putative new polyclonal antibody Search Results


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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).
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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).
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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).
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MD Biosciences rabbit anti-rat polyclonal igg fibronectin
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).
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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).
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Biomeda corporation outer membrane proteins 18 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).
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US Biological Life Sciences antibody rabbit polyclonal anti-human l-pgds
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).
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GeneTex rabbit polyclonal agrin ab 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).
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Becton Dickinson polyclonal fitc-conjugated rabbit anti-mouse inos
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).
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Image Search Results


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