hrp conjugate Bio Rad Search Results


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  • 99
    Thermo Fisher hrp conjugated secondary antibodies
    Hrp Conjugated Secondary Antibodies, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 6418 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Bio-Rad appropriate hrp conjugated anti mouse bio rad
    Appropriate Hrp Conjugated Anti Mouse Bio Rad, supplied by Bio-Rad, 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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    99
    Bio-Rad hrp substrate bio rad
    Transiently expressed HCF-1 protein promotes the synthesis of NPV DNA and proteins in non-permissive Tn368 cells. Tn368 cells were transfected with 2 μg of pFBD/luc (Luc) or pFBD/hcf-1 (HCF-1) DNA, which express luciferase or HCF-1 protein, respectively, under control of the heat shock protein 70 promoter ( hsp70 pro). At 24 h post-transfection, the transfected cells were heat-shocked at 42 °C for 30 min, incubated for 6 h at 28 °C, and were then infected with HycuMNPV (Hycu), OpMNPV (Op), BmNPV (Bm) and LdMNPV (Ld) at MOIs of 10, 50, 10 and 3, respectively. ( a ) Schematic representation of the plasmids pFBD/luc and pFBD/hcf-1 used in these experiments. ( b ) Microscopic images of Tn368 cells at 72 h post-infection. The arrowheads indicate polyhedra-containing cells. Scale bar, 50 μm. ( c ) BV yields in virus-infected Tn368 cells at 72 h post-infection (pi). BV titers were determined by a plaque assay using SpIm cells for HycuMNPV, BM-N cells for BmNPV and Ld652Y cells for OpMNPV and LdMNPV. The vertical bars represent the standard deviations of the averages from three determinations. ( d ) Viral DNA production at 24 h post-infection. Viral DNA was quantified by qPCR. The vertical bars represent the standard deviations of the averages from three determinations. ( e ) Immunoblot analysis of VP39 and polyhedrin (Polh) proteins at 72 h post-infection. Polypeptides from infected Tn368 cells were resolved on 12% SDS-polyacrylamide gels and transferred onto Immobilon-P (for VP39 protein) or nitrocellulose membranes (for polyhedrin). VP39 protein was probed using anti-BmNPV/AcMNPV VP39 polyclonal antibody and visualized with <t>ECL</t> Select Western Blotting Detection Reagent. Polyhedrin protein was probed with anti-BmNPV polyhedrin polyclonal antibody and visualized using a <t>HRP</t> Conjugate Substrate Kit. ( f ) Immunoblot analysis of luciferase and HCF-1 proteins in infected Tn368 cells. Luciferase and HCF-1 proteins were probed by anti-HA monoclonal antibody and visualized using ECL Western Blotting Detection Reagent and ECL Select Western Blotting Detection Reagent, respectively. In panels ( e ) and ( f ), polypeptides equivalent to 1 × 10 5 cells were analyzed in each lane.
    Hrp Substrate Bio Rad, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 44 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Bio-Rad hrp avidin
    AADA hydrolyzes soluble and insoluble carboxylesters. Twenty micrograms of membrane protein prepared from McA cells stably transfected with an empty pCIneo vector, FLAG-tagged mouse AADA, or human TGH cDNAs were incubated with pNP-acetate (A) or 4-MUH (B). The release of pNP was monitored at 405 nm and that of 4-umbelliferyl at 460 nm. The results are presented as an average from triplicate measurements. C: Hydrolysis of microsomal lipids. Cells were incubated with radiolabeled oleic acid, and microsomes were isolated and incubated for 4 h as described in Materials and Methods. Lipids were extracted and resolved on TLC plates, and radioactivity was determined by scintillation counting. Data (mean ± SD) from three separate experiments performed in triplicate are presented with radioactivity in DG in pNeo microsomes at time 0 set as 100%. Equal amounts of microsomal protein were used for the assay. The actual starting dpm in microsomal lipid fractions at time 0 were 22,000–25,000 for PC, 12,000–18,000 for TG, and 1,500–2,300 for DG. D: Thirty micrograms of total cellular membrane proteins from McA cells stably transfected with pCI-neo, A13, A23, and human TGH were either not treated (pNeo-NT) or treated with FP-biotin, resolved in SDS-PAGE, and transferred to nitrocellulose membrane, and <t>biotinylated</t> proteins were visualized with <t>streptavidin-HRP.</t> Asterisks indicate other potential endogenous serine hydrolases present in McA cells.
    Hrp Avidin, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 31 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    hrp  (Bio-Rad)
    99
    Bio-Rad hrp
    dE2F expression correlates with E2F activity. A is at a lower magnification than panels B–D . ( A ) β-Galactosidase staining of egg chambers from dE2F rm729 /+, a dE2F enhancer trap line in which the expression of β-galactosidase profiles the level of dE2F ). A stage-9 egg chamber is embedded between two stage-10 egg chambers. The β-galactosidase reporter is induced at stage 10 in all of the follicle cells of the egg chamber. This induction correlates with the transition to amplification in the follicle cells. The level of β-galactosidase is highest in the follicle cells covering the anterior region of the oocyte, correlating with a gradient of <t>BrdU</t> incorporation from anterior to posterior in the follicle cells of the egg chamber (data not shown). The small blue cells are the follicle cells (short arrow); the larger cells are nurse cells (large arrow). ( B–D ). The antibody staining was detected by a <t>HRP</t> reaction, and a field of follicle cells is shown in each panel at the same magnification. ( B ) In a stage-9 (and earlier stages) wild-type egg chambers some follicle cells are positive for dE2F staining and others are not. Note that even in the follicle cells that show dE2F expression, the levels of dE2F protein are low. ( C ) In wild-type stage-10 follicle cells there is an increase in the levels of dE2F protein in all the follicle cells. ( D ) dE2F protein is also detected in dE2F i1 mutant follicle cells. The same staining pattern was observed for the dE2F i2 and dDP a1 mutant.
    Hrp, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 891 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Bio-Rad hrp protein g
    dE2F expression correlates with E2F activity. A is at a lower magnification than panels B–D . ( A ) β-Galactosidase staining of egg chambers from dE2F rm729 /+, a dE2F enhancer trap line in which the expression of β-galactosidase profiles the level of dE2F ). A stage-9 egg chamber is embedded between two stage-10 egg chambers. The β-galactosidase reporter is induced at stage 10 in all of the follicle cells of the egg chamber. This induction correlates with the transition to amplification in the follicle cells. The level of β-galactosidase is highest in the follicle cells covering the anterior region of the oocyte, correlating with a gradient of <t>BrdU</t> incorporation from anterior to posterior in the follicle cells of the egg chamber (data not shown). The small blue cells are the follicle cells (short arrow); the larger cells are nurse cells (large arrow). ( B–D ). The antibody staining was detected by a <t>HRP</t> reaction, and a field of follicle cells is shown in each panel at the same magnification. ( B ) In a stage-9 (and earlier stages) wild-type egg chambers some follicle cells are positive for dE2F staining and others are not. Note that even in the follicle cells that show dE2F expression, the levels of dE2F protein are low. ( C ) In wild-type stage-10 follicle cells there is an increase in the levels of dE2F protein in all the follicle cells. ( D ) dE2F protein is also detected in dE2F i1 mutant follicle cells. The same staining pattern was observed for the dE2F i2 and dDP a1 mutant.
    Hrp Protein G, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 31 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Bio-Rad antibody goat anti rabbit igg h l hrp conjugate bio rad
    dE2F expression correlates with E2F activity. A is at a lower magnification than panels B–D . ( A ) β-Galactosidase staining of egg chambers from dE2F rm729 /+, a dE2F enhancer trap line in which the expression of β-galactosidase profiles the level of dE2F ). A stage-9 egg chamber is embedded between two stage-10 egg chambers. The β-galactosidase reporter is induced at stage 10 in all of the follicle cells of the egg chamber. This induction correlates with the transition to amplification in the follicle cells. The level of β-galactosidase is highest in the follicle cells covering the anterior region of the oocyte, correlating with a gradient of <t>BrdU</t> incorporation from anterior to posterior in the follicle cells of the egg chamber (data not shown). The small blue cells are the follicle cells (short arrow); the larger cells are nurse cells (large arrow). ( B–D ). The antibody staining was detected by a <t>HRP</t> reaction, and a field of follicle cells is shown in each panel at the same magnification. ( B ) In a stage-9 (and earlier stages) wild-type egg chambers some follicle cells are positive for dE2F staining and others are not. Note that even in the follicle cells that show dE2F expression, the levels of dE2F protein are low. ( C ) In wild-type stage-10 follicle cells there is an increase in the levels of dE2F protein in all the follicle cells. ( D ) dE2F protein is also detected in dE2F i1 mutant follicle cells. The same staining pattern was observed for the dE2F i2 and dDP a1 mutant.
    Antibody Goat Anti Rabbit Igg H L Hrp Conjugate Bio Rad, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Bio-Rad hrp conjugated goat anti mouse bio rad laboratories hercules
    dE2F expression correlates with E2F activity. A is at a lower magnification than panels B–D . ( A ) β-Galactosidase staining of egg chambers from dE2F rm729 /+, a dE2F enhancer trap line in which the expression of β-galactosidase profiles the level of dE2F ). A stage-9 egg chamber is embedded between two stage-10 egg chambers. The β-galactosidase reporter is induced at stage 10 in all of the follicle cells of the egg chamber. This induction correlates with the transition to amplification in the follicle cells. The level of β-galactosidase is highest in the follicle cells covering the anterior region of the oocyte, correlating with a gradient of <t>BrdU</t> incorporation from anterior to posterior in the follicle cells of the egg chamber (data not shown). The small blue cells are the follicle cells (short arrow); the larger cells are nurse cells (large arrow). ( B–D ). The antibody staining was detected by a <t>HRP</t> reaction, and a field of follicle cells is shown in each panel at the same magnification. ( B ) In a stage-9 (and earlier stages) wild-type egg chambers some follicle cells are positive for dE2F staining and others are not. Note that even in the follicle cells that show dE2F expression, the levels of dE2F protein are low. ( C ) In wild-type stage-10 follicle cells there is an increase in the levels of dE2F protein in all the follicle cells. ( D ) dE2F protein is also detected in dE2F i1 mutant follicle cells. The same staining pattern was observed for the dE2F i2 and dDP a1 mutant.
    Hrp Conjugated Goat Anti Mouse Bio Rad Laboratories Hercules, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Bio-Rad hrp conjugate bio rad clarity western ecl substrate
    dE2F expression correlates with E2F activity. A is at a lower magnification than panels B–D . ( A ) β-Galactosidase staining of egg chambers from dE2F rm729 /+, a dE2F enhancer trap line in which the expression of β-galactosidase profiles the level of dE2F ). A stage-9 egg chamber is embedded between two stage-10 egg chambers. The β-galactosidase reporter is induced at stage 10 in all of the follicle cells of the egg chamber. This induction correlates with the transition to amplification in the follicle cells. The level of β-galactosidase is highest in the follicle cells covering the anterior region of the oocyte, correlating with a gradient of <t>BrdU</t> incorporation from anterior to posterior in the follicle cells of the egg chamber (data not shown). The small blue cells are the follicle cells (short arrow); the larger cells are nurse cells (large arrow). ( B–D ). The antibody staining was detected by a <t>HRP</t> reaction, and a field of follicle cells is shown in each panel at the same magnification. ( B ) In a stage-9 (and earlier stages) wild-type egg chambers some follicle cells are positive for dE2F staining and others are not. Note that even in the follicle cells that show dE2F expression, the levels of dE2F protein are low. ( C ) In wild-type stage-10 follicle cells there is an increase in the levels of dE2F protein in all the follicle cells. ( D ) dE2F protein is also detected in dE2F i1 mutant follicle cells. The same staining pattern was observed for the dE2F i2 and dDP a1 mutant.
    Hrp Conjugate Bio Rad Clarity Western Ecl Substrate, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    Bio-Rad streptactin hrp conjugate
    dE2F expression correlates with E2F activity. A is at a lower magnification than panels B–D . ( A ) β-Galactosidase staining of egg chambers from dE2F rm729 /+, a dE2F enhancer trap line in which the expression of β-galactosidase profiles the level of dE2F ). A stage-9 egg chamber is embedded between two stage-10 egg chambers. The β-galactosidase reporter is induced at stage 10 in all of the follicle cells of the egg chamber. This induction correlates with the transition to amplification in the follicle cells. The level of β-galactosidase is highest in the follicle cells covering the anterior region of the oocyte, correlating with a gradient of <t>BrdU</t> incorporation from anterior to posterior in the follicle cells of the egg chamber (data not shown). The small blue cells are the follicle cells (short arrow); the larger cells are nurse cells (large arrow). ( B–D ). The antibody staining was detected by a <t>HRP</t> reaction, and a field of follicle cells is shown in each panel at the same magnification. ( B ) In a stage-9 (and earlier stages) wild-type egg chambers some follicle cells are positive for dE2F staining and others are not. Note that even in the follicle cells that show dE2F expression, the levels of dE2F protein are low. ( C ) In wild-type stage-10 follicle cells there is an increase in the levels of dE2F protein in all the follicle cells. ( D ) dE2F protein is also detected in dE2F i1 mutant follicle cells. The same staining pattern was observed for the dE2F i2 and dDP a1 mutant.
    Streptactin Hrp Conjugate, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 149 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    87
    Bio-Rad antirabbit hrp conjugate
    Multimerization of SAA. Human recombinant SAA was blotted onto nitrocellulose membranes and overlayed with polyclonal antibodies against synthetic SAA human peptides ranging from the indicated amino acid sequences: lane 1: SAA1–17, lane 2: SAA14–30, lane 3: SAA27–44, lane 4: SAA40–63, lane 5: SAA59–72, lane 6: SAA68–84, lane 7: SAA79–94, and lane 8: SAA 89–104. <t>HRP-labeled</t> secondary goat <t>antirabbit</t> antibody was used for secondary incubation followed by luminol and chemiluminescent detection. The SAA monomer at around 12 kD is indicated.
    Antirabbit Hrp Conjugate, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 87/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Bio-Rad hrp protein a
    Multimerization of SAA. Human recombinant SAA was blotted onto nitrocellulose membranes and overlayed with polyclonal antibodies against synthetic SAA human peptides ranging from the indicated amino acid sequences: lane 1: SAA1–17, lane 2: SAA14–30, lane 3: SAA27–44, lane 4: SAA40–63, lane 5: SAA59–72, lane 6: SAA68–84, lane 7: SAA79–94, and lane 8: SAA 89–104. <t>HRP-labeled</t> secondary goat <t>antirabbit</t> antibody was used for secondary incubation followed by luminol and chemiluminescent detection. The SAA monomer at around 12 kD is indicated.
    Hrp Protein A, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Bio-Rad streptacin hrp conjugate
    Multimerization of SAA. Human recombinant SAA was blotted onto nitrocellulose membranes and overlayed with polyclonal antibodies against synthetic SAA human peptides ranging from the indicated amino acid sequences: lane 1: SAA1–17, lane 2: SAA14–30, lane 3: SAA27–44, lane 4: SAA40–63, lane 5: SAA59–72, lane 6: SAA68–84, lane 7: SAA79–94, and lane 8: SAA 89–104. <t>HRP-labeled</t> secondary goat <t>antirabbit</t> antibody was used for secondary incubation followed by luminol and chemiluminescent detection. The SAA monomer at around 12 kD is indicated.
    Streptacin Hrp Conjugate, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 94/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Bio-Rad bio rad goat anti mouse
    Multimerization of SAA. Human recombinant SAA was blotted onto nitrocellulose membranes and overlayed with polyclonal antibodies against synthetic SAA human peptides ranging from the indicated amino acid sequences: lane 1: SAA1–17, lane 2: SAA14–30, lane 3: SAA27–44, lane 4: SAA40–63, lane 5: SAA59–72, lane 6: SAA68–84, lane 7: SAA79–94, and lane 8: SAA 89–104. <t>HRP-labeled</t> secondary goat <t>antirabbit</t> antibody was used for secondary incubation followed by luminol and chemiluminescent detection. The SAA monomer at around 12 kD is indicated.
    Bio Rad Goat Anti Mouse, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Bio-Rad hrp conjugated
    Western Blotting of heart tissue showing a strong protein band at about 80 kD indicating the presence of an octopamine receptor. Pan TAAR 1° antibodies (goat polyclonal) and <t>HRP-conjugated</t> <t>2°</t> antibodies were used. The right lane contains
    Hrp Conjugated, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 95/100, based on 117 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Bio-Rad eb a2 conjugated to hrp all from platelia aspergillus eia kit bio rad
    Western Blotting of heart tissue showing a strong protein band at about 80 kD indicating the presence of an octopamine receptor. Pan TAAR 1° antibodies (goat polyclonal) and <t>HRP-conjugated</t> <t>2°</t> antibodies were used. The right lane contains
    Eb A2 Conjugated To Hrp All From Platelia Aspergillus Eia Kit Bio Rad, supplied by Bio-Rad, 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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    99
    Bio-Rad hrp enzyme
    Western Blotting of heart tissue showing a strong protein band at about 80 kD indicating the presence of an octopamine receptor. Pan TAAR 1° antibodies (goat polyclonal) and <t>HRP-conjugated</t> <t>2°</t> antibodies were used. The right lane contains
    Hrp Enzyme, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Bio-Rad streptavidin hrp conjugate
    GECX-MS to capture and identify affibody binding to Z in E. coli . a Structure of the affibody–Z protein complex (PDB ID 1LP1), with two proximal sites, Lys7 in the affibody and Glu24 in the Z protein, highlighted. b Western blot of cell lysate of cells co-expressing MPB-Z(24BprY) with affibody(7Cys) and of cells co-expressing MPB-Z(24EB3) with affibody(7Cys). The cross-linked MBP–Z/affibody complex is indicated with a star. c SDS-PAGE of proteins His-tag purified from cells co-expressing affibody(7Cys) with MPB-Z(24BprY), or with MBP-Z(24EB3). In the absence of Uaa, background suppression of the TAG codon at site 24 resulted in small amount of full-length MBP–Z. d Mass spectrum of the cross-linked peptide between affibody(7Cys) and MBP-Z(24BprY). U represents BprY in the peptide sequence. e His-tag purified affibody(7Cys)/MBP-Z(24EB3) was labeled with biotin via CuAAC and then western blotted with <t>streptavidin-HRP</t> conjugate. f Biotin based enrichment of cross-linked affibody(7Cys)/MBP-Z(24EB3). g Mass spectrum of the cross-linked peptide between affibody(7Cys) and MBP-Z(24EB3) before biotin labeling. U represents EB3 in the peptide sequence. h Mass spectrum of biotinylated cross-linked peptide between affibody(7Cys) and MBP-Z(24EB3). U represents EB3 in the peptide sequence. i Extracted ion chromatography of biotinylated cross-linked peptide from input sample of biotin enrichment. j Extracted ion chromatography of biotinylated cross-linked peptide from elute sample of biotin enrichment. RT retention time, MA peak area, MH peak height
    Streptavidin Hrp Conjugate, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 93/100, based on 24 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    97
    Bio-Rad precision protein streptactin hrp conjugate
    GECX-MS to capture and identify affibody binding to Z in E. coli . a Structure of the affibody–Z protein complex (PDB ID 1LP1), with two proximal sites, Lys7 in the affibody and Glu24 in the Z protein, highlighted. b Western blot of cell lysate of cells co-expressing MPB-Z(24BprY) with affibody(7Cys) and of cells co-expressing MPB-Z(24EB3) with affibody(7Cys). The cross-linked MBP–Z/affibody complex is indicated with a star. c SDS-PAGE of proteins His-tag purified from cells co-expressing affibody(7Cys) with MPB-Z(24BprY), or with MBP-Z(24EB3). In the absence of Uaa, background suppression of the TAG codon at site 24 resulted in small amount of full-length MBP–Z. d Mass spectrum of the cross-linked peptide between affibody(7Cys) and MBP-Z(24BprY). U represents BprY in the peptide sequence. e His-tag purified affibody(7Cys)/MBP-Z(24EB3) was labeled with biotin via CuAAC and then western blotted with <t>streptavidin-HRP</t> conjugate. f Biotin based enrichment of cross-linked affibody(7Cys)/MBP-Z(24EB3). g Mass spectrum of the cross-linked peptide between affibody(7Cys) and MBP-Z(24EB3) before biotin labeling. U represents EB3 in the peptide sequence. h Mass spectrum of biotinylated cross-linked peptide between affibody(7Cys) and MBP-Z(24EB3). U represents EB3 in the peptide sequence. i Extracted ion chromatography of biotinylated cross-linked peptide from input sample of biotin enrichment. j Extracted ion chromatography of biotinylated cross-linked peptide from elute sample of biotin enrichment. RT retention time, MA peak area, MH peak height
    Precision Protein Streptactin Hrp Conjugate, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 97/100, based on 234 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Bio-Rad hrp conjugated streptavidin
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    Image Search Results


    Transiently expressed HCF-1 protein promotes the synthesis of NPV DNA and proteins in non-permissive Tn368 cells. Tn368 cells were transfected with 2 μg of pFBD/luc (Luc) or pFBD/hcf-1 (HCF-1) DNA, which express luciferase or HCF-1 protein, respectively, under control of the heat shock protein 70 promoter ( hsp70 pro). At 24 h post-transfection, the transfected cells were heat-shocked at 42 °C for 30 min, incubated for 6 h at 28 °C, and were then infected with HycuMNPV (Hycu), OpMNPV (Op), BmNPV (Bm) and LdMNPV (Ld) at MOIs of 10, 50, 10 and 3, respectively. ( a ) Schematic representation of the plasmids pFBD/luc and pFBD/hcf-1 used in these experiments. ( b ) Microscopic images of Tn368 cells at 72 h post-infection. The arrowheads indicate polyhedra-containing cells. Scale bar, 50 μm. ( c ) BV yields in virus-infected Tn368 cells at 72 h post-infection (pi). BV titers were determined by a plaque assay using SpIm cells for HycuMNPV, BM-N cells for BmNPV and Ld652Y cells for OpMNPV and LdMNPV. The vertical bars represent the standard deviations of the averages from three determinations. ( d ) Viral DNA production at 24 h post-infection. Viral DNA was quantified by qPCR. The vertical bars represent the standard deviations of the averages from three determinations. ( e ) Immunoblot analysis of VP39 and polyhedrin (Polh) proteins at 72 h post-infection. Polypeptides from infected Tn368 cells were resolved on 12% SDS-polyacrylamide gels and transferred onto Immobilon-P (for VP39 protein) or nitrocellulose membranes (for polyhedrin). VP39 protein was probed using anti-BmNPV/AcMNPV VP39 polyclonal antibody and visualized with ECL Select Western Blotting Detection Reagent. Polyhedrin protein was probed with anti-BmNPV polyhedrin polyclonal antibody and visualized using a HRP Conjugate Substrate Kit. ( f ) Immunoblot analysis of luciferase and HCF-1 proteins in infected Tn368 cells. Luciferase and HCF-1 proteins were probed by anti-HA monoclonal antibody and visualized using ECL Western Blotting Detection Reagent and ECL Select Western Blotting Detection Reagent, respectively. In panels ( e ) and ( f ), polypeptides equivalent to 1 × 10 5 cells were analyzed in each lane.

    Journal: Scientific Reports

    Article Title: HCF-1 encoded by baculovirus AcMNPV is required for productive nucleopolyhedrovirus infection of non-permissive Tn368 cells

    doi: 10.1038/s41598-017-03710-z

    Figure Lengend Snippet: Transiently expressed HCF-1 protein promotes the synthesis of NPV DNA and proteins in non-permissive Tn368 cells. Tn368 cells were transfected with 2 μg of pFBD/luc (Luc) or pFBD/hcf-1 (HCF-1) DNA, which express luciferase or HCF-1 protein, respectively, under control of the heat shock protein 70 promoter ( hsp70 pro). At 24 h post-transfection, the transfected cells were heat-shocked at 42 °C for 30 min, incubated for 6 h at 28 °C, and were then infected with HycuMNPV (Hycu), OpMNPV (Op), BmNPV (Bm) and LdMNPV (Ld) at MOIs of 10, 50, 10 and 3, respectively. ( a ) Schematic representation of the plasmids pFBD/luc and pFBD/hcf-1 used in these experiments. ( b ) Microscopic images of Tn368 cells at 72 h post-infection. The arrowheads indicate polyhedra-containing cells. Scale bar, 50 μm. ( c ) BV yields in virus-infected Tn368 cells at 72 h post-infection (pi). BV titers were determined by a plaque assay using SpIm cells for HycuMNPV, BM-N cells for BmNPV and Ld652Y cells for OpMNPV and LdMNPV. The vertical bars represent the standard deviations of the averages from three determinations. ( d ) Viral DNA production at 24 h post-infection. Viral DNA was quantified by qPCR. The vertical bars represent the standard deviations of the averages from three determinations. ( e ) Immunoblot analysis of VP39 and polyhedrin (Polh) proteins at 72 h post-infection. Polypeptides from infected Tn368 cells were resolved on 12% SDS-polyacrylamide gels and transferred onto Immobilon-P (for VP39 protein) or nitrocellulose membranes (for polyhedrin). VP39 protein was probed using anti-BmNPV/AcMNPV VP39 polyclonal antibody and visualized with ECL Select Western Blotting Detection Reagent. Polyhedrin protein was probed with anti-BmNPV polyhedrin polyclonal antibody and visualized using a HRP Conjugate Substrate Kit. ( f ) Immunoblot analysis of luciferase and HCF-1 proteins in infected Tn368 cells. Luciferase and HCF-1 proteins were probed by anti-HA monoclonal antibody and visualized using ECL Western Blotting Detection Reagent and ECL Select Western Blotting Detection Reagent, respectively. In panels ( e ) and ( f ), polypeptides equivalent to 1 × 10 5 cells were analyzed in each lane.

    Article Snippet: Positive signals were visualized using ECL Western Blotting Detection Reagent (GE Healthcare), ECL Select Western Blotting Detection Reagent (GE Healthcare) or an HRP Conjugate Substrate Kit (Bio-Rad).

    Techniques: Transfection, Luciferase, Incubation, Infection, Plaque Assay, Real-time Polymerase Chain Reaction, Western Blot

    AADA hydrolyzes soluble and insoluble carboxylesters. Twenty micrograms of membrane protein prepared from McA cells stably transfected with an empty pCIneo vector, FLAG-tagged mouse AADA, or human TGH cDNAs were incubated with pNP-acetate (A) or 4-MUH (B). The release of pNP was monitored at 405 nm and that of 4-umbelliferyl at 460 nm. The results are presented as an average from triplicate measurements. C: Hydrolysis of microsomal lipids. Cells were incubated with radiolabeled oleic acid, and microsomes were isolated and incubated for 4 h as described in Materials and Methods. Lipids were extracted and resolved on TLC plates, and radioactivity was determined by scintillation counting. Data (mean ± SD) from three separate experiments performed in triplicate are presented with radioactivity in DG in pNeo microsomes at time 0 set as 100%. Equal amounts of microsomal protein were used for the assay. The actual starting dpm in microsomal lipid fractions at time 0 were 22,000–25,000 for PC, 12,000–18,000 for TG, and 1,500–2,300 for DG. D: Thirty micrograms of total cellular membrane proteins from McA cells stably transfected with pCI-neo, A13, A23, and human TGH were either not treated (pNeo-NT) or treated with FP-biotin, resolved in SDS-PAGE, and transferred to nitrocellulose membrane, and biotinylated proteins were visualized with streptavidin-HRP. Asterisks indicate other potential endogenous serine hydrolases present in McA cells.

    Journal: Journal of Lipid Research

    Article Title: Arylacetamide deacetylase attenuates fatty-acid-induced triacylglycerol accumulation in rat hepatoma cells

    doi: 10.1194/jlr.M000596

    Figure Lengend Snippet: AADA hydrolyzes soluble and insoluble carboxylesters. Twenty micrograms of membrane protein prepared from McA cells stably transfected with an empty pCIneo vector, FLAG-tagged mouse AADA, or human TGH cDNAs were incubated with pNP-acetate (A) or 4-MUH (B). The release of pNP was monitored at 405 nm and that of 4-umbelliferyl at 460 nm. The results are presented as an average from triplicate measurements. C: Hydrolysis of microsomal lipids. Cells were incubated with radiolabeled oleic acid, and microsomes were isolated and incubated for 4 h as described in Materials and Methods. Lipids were extracted and resolved on TLC plates, and radioactivity was determined by scintillation counting. Data (mean ± SD) from three separate experiments performed in triplicate are presented with radioactivity in DG in pNeo microsomes at time 0 set as 100%. Equal amounts of microsomal protein were used for the assay. The actual starting dpm in microsomal lipid fractions at time 0 were 22,000–25,000 for PC, 12,000–18,000 for TG, and 1,500–2,300 for DG. D: Thirty micrograms of total cellular membrane proteins from McA cells stably transfected with pCI-neo, A13, A23, and human TGH were either not treated (pNeo-NT) or treated with FP-biotin, resolved in SDS-PAGE, and transferred to nitrocellulose membrane, and biotinylated proteins were visualized with streptavidin-HRP. Asterisks indicate other potential endogenous serine hydrolases present in McA cells.

    Article Snippet: Following transfer to nitrocellulose, biotinylated proteins were visualized by probing with avidin-HRP and enhanced chemiluminescence (ECL).

    Techniques: Stable Transfection, Transfection, Plasmid Preparation, Incubation, Isolation, Thin Layer Chromatography, Radioactivity, SDS Page

    dE2F expression correlates with E2F activity. A is at a lower magnification than panels B–D . ( A ) β-Galactosidase staining of egg chambers from dE2F rm729 /+, a dE2F enhancer trap line in which the expression of β-galactosidase profiles the level of dE2F ). A stage-9 egg chamber is embedded between two stage-10 egg chambers. The β-galactosidase reporter is induced at stage 10 in all of the follicle cells of the egg chamber. This induction correlates with the transition to amplification in the follicle cells. The level of β-galactosidase is highest in the follicle cells covering the anterior region of the oocyte, correlating with a gradient of BrdU incorporation from anterior to posterior in the follicle cells of the egg chamber (data not shown). The small blue cells are the follicle cells (short arrow); the larger cells are nurse cells (large arrow). ( B–D ). The antibody staining was detected by a HRP reaction, and a field of follicle cells is shown in each panel at the same magnification. ( B ) In a stage-9 (and earlier stages) wild-type egg chambers some follicle cells are positive for dE2F staining and others are not. Note that even in the follicle cells that show dE2F expression, the levels of dE2F protein are low. ( C ) In wild-type stage-10 follicle cells there is an increase in the levels of dE2F protein in all the follicle cells. ( D ) dE2F protein is also detected in dE2F i1 mutant follicle cells. The same staining pattern was observed for the dE2F i2 and dDP a1 mutant.

    Journal: Genes & Development

    Article Title: ORC localization in Drosophila follicle cells and the effects of mutations in dE2F and dDP

    doi:

    Figure Lengend Snippet: dE2F expression correlates with E2F activity. A is at a lower magnification than panels B–D . ( A ) β-Galactosidase staining of egg chambers from dE2F rm729 /+, a dE2F enhancer trap line in which the expression of β-galactosidase profiles the level of dE2F ). A stage-9 egg chamber is embedded between two stage-10 egg chambers. The β-galactosidase reporter is induced at stage 10 in all of the follicle cells of the egg chamber. This induction correlates with the transition to amplification in the follicle cells. The level of β-galactosidase is highest in the follicle cells covering the anterior region of the oocyte, correlating with a gradient of BrdU incorporation from anterior to posterior in the follicle cells of the egg chamber (data not shown). The small blue cells are the follicle cells (short arrow); the larger cells are nurse cells (large arrow). ( B–D ). The antibody staining was detected by a HRP reaction, and a field of follicle cells is shown in each panel at the same magnification. ( B ) In a stage-9 (and earlier stages) wild-type egg chambers some follicle cells are positive for dE2F staining and others are not. Note that even in the follicle cells that show dE2F expression, the levels of dE2F protein are low. ( C ) In wild-type stage-10 follicle cells there is an increase in the levels of dE2F protein in all the follicle cells. ( D ) dE2F protein is also detected in dE2F i1 mutant follicle cells. The same staining pattern was observed for the dE2F i2 and dDP a1 mutant.

    Article Snippet: BrdU labeling was visualized using a goat anti-mouse antibody conjugated to horseradish peroxidase (HRP) (Bio-Rad) at a dilution of 1:200, or a DTAF goat anti-mouse secondary antibody (Jackson) at a dilution of 1:150.

    Techniques: Expressing, Activity Assay, Staining, Amplification, BrdU Incorporation Assay, Mutagenesis

    Oxidative adducts are enhanced in experimental and human myocardium during Chagas disease. ( A ) Sprague-Dawley rats (or C3H/HeN mice) were infected with T. cruzi, and cells were harvested at day 40 (acute stage) and 180 (chronic stage) post-infection. Heart homogenates were resolved on 10% acrylamide gels, and Western blotting was performed with specific antibodies to detect 4 hydroxynonenal (4-HNE, panel a ), malondialdehyde (MDA, panel b ), dinitrophenyl (DNP)-derivatized carbonyl ( panel c ), and 3-nitrotyrosine (3NT, panel d ) adducts. Coomassie blue staining of membranes ( panel e ) confirmed the equal loading of samples. ( B ) Cryostat sections of human cardiac biopsies (5-µm) from normal healthy donors ( panels a, c, e ) and chagasic patients ( panels b, d, f ) were submitted to immunohistochemistry as described in Materials and Methods . Shown are representative images of immunostaining with anti-4-HNE antibodies ( panels a, b ). Tissue sections were incubated with DNPH to derivatize carbonyl proteins, and immunostaining was performed with anti-DNP antibody ( panels c–f ). HRP-conjugated ( panels a–d ) and rhodamine-conjugated ( panels e, f ) secondary antibodies were utilized to capture the color (brown) or fluorescence signal, respectively.

    Journal: PLoS ONE

    Article Title: Cardiac-Oxidized Antigens Are Targets of Immune Recognition by Antibodies and Potential Molecular Determinants in Chagas Disease Pathogenesis

    doi: 10.1371/journal.pone.0028449

    Figure Lengend Snippet: Oxidative adducts are enhanced in experimental and human myocardium during Chagas disease. ( A ) Sprague-Dawley rats (or C3H/HeN mice) were infected with T. cruzi, and cells were harvested at day 40 (acute stage) and 180 (chronic stage) post-infection. Heart homogenates were resolved on 10% acrylamide gels, and Western blotting was performed with specific antibodies to detect 4 hydroxynonenal (4-HNE, panel a ), malondialdehyde (MDA, panel b ), dinitrophenyl (DNP)-derivatized carbonyl ( panel c ), and 3-nitrotyrosine (3NT, panel d ) adducts. Coomassie blue staining of membranes ( panel e ) confirmed the equal loading of samples. ( B ) Cryostat sections of human cardiac biopsies (5-µm) from normal healthy donors ( panels a, c, e ) and chagasic patients ( panels b, d, f ) were submitted to immunohistochemistry as described in Materials and Methods . Shown are representative images of immunostaining with anti-4-HNE antibodies ( panels a, b ). Tissue sections were incubated with DNPH to derivatize carbonyl proteins, and immunostaining was performed with anti-DNP antibody ( panels c–f ). HRP-conjugated ( panels a–d ) and rhodamine-conjugated ( panels e, f ) secondary antibodies were utilized to capture the color (brown) or fluorescence signal, respectively.

    Article Snippet: Membranes were probed with sera from normal or chagasic rats, mice or human patients (1∶100 dilution) followed by HRP-conjugated secondary antibody (1∶5000, BioRad), and signal was detected by an ECL plus chemiluminiscence detection system (GE-Healthcare).

    Techniques: Mouse Assay, Infection, Western Blot, Multiple Displacement Amplification, Staining, Immunohistochemistry, Immunostaining, Incubation, Fluorescence

    Multimerization of SAA. Human recombinant SAA was blotted onto nitrocellulose membranes and overlayed with polyclonal antibodies against synthetic SAA human peptides ranging from the indicated amino acid sequences: lane 1: SAA1–17, lane 2: SAA14–30, lane 3: SAA27–44, lane 4: SAA40–63, lane 5: SAA59–72, lane 6: SAA68–84, lane 7: SAA79–94, and lane 8: SAA 89–104. HRP-labeled secondary goat antirabbit antibody was used for secondary incubation followed by luminol and chemiluminescent detection. The SAA monomer at around 12 kD is indicated.

    Journal: Journal of Biomedicine and Biotechnology

    Article Title: Colocalization of Serum Amyloid A with Microtubules in Human Coronary Artery Endothelial Cells

    doi: 10.1155/2011/528276

    Figure Lengend Snippet: Multimerization of SAA. Human recombinant SAA was blotted onto nitrocellulose membranes and overlayed with polyclonal antibodies against synthetic SAA human peptides ranging from the indicated amino acid sequences: lane 1: SAA1–17, lane 2: SAA14–30, lane 3: SAA27–44, lane 4: SAA40–63, lane 5: SAA59–72, lane 6: SAA68–84, lane 7: SAA79–94, and lane 8: SAA 89–104. HRP-labeled secondary goat antirabbit antibody was used for secondary incubation followed by luminol and chemiluminescent detection. The SAA monomer at around 12 kD is indicated.

    Article Snippet: Following washing, secondary incubation was done with antirabbit HRP conjugate (Biorad, Munich, Germany) at 1 : 200 dilution with subsequent Western blot luminol reagent (Santa Cruz, Calif, USA) and chemiluminescent detection performed following manufacturer's instructions.

    Techniques: Recombinant, Labeling, Incubation

    Western Blotting of heart tissue showing a strong protein band at about 80 kD indicating the presence of an octopamine receptor. Pan TAAR 1° antibodies (goat polyclonal) and HRP-conjugated 2° antibodies were used. The right lane contains

    Journal: In vivo

    Article Title: Presence of Octopamine and an Octopamine Receptor in Crassostrea virginica

    doi:

    Figure Lengend Snippet: Western Blotting of heart tissue showing a strong protein band at about 80 kD indicating the presence of an octopamine receptor. Pan TAAR 1° antibodies (goat polyclonal) and HRP-conjugated 2° antibodies were used. The right lane contains

    Article Snippet: The Pan TAAR 1° antibodies were diluted in TBS-T and 2% blocker for 24 hours, then the membranes were washed extensively with TBS-T, followed by incubation at room temperature for 60 min with HRP-conjugated 2° antibody (1:4000 dilution) in TBS-T and 2% blocker, and Bio-Rad Precision Protein StrepTactin-HRP conjugate (1:5000 dilution) was used to resolve protein standards.

    Techniques: Western Blot

    GECX-MS to capture and identify affibody binding to Z in E. coli . a Structure of the affibody–Z protein complex (PDB ID 1LP1), with two proximal sites, Lys7 in the affibody and Glu24 in the Z protein, highlighted. b Western blot of cell lysate of cells co-expressing MPB-Z(24BprY) with affibody(7Cys) and of cells co-expressing MPB-Z(24EB3) with affibody(7Cys). The cross-linked MBP–Z/affibody complex is indicated with a star. c SDS-PAGE of proteins His-tag purified from cells co-expressing affibody(7Cys) with MPB-Z(24BprY), or with MBP-Z(24EB3). In the absence of Uaa, background suppression of the TAG codon at site 24 resulted in small amount of full-length MBP–Z. d Mass spectrum of the cross-linked peptide between affibody(7Cys) and MBP-Z(24BprY). U represents BprY in the peptide sequence. e His-tag purified affibody(7Cys)/MBP-Z(24EB3) was labeled with biotin via CuAAC and then western blotted with streptavidin-HRP conjugate. f Biotin based enrichment of cross-linked affibody(7Cys)/MBP-Z(24EB3). g Mass spectrum of the cross-linked peptide between affibody(7Cys) and MBP-Z(24EB3) before biotin labeling. U represents EB3 in the peptide sequence. h Mass spectrum of biotinylated cross-linked peptide between affibody(7Cys) and MBP-Z(24EB3). U represents EB3 in the peptide sequence. i Extracted ion chromatography of biotinylated cross-linked peptide from input sample of biotin enrichment. j Extracted ion chromatography of biotinylated cross-linked peptide from elute sample of biotin enrichment. RT retention time, MA peak area, MH peak height

    Journal: Nature Communications

    Article Title: Spontaneous and specific chemical cross-linking in live cells to capture and identify protein interactions

    doi: 10.1038/s41467-017-02409-z

    Figure Lengend Snippet: GECX-MS to capture and identify affibody binding to Z in E. coli . a Structure of the affibody–Z protein complex (PDB ID 1LP1), with two proximal sites, Lys7 in the affibody and Glu24 in the Z protein, highlighted. b Western blot of cell lysate of cells co-expressing MPB-Z(24BprY) with affibody(7Cys) and of cells co-expressing MPB-Z(24EB3) with affibody(7Cys). The cross-linked MBP–Z/affibody complex is indicated with a star. c SDS-PAGE of proteins His-tag purified from cells co-expressing affibody(7Cys) with MPB-Z(24BprY), or with MBP-Z(24EB3). In the absence of Uaa, background suppression of the TAG codon at site 24 resulted in small amount of full-length MBP–Z. d Mass spectrum of the cross-linked peptide between affibody(7Cys) and MBP-Z(24BprY). U represents BprY in the peptide sequence. e His-tag purified affibody(7Cys)/MBP-Z(24EB3) was labeled with biotin via CuAAC and then western blotted with streptavidin-HRP conjugate. f Biotin based enrichment of cross-linked affibody(7Cys)/MBP-Z(24EB3). g Mass spectrum of the cross-linked peptide between affibody(7Cys) and MBP-Z(24EB3) before biotin labeling. U represents EB3 in the peptide sequence. h Mass spectrum of biotinylated cross-linked peptide between affibody(7Cys) and MBP-Z(24EB3). U represents EB3 in the peptide sequence. i Extracted ion chromatography of biotinylated cross-linked peptide from input sample of biotin enrichment. j Extracted ion chromatography of biotinylated cross-linked peptide from elute sample of biotin enrichment. RT retention time, MA peak area, MH peak height

    Article Snippet: For western blot analysis of biotin labeling, streptavidin-HRP conjugate from Bio-Rad (Catalog number 1610381) was used.

    Techniques: Mass Spectrometry, Binding Assay, Western Blot, Expressing, SDS Page, Purification, Sequencing, Labeling, Ion Chromatography