elisa plates 96-well Search Results


well plate  (Zymo Research)
94
Zymo Research well plate
Well Plate, supplied by Zymo Research, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/elisa+plates+96-well/bio_rxiv__2025__06__15__659618-173-4-10?v=Zymo+Research
Average 94 stars, based on 1 article reviews
well plate - by Bioz Stars, 2026-08
94/100 stars
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microplate readers infinite f50  (Tecan Systems)
94
Tecan Systems microplate readers infinite f50
Microplate Readers Infinite F50, supplied by Tecan Systems, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/elisa+plates+96-well/pmc06284046-70-7-12?v=Tecan+Systems
Average 94 stars, based on 1 article reviews
microplate readers infinite f50 - by Bioz Stars, 2026-08
94/100 stars
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elisa plate  (Santa Cruz Biotechnology)
93
Santa Cruz Biotechnology elisa plate
(A) <t>ELISA</t> plates were coated with c-myc peptide, purified R5-6 or R5-6C, or null eluent from empty-vector transformed bacteria as a control (Ctrl), and then incubated with RAW 264.7 cell lysates. The apoER2 <t>and</t> <t>VLDLR</t> in RAW 264.7 cell lysates bound to ELISA plates were detected using antibodies against apoER2 and VLDLR. (B) RAW 264.7 cells were transfected with empty pcDNA3.1B vector or apoER2-GFP expression plasmid, and then incubated with 30 μg/ml of apoB-carrying and apoE-free lipoproteins (+LP) or without lipoproteins (-LP) in the presence or absence of 0.2 μg/ml purified R5-6 protein. The amount of R5-6 bound to the cell surface was determined by ELISA using an antibody against c-myc epitope. The background binding was determined using a normal mouse IgG. (C-D) RAW 264.7 cells were treated with 0.2 μg/ml of purified R5-6 protein or culture medium alone (Ctrl). The protein level of ABCA1 was determined by immunoblotting and quantified relative to β-actin. (E) RAW 246.7 cells were treated as described in plane B. The mRNA level of ABCA1 was determined by quantitative real-time RT-PCR and normalized relative to GAPDH mRNA. (F) RAW 264.7 cells were labeled with 0.25 μCi/ml of 3 H-cholesterol, followed by incubation with 5 μg/ml c-myc peptide, 0.2 μg/ml purified R5-6 protein or vehicle control (Ctrl). Cholesterol efflux was determined in cells incubated with or without apoAI treatment, and was expressed as the percentage of radioactivity in the medium compared to the total radioactivity in the cells and medium. ApoAI-mediated cholesterol efflux was calculated as the difference of efflux from cells in the presence and absence of apoAI treatment. Data represent the mean ± SEM of four or more independent experiments. * p < 0.05 vs . Ctrl; † , p <0.05 vs . c-myc-immobilized ELISA plates or treated cells; ‡ , p < 0.05 vs . cells transfected with the same plasmids and untreated with R5-6; $ , p < 0.05 vs . cells transfected with empty vector and treated with R5-6; and # , p < 0.05 vs . cells transfected with apoER2-GFP-expression plasmid and untreated with lipoproteins.
Elisa Plate, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/elisa+plates+96-well/pmc04552883-40-9-37?v=Santa+Cruz+Biotechnology
Average 93 stars, based on 1 article reviews
elisa plate - by Bioz Stars, 2026-08
93/100 stars
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tecan plate reader infinitem200pro  (Tecan Systems)
94
Tecan Systems tecan plate reader infinitem200pro
(A) <t>ELISA</t> plates were coated with c-myc peptide, purified R5-6 or R5-6C, or null eluent from empty-vector transformed bacteria as a control (Ctrl), and then incubated with RAW 264.7 cell lysates. The apoER2 <t>and</t> <t>VLDLR</t> in RAW 264.7 cell lysates bound to ELISA plates were detected using antibodies against apoER2 and VLDLR. (B) RAW 264.7 cells were transfected with empty pcDNA3.1B vector or apoER2-GFP expression plasmid, and then incubated with 30 μg/ml of apoB-carrying and apoE-free lipoproteins (+LP) or without lipoproteins (-LP) in the presence or absence of 0.2 μg/ml purified R5-6 protein. The amount of R5-6 bound to the cell surface was determined by ELISA using an antibody against c-myc epitope. The background binding was determined using a normal mouse IgG. (C-D) RAW 264.7 cells were treated with 0.2 μg/ml of purified R5-6 protein or culture medium alone (Ctrl). The protein level of ABCA1 was determined by immunoblotting and quantified relative to β-actin. (E) RAW 246.7 cells were treated as described in plane B. The mRNA level of ABCA1 was determined by quantitative real-time RT-PCR and normalized relative to GAPDH mRNA. (F) RAW 264.7 cells were labeled with 0.25 μCi/ml of 3 H-cholesterol, followed by incubation with 5 μg/ml c-myc peptide, 0.2 μg/ml purified R5-6 protein or vehicle control (Ctrl). Cholesterol efflux was determined in cells incubated with or without apoAI treatment, and was expressed as the percentage of radioactivity in the medium compared to the total radioactivity in the cells and medium. ApoAI-mediated cholesterol efflux was calculated as the difference of efflux from cells in the presence and absence of apoAI treatment. Data represent the mean ± SEM of four or more independent experiments. * p < 0.05 vs . Ctrl; † , p <0.05 vs . c-myc-immobilized ELISA plates or treated cells; ‡ , p < 0.05 vs . cells transfected with the same plasmids and untreated with R5-6; $ , p < 0.05 vs . cells transfected with empty vector and treated with R5-6; and # , p < 0.05 vs . cells transfected with apoER2-GFP-expression plasmid and untreated with lipoproteins.
Tecan Plate Reader Infinitem200pro, supplied by Tecan Systems, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/elisa+plates+96-well/pmc11353697-190-37-37?v=Tecan+Systems
Average 94 stars, based on 1 article reviews
tecan plate reader infinitem200pro - by Bioz Stars, 2026-08
94/100 stars
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96 well elisa plates  (Guangzhou JET Bio-Filtration)
94
Guangzhou JET Bio-Filtration 96 well elisa plates
(A) <t>ELISA</t> plates were coated with c-myc peptide, purified R5-6 or R5-6C, or null eluent from empty-vector transformed bacteria as a control (Ctrl), and then incubated with RAW 264.7 cell lysates. The apoER2 <t>and</t> <t>VLDLR</t> in RAW 264.7 cell lysates bound to ELISA plates were detected using antibodies against apoER2 and VLDLR. (B) RAW 264.7 cells were transfected with empty pcDNA3.1B vector or apoER2-GFP expression plasmid, and then incubated with 30 μg/ml of apoB-carrying and apoE-free lipoproteins (+LP) or without lipoproteins (-LP) in the presence or absence of 0.2 μg/ml purified R5-6 protein. The amount of R5-6 bound to the cell surface was determined by ELISA using an antibody against c-myc epitope. The background binding was determined using a normal mouse IgG. (C-D) RAW 264.7 cells were treated with 0.2 μg/ml of purified R5-6 protein or culture medium alone (Ctrl). The protein level of ABCA1 was determined by immunoblotting and quantified relative to β-actin. (E) RAW 246.7 cells were treated as described in plane B. The mRNA level of ABCA1 was determined by quantitative real-time RT-PCR and normalized relative to GAPDH mRNA. (F) RAW 264.7 cells were labeled with 0.25 μCi/ml of 3 H-cholesterol, followed by incubation with 5 μg/ml c-myc peptide, 0.2 μg/ml purified R5-6 protein or vehicle control (Ctrl). Cholesterol efflux was determined in cells incubated with or without apoAI treatment, and was expressed as the percentage of radioactivity in the medium compared to the total radioactivity in the cells and medium. ApoAI-mediated cholesterol efflux was calculated as the difference of efflux from cells in the presence and absence of apoAI treatment. Data represent the mean ± SEM of four or more independent experiments. * p < 0.05 vs . Ctrl; † , p <0.05 vs . c-myc-immobilized ELISA plates or treated cells; ‡ , p < 0.05 vs . cells transfected with the same plasmids and untreated with R5-6; $ , p < 0.05 vs . cells transfected with empty vector and treated with R5-6; and # , p < 0.05 vs . cells transfected with apoER2-GFP-expression plasmid and untreated with lipoproteins.
96 Well Elisa Plates, supplied by Guangzhou JET Bio-Filtration, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/elisa+plates+96-well/pm39999840-252-51-54?v=Guangzhou+JET+Bio-Filtration
Average 94 stars, based on 1 article reviews
96 well elisa plates - by Bioz Stars, 2026-08
94/100 stars
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flat bottom 96 well elisa plate  (Guangzhou JET Bio-Filtration)
94
Guangzhou JET Bio-Filtration flat bottom 96 well elisa plate
(A) <t>ELISA</t> plates were coated with c-myc peptide, purified R5-6 or R5-6C, or null eluent from empty-vector transformed bacteria as a control (Ctrl), and then incubated with RAW 264.7 cell lysates. The apoER2 <t>and</t> <t>VLDLR</t> in RAW 264.7 cell lysates bound to ELISA plates were detected using antibodies against apoER2 and VLDLR. (B) RAW 264.7 cells were transfected with empty pcDNA3.1B vector or apoER2-GFP expression plasmid, and then incubated with 30 μg/ml of apoB-carrying and apoE-free lipoproteins (+LP) or without lipoproteins (-LP) in the presence or absence of 0.2 μg/ml purified R5-6 protein. The amount of R5-6 bound to the cell surface was determined by ELISA using an antibody against c-myc epitope. The background binding was determined using a normal mouse IgG. (C-D) RAW 264.7 cells were treated with 0.2 μg/ml of purified R5-6 protein or culture medium alone (Ctrl). The protein level of ABCA1 was determined by immunoblotting and quantified relative to β-actin. (E) RAW 246.7 cells were treated as described in plane B. The mRNA level of ABCA1 was determined by quantitative real-time RT-PCR and normalized relative to GAPDH mRNA. (F) RAW 264.7 cells were labeled with 0.25 μCi/ml of 3 H-cholesterol, followed by incubation with 5 μg/ml c-myc peptide, 0.2 μg/ml purified R5-6 protein or vehicle control (Ctrl). Cholesterol efflux was determined in cells incubated with or without apoAI treatment, and was expressed as the percentage of radioactivity in the medium compared to the total radioactivity in the cells and medium. ApoAI-mediated cholesterol efflux was calculated as the difference of efflux from cells in the presence and absence of apoAI treatment. Data represent the mean ± SEM of four or more independent experiments. * p < 0.05 vs . Ctrl; † , p <0.05 vs . c-myc-immobilized ELISA plates or treated cells; ‡ , p < 0.05 vs . cells transfected with the same plasmids and untreated with R5-6; $ , p < 0.05 vs . cells transfected with empty vector and treated with R5-6; and # , p < 0.05 vs . cells transfected with apoER2-GFP-expression plasmid and untreated with lipoproteins.
Flat Bottom 96 Well Elisa Plate, supplied by Guangzhou JET Bio-Filtration, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/elisa+plates+96-well/pm23936063-83-1-5?v=Guangzhou+JET+Bio-Filtration
Average 94 stars, based on 1 article reviews
flat bottom 96 well elisa plate - by Bioz Stars, 2026-08
94/100 stars
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96-well elisa plate sumilon #ms-8996f  (Sumilon Polyester)
90
Sumilon Polyester 96-well elisa plate sumilon #ms-8996f
(A) <t>ELISA</t> plates were coated with c-myc peptide, purified R5-6 or R5-6C, or null eluent from empty-vector transformed bacteria as a control (Ctrl), and then incubated with RAW 264.7 cell lysates. The apoER2 <t>and</t> <t>VLDLR</t> in RAW 264.7 cell lysates bound to ELISA plates were detected using antibodies against apoER2 and VLDLR. (B) RAW 264.7 cells were transfected with empty pcDNA3.1B vector or apoER2-GFP expression plasmid, and then incubated with 30 μg/ml of apoB-carrying and apoE-free lipoproteins (+LP) or without lipoproteins (-LP) in the presence or absence of 0.2 μg/ml purified R5-6 protein. The amount of R5-6 bound to the cell surface was determined by ELISA using an antibody against c-myc epitope. The background binding was determined using a normal mouse IgG. (C-D) RAW 264.7 cells were treated with 0.2 μg/ml of purified R5-6 protein or culture medium alone (Ctrl). The protein level of ABCA1 was determined by immunoblotting and quantified relative to β-actin. (E) RAW 246.7 cells were treated as described in plane B. The mRNA level of ABCA1 was determined by quantitative real-time RT-PCR and normalized relative to GAPDH mRNA. (F) RAW 264.7 cells were labeled with 0.25 μCi/ml of 3 H-cholesterol, followed by incubation with 5 μg/ml c-myc peptide, 0.2 μg/ml purified R5-6 protein or vehicle control (Ctrl). Cholesterol efflux was determined in cells incubated with or without apoAI treatment, and was expressed as the percentage of radioactivity in the medium compared to the total radioactivity in the cells and medium. ApoAI-mediated cholesterol efflux was calculated as the difference of efflux from cells in the presence and absence of apoAI treatment. Data represent the mean ± SEM of four or more independent experiments. * p < 0.05 vs . Ctrl; † , p <0.05 vs . c-myc-immobilized ELISA plates or treated cells; ‡ , p < 0.05 vs . cells transfected with the same plasmids and untreated with R5-6; $ , p < 0.05 vs . cells transfected with empty vector and treated with R5-6; and # , p < 0.05 vs . cells transfected with apoER2-GFP-expression plasmid and untreated with lipoproteins.
96 Well Elisa Plate Sumilon #Ms 8996f, supplied by Sumilon Polyester, 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/elisa+plates+96-well/us07329739-186-0-3?v=Sumilon+Polyester
Average 90 stars, based on 1 article reviews
96-well elisa plate sumilon #ms-8996f - by Bioz Stars, 2026-08
90/100 stars
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96-well plate bd falcon 96-well flat-bottom elisa plates  (Becton Dickinson)
90
Becton Dickinson 96-well plate bd falcon 96-well flat-bottom elisa plates
(A) <t>ELISA</t> plates were coated with c-myc peptide, purified R5-6 or R5-6C, or null eluent from empty-vector transformed bacteria as a control (Ctrl), and then incubated with RAW 264.7 cell lysates. The apoER2 <t>and</t> <t>VLDLR</t> in RAW 264.7 cell lysates bound to ELISA plates were detected using antibodies against apoER2 and VLDLR. (B) RAW 264.7 cells were transfected with empty pcDNA3.1B vector or apoER2-GFP expression plasmid, and then incubated with 30 μg/ml of apoB-carrying and apoE-free lipoproteins (+LP) or without lipoproteins (-LP) in the presence or absence of 0.2 μg/ml purified R5-6 protein. The amount of R5-6 bound to the cell surface was determined by ELISA using an antibody against c-myc epitope. The background binding was determined using a normal mouse IgG. (C-D) RAW 264.7 cells were treated with 0.2 μg/ml of purified R5-6 protein or culture medium alone (Ctrl). The protein level of ABCA1 was determined by immunoblotting and quantified relative to β-actin. (E) RAW 246.7 cells were treated as described in plane B. The mRNA level of ABCA1 was determined by quantitative real-time RT-PCR and normalized relative to GAPDH mRNA. (F) RAW 264.7 cells were labeled with 0.25 μCi/ml of 3 H-cholesterol, followed by incubation with 5 μg/ml c-myc peptide, 0.2 μg/ml purified R5-6 protein or vehicle control (Ctrl). Cholesterol efflux was determined in cells incubated with or without apoAI treatment, and was expressed as the percentage of radioactivity in the medium compared to the total radioactivity in the cells and medium. ApoAI-mediated cholesterol efflux was calculated as the difference of efflux from cells in the presence and absence of apoAI treatment. Data represent the mean ± SEM of four or more independent experiments. * p < 0.05 vs . Ctrl; † , p <0.05 vs . c-myc-immobilized ELISA plates or treated cells; ‡ , p < 0.05 vs . cells transfected with the same plasmids and untreated with R5-6; $ , p < 0.05 vs . cells transfected with empty vector and treated with R5-6; and # , p < 0.05 vs . cells transfected with apoER2-GFP-expression plasmid and untreated with lipoproteins.
96 Well Plate Bd Falcon 96 Well Flat Bottom Elisa Plates, supplied by Becton Dickinson, 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/elisa+plates+96-well/10__1080_slash_09712119__2017__1361828-36-24-26?v=Becton+Dickinson
Average 90 stars, based on 1 article reviews
96-well plate bd falcon 96-well flat-bottom elisa plates - by Bioz Stars, 2026-08
90/100 stars
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96-well elisa plates  (NISSHO CORPORATION)
90
NISSHO CORPORATION 96-well elisa plates
(A) <t>ELISA</t> plates were coated with c-myc peptide, purified R5-6 or R5-6C, or null eluent from empty-vector transformed bacteria as a control (Ctrl), and then incubated with RAW 264.7 cell lysates. The apoER2 <t>and</t> <t>VLDLR</t> in RAW 264.7 cell lysates bound to ELISA plates were detected using antibodies against apoER2 and VLDLR. (B) RAW 264.7 cells were transfected with empty pcDNA3.1B vector or apoER2-GFP expression plasmid, and then incubated with 30 μg/ml of apoB-carrying and apoE-free lipoproteins (+LP) or without lipoproteins (-LP) in the presence or absence of 0.2 μg/ml purified R5-6 protein. The amount of R5-6 bound to the cell surface was determined by ELISA using an antibody against c-myc epitope. The background binding was determined using a normal mouse IgG. (C-D) RAW 264.7 cells were treated with 0.2 μg/ml of purified R5-6 protein or culture medium alone (Ctrl). The protein level of ABCA1 was determined by immunoblotting and quantified relative to β-actin. (E) RAW 246.7 cells were treated as described in plane B. The mRNA level of ABCA1 was determined by quantitative real-time RT-PCR and normalized relative to GAPDH mRNA. (F) RAW 264.7 cells were labeled with 0.25 μCi/ml of 3 H-cholesterol, followed by incubation with 5 μg/ml c-myc peptide, 0.2 μg/ml purified R5-6 protein or vehicle control (Ctrl). Cholesterol efflux was determined in cells incubated with or without apoAI treatment, and was expressed as the percentage of radioactivity in the medium compared to the total radioactivity in the cells and medium. ApoAI-mediated cholesterol efflux was calculated as the difference of efflux from cells in the presence and absence of apoAI treatment. Data represent the mean ± SEM of four or more independent experiments. * p < 0.05 vs . Ctrl; † , p <0.05 vs . c-myc-immobilized ELISA plates or treated cells; ‡ , p < 0.05 vs . cells transfected with the same plasmids and untreated with R5-6; $ , p < 0.05 vs . cells transfected with empty vector and treated with R5-6; and # , p < 0.05 vs . cells transfected with apoER2-GFP-expression plasmid and untreated with lipoproteins.
96 Well Elisa Plates, supplied by NISSHO CORPORATION, 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/elisa+plates+96-well/pm11095466-75-0-14?v=NISSHO+CORPORATION
Average 90 stars, based on 1 article reviews
96-well elisa plates - by Bioz Stars, 2026-08
90/100 stars
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96-well elisa plate  (Dynatech Laboratories)
90
Dynatech Laboratories 96-well elisa plate
(A) <t>ELISA</t> plates were coated with c-myc peptide, purified R5-6 or R5-6C, or null eluent from empty-vector transformed bacteria as a control (Ctrl), and then incubated with RAW 264.7 cell lysates. The apoER2 <t>and</t> <t>VLDLR</t> in RAW 264.7 cell lysates bound to ELISA plates were detected using antibodies against apoER2 and VLDLR. (B) RAW 264.7 cells were transfected with empty pcDNA3.1B vector or apoER2-GFP expression plasmid, and then incubated with 30 μg/ml of apoB-carrying and apoE-free lipoproteins (+LP) or without lipoproteins (-LP) in the presence or absence of 0.2 μg/ml purified R5-6 protein. The amount of R5-6 bound to the cell surface was determined by ELISA using an antibody against c-myc epitope. The background binding was determined using a normal mouse IgG. (C-D) RAW 264.7 cells were treated with 0.2 μg/ml of purified R5-6 protein or culture medium alone (Ctrl). The protein level of ABCA1 was determined by immunoblotting and quantified relative to β-actin. (E) RAW 246.7 cells were treated as described in plane B. The mRNA level of ABCA1 was determined by quantitative real-time RT-PCR and normalized relative to GAPDH mRNA. (F) RAW 264.7 cells were labeled with 0.25 μCi/ml of 3 H-cholesterol, followed by incubation with 5 μg/ml c-myc peptide, 0.2 μg/ml purified R5-6 protein or vehicle control (Ctrl). Cholesterol efflux was determined in cells incubated with or without apoAI treatment, and was expressed as the percentage of radioactivity in the medium compared to the total radioactivity in the cells and medium. ApoAI-mediated cholesterol efflux was calculated as the difference of efflux from cells in the presence and absence of apoAI treatment. Data represent the mean ± SEM of four or more independent experiments. * p < 0.05 vs . Ctrl; † , p <0.05 vs . c-myc-immobilized ELISA plates or treated cells; ‡ , p < 0.05 vs . cells transfected with the same plasmids and untreated with R5-6; $ , p < 0.05 vs . cells transfected with empty vector and treated with R5-6; and # , p < 0.05 vs . cells transfected with apoER2-GFP-expression plasmid and untreated with lipoproteins.
96 Well Elisa Plate, supplied by Dynatech Laboratories, 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/elisa+plates+96-well/us06995236-186-1-6?v=Dynatech+Laboratories
Average 90 stars, based on 1 article reviews
96-well elisa plate - by Bioz Stars, 2026-08
90/100 stars
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96-well elisa plate pre-coated with mouse anti-rabbit igg  (Cayman Chemical)
90
Cayman Chemical 96-well elisa plate pre-coated with mouse anti-rabbit igg
(A) <t>ELISA</t> plates were coated with c-myc peptide, purified R5-6 or R5-6C, or null eluent from empty-vector transformed bacteria as a control (Ctrl), and then incubated with RAW 264.7 cell lysates. The apoER2 <t>and</t> <t>VLDLR</t> in RAW 264.7 cell lysates bound to ELISA plates were detected using antibodies against apoER2 and VLDLR. (B) RAW 264.7 cells were transfected with empty pcDNA3.1B vector or apoER2-GFP expression plasmid, and then incubated with 30 μg/ml of apoB-carrying and apoE-free lipoproteins (+LP) or without lipoproteins (-LP) in the presence or absence of 0.2 μg/ml purified R5-6 protein. The amount of R5-6 bound to the cell surface was determined by ELISA using an antibody against c-myc epitope. The background binding was determined using a normal mouse IgG. (C-D) RAW 264.7 cells were treated with 0.2 μg/ml of purified R5-6 protein or culture medium alone (Ctrl). The protein level of ABCA1 was determined by immunoblotting and quantified relative to β-actin. (E) RAW 246.7 cells were treated as described in plane B. The mRNA level of ABCA1 was determined by quantitative real-time RT-PCR and normalized relative to GAPDH mRNA. (F) RAW 264.7 cells were labeled with 0.25 μCi/ml of 3 H-cholesterol, followed by incubation with 5 μg/ml c-myc peptide, 0.2 μg/ml purified R5-6 protein or vehicle control (Ctrl). Cholesterol efflux was determined in cells incubated with or without apoAI treatment, and was expressed as the percentage of radioactivity in the medium compared to the total radioactivity in the cells and medium. ApoAI-mediated cholesterol efflux was calculated as the difference of efflux from cells in the presence and absence of apoAI treatment. Data represent the mean ± SEM of four or more independent experiments. * p < 0.05 vs . Ctrl; † , p <0.05 vs . c-myc-immobilized ELISA plates or treated cells; ‡ , p < 0.05 vs . cells transfected with the same plasmids and untreated with R5-6; $ , p < 0.05 vs . cells transfected with empty vector and treated with R5-6; and # , p < 0.05 vs . cells transfected with apoER2-GFP-expression plasmid and untreated with lipoproteins.
96 Well Elisa Plate Pre Coated With Mouse Anti Rabbit Igg, supplied by Cayman Chemical, 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/elisa+plates+96-well/pm30416167-20-6-12?v=Cayman+Chemical
Average 90 stars, based on 1 article reviews
96-well elisa plate pre-coated with mouse anti-rabbit igg - by Bioz Stars, 2026-08
90/100 stars
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elisa plates 96 well  (DYNEX tech)
90
DYNEX tech elisa plates 96 well
(A) <t>ELISA</t> plates were coated with c-myc peptide, purified R5-6 or R5-6C, or null eluent from empty-vector transformed bacteria as a control (Ctrl), and then incubated with RAW 264.7 cell lysates. The apoER2 <t>and</t> <t>VLDLR</t> in RAW 264.7 cell lysates bound to ELISA plates were detected using antibodies against apoER2 and VLDLR. (B) RAW 264.7 cells were transfected with empty pcDNA3.1B vector or apoER2-GFP expression plasmid, and then incubated with 30 μg/ml of apoB-carrying and apoE-free lipoproteins (+LP) or without lipoproteins (-LP) in the presence or absence of 0.2 μg/ml purified R5-6 protein. The amount of R5-6 bound to the cell surface was determined by ELISA using an antibody against c-myc epitope. The background binding was determined using a normal mouse IgG. (C-D) RAW 264.7 cells were treated with 0.2 μg/ml of purified R5-6 protein or culture medium alone (Ctrl). The protein level of ABCA1 was determined by immunoblotting and quantified relative to β-actin. (E) RAW 246.7 cells were treated as described in plane B. The mRNA level of ABCA1 was determined by quantitative real-time RT-PCR and normalized relative to GAPDH mRNA. (F) RAW 264.7 cells were labeled with 0.25 μCi/ml of 3 H-cholesterol, followed by incubation with 5 μg/ml c-myc peptide, 0.2 μg/ml purified R5-6 protein or vehicle control (Ctrl). Cholesterol efflux was determined in cells incubated with or without apoAI treatment, and was expressed as the percentage of radioactivity in the medium compared to the total radioactivity in the cells and medium. ApoAI-mediated cholesterol efflux was calculated as the difference of efflux from cells in the presence and absence of apoAI treatment. Data represent the mean ± SEM of four or more independent experiments. * p < 0.05 vs . Ctrl; † , p <0.05 vs . c-myc-immobilized ELISA plates or treated cells; ‡ , p < 0.05 vs . cells transfected with the same plasmids and untreated with R5-6; $ , p < 0.05 vs . cells transfected with empty vector and treated with R5-6; and # , p < 0.05 vs . cells transfected with apoER2-GFP-expression plasmid and untreated with lipoproteins.
Elisa Plates 96 Well, supplied by DYNEX tech, 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/elisa+plates+96-well/pmc06346709-89-0-4?v=DYNEX+tech
Average 90 stars, based on 1 article reviews
elisa plates 96 well - by Bioz Stars, 2026-08
90/100 stars
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(A) ELISA plates were coated with c-myc peptide, purified R5-6 or R5-6C, or null eluent from empty-vector transformed bacteria as a control (Ctrl), and then incubated with RAW 264.7 cell lysates. The apoER2 and VLDLR in RAW 264.7 cell lysates bound to ELISA plates were detected using antibodies against apoER2 and VLDLR. (B) RAW 264.7 cells were transfected with empty pcDNA3.1B vector or apoER2-GFP expression plasmid, and then incubated with 30 μg/ml of apoB-carrying and apoE-free lipoproteins (+LP) or without lipoproteins (-LP) in the presence or absence of 0.2 μg/ml purified R5-6 protein. The amount of R5-6 bound to the cell surface was determined by ELISA using an antibody against c-myc epitope. The background binding was determined using a normal mouse IgG. (C-D) RAW 264.7 cells were treated with 0.2 μg/ml of purified R5-6 protein or culture medium alone (Ctrl). The protein level of ABCA1 was determined by immunoblotting and quantified relative to β-actin. (E) RAW 246.7 cells were treated as described in plane B. The mRNA level of ABCA1 was determined by quantitative real-time RT-PCR and normalized relative to GAPDH mRNA. (F) RAW 264.7 cells were labeled with 0.25 μCi/ml of 3 H-cholesterol, followed by incubation with 5 μg/ml c-myc peptide, 0.2 μg/ml purified R5-6 protein or vehicle control (Ctrl). Cholesterol efflux was determined in cells incubated with or without apoAI treatment, and was expressed as the percentage of radioactivity in the medium compared to the total radioactivity in the cells and medium. ApoAI-mediated cholesterol efflux was calculated as the difference of efflux from cells in the presence and absence of apoAI treatment. Data represent the mean ± SEM of four or more independent experiments. * p < 0.05 vs . Ctrl; † , p <0.05 vs . c-myc-immobilized ELISA plates or treated cells; ‡ , p < 0.05 vs . cells transfected with the same plasmids and untreated with R5-6; $ , p < 0.05 vs . cells transfected with empty vector and treated with R5-6; and # , p < 0.05 vs . cells transfected with apoER2-GFP-expression plasmid and untreated with lipoproteins.

Journal: PLoS ONE

Article Title: A Subregion of Reelin Suppresses Lipoprotein-Induced Cholesterol Accumulation in Macrophages

doi: 10.1371/journal.pone.0136895

Figure Lengend Snippet: (A) ELISA plates were coated with c-myc peptide, purified R5-6 or R5-6C, or null eluent from empty-vector transformed bacteria as a control (Ctrl), and then incubated with RAW 264.7 cell lysates. The apoER2 and VLDLR in RAW 264.7 cell lysates bound to ELISA plates were detected using antibodies against apoER2 and VLDLR. (B) RAW 264.7 cells were transfected with empty pcDNA3.1B vector or apoER2-GFP expression plasmid, and then incubated with 30 μg/ml of apoB-carrying and apoE-free lipoproteins (+LP) or without lipoproteins (-LP) in the presence or absence of 0.2 μg/ml purified R5-6 protein. The amount of R5-6 bound to the cell surface was determined by ELISA using an antibody against c-myc epitope. The background binding was determined using a normal mouse IgG. (C-D) RAW 264.7 cells were treated with 0.2 μg/ml of purified R5-6 protein or culture medium alone (Ctrl). The protein level of ABCA1 was determined by immunoblotting and quantified relative to β-actin. (E) RAW 246.7 cells were treated as described in plane B. The mRNA level of ABCA1 was determined by quantitative real-time RT-PCR and normalized relative to GAPDH mRNA. (F) RAW 264.7 cells were labeled with 0.25 μCi/ml of 3 H-cholesterol, followed by incubation with 5 μg/ml c-myc peptide, 0.2 μg/ml purified R5-6 protein or vehicle control (Ctrl). Cholesterol efflux was determined in cells incubated with or without apoAI treatment, and was expressed as the percentage of radioactivity in the medium compared to the total radioactivity in the cells and medium. ApoAI-mediated cholesterol efflux was calculated as the difference of efflux from cells in the presence and absence of apoAI treatment. Data represent the mean ± SEM of four or more independent experiments. * p < 0.05 vs . Ctrl; † , p <0.05 vs . c-myc-immobilized ELISA plates or treated cells; ‡ , p < 0.05 vs . cells transfected with the same plasmids and untreated with R5-6; $ , p < 0.05 vs . cells transfected with empty vector and treated with R5-6; and # , p < 0.05 vs . cells transfected with apoER2-GFP-expression plasmid and untreated with lipoproteins.

Article Snippet: PI3K inhibitor LY294002 (sc-201426), Sp1 inhibitor mithramycin A (sc-200909), ELISA plate (sc-204463), scrambled siRNA, and siRNAs specific for VLDLR or apoER2, antibodies against ABCA1 (sc-58219), β-actin (sc-47778), apoER2 (sc-20746), VLDLR (sc-18824), and mouse IgG were purchased from Santa Cruz Biotechnology (Santa Cruz, CA).

Techniques: Enzyme-linked Immunosorbent Assay, Purification, Plasmid Preparation, Transformation Assay, Bacteria, Control, Incubation, Transfection, Expressing, Binding Assay, Western Blot, Quantitative RT-PCR, Labeling, Radioactivity