika Corporation LLC rabbit polyclonal anti-β-galactosidase antiserum
Subcellular localization of <t>β-gal–Vpr</t> fusion proteins in HeLa cells. Monolayers were transfected with wild-type (A) or A30P mutant (C) expression vectors and analyzed by indirect immunofluorescence with a <t>β-galactosidase-specific</t> antiserum. The phase-contrast analyses are also shown (B and D).
Rabbit Polyclonal Anti β Galactosidase Antiserum, supplied by Organon Teknika Corporation LLC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/rabbit+anti+%CE%B2+galactosidase/rabbit+polyclonal+anti+%CE%B2+galactosidase+antiserum/pmc00110405-152-30-34
Average 90 stars, based on 1 article reviews
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ICN Biomedicals rabbit anti-β-galactosidase
Subcellular localization of <t>β-gal–Vpr</t> fusion proteins in HeLa cells. Monolayers were transfected with wild-type (A) or A30P mutant (C) expression vectors and analyzed by indirect immunofluorescence with a <t>β-galactosidase-specific</t> antiserum. The phase-contrast analyses are also shown (B and D).
Rabbit Anti β Galactosidase, supplied by ICN Biomedicals, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/rabbit+anti+%CE%B2+galactosidase/rabbit+anti+%CE%B2+galactosidase/pmc10397273-306-28-30
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Promega rabbit anti-β-gal
Subcellular localization of <t>β-gal–Vpr</t> fusion proteins in HeLa cells. Monolayers were transfected with wild-type (A) or A30P mutant (C) expression vectors and analyzed by indirect immunofluorescence with a <t>β-galactosidase-specific</t> antiserum. The phase-contrast analyses are also shown (B and D).
Rabbit Anti β Gal, supplied by Promega, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/rabbit+anti+%CE%B2+galactosidase/rabbit+anti+%CE%B2+galactosidase/pmc02653810-70-7-11
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Cortex Biochem Inc rabbit anti-galactosidase
Subcellular localization of <t>β-gal–Vpr</t> fusion proteins in HeLa cells. Monolayers were transfected with wild-type (A) or A30P mutant (C) expression vectors and analyzed by indirect immunofluorescence with a <t>β-galactosidase-specific</t> antiserum. The phase-contrast analyses are also shown (B and D).
Rabbit Anti Galactosidase, supplied by Cortex Biochem Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/rabbit+anti+%CE%B2+galactosidase/rabbit+anti+%CE%B2+galactosidase/10__1523_slash_JNEUROSCI__23___13___05919__2003_ascii32_-82-3-8
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Cortex Biochem Inc anti-beta-galactosidase rabbit polyclonal antibody cr7001rp1
Subcellular localization of <t>β-gal–Vpr</t> fusion proteins in HeLa cells. Monolayers were transfected with wild-type (A) or A30P mutant (C) expression vectors and analyzed by indirect immunofluorescence with a <t>β-galactosidase-specific</t> antiserum. The phase-contrast analyses are also shown (B and D).
Anti Beta Galactosidase Rabbit Polyclonal Antibody Cr7001rp1, supplied by Cortex Biochem Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/rabbit+anti+%CE%B2+galactosidase/anti+beta+galactosidase+rabbit+polyclonal+antibody+cr7001rp1/10__1074_slash_jbc__m500059200-92-27-33
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Promega rabbit anti–β-galactosidase polyclonal antiserum
Subcellular localization of <t>β-gal–Vpr</t> fusion proteins in HeLa cells. Monolayers were transfected with wild-type (A) or A30P mutant (C) expression vectors and analyzed by indirect immunofluorescence with a <t>β-galactosidase-specific</t> antiserum. The phase-contrast analyses are also shown (B and D).
Rabbit Anti–β Galactosidase Polyclonal Antiserum, supplied by Promega, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/rabbit+anti+%CE%B2+galactosidase/rabbit+anti+%CE%B2+galactosidase+polyclonal+antiserum/pmc02132482-28-0-6
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Corning Life Sciences polyclonal rabbit anti– β-galactosidase antibody
Subcellular localization of <t>β-gal–Vpr</t> fusion proteins in HeLa cells. Monolayers were transfected with wild-type (A) or A30P mutant (C) expression vectors and analyzed by indirect immunofluorescence with a <t>β-galactosidase-specific</t> antiserum. The phase-contrast analyses are also shown (B and D).
Polyclonal Rabbit Anti– β Galactosidase Antibody, supplied by Corning Life Sciences, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/rabbit+anti+%CE%B2+galactosidase/polyclonal+rabbit+anti++%CE%B2+galactosidase+antibody/pm11772882-66-9-14
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Promega monoclonal rabbit anti-β-galactosidase (β-gal
Subcellular localization of <t>β-gal–Vpr</t> fusion proteins in HeLa cells. Monolayers were transfected with wild-type (A) or A30P mutant (C) expression vectors and analyzed by indirect immunofluorescence with a <t>β-galactosidase-specific</t> antiserum. The phase-contrast analyses are also shown (B and D).
Monoclonal Rabbit Anti β Galactosidase (β Gal, supplied by Promega, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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MBL Life science anti- β-galactosidase pm049
Antibodies’ source, dilution, antigen retrieval, and heating condition.
Anti β Galactosidase Pm049, supplied by MBL Life science, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/rabbit+anti+%CE%B2+galactosidase/rabbit+anti+%CE%B2+galactosidase/pmc10922004-9-5-6
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Image Search Results


Immunohistochemical detection of vector-mediated transgene expression (β-galactosidase or luciferase; a1 to a6 and d1 to d6), macrophage activation (ED1; b1 to b6 and e1 to e6), and vector diffusion (hexon; c1 to c6) in 40-μm brain sections 3 days after injection into the brain of 1 × 109 (a to c) or 5 × 107 (d to e) particles of vector. Scale bars: panels a6, b6, and d6, 1 mm; c6, 250 μm; e6, 500 μm.

Journal:

Article Title: Adenovirus Binding to the Coxsackievirus and Adenovirus Receptor or Integrins Is Not Required To Elicit Brain Inflammation but Is Necessary To Transduce Specific Neural Cell Types

doi: 10.1128/JVI.76.7.3452-3460.2002

Figure Lengend Snippet: Immunohistochemical detection of vector-mediated transgene expression (β-galactosidase or luciferase; a1 to a6 and d1 to d6), macrophage activation (ED1; b1 to b6 and e1 to e6), and vector diffusion (hexon; c1 to c6) in 40-μm brain sections 3 days after injection into the brain of 1 × 109 (a to c) or 5 × 107 (d to e) particles of vector. Scale bars: panels a6, b6, and d6, 1 mm; c6, 250 μm; e6, 500 μm.

Article Snippet: Fluorescent double labeling of cell types transduced by AdZ versus AdZF* was performed on 20-μm-thick brain sections, as described in reference 27 , by using rabbit anti-β-galactosidase antibody (1:750; a kind gift of R. Goya, School of Medicine, University of La Plata, Argentina), mouse anti-CNP (2′,3′-cyclic nucleotide 3′-phosphodiesterase, a cytoplasmic protein expressed exclusively by oligodendrocytes; 1:1,000; Promega), and mouse anti-ED1 (activated macrophages, 1:1,000; Serotec) as primary antibodies.

Techniques: Immunohistochemical staining, Plasmid Preparation, Expressing, Luciferase, Activation Assay, Diffusion-based Assay, Injection

Immunohistochemical detection of the transgene product β-galactosidase in 40-μm brain sections from animals intrastriatally injected with AdZ (a to e) or AdZF* (f to j). Differences in the morphology of cell types transduced by AdZ versus AdZF* were clearly visible, particularly at high magnification in the corpus callosum (a versus f) and striatum (e and j). Scale bars: panels a and f, 50 μm; b and g, 100 μm; c and h, 1 mm; d and i, 200 μm; e and j, 100 μm.

Journal:

Article Title: Adenovirus Binding to the Coxsackievirus and Adenovirus Receptor or Integrins Is Not Required To Elicit Brain Inflammation but Is Necessary To Transduce Specific Neural Cell Types

doi: 10.1128/JVI.76.7.3452-3460.2002

Figure Lengend Snippet: Immunohistochemical detection of the transgene product β-galactosidase in 40-μm brain sections from animals intrastriatally injected with AdZ (a to e) or AdZF* (f to j). Differences in the morphology of cell types transduced by AdZ versus AdZF* were clearly visible, particularly at high magnification in the corpus callosum (a versus f) and striatum (e and j). Scale bars: panels a and f, 50 μm; b and g, 100 μm; c and h, 1 mm; d and i, 200 μm; e and j, 100 μm.

Article Snippet: Fluorescent double labeling of cell types transduced by AdZ versus AdZF* was performed on 20-μm-thick brain sections, as described in reference 27 , by using rabbit anti-β-galactosidase antibody (1:750; a kind gift of R. Goya, School of Medicine, University of La Plata, Argentina), mouse anti-CNP (2′,3′-cyclic nucleotide 3′-phosphodiesterase, a cytoplasmic protein expressed exclusively by oligodendrocytes; 1:1,000; Promega), and mouse anti-ED1 (activated macrophages, 1:1,000; Serotec) as primary antibodies.

Techniques: Immunohistochemical staining, Injection

Immunohistochemical colocalization of β-galactosidase expression with the oligodendrocyte marker CNP (a and b) or the marker of activated macrophages ED1 (c and d) in 20-μm sections from brains injected with AdZ (a and c) or AdZF* (b and d). Scale bars (shown in β-galactosidase panels), 50 μm.

Journal:

Article Title: Adenovirus Binding to the Coxsackievirus and Adenovirus Receptor or Integrins Is Not Required To Elicit Brain Inflammation but Is Necessary To Transduce Specific Neural Cell Types

doi: 10.1128/JVI.76.7.3452-3460.2002

Figure Lengend Snippet: Immunohistochemical colocalization of β-galactosidase expression with the oligodendrocyte marker CNP (a and b) or the marker of activated macrophages ED1 (c and d) in 20-μm sections from brains injected with AdZ (a and c) or AdZF* (b and d). Scale bars (shown in β-galactosidase panels), 50 μm.

Article Snippet: Fluorescent double labeling of cell types transduced by AdZ versus AdZF* was performed on 20-μm-thick brain sections, as described in reference 27 , by using rabbit anti-β-galactosidase antibody (1:750; a kind gift of R. Goya, School of Medicine, University of La Plata, Argentina), mouse anti-CNP (2′,3′-cyclic nucleotide 3′-phosphodiesterase, a cytoplasmic protein expressed exclusively by oligodendrocytes; 1:1,000; Promega), and mouse anti-ED1 (activated macrophages, 1:1,000; Serotec) as primary antibodies.

Techniques: Immunohistochemical staining, Expressing, Marker, Injection

Subcellular localization of β-gal–Vpr fusion proteins in HeLa cells. Monolayers were transfected with wild-type (A) or A30P mutant (C) expression vectors and analyzed by indirect immunofluorescence with a β-galactosidase-specific antiserum. The phase-contrast analyses are also shown (B and D).

Journal:

Article Title: Interaction of the Human Immunodeficiency Virus Type 1 Vpr Protein with the Nuclear Pore Complex

doi:

Figure Lengend Snippet: Subcellular localization of β-gal–Vpr fusion proteins in HeLa cells. Monolayers were transfected with wild-type (A) or A30P mutant (C) expression vectors and analyzed by indirect immunofluorescence with a β-galactosidase-specific antiserum. The phase-contrast analyses are also shown (B and D).

Article Snippet: For single-label analyses, the Vpr-Myc, MBP-Vpr, and β-gal–Vpr proteins were detected, respectively, with the Myc-specific monoclonal antibody 9E10 ( 19 ), a rabbit polyclonal anti-MBP antiserum (U.S. Biochemical), and a rabbit polyclonal anti-β-galactosidase antiserum (Organon Teknika).

Techniques: Transfection, Mutagenesis, Expressing, Immunofluorescence

Colocalization of wild-type β-gal–Vpr and importin-β at NPCs. Transfected HeLa cells were subjected to double-label immunofluorescence with primary antibodies specific for β-galactosidase (A) or β-importin (B) and analyzed by laser-scanning confocal microscopy. The superimposed images are shown (dual [C]) together with the corresponding differential interference contrast image (DIC [D]).

Journal:

Article Title: Interaction of the Human Immunodeficiency Virus Type 1 Vpr Protein with the Nuclear Pore Complex

doi:

Figure Lengend Snippet: Colocalization of wild-type β-gal–Vpr and importin-β at NPCs. Transfected HeLa cells were subjected to double-label immunofluorescence with primary antibodies specific for β-galactosidase (A) or β-importin (B) and analyzed by laser-scanning confocal microscopy. The superimposed images are shown (dual [C]) together with the corresponding differential interference contrast image (DIC [D]).

Article Snippet: For single-label analyses, the Vpr-Myc, MBP-Vpr, and β-gal–Vpr proteins were detected, respectively, with the Myc-specific monoclonal antibody 9E10 ( 19 ), a rabbit polyclonal anti-MBP antiserum (U.S. Biochemical), and a rabbit polyclonal anti-β-galactosidase antiserum (Organon Teknika).

Techniques: Transfection, Immunofluorescence, Confocal Microscopy

Antibodies’ source, dilution, antigen retrieval, and heating condition.

Journal: Frontiers in Molecular Biosciences

Article Title: Diosgenin alleviates D-galactose-induced oxidative stress in rats’ brain and liver targeting aging and apoptotic marker genes

doi: 10.3389/fmolb.2024.1303379

Figure Lengend Snippet: Antibodies’ source, dilution, antigen retrieval, and heating condition.

Article Snippet: Rabbit polyclonal anti- β-galactosidase , (PM049, MBL, WOBURN, MA, United States) , 1:100 , 10 mM citrate buffer (pH 6.0) , 105°C, 20 min.

Techniques: