biotinylated probe Search Results


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  • 97
    Thermo Fisher avidin biotin blocking kit
    Avidin Biotin Blocking Kit, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 97/100, based on 611 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/avidin biotin blocking kit/product/Thermo Fisher
    Average 97 stars, based on 611 article reviews
    Price from $9.99 to $1999.99
    avidin biotin blocking kit - by Bioz Stars, 2020-05
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    99
    Millipore biotinylated probes
    GST pull-downs and Far Western blots indicate increased Src SH3-SH2 interaction with KDR/Flk-1 upon VEGF stimulation . (A) HUVECs were either serum-starved (0') or starved and then VEGF-treated (15 ng/mL for 15 min) (15'). The indicated GST-Src domain fusion proteins (see below) bound to glutathione-agarose beads were used (500 pmol equimolar amounts each), in pull-down incubations with equal amounts of protein lysate samples (500 μg each). The pull-down complexes were resolved on a 7% acrylamide SDS-PAGE gel and transferred to nitrocellulose. Immunoblotting was then performed using α-KDR/Flk-1 (A-3) or α-Flt-1 (H-225). GU, GST-Src unique domain fusion protein; GU32, GST-Src unique SH3 SH2 domain fusion protein; G32, GST-Src SH3 SH2 domain fusion protein. (B) Cell extract (pre-pull-down) input levels of phosphotyrosine KDR/Flk-1 and KDR/Flk-1, from HUVECs either serum-starved (0') or starved and then VEGF-treated (15'). (C) Cell extract (pre-pull-down) input levels of phosphotyrosine Flt-1 and Flt-1, from HUVECs either serum-starved (0') or starved and then VEGF-treated (15'). (D) HUVECs were serum-starved (-) or VEGF-treated with VEGF (15 ng/mL for 15 min) (+). The cell extracts were then immunoprecipitated using α-KDR/Flk-1 (N-931). The immunocomplexes were resolved on a 7% acrylamide SDS-PAGE gel. <t>Biotinylated</t> GST and biotinylated GST-Src SH3-SH2 fusion protein were used in Far Western blotting. Detection was performed using horseradish peroxidase-conjugated ExtrAvidin ® , followed by enhanced chemiluminescence detection reagents. Immunoprecipitation-Western blots for levels of phosphotyrosine KDR/Flk-1 and KDR/Flk-1 of the serum-starved (-) or VEGF-treated HUVEC (+) cell extracts were also performed in parallel.
    Biotinylated Probes, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 76 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 99 stars, based on 76 article reviews
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    92
    Agilent technologies biotinylated probes
    Accumulation of replicated plasmid DNA in BJAB cells and BJAB cells stably expressing the indicated EBNA-1 derivatives at 48 h after transfection with the oriP plasmid pOLP DNA. Nonchromosomal DNA was extracted from the indicated number of transfected cells (lanes 6–15) or from control BJAB cells (10 6 ) that were mixed with the indicated amounts of pOLP DNA (lanes 1–5) and assayed for the plasmid DNA by Southern blot analysis after Xho I digestion to linearize the plasmid DNA. DNAs in lanes 6–10 were also digested by Dpn I. The sizes (kb) of <t>biotinylated</t> λ Hin dIII DNA markers are indicated on the left. The signal intensity increased linearly for amounts of input pOLP DNA up to at least 3 ng (data not shown). The amounts of full-length (9.3 kb) pOLP DNA in lanes 6–15 were estimated by comparing the intensity with that of lanes 1–5. The percentage of Dpn I-resistant pOLP DNA was calculated by dividing the amount of the full-length pOLP DNA in the Dpn I-digested sample by that in the undigested sample after correction to the same number of cells.
    Biotinylated Probes, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 92/100, based on 228 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/biotinylated probes/product/Agilent technologies
    Average 92 stars, based on 228 article reviews
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    biotinylated probes - by Bioz Stars, 2020-05
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    91
    TIB MOLBIOL biotinylated probe
    Accumulation of replicated plasmid DNA in BJAB cells and BJAB cells stably expressing the indicated EBNA-1 derivatives at 48 h after transfection with the oriP plasmid pOLP DNA. Nonchromosomal DNA was extracted from the indicated number of transfected cells (lanes 6–15) or from control BJAB cells (10 6 ) that were mixed with the indicated amounts of pOLP DNA (lanes 1–5) and assayed for the plasmid DNA by Southern blot analysis after Xho I digestion to linearize the plasmid DNA. DNAs in lanes 6–10 were also digested by Dpn I. The sizes (kb) of <t>biotinylated</t> λ Hin dIII DNA markers are indicated on the left. The signal intensity increased linearly for amounts of input pOLP DNA up to at least 3 ng (data not shown). The amounts of full-length (9.3 kb) pOLP DNA in lanes 6–15 were estimated by comparing the intensity with that of lanes 1–5. The percentage of Dpn I-resistant pOLP DNA was calculated by dividing the amount of the full-length pOLP DNA in the Dpn I-digested sample by that in the undigested sample after correction to the same number of cells.
    Biotinylated Probe, supplied by TIB MOLBIOL, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/biotinylated probe/product/TIB MOLBIOL
    Average 91 stars, based on 1 article reviews
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    90
    Enzo Biochem biotinylated probes
    Accumulation of replicated plasmid DNA in BJAB cells and BJAB cells stably expressing the indicated EBNA-1 derivatives at 48 h after transfection with the oriP plasmid pOLP DNA. Nonchromosomal DNA was extracted from the indicated number of transfected cells (lanes 6–15) or from control BJAB cells (10 6 ) that were mixed with the indicated amounts of pOLP DNA (lanes 1–5) and assayed for the plasmid DNA by Southern blot analysis after Xho I digestion to linearize the plasmid DNA. DNAs in lanes 6–10 were also digested by Dpn I. The sizes (kb) of <t>biotinylated</t> λ Hin dIII DNA markers are indicated on the left. The signal intensity increased linearly for amounts of input pOLP DNA up to at least 3 ng (data not shown). The amounts of full-length (9.3 kb) pOLP DNA in lanes 6–15 were estimated by comparing the intensity with that of lanes 1–5. The percentage of Dpn I-resistant pOLP DNA was calculated by dividing the amount of the full-length pOLP DNA in the Dpn I-digested sample by that in the undigested sample after correction to the same number of cells.
    Biotinylated Probes, supplied by Enzo Biochem, used in various techniques. Bioz Stars score: 90/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 90 stars, based on 15 article reviews
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    92
    ValueGene biotinylated tg probes
    Accumulation of replicated plasmid DNA in BJAB cells and BJAB cells stably expressing the indicated EBNA-1 derivatives at 48 h after transfection with the oriP plasmid pOLP DNA. Nonchromosomal DNA was extracted from the indicated number of transfected cells (lanes 6–15) or from control BJAB cells (10 6 ) that were mixed with the indicated amounts of pOLP DNA (lanes 1–5) and assayed for the plasmid DNA by Southern blot analysis after Xho I digestion to linearize the plasmid DNA. DNAs in lanes 6–10 were also digested by Dpn I. The sizes (kb) of <t>biotinylated</t> λ Hin dIII DNA markers are indicated on the left. The signal intensity increased linearly for amounts of input pOLP DNA up to at least 3 ng (data not shown). The amounts of full-length (9.3 kb) pOLP DNA in lanes 6–15 were estimated by comparing the intensity with that of lanes 1–5. The percentage of Dpn I-resistant pOLP DNA was calculated by dividing the amount of the full-length pOLP DNA in the Dpn I-digested sample by that in the undigested sample after correction to the same number of cells.
    Biotinylated Tg Probes, supplied by ValueGene, used in various techniques. Bioz Stars score: 92/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 92 stars, based on 12 article reviews
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    92
    Thermo Fisher biotinylated probe
    Expression of CCL9 in mouse testis. (A): Immunofluorescence of 8-day WT mouse testis showing strong expression of CCL9 in Sertoli cells (green Alexa Fluor 488 staining). Arrows indicate locations of stem/progenitor spermatogonia, which are negative for CCL9. Scale bar = 25 µm. (B): Immunofluorescence of 8-day Etv5 -/- mouse testis showing a sharp decrease of CCL9 expression in Sertoli cells. Scale bar = 15 µm. (C): Immunofluorescence of 8-day WT mouse testis showing expression of CCR1, the receptor for CCL9, in stem/progenitor spermatogonia. Type A spermatogonia show double-staining for CCR1 (green Alexa Fluor 488 staining) and GCNA1 (pink Alexa Fluor 594 staining). The green staining in the lumen is background staining. Scale bar = 25 µm. (D): Immunohistochemistry of 6-day WT mouse testis showing expression of CCR1 in stem/progenitor spermatogonia (arrows). Scale bar = 15 µm. (E): Western blot of protein extracts from isolated WT seminiferous tubules of 4-, 10-, 35- and 90-day-old mice with anti-CCL9 and anti-WT1 antibodies, showing that CCl9 expression is restricted to early steps of spermatogenesis. (F): Electrophoretic mobility shift assays to investigate ETV5 binding to its consensus sequence in the Ccl9 promoter. The left panel shows gel shifts using nuclear extracts of TM4 cells after transfection with the pERMFLAG construct (pERMFLAG TM4). 1: <t>biotinylated</t> probe alone (B EBS3); 2: nuclear extract of pERMFLAG TM4 and B EBS3, with apparent gel shift (arrow); 3: nuclear extract of pERMFLAG TM4 with B EBS3 and nonbiotinylated probe (NB EBS3) showing outcompetition; and 4: nuclear extract of pERMFLAG TM4 with B EBS3 and ETV5 antibody (ETV5 Ab) showing a decrease of DNA/protein binding. The middle panel shows gel shifts using again pERMFLAG TM4 nuclear extracts. 1: B EBS3 alone; 2: pERMFLAG TM4 with B EBS3, showing apparent gel shift (arrow); 3: pERMFLAG TM4 with B EBS3 and ETV5 Ab showing decrease of protein-DNA binding; 4: nuclear extract of TM4 cells after transfection with control vector (Control TM4), and incubated with B EBS3; 5: control TM4 with B EBS3 and NB EBS3, 6: pERMFLAG TM4 with mutant B EBS3, and 7: pERMFLAG TM4 with mutant NB EBS3. Gel shifts with NB EBS3 substantially, but not completely outcompeted the protein-DNA complex suggesting the presence of other factors in the complex. There was no shift of protein-DNA complexes with mutant EBS3 sequences or TM4 cells transfected with control vector. The right panel shows gel shifts of purified ETV5 protein using pET vector (ETV5 protein). 1: ETV5 protein with B EBS3, showing gel shift (arrow) and 2: ETV5 protein with B EBS3 and NB EBS3 showing outcompetition. The data confirms a possible ETV5-EBS3 binding. Abbreviations: CCL9, C-C-motif ligand 9; CCR1, C-C-receptor type 1; GCNA, germ cell nuclear antigen 1; Etv5 , Ets variant gene; ETV5 protein, Ets variant protein; B EBS3, biotinylated Ets binding site 3; NB EBS3, nonbiotinylated Ets binding site 3; WT, wild type.
    Biotinylated Probe, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/biotinylated probe/product/Thermo Fisher
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    93
    Agilent technologies biotinylated haloplex probes
    Expression of CCL9 in mouse testis. (A): Immunofluorescence of 8-day WT mouse testis showing strong expression of CCL9 in Sertoli cells (green Alexa Fluor 488 staining). Arrows indicate locations of stem/progenitor spermatogonia, which are negative for CCL9. Scale bar = 25 µm. (B): Immunofluorescence of 8-day Etv5 -/- mouse testis showing a sharp decrease of CCL9 expression in Sertoli cells. Scale bar = 15 µm. (C): Immunofluorescence of 8-day WT mouse testis showing expression of CCR1, the receptor for CCL9, in stem/progenitor spermatogonia. Type A spermatogonia show double-staining for CCR1 (green Alexa Fluor 488 staining) and GCNA1 (pink Alexa Fluor 594 staining). The green staining in the lumen is background staining. Scale bar = 25 µm. (D): Immunohistochemistry of 6-day WT mouse testis showing expression of CCR1 in stem/progenitor spermatogonia (arrows). Scale bar = 15 µm. (E): Western blot of protein extracts from isolated WT seminiferous tubules of 4-, 10-, 35- and 90-day-old mice with anti-CCL9 and anti-WT1 antibodies, showing that CCl9 expression is restricted to early steps of spermatogenesis. (F): Electrophoretic mobility shift assays to investigate ETV5 binding to its consensus sequence in the Ccl9 promoter. The left panel shows gel shifts using nuclear extracts of TM4 cells after transfection with the pERMFLAG construct (pERMFLAG TM4). 1: <t>biotinylated</t> probe alone (B EBS3); 2: nuclear extract of pERMFLAG TM4 and B EBS3, with apparent gel shift (arrow); 3: nuclear extract of pERMFLAG TM4 with B EBS3 and nonbiotinylated probe (NB EBS3) showing outcompetition; and 4: nuclear extract of pERMFLAG TM4 with B EBS3 and ETV5 antibody (ETV5 Ab) showing a decrease of DNA/protein binding. The middle panel shows gel shifts using again pERMFLAG TM4 nuclear extracts. 1: B EBS3 alone; 2: pERMFLAG TM4 with B EBS3, showing apparent gel shift (arrow); 3: pERMFLAG TM4 with B EBS3 and ETV5 Ab showing decrease of protein-DNA binding; 4: nuclear extract of TM4 cells after transfection with control vector (Control TM4), and incubated with B EBS3; 5: control TM4 with B EBS3 and NB EBS3, 6: pERMFLAG TM4 with mutant B EBS3, and 7: pERMFLAG TM4 with mutant NB EBS3. Gel shifts with NB EBS3 substantially, but not completely outcompeted the protein-DNA complex suggesting the presence of other factors in the complex. There was no shift of protein-DNA complexes with mutant EBS3 sequences or TM4 cells transfected with control vector. The right panel shows gel shifts of purified ETV5 protein using pET vector (ETV5 protein). 1: ETV5 protein with B EBS3, showing gel shift (arrow) and 2: ETV5 protein with B EBS3 and NB EBS3 showing outcompetition. The data confirms a possible ETV5-EBS3 binding. Abbreviations: CCL9, C-C-motif ligand 9; CCR1, C-C-receptor type 1; GCNA, germ cell nuclear antigen 1; Etv5 , Ets variant gene; ETV5 protein, Ets variant protein; B EBS3, biotinylated Ets binding site 3; NB EBS3, nonbiotinylated Ets binding site 3; WT, wild type.
    Biotinylated Haloplex Probes, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 93/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/biotinylated haloplex probes/product/Agilent technologies
    Average 93 stars, based on 9 article reviews
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    88
    Bioneer Corporation biotinylated oligonucleotide probe
    Expression of CCL9 in mouse testis. (A): Immunofluorescence of 8-day WT mouse testis showing strong expression of CCL9 in Sertoli cells (green Alexa Fluor 488 staining). Arrows indicate locations of stem/progenitor spermatogonia, which are negative for CCL9. Scale bar = 25 µm. (B): Immunofluorescence of 8-day Etv5 -/- mouse testis showing a sharp decrease of CCL9 expression in Sertoli cells. Scale bar = 15 µm. (C): Immunofluorescence of 8-day WT mouse testis showing expression of CCR1, the receptor for CCL9, in stem/progenitor spermatogonia. Type A spermatogonia show double-staining for CCR1 (green Alexa Fluor 488 staining) and GCNA1 (pink Alexa Fluor 594 staining). The green staining in the lumen is background staining. Scale bar = 25 µm. (D): Immunohistochemistry of 6-day WT mouse testis showing expression of CCR1 in stem/progenitor spermatogonia (arrows). Scale bar = 15 µm. (E): Western blot of protein extracts from isolated WT seminiferous tubules of 4-, 10-, 35- and 90-day-old mice with anti-CCL9 and anti-WT1 antibodies, showing that CCl9 expression is restricted to early steps of spermatogenesis. (F): Electrophoretic mobility shift assays to investigate ETV5 binding to its consensus sequence in the Ccl9 promoter. The left panel shows gel shifts using nuclear extracts of TM4 cells after transfection with the pERMFLAG construct (pERMFLAG TM4). 1: <t>biotinylated</t> probe alone (B EBS3); 2: nuclear extract of pERMFLAG TM4 and B EBS3, with apparent gel shift (arrow); 3: nuclear extract of pERMFLAG TM4 with B EBS3 and nonbiotinylated probe (NB EBS3) showing outcompetition; and 4: nuclear extract of pERMFLAG TM4 with B EBS3 and ETV5 antibody (ETV5 Ab) showing a decrease of DNA/protein binding. The middle panel shows gel shifts using again pERMFLAG TM4 nuclear extracts. 1: B EBS3 alone; 2: pERMFLAG TM4 with B EBS3, showing apparent gel shift (arrow); 3: pERMFLAG TM4 with B EBS3 and ETV5 Ab showing decrease of protein-DNA binding; 4: nuclear extract of TM4 cells after transfection with control vector (Control TM4), and incubated with B EBS3; 5: control TM4 with B EBS3 and NB EBS3, 6: pERMFLAG TM4 with mutant B EBS3, and 7: pERMFLAG TM4 with mutant NB EBS3. Gel shifts with NB EBS3 substantially, but not completely outcompeted the protein-DNA complex suggesting the presence of other factors in the complex. There was no shift of protein-DNA complexes with mutant EBS3 sequences or TM4 cells transfected with control vector. The right panel shows gel shifts of purified ETV5 protein using pET vector (ETV5 protein). 1: ETV5 protein with B EBS3, showing gel shift (arrow) and 2: ETV5 protein with B EBS3 and NB EBS3 showing outcompetition. The data confirms a possible ETV5-EBS3 binding. Abbreviations: CCL9, C-C-motif ligand 9; CCR1, C-C-receptor type 1; GCNA, germ cell nuclear antigen 1; Etv5 , Ets variant gene; ETV5 protein, Ets variant protein; B EBS3, biotinylated Ets binding site 3; NB EBS3, nonbiotinylated Ets binding site 3; WT, wild type.
    Biotinylated Oligonucleotide Probe, supplied by Bioneer Corporation, used in various techniques. Bioz Stars score: 88/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/biotinylated oligonucleotide probe/product/Bioneer Corporation
    Average 88 stars, based on 3 article reviews
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    biotinylated oligonucleotide probe - by Bioz Stars, 2020-05
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    90
    GenScript 3 biotinylated probes
    Expression of CCL9 in mouse testis. (A): Immunofluorescence of 8-day WT mouse testis showing strong expression of CCL9 in Sertoli cells (green Alexa Fluor 488 staining). Arrows indicate locations of stem/progenitor spermatogonia, which are negative for CCL9. Scale bar = 25 µm. (B): Immunofluorescence of 8-day Etv5 -/- mouse testis showing a sharp decrease of CCL9 expression in Sertoli cells. Scale bar = 15 µm. (C): Immunofluorescence of 8-day WT mouse testis showing expression of CCR1, the receptor for CCL9, in stem/progenitor spermatogonia. Type A spermatogonia show double-staining for CCR1 (green Alexa Fluor 488 staining) and GCNA1 (pink Alexa Fluor 594 staining). The green staining in the lumen is background staining. Scale bar = 25 µm. (D): Immunohistochemistry of 6-day WT mouse testis showing expression of CCR1 in stem/progenitor spermatogonia (arrows). Scale bar = 15 µm. (E): Western blot of protein extracts from isolated WT seminiferous tubules of 4-, 10-, 35- and 90-day-old mice with anti-CCL9 and anti-WT1 antibodies, showing that CCl9 expression is restricted to early steps of spermatogenesis. (F): Electrophoretic mobility shift assays to investigate ETV5 binding to its consensus sequence in the Ccl9 promoter. The left panel shows gel shifts using nuclear extracts of TM4 cells after transfection with the pERMFLAG construct (pERMFLAG TM4). 1: <t>biotinylated</t> probe alone (B EBS3); 2: nuclear extract of pERMFLAG TM4 and B EBS3, with apparent gel shift (arrow); 3: nuclear extract of pERMFLAG TM4 with B EBS3 and nonbiotinylated probe (NB EBS3) showing outcompetition; and 4: nuclear extract of pERMFLAG TM4 with B EBS3 and ETV5 antibody (ETV5 Ab) showing a decrease of DNA/protein binding. The middle panel shows gel shifts using again pERMFLAG TM4 nuclear extracts. 1: B EBS3 alone; 2: pERMFLAG TM4 with B EBS3, showing apparent gel shift (arrow); 3: pERMFLAG TM4 with B EBS3 and ETV5 Ab showing decrease of protein-DNA binding; 4: nuclear extract of TM4 cells after transfection with control vector (Control TM4), and incubated with B EBS3; 5: control TM4 with B EBS3 and NB EBS3, 6: pERMFLAG TM4 with mutant B EBS3, and 7: pERMFLAG TM4 with mutant NB EBS3. Gel shifts with NB EBS3 substantially, but not completely outcompeted the protein-DNA complex suggesting the presence of other factors in the complex. There was no shift of protein-DNA complexes with mutant EBS3 sequences or TM4 cells transfected with control vector. The right panel shows gel shifts of purified ETV5 protein using pET vector (ETV5 protein). 1: ETV5 protein with B EBS3, showing gel shift (arrow) and 2: ETV5 protein with B EBS3 and NB EBS3 showing outcompetition. The data confirms a possible ETV5-EBS3 binding. Abbreviations: CCL9, C-C-motif ligand 9; CCR1, C-C-receptor type 1; GCNA, germ cell nuclear antigen 1; Etv5 , Ets variant gene; ETV5 protein, Ets variant protein; B EBS3, biotinylated Ets binding site 3; NB EBS3, nonbiotinylated Ets binding site 3; WT, wild type.
    3 Biotinylated Probes, supplied by GenScript, used in various techniques. Bioz Stars score: 90/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/3 biotinylated probes/product/GenScript
    Average 90 stars, based on 9 article reviews
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    3 biotinylated probes - by Bioz Stars, 2020-05
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    84
    Roche biotinylated hybridization probes
    Expression of CCL9 in mouse testis. (A): Immunofluorescence of 8-day WT mouse testis showing strong expression of CCL9 in Sertoli cells (green Alexa Fluor 488 staining). Arrows indicate locations of stem/progenitor spermatogonia, which are negative for CCL9. Scale bar = 25 µm. (B): Immunofluorescence of 8-day Etv5 -/- mouse testis showing a sharp decrease of CCL9 expression in Sertoli cells. Scale bar = 15 µm. (C): Immunofluorescence of 8-day WT mouse testis showing expression of CCR1, the receptor for CCL9, in stem/progenitor spermatogonia. Type A spermatogonia show double-staining for CCR1 (green Alexa Fluor 488 staining) and GCNA1 (pink Alexa Fluor 594 staining). The green staining in the lumen is background staining. Scale bar = 25 µm. (D): Immunohistochemistry of 6-day WT mouse testis showing expression of CCR1 in stem/progenitor spermatogonia (arrows). Scale bar = 15 µm. (E): Western blot of protein extracts from isolated WT seminiferous tubules of 4-, 10-, 35- and 90-day-old mice with anti-CCL9 and anti-WT1 antibodies, showing that CCl9 expression is restricted to early steps of spermatogenesis. (F): Electrophoretic mobility shift assays to investigate ETV5 binding to its consensus sequence in the Ccl9 promoter. The left panel shows gel shifts using nuclear extracts of TM4 cells after transfection with the pERMFLAG construct (pERMFLAG TM4). 1: <t>biotinylated</t> probe alone (B EBS3); 2: nuclear extract of pERMFLAG TM4 and B EBS3, with apparent gel shift (arrow); 3: nuclear extract of pERMFLAG TM4 with B EBS3 and nonbiotinylated probe (NB EBS3) showing outcompetition; and 4: nuclear extract of pERMFLAG TM4 with B EBS3 and ETV5 antibody (ETV5 Ab) showing a decrease of DNA/protein binding. The middle panel shows gel shifts using again pERMFLAG TM4 nuclear extracts. 1: B EBS3 alone; 2: pERMFLAG TM4 with B EBS3, showing apparent gel shift (arrow); 3: pERMFLAG TM4 with B EBS3 and ETV5 Ab showing decrease of protein-DNA binding; 4: nuclear extract of TM4 cells after transfection with control vector (Control TM4), and incubated with B EBS3; 5: control TM4 with B EBS3 and NB EBS3, 6: pERMFLAG TM4 with mutant B EBS3, and 7: pERMFLAG TM4 with mutant NB EBS3. Gel shifts with NB EBS3 substantially, but not completely outcompeted the protein-DNA complex suggesting the presence of other factors in the complex. There was no shift of protein-DNA complexes with mutant EBS3 sequences or TM4 cells transfected with control vector. The right panel shows gel shifts of purified ETV5 protein using pET vector (ETV5 protein). 1: ETV5 protein with B EBS3, showing gel shift (arrow) and 2: ETV5 protein with B EBS3 and NB EBS3 showing outcompetition. The data confirms a possible ETV5-EBS3 binding. Abbreviations: CCL9, C-C-motif ligand 9; CCR1, C-C-receptor type 1; GCNA, germ cell nuclear antigen 1; Etv5 , Ets variant gene; ETV5 protein, Ets variant protein; B EBS3, biotinylated Ets binding site 3; NB EBS3, nonbiotinylated Ets binding site 3; WT, wild type.
    Biotinylated Hybridization Probes, supplied by Roche, used in various techniques. Bioz Stars score: 84/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/biotinylated hybridization probes/product/Roche
    Average 84 stars, based on 1 article reviews
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    biotinylated hybridization probes - by Bioz Stars, 2020-05
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    91
    Roche biotinylated oligo probes
    Expression of CCL9 in mouse testis. (A): Immunofluorescence of 8-day WT mouse testis showing strong expression of CCL9 in Sertoli cells (green Alexa Fluor 488 staining). Arrows indicate locations of stem/progenitor spermatogonia, which are negative for CCL9. Scale bar = 25 µm. (B): Immunofluorescence of 8-day Etv5 -/- mouse testis showing a sharp decrease of CCL9 expression in Sertoli cells. Scale bar = 15 µm. (C): Immunofluorescence of 8-day WT mouse testis showing expression of CCR1, the receptor for CCL9, in stem/progenitor spermatogonia. Type A spermatogonia show double-staining for CCR1 (green Alexa Fluor 488 staining) and GCNA1 (pink Alexa Fluor 594 staining). The green staining in the lumen is background staining. Scale bar = 25 µm. (D): Immunohistochemistry of 6-day WT mouse testis showing expression of CCR1 in stem/progenitor spermatogonia (arrows). Scale bar = 15 µm. (E): Western blot of protein extracts from isolated WT seminiferous tubules of 4-, 10-, 35- and 90-day-old mice with anti-CCL9 and anti-WT1 antibodies, showing that CCl9 expression is restricted to early steps of spermatogenesis. (F): Electrophoretic mobility shift assays to investigate ETV5 binding to its consensus sequence in the Ccl9 promoter. The left panel shows gel shifts using nuclear extracts of TM4 cells after transfection with the pERMFLAG construct (pERMFLAG TM4). 1: <t>biotinylated</t> probe alone (B EBS3); 2: nuclear extract of pERMFLAG TM4 and B EBS3, with apparent gel shift (arrow); 3: nuclear extract of pERMFLAG TM4 with B EBS3 and nonbiotinylated probe (NB EBS3) showing outcompetition; and 4: nuclear extract of pERMFLAG TM4 with B EBS3 and ETV5 antibody (ETV5 Ab) showing a decrease of DNA/protein binding. The middle panel shows gel shifts using again pERMFLAG TM4 nuclear extracts. 1: B EBS3 alone; 2: pERMFLAG TM4 with B EBS3, showing apparent gel shift (arrow); 3: pERMFLAG TM4 with B EBS3 and ETV5 Ab showing decrease of protein-DNA binding; 4: nuclear extract of TM4 cells after transfection with control vector (Control TM4), and incubated with B EBS3; 5: control TM4 with B EBS3 and NB EBS3, 6: pERMFLAG TM4 with mutant B EBS3, and 7: pERMFLAG TM4 with mutant NB EBS3. Gel shifts with NB EBS3 substantially, but not completely outcompeted the protein-DNA complex suggesting the presence of other factors in the complex. There was no shift of protein-DNA complexes with mutant EBS3 sequences or TM4 cells transfected with control vector. The right panel shows gel shifts of purified ETV5 protein using pET vector (ETV5 protein). 1: ETV5 protein with B EBS3, showing gel shift (arrow) and 2: ETV5 protein with B EBS3 and NB EBS3 showing outcompetition. The data confirms a possible ETV5-EBS3 binding. Abbreviations: CCL9, C-C-motif ligand 9; CCR1, C-C-receptor type 1; GCNA, germ cell nuclear antigen 1; Etv5 , Ets variant gene; ETV5 protein, Ets variant protein; B EBS3, biotinylated Ets binding site 3; NB EBS3, nonbiotinylated Ets binding site 3; WT, wild type.
    Biotinylated Oligo Probes, supplied by Roche, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher 5 biotinylated oligonucleotide probe
    Expression of CCL9 in mouse testis. (A): Immunofluorescence of 8-day WT mouse testis showing strong expression of CCL9 in Sertoli cells (green Alexa Fluor 488 staining). Arrows indicate locations of stem/progenitor spermatogonia, which are negative for CCL9. Scale bar = 25 µm. (B): Immunofluorescence of 8-day Etv5 -/- mouse testis showing a sharp decrease of CCL9 expression in Sertoli cells. Scale bar = 15 µm. (C): Immunofluorescence of 8-day WT mouse testis showing expression of CCR1, the receptor for CCL9, in stem/progenitor spermatogonia. Type A spermatogonia show double-staining for CCR1 (green Alexa Fluor 488 staining) and GCNA1 (pink Alexa Fluor 594 staining). The green staining in the lumen is background staining. Scale bar = 25 µm. (D): Immunohistochemistry of 6-day WT mouse testis showing expression of CCR1 in stem/progenitor spermatogonia (arrows). Scale bar = 15 µm. (E): Western blot of protein extracts from isolated WT seminiferous tubules of 4-, 10-, 35- and 90-day-old mice with anti-CCL9 and anti-WT1 antibodies, showing that CCl9 expression is restricted to early steps of spermatogenesis. (F): Electrophoretic mobility shift assays to investigate ETV5 binding to its consensus sequence in the Ccl9 promoter. The left panel shows gel shifts using nuclear extracts of TM4 cells after transfection with the pERMFLAG construct (pERMFLAG TM4). 1: <t>biotinylated</t> probe alone (B EBS3); 2: nuclear extract of pERMFLAG TM4 and B EBS3, with apparent gel shift (arrow); 3: nuclear extract of pERMFLAG TM4 with B EBS3 and nonbiotinylated probe (NB EBS3) showing outcompetition; and 4: nuclear extract of pERMFLAG TM4 with B EBS3 and ETV5 antibody (ETV5 Ab) showing a decrease of DNA/protein binding. The middle panel shows gel shifts using again pERMFLAG TM4 nuclear extracts. 1: B EBS3 alone; 2: pERMFLAG TM4 with B EBS3, showing apparent gel shift (arrow); 3: pERMFLAG TM4 with B EBS3 and ETV5 Ab showing decrease of protein-DNA binding; 4: nuclear extract of TM4 cells after transfection with control vector (Control TM4), and incubated with B EBS3; 5: control TM4 with B EBS3 and NB EBS3, 6: pERMFLAG TM4 with mutant B EBS3, and 7: pERMFLAG TM4 with mutant NB EBS3. Gel shifts with NB EBS3 substantially, but not completely outcompeted the protein-DNA complex suggesting the presence of other factors in the complex. There was no shift of protein-DNA complexes with mutant EBS3 sequences or TM4 cells transfected with control vector. The right panel shows gel shifts of purified ETV5 protein using pET vector (ETV5 protein). 1: ETV5 protein with B EBS3, showing gel shift (arrow) and 2: ETV5 protein with B EBS3 and NB EBS3 showing outcompetition. The data confirms a possible ETV5-EBS3 binding. Abbreviations: CCL9, C-C-motif ligand 9; CCR1, C-C-receptor type 1; GCNA, germ cell nuclear antigen 1; Etv5 , Ets variant gene; ETV5 protein, Ets variant protein; B EBS3, biotinylated Ets binding site 3; NB EBS3, nonbiotinylated Ets binding site 3; WT, wild type.
    5 Biotinylated Oligonucleotide Probe, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 88/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher biotinylated dna probes
    Expression of CCL9 in mouse testis. (A): Immunofluorescence of 8-day WT mouse testis showing strong expression of CCL9 in Sertoli cells (green Alexa Fluor 488 staining). Arrows indicate locations of stem/progenitor spermatogonia, which are negative for CCL9. Scale bar = 25 µm. (B): Immunofluorescence of 8-day Etv5 -/- mouse testis showing a sharp decrease of CCL9 expression in Sertoli cells. Scale bar = 15 µm. (C): Immunofluorescence of 8-day WT mouse testis showing expression of CCR1, the receptor for CCL9, in stem/progenitor spermatogonia. Type A spermatogonia show double-staining for CCR1 (green Alexa Fluor 488 staining) and GCNA1 (pink Alexa Fluor 594 staining). The green staining in the lumen is background staining. Scale bar = 25 µm. (D): Immunohistochemistry of 6-day WT mouse testis showing expression of CCR1 in stem/progenitor spermatogonia (arrows). Scale bar = 15 µm. (E): Western blot of protein extracts from isolated WT seminiferous tubules of 4-, 10-, 35- and 90-day-old mice with anti-CCL9 and anti-WT1 antibodies, showing that CCl9 expression is restricted to early steps of spermatogenesis. (F): Electrophoretic mobility shift assays to investigate ETV5 binding to its consensus sequence in the Ccl9 promoter. The left panel shows gel shifts using nuclear extracts of TM4 cells after transfection with the pERMFLAG construct (pERMFLAG TM4). 1: <t>biotinylated</t> probe alone (B EBS3); 2: nuclear extract of pERMFLAG TM4 and B EBS3, with apparent gel shift (arrow); 3: nuclear extract of pERMFLAG TM4 with B EBS3 and nonbiotinylated probe (NB EBS3) showing outcompetition; and 4: nuclear extract of pERMFLAG TM4 with B EBS3 and ETV5 antibody (ETV5 Ab) showing a decrease of DNA/protein binding. The middle panel shows gel shifts using again pERMFLAG TM4 nuclear extracts. 1: B EBS3 alone; 2: pERMFLAG TM4 with B EBS3, showing apparent gel shift (arrow); 3: pERMFLAG TM4 with B EBS3 and ETV5 Ab showing decrease of protein-DNA binding; 4: nuclear extract of TM4 cells after transfection with control vector (Control TM4), and incubated with B EBS3; 5: control TM4 with B EBS3 and NB EBS3, 6: pERMFLAG TM4 with mutant B EBS3, and 7: pERMFLAG TM4 with mutant NB EBS3. Gel shifts with NB EBS3 substantially, but not completely outcompeted the protein-DNA complex suggesting the presence of other factors in the complex. There was no shift of protein-DNA complexes with mutant EBS3 sequences or TM4 cells transfected with control vector. The right panel shows gel shifts of purified ETV5 protein using pET vector (ETV5 protein). 1: ETV5 protein with B EBS3, showing gel shift (arrow) and 2: ETV5 protein with B EBS3 and NB EBS3 showing outcompetition. The data confirms a possible ETV5-EBS3 binding. Abbreviations: CCL9, C-C-motif ligand 9; CCR1, C-C-receptor type 1; GCNA, germ cell nuclear antigen 1; Etv5 , Ets variant gene; ETV5 protein, Ets variant protein; B EBS3, biotinylated Ets binding site 3; NB EBS3, nonbiotinylated Ets binding site 3; WT, wild type.
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    Millipore 5 biotinylated oligonucleotide probe
    Expression of CCL9 in mouse testis. (A): Immunofluorescence of 8-day WT mouse testis showing strong expression of CCL9 in Sertoli cells (green Alexa Fluor 488 staining). Arrows indicate locations of stem/progenitor spermatogonia, which are negative for CCL9. Scale bar = 25 µm. (B): Immunofluorescence of 8-day Etv5 -/- mouse testis showing a sharp decrease of CCL9 expression in Sertoli cells. Scale bar = 15 µm. (C): Immunofluorescence of 8-day WT mouse testis showing expression of CCR1, the receptor for CCL9, in stem/progenitor spermatogonia. Type A spermatogonia show double-staining for CCR1 (green Alexa Fluor 488 staining) and GCNA1 (pink Alexa Fluor 594 staining). The green staining in the lumen is background staining. Scale bar = 25 µm. (D): Immunohistochemistry of 6-day WT mouse testis showing expression of CCR1 in stem/progenitor spermatogonia (arrows). Scale bar = 15 µm. (E): Western blot of protein extracts from isolated WT seminiferous tubules of 4-, 10-, 35- and 90-day-old mice with anti-CCL9 and anti-WT1 antibodies, showing that CCl9 expression is restricted to early steps of spermatogenesis. (F): Electrophoretic mobility shift assays to investigate ETV5 binding to its consensus sequence in the Ccl9 promoter. The left panel shows gel shifts using nuclear extracts of TM4 cells after transfection with the pERMFLAG construct (pERMFLAG TM4). 1: <t>biotinylated</t> probe alone (B EBS3); 2: nuclear extract of pERMFLAG TM4 and B EBS3, with apparent gel shift (arrow); 3: nuclear extract of pERMFLAG TM4 with B EBS3 and nonbiotinylated probe (NB EBS3) showing outcompetition; and 4: nuclear extract of pERMFLAG TM4 with B EBS3 and ETV5 antibody (ETV5 Ab) showing a decrease of DNA/protein binding. The middle panel shows gel shifts using again pERMFLAG TM4 nuclear extracts. 1: B EBS3 alone; 2: pERMFLAG TM4 with B EBS3, showing apparent gel shift (arrow); 3: pERMFLAG TM4 with B EBS3 and ETV5 Ab showing decrease of protein-DNA binding; 4: nuclear extract of TM4 cells after transfection with control vector (Control TM4), and incubated with B EBS3; 5: control TM4 with B EBS3 and NB EBS3, 6: pERMFLAG TM4 with mutant B EBS3, and 7: pERMFLAG TM4 with mutant NB EBS3. Gel shifts with NB EBS3 substantially, but not completely outcompeted the protein-DNA complex suggesting the presence of other factors in the complex. There was no shift of protein-DNA complexes with mutant EBS3 sequences or TM4 cells transfected with control vector. The right panel shows gel shifts of purified ETV5 protein using pET vector (ETV5 protein). 1: ETV5 protein with B EBS3, showing gel shift (arrow) and 2: ETV5 protein with B EBS3 and NB EBS3 showing outcompetition. The data confirms a possible ETV5-EBS3 binding. Abbreviations: CCL9, C-C-motif ligand 9; CCR1, C-C-receptor type 1; GCNA, germ cell nuclear antigen 1; Etv5 , Ets variant gene; ETV5 protein, Ets variant protein; B EBS3, biotinylated Ets binding site 3; NB EBS3, nonbiotinylated Ets binding site 3; WT, wild type.
    5 Biotinylated Oligonucleotide Probe, supplied by Millipore, used in various techniques. Bioz Stars score: 85/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Promega biotinylated oligo dt25 probe
    Localization of 7-Helix-1 in SGs and interaction with translational repressors. (A) Co-localization of 7-Helix-1 with mRNA-aggregates. Mature WF NF54 gametocytes were subjected to mRNA-FISH-IFA and mRNA was labeled with a <t>biotinylated</t> <t>oligo-dT25</t> probe (red); counterlabeling was performed using mouse anti-7-Helix-1rp2 antisera (green). Nuclei were highlighted by Hoechst33342 nuclear stain (blue). Frame indicates the area chosen for enlargement. DIC, differential interference contrast. Bar, 5 μm; enlargement, 1 μm. (B) Accumulation of 7-Helix-1 in SG fractions. Gametocytes of line 7-Helix-1-HA were stressed by treatment with sodium arsenite for 1 h and a SG core fraction enrichment was conducted. Lysates of 7-Helix-1-HA gametocytes (-) and of enriched SGs (+) were subjected to WB, using mouse antisera directed against Pf39 (~39 kDa) or PfM1-AP (~126 and 68 kDa, black arrows) or rabbit antibodies against HSP70-1 (~70 kDa) or the HA-tag to detect 7-Helix-1-HA (~60 kDa). (C) Co-immunoprecipitation of 7-Helix-1 with CITH, PABP1 and DOZI. Lysates of WT NF54 or 7-Helix-1-HA gametocytes were subjected to co-immunoprecipitation assays using polyclonal mouse anti-7-Helix-1rp2 antisera or polyclonal rabbit anti-DOZI antisera, followed by WB using rabbit anti-CITH, anti-PABP1 and anti-HA antibodies or mouse anti-Pf39 antibody to detect precipitated proteins. Grey arrow indicates the expected running line in the negative control. Asterisk indicates a band corresponding to the precipitation antibody. (D) Co-localization of 7-Helix-1 with CITH, PABP1 and DOZI. WT NF54 gametocytes were immunolabeled with mouse anti-7-Helix-1rp2 antisera (green) and rabbit anti-CITH, anti-PABP1, or anti-DOZI antibodies (red). Nuclei were highlighted by Hoechst33342 nuclear stain (blue). DIC, differential interference contrast. Bar, 5 μm. Results are representative of three independent experiments.
    Biotinylated Oligo Dt25 Probe, supplied by Promega, used in various techniques. Bioz Stars score: 92/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Eurofins biotinylated dna probe
    Localization of 7-Helix-1 in SGs and interaction with translational repressors. (A) Co-localization of 7-Helix-1 with mRNA-aggregates. Mature WF NF54 gametocytes were subjected to mRNA-FISH-IFA and mRNA was labeled with a <t>biotinylated</t> <t>oligo-dT25</t> probe (red); counterlabeling was performed using mouse anti-7-Helix-1rp2 antisera (green). Nuclei were highlighted by Hoechst33342 nuclear stain (blue). Frame indicates the area chosen for enlargement. DIC, differential interference contrast. Bar, 5 μm; enlargement, 1 μm. (B) Accumulation of 7-Helix-1 in SG fractions. Gametocytes of line 7-Helix-1-HA were stressed by treatment with sodium arsenite for 1 h and a SG core fraction enrichment was conducted. Lysates of 7-Helix-1-HA gametocytes (-) and of enriched SGs (+) were subjected to WB, using mouse antisera directed against Pf39 (~39 kDa) or PfM1-AP (~126 and 68 kDa, black arrows) or rabbit antibodies against HSP70-1 (~70 kDa) or the HA-tag to detect 7-Helix-1-HA (~60 kDa). (C) Co-immunoprecipitation of 7-Helix-1 with CITH, PABP1 and DOZI. Lysates of WT NF54 or 7-Helix-1-HA gametocytes were subjected to co-immunoprecipitation assays using polyclonal mouse anti-7-Helix-1rp2 antisera or polyclonal rabbit anti-DOZI antisera, followed by WB using rabbit anti-CITH, anti-PABP1 and anti-HA antibodies or mouse anti-Pf39 antibody to detect precipitated proteins. Grey arrow indicates the expected running line in the negative control. Asterisk indicates a band corresponding to the precipitation antibody. (D) Co-localization of 7-Helix-1 with CITH, PABP1 and DOZI. WT NF54 gametocytes were immunolabeled with mouse anti-7-Helix-1rp2 antisera (green) and rabbit anti-CITH, anti-PABP1, or anti-DOZI antibodies (red). Nuclei were highlighted by Hoechst33342 nuclear stain (blue). DIC, differential interference contrast. Bar, 5 μm. Results are representative of three independent experiments.
    Biotinylated Dna Probe, supplied by Eurofins, used in various techniques. Bioz Stars score: 93/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Roche biotinylated probes
    Binding of SP1 to MRE1.3, MRE1.3a and MRE1.3c in EMSAs. ( A ) Sequences of MRE1.3 with in silico predicted SP1-binding sites, different MRE1.3 deletion constructs and constructs with mutated SP1-binding site are depicted. ( B ) EMSAs for detection of SP1 binding were performed with <t>biotinylated</t> MRE1.3 (lanes 1–3) or MRE1.3a (lanes 4–6) probe. Probes were either incubated with buffer (probe), 300 ng BSA as control for unspecific protein interactions (BSA) or with 300 ng of rhSP1. ( C ) To identify the relevant SP1-binding site for the interaction, we compared biotinylated MRE1.3c (lanes 1–3) with biotinylated MRE1.3 (lanes 4–6). Probes were either incubated with only buffer (probe), 300 ng of BSA as control for unspecific protein interactions (BSA) or with 300 ng of rhSP1. ( D ) To exclude unspecific SP1-DNA interactions, EMSAs with biotinylated MRE1.3 (lanes 1–3) were compared with EMSAs with biotinylated CRE (cAMP response element) (lanes 4–6) probe. Probes were either incubated with only buffer (probe), 300 ng of BSA as control for unspecific protein interactions (BSA) or with 300 ng of rhSP1 ( N = 6). ( E ) To verify in vivo binding of SP1 to MRE1.3, we analyzed binding of protein from nuclear extracts to MRE1.3 and MRE1.3 with mutations in the SP1-binding sequence, MRE1.3mut1 and MRE1.3mut2. Biotinylated SP1 consensus sequence was used as a positive control. Probes were either incubated with only buffer (probe) or nuclear extracts (NE) ( N = 4).
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    Illumina Inc biotinylated probes
    Binding of SP1 to MRE1.3, MRE1.3a and MRE1.3c in EMSAs. ( A ) Sequences of MRE1.3 with in silico predicted SP1-binding sites, different MRE1.3 deletion constructs and constructs with mutated SP1-binding site are depicted. ( B ) EMSAs for detection of SP1 binding were performed with <t>biotinylated</t> MRE1.3 (lanes 1–3) or MRE1.3a (lanes 4–6) probe. Probes were either incubated with buffer (probe), 300 ng BSA as control for unspecific protein interactions (BSA) or with 300 ng of rhSP1. ( C ) To identify the relevant SP1-binding site for the interaction, we compared biotinylated MRE1.3c (lanes 1–3) with biotinylated MRE1.3 (lanes 4–6). Probes were either incubated with only buffer (probe), 300 ng of BSA as control for unspecific protein interactions (BSA) or with 300 ng of rhSP1. ( D ) To exclude unspecific SP1-DNA interactions, EMSAs with biotinylated MRE1.3 (lanes 1–3) were compared with EMSAs with biotinylated CRE (cAMP response element) (lanes 4–6) probe. Probes were either incubated with only buffer (probe), 300 ng of BSA as control for unspecific protein interactions (BSA) or with 300 ng of rhSP1 ( N = 6). ( E ) To verify in vivo binding of SP1 to MRE1.3, we analyzed binding of protein from nuclear extracts to MRE1.3 and MRE1.3 with mutations in the SP1-binding sequence, MRE1.3mut1 and MRE1.3mut2. Biotinylated SP1 consensus sequence was used as a positive control. Probes were either incubated with only buffer (probe) or nuclear extracts (NE) ( N = 4).
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    Lofstrand biotinylated probe
    Binding of SP1 to MRE1.3, MRE1.3a and MRE1.3c in EMSAs. ( A ) Sequences of MRE1.3 with in silico predicted SP1-binding sites, different MRE1.3 deletion constructs and constructs with mutated SP1-binding site are depicted. ( B ) EMSAs for detection of SP1 binding were performed with <t>biotinylated</t> MRE1.3 (lanes 1–3) or MRE1.3a (lanes 4–6) probe. Probes were either incubated with buffer (probe), 300 ng BSA as control for unspecific protein interactions (BSA) or with 300 ng of rhSP1. ( C ) To identify the relevant SP1-binding site for the interaction, we compared biotinylated MRE1.3c (lanes 1–3) with biotinylated MRE1.3 (lanes 4–6). Probes were either incubated with only buffer (probe), 300 ng of BSA as control for unspecific protein interactions (BSA) or with 300 ng of rhSP1. ( D ) To exclude unspecific SP1-DNA interactions, EMSAs with biotinylated MRE1.3 (lanes 1–3) were compared with EMSAs with biotinylated CRE (cAMP response element) (lanes 4–6) probe. Probes were either incubated with only buffer (probe), 300 ng of BSA as control for unspecific protein interactions (BSA) or with 300 ng of rhSP1 ( N = 6). ( E ) To verify in vivo binding of SP1 to MRE1.3, we analyzed binding of protein from nuclear extracts to MRE1.3 and MRE1.3 with mutations in the SP1-binding sequence, MRE1.3mut1 and MRE1.3mut2. Biotinylated SP1 consensus sequence was used as a positive control. Probes were either incubated with only buffer (probe) or nuclear extracts (NE) ( N = 4).
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    Toyobo biotinylated probe
    Binding of SP1 to MRE1.3, MRE1.3a and MRE1.3c in EMSAs. ( A ) Sequences of MRE1.3 with in silico predicted SP1-binding sites, different MRE1.3 deletion constructs and constructs with mutated SP1-binding site are depicted. ( B ) EMSAs for detection of SP1 binding were performed with <t>biotinylated</t> MRE1.3 (lanes 1–3) or MRE1.3a (lanes 4–6) probe. Probes were either incubated with buffer (probe), 300 ng BSA as control for unspecific protein interactions (BSA) or with 300 ng of rhSP1. ( C ) To identify the relevant SP1-binding site for the interaction, we compared biotinylated MRE1.3c (lanes 1–3) with biotinylated MRE1.3 (lanes 4–6). Probes were either incubated with only buffer (probe), 300 ng of BSA as control for unspecific protein interactions (BSA) or with 300 ng of rhSP1. ( D ) To exclude unspecific SP1-DNA interactions, EMSAs with biotinylated MRE1.3 (lanes 1–3) were compared with EMSAs with biotinylated CRE (cAMP response element) (lanes 4–6) probe. Probes were either incubated with only buffer (probe), 300 ng of BSA as control for unspecific protein interactions (BSA) or with 300 ng of rhSP1 ( N = 6). ( E ) To verify in vivo binding of SP1 to MRE1.3, we analyzed binding of protein from nuclear extracts to MRE1.3 and MRE1.3 with mutations in the SP1-binding sequence, MRE1.3mut1 and MRE1.3mut2. Biotinylated SP1 consensus sequence was used as a positive control. Probes were either incubated with only buffer (probe) or nuclear extracts (NE) ( N = 4).
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    Enzo Biochem biotinylated adv type 5 probe
    Binding of SP1 to MRE1.3, MRE1.3a and MRE1.3c in EMSAs. ( A ) Sequences of MRE1.3 with in silico predicted SP1-binding sites, different MRE1.3 deletion constructs and constructs with mutated SP1-binding site are depicted. ( B ) EMSAs for detection of SP1 binding were performed with <t>biotinylated</t> MRE1.3 (lanes 1–3) or MRE1.3a (lanes 4–6) probe. Probes were either incubated with buffer (probe), 300 ng BSA as control for unspecific protein interactions (BSA) or with 300 ng of rhSP1. ( C ) To identify the relevant SP1-binding site for the interaction, we compared biotinylated MRE1.3c (lanes 1–3) with biotinylated MRE1.3 (lanes 4–6). Probes were either incubated with only buffer (probe), 300 ng of BSA as control for unspecific protein interactions (BSA) or with 300 ng of rhSP1. ( D ) To exclude unspecific SP1-DNA interactions, EMSAs with biotinylated MRE1.3 (lanes 1–3) were compared with EMSAs with biotinylated CRE (cAMP response element) (lanes 4–6) probe. Probes were either incubated with only buffer (probe), 300 ng of BSA as control for unspecific protein interactions (BSA) or with 300 ng of rhSP1 ( N = 6). ( E ) To verify in vivo binding of SP1 to MRE1.3, we analyzed binding of protein from nuclear extracts to MRE1.3 and MRE1.3 with mutations in the SP1-binding sequence, MRE1.3mut1 and MRE1.3mut2. Biotinylated SP1 consensus sequence was used as a positive control. Probes were either incubated with only buffer (probe) or nuclear extracts (NE) ( N = 4).
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    GST pull-downs and Far Western blots indicate increased Src SH3-SH2 interaction with KDR/Flk-1 upon VEGF stimulation . (A) HUVECs were either serum-starved (0') or starved and then VEGF-treated (15 ng/mL for 15 min) (15'). The indicated GST-Src domain fusion proteins (see below) bound to glutathione-agarose beads were used (500 pmol equimolar amounts each), in pull-down incubations with equal amounts of protein lysate samples (500 μg each). The pull-down complexes were resolved on a 7% acrylamide SDS-PAGE gel and transferred to nitrocellulose. Immunoblotting was then performed using α-KDR/Flk-1 (A-3) or α-Flt-1 (H-225). GU, GST-Src unique domain fusion protein; GU32, GST-Src unique SH3 SH2 domain fusion protein; G32, GST-Src SH3 SH2 domain fusion protein. (B) Cell extract (pre-pull-down) input levels of phosphotyrosine KDR/Flk-1 and KDR/Flk-1, from HUVECs either serum-starved (0') or starved and then VEGF-treated (15'). (C) Cell extract (pre-pull-down) input levels of phosphotyrosine Flt-1 and Flt-1, from HUVECs either serum-starved (0') or starved and then VEGF-treated (15'). (D) HUVECs were serum-starved (-) or VEGF-treated with VEGF (15 ng/mL for 15 min) (+). The cell extracts were then immunoprecipitated using α-KDR/Flk-1 (N-931). The immunocomplexes were resolved on a 7% acrylamide SDS-PAGE gel. Biotinylated GST and biotinylated GST-Src SH3-SH2 fusion protein were used in Far Western blotting. Detection was performed using horseradish peroxidase-conjugated ExtrAvidin ® , followed by enhanced chemiluminescence detection reagents. Immunoprecipitation-Western blots for levels of phosphotyrosine KDR/Flk-1 and KDR/Flk-1 of the serum-starved (-) or VEGF-treated HUVEC (+) cell extracts were also performed in parallel.

    Journal: BMC Biochemistry

    Article Title: Src Kinase becomes preferentially associated with the VEGFR, KDR/Flk-1, following VEGF stimulation of vascular endothelial cells

    doi: 10.1186/1471-2091-3-32

    Figure Lengend Snippet: GST pull-downs and Far Western blots indicate increased Src SH3-SH2 interaction with KDR/Flk-1 upon VEGF stimulation . (A) HUVECs were either serum-starved (0') or starved and then VEGF-treated (15 ng/mL for 15 min) (15'). The indicated GST-Src domain fusion proteins (see below) bound to glutathione-agarose beads were used (500 pmol equimolar amounts each), in pull-down incubations with equal amounts of protein lysate samples (500 μg each). The pull-down complexes were resolved on a 7% acrylamide SDS-PAGE gel and transferred to nitrocellulose. Immunoblotting was then performed using α-KDR/Flk-1 (A-3) or α-Flt-1 (H-225). GU, GST-Src unique domain fusion protein; GU32, GST-Src unique SH3 SH2 domain fusion protein; G32, GST-Src SH3 SH2 domain fusion protein. (B) Cell extract (pre-pull-down) input levels of phosphotyrosine KDR/Flk-1 and KDR/Flk-1, from HUVECs either serum-starved (0') or starved and then VEGF-treated (15'). (C) Cell extract (pre-pull-down) input levels of phosphotyrosine Flt-1 and Flt-1, from HUVECs either serum-starved (0') or starved and then VEGF-treated (15'). (D) HUVECs were serum-starved (-) or VEGF-treated with VEGF (15 ng/mL for 15 min) (+). The cell extracts were then immunoprecipitated using α-KDR/Flk-1 (N-931). The immunocomplexes were resolved on a 7% acrylamide SDS-PAGE gel. Biotinylated GST and biotinylated GST-Src SH3-SH2 fusion protein were used in Far Western blotting. Detection was performed using horseradish peroxidase-conjugated ExtrAvidin ® , followed by enhanced chemiluminescence detection reagents. Immunoprecipitation-Western blots for levels of phosphotyrosine KDR/Flk-1 and KDR/Flk-1 of the serum-starved (-) or VEGF-treated HUVEC (+) cell extracts were also performed in parallel.

    Article Snippet: Biotinylated probes were detected with horseradish peroxidase-conjugated ExtrAvidin® (Sigma) at 1:2000 dilution in PBS, 3 % BSA, 0.05% Tween-20.

    Techniques: Western Blot, SDS Page, Immunoprecipitation, Far Western Blot

    Accumulation of replicated plasmid DNA in BJAB cells and BJAB cells stably expressing the indicated EBNA-1 derivatives at 48 h after transfection with the oriP plasmid pOLP DNA. Nonchromosomal DNA was extracted from the indicated number of transfected cells (lanes 6–15) or from control BJAB cells (10 6 ) that were mixed with the indicated amounts of pOLP DNA (lanes 1–5) and assayed for the plasmid DNA by Southern blot analysis after Xho I digestion to linearize the plasmid DNA. DNAs in lanes 6–10 were also digested by Dpn I. The sizes (kb) of biotinylated λ Hin dIII DNA markers are indicated on the left. The signal intensity increased linearly for amounts of input pOLP DNA up to at least 3 ng (data not shown). The amounts of full-length (9.3 kb) pOLP DNA in lanes 6–15 were estimated by comparing the intensity with that of lanes 1–5. The percentage of Dpn I-resistant pOLP DNA was calculated by dividing the amount of the full-length pOLP DNA in the Dpn I-digested sample by that in the undigested sample after correction to the same number of cells.

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

    Article Title: Maintenance of Epstein-Barr virus (EBV)oriP-based episomes requires EBV-encoded nuclear antigen-1 chromosome-binding domains, which can be replaced by high-mobility group-I or histone H1

    doi:

    Figure Lengend Snippet: Accumulation of replicated plasmid DNA in BJAB cells and BJAB cells stably expressing the indicated EBNA-1 derivatives at 48 h after transfection with the oriP plasmid pOLP DNA. Nonchromosomal DNA was extracted from the indicated number of transfected cells (lanes 6–15) or from control BJAB cells (10 6 ) that were mixed with the indicated amounts of pOLP DNA (lanes 1–5) and assayed for the plasmid DNA by Southern blot analysis after Xho I digestion to linearize the plasmid DNA. DNAs in lanes 6–10 were also digested by Dpn I. The sizes (kb) of biotinylated λ Hin dIII DNA markers are indicated on the left. The signal intensity increased linearly for amounts of input pOLP DNA up to at least 3 ng (data not shown). The amounts of full-length (9.3 kb) pOLP DNA in lanes 6–15 were estimated by comparing the intensity with that of lanes 1–5. The percentage of Dpn I-resistant pOLP DNA was calculated by dividing the amount of the full-length pOLP DNA in the Dpn I-digested sample by that in the undigested sample after correction to the same number of cells.

    Article Snippet: Biotinylated probes were prepared from the 4.7-kb Aat II– Ase I oriP -firefly luciferase gene fragment of pOL and dissolved in in situ hybridization solution (Dako) at 5 ng/μl.

    Techniques: Plasmid Preparation, Stable Transfection, Expressing, Transfection, Southern Blot

    Southern blot of plasmid DNA stably persisting in BJAB cells expressing the indicated EBNA-1 derivatives after transfection with oriP -positive pOLP or oriP -negative pLP plasmid DNA. Transfected cells were grown for 31 days in puromycin (0.5 μg/ml). Controls for the number of plasmids per cell (lanes 1–4) were made by adding the appropriate amounts of plasmid DNA to 10 6 BJAB cells before extraction. Nonchromosomal DNA was extracted from 10 6 transfected or control cells and assayed for plasmid DNA after digestion with Xho I to linearize the plasmid DNA. The sizes (kb) of the biotinylated λ Hin dIII DNA markers are indicated on the left. Similar results were obtained in an identical experiment (data not shown).

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

    Article Title: Maintenance of Epstein-Barr virus (EBV)oriP-based episomes requires EBV-encoded nuclear antigen-1 chromosome-binding domains, which can be replaced by high-mobility group-I or histone H1

    doi:

    Figure Lengend Snippet: Southern blot of plasmid DNA stably persisting in BJAB cells expressing the indicated EBNA-1 derivatives after transfection with oriP -positive pOLP or oriP -negative pLP plasmid DNA. Transfected cells were grown for 31 days in puromycin (0.5 μg/ml). Controls for the number of plasmids per cell (lanes 1–4) were made by adding the appropriate amounts of plasmid DNA to 10 6 BJAB cells before extraction. Nonchromosomal DNA was extracted from 10 6 transfected or control cells and assayed for plasmid DNA after digestion with Xho I to linearize the plasmid DNA. The sizes (kb) of the biotinylated λ Hin dIII DNA markers are indicated on the left. Similar results were obtained in an identical experiment (data not shown).

    Article Snippet: Biotinylated probes were prepared from the 4.7-kb Aat II– Ase I oriP -firefly luciferase gene fragment of pOL and dissolved in in situ hybridization solution (Dako) at 5 ng/μl.

    Techniques: Southern Blot, Plasmid Preparation, Stable Transfection, Expressing, Transfection, Plasmid Purification

    Receiver operating characteristic curves for head and neck squamous cell carcinomas by combined p16 immuno-histochemistry and HPV DNA testing by in-situ hybridization using the INFORM ® HPV-III Fam16(B) (Ventana, CA) and HPV16/18 biotinylated GenPoint ™ (Dako, CA) probes, or by MY-PCR, compared to HPV16 E6/E7 RT-PCR. Non-parametric receiver operating characteristic curves shown for combined test results with p16 immuno-histochemistry (assuming a 1+/≥10% cut-off) stratified by HPV Ventana in-situ hybridization (-■-), Dako in-situ hybridization (-▲-), or MY-PCR (-●-) results. Solitary markers shown reflect single test performance statistics for p16 IHC (assuming a 2+/≥75% cut-off) ( + ) and MY-PCR for HPV16 ( X ) alone. The dashed line indicates a reference test threshold with area under the receiver operating characteristic curve of 0.5.

    Journal: Modern pathology : an official journal of the United States and Canadian Academy of Pathology, Inc

    Article Title: A comparison of clinically utilized human papillomavirus detection methods in head and neck cancer

    doi: 10.1038/modpathol.2011.91

    Figure Lengend Snippet: Receiver operating characteristic curves for head and neck squamous cell carcinomas by combined p16 immuno-histochemistry and HPV DNA testing by in-situ hybridization using the INFORM ® HPV-III Fam16(B) (Ventana, CA) and HPV16/18 biotinylated GenPoint ™ (Dako, CA) probes, or by MY-PCR, compared to HPV16 E6/E7 RT-PCR. Non-parametric receiver operating characteristic curves shown for combined test results with p16 immuno-histochemistry (assuming a 1+/≥10% cut-off) stratified by HPV Ventana in-situ hybridization (-■-), Dako in-situ hybridization (-▲-), or MY-PCR (-●-) results. Solitary markers shown reflect single test performance statistics for p16 IHC (assuming a 2+/≥75% cut-off) ( + ) and MY-PCR for HPV16 ( X ) alone. The dashed line indicates a reference test threshold with area under the receiver operating characteristic curve of 0.5.

    Article Snippet: One hundred-and-ten prospectively collected, formalin fixed tumor specimens were compiled onto tissue microarrays and tested for human papillomavirus DNA by in-situ hybridization with two probe sets: a biotinylated probe for high-risk human papillomavirus types 16/18 (Dako, CA), and a probe cocktail for 16/18 plus 10 additional high-risk types (Ventana, AZ).

    Techniques: Immunohistochemistry, DNA In Situ Hybridization, Polymerase Chain Reaction, Reverse Transcription Polymerase Chain Reaction, In Situ Hybridization

    Expression of CCL9 in mouse testis. (A): Immunofluorescence of 8-day WT mouse testis showing strong expression of CCL9 in Sertoli cells (green Alexa Fluor 488 staining). Arrows indicate locations of stem/progenitor spermatogonia, which are negative for CCL9. Scale bar = 25 µm. (B): Immunofluorescence of 8-day Etv5 -/- mouse testis showing a sharp decrease of CCL9 expression in Sertoli cells. Scale bar = 15 µm. (C): Immunofluorescence of 8-day WT mouse testis showing expression of CCR1, the receptor for CCL9, in stem/progenitor spermatogonia. Type A spermatogonia show double-staining for CCR1 (green Alexa Fluor 488 staining) and GCNA1 (pink Alexa Fluor 594 staining). The green staining in the lumen is background staining. Scale bar = 25 µm. (D): Immunohistochemistry of 6-day WT mouse testis showing expression of CCR1 in stem/progenitor spermatogonia (arrows). Scale bar = 15 µm. (E): Western blot of protein extracts from isolated WT seminiferous tubules of 4-, 10-, 35- and 90-day-old mice with anti-CCL9 and anti-WT1 antibodies, showing that CCl9 expression is restricted to early steps of spermatogenesis. (F): Electrophoretic mobility shift assays to investigate ETV5 binding to its consensus sequence in the Ccl9 promoter. The left panel shows gel shifts using nuclear extracts of TM4 cells after transfection with the pERMFLAG construct (pERMFLAG TM4). 1: biotinylated probe alone (B EBS3); 2: nuclear extract of pERMFLAG TM4 and B EBS3, with apparent gel shift (arrow); 3: nuclear extract of pERMFLAG TM4 with B EBS3 and nonbiotinylated probe (NB EBS3) showing outcompetition; and 4: nuclear extract of pERMFLAG TM4 with B EBS3 and ETV5 antibody (ETV5 Ab) showing a decrease of DNA/protein binding. The middle panel shows gel shifts using again pERMFLAG TM4 nuclear extracts. 1: B EBS3 alone; 2: pERMFLAG TM4 with B EBS3, showing apparent gel shift (arrow); 3: pERMFLAG TM4 with B EBS3 and ETV5 Ab showing decrease of protein-DNA binding; 4: nuclear extract of TM4 cells after transfection with control vector (Control TM4), and incubated with B EBS3; 5: control TM4 with B EBS3 and NB EBS3, 6: pERMFLAG TM4 with mutant B EBS3, and 7: pERMFLAG TM4 with mutant NB EBS3. Gel shifts with NB EBS3 substantially, but not completely outcompeted the protein-DNA complex suggesting the presence of other factors in the complex. There was no shift of protein-DNA complexes with mutant EBS3 sequences or TM4 cells transfected with control vector. The right panel shows gel shifts of purified ETV5 protein using pET vector (ETV5 protein). 1: ETV5 protein with B EBS3, showing gel shift (arrow) and 2: ETV5 protein with B EBS3 and NB EBS3 showing outcompetition. The data confirms a possible ETV5-EBS3 binding. Abbreviations: CCL9, C-C-motif ligand 9; CCR1, C-C-receptor type 1; GCNA, germ cell nuclear antigen 1; Etv5 , Ets variant gene; ETV5 protein, Ets variant protein; B EBS3, biotinylated Ets binding site 3; NB EBS3, nonbiotinylated Ets binding site 3; WT, wild type.

    Journal: Stem Cells (Dayton, Ohio)

    Article Title: ETV5 Regulates Sertoli Cell Chemokines Involved in Mouse Stem/Progenitor Spermatogonia Maintenance

    doi: 10.1002/stem.508

    Figure Lengend Snippet: Expression of CCL9 in mouse testis. (A): Immunofluorescence of 8-day WT mouse testis showing strong expression of CCL9 in Sertoli cells (green Alexa Fluor 488 staining). Arrows indicate locations of stem/progenitor spermatogonia, which are negative for CCL9. Scale bar = 25 µm. (B): Immunofluorescence of 8-day Etv5 -/- mouse testis showing a sharp decrease of CCL9 expression in Sertoli cells. Scale bar = 15 µm. (C): Immunofluorescence of 8-day WT mouse testis showing expression of CCR1, the receptor for CCL9, in stem/progenitor spermatogonia. Type A spermatogonia show double-staining for CCR1 (green Alexa Fluor 488 staining) and GCNA1 (pink Alexa Fluor 594 staining). The green staining in the lumen is background staining. Scale bar = 25 µm. (D): Immunohistochemistry of 6-day WT mouse testis showing expression of CCR1 in stem/progenitor spermatogonia (arrows). Scale bar = 15 µm. (E): Western blot of protein extracts from isolated WT seminiferous tubules of 4-, 10-, 35- and 90-day-old mice with anti-CCL9 and anti-WT1 antibodies, showing that CCl9 expression is restricted to early steps of spermatogenesis. (F): Electrophoretic mobility shift assays to investigate ETV5 binding to its consensus sequence in the Ccl9 promoter. The left panel shows gel shifts using nuclear extracts of TM4 cells after transfection with the pERMFLAG construct (pERMFLAG TM4). 1: biotinylated probe alone (B EBS3); 2: nuclear extract of pERMFLAG TM4 and B EBS3, with apparent gel shift (arrow); 3: nuclear extract of pERMFLAG TM4 with B EBS3 and nonbiotinylated probe (NB EBS3) showing outcompetition; and 4: nuclear extract of pERMFLAG TM4 with B EBS3 and ETV5 antibody (ETV5 Ab) showing a decrease of DNA/protein binding. The middle panel shows gel shifts using again pERMFLAG TM4 nuclear extracts. 1: B EBS3 alone; 2: pERMFLAG TM4 with B EBS3, showing apparent gel shift (arrow); 3: pERMFLAG TM4 with B EBS3 and ETV5 Ab showing decrease of protein-DNA binding; 4: nuclear extract of TM4 cells after transfection with control vector (Control TM4), and incubated with B EBS3; 5: control TM4 with B EBS3 and NB EBS3, 6: pERMFLAG TM4 with mutant B EBS3, and 7: pERMFLAG TM4 with mutant NB EBS3. Gel shifts with NB EBS3 substantially, but not completely outcompeted the protein-DNA complex suggesting the presence of other factors in the complex. There was no shift of protein-DNA complexes with mutant EBS3 sequences or TM4 cells transfected with control vector. The right panel shows gel shifts of purified ETV5 protein using pET vector (ETV5 protein). 1: ETV5 protein with B EBS3, showing gel shift (arrow) and 2: ETV5 protein with B EBS3 and NB EBS3 showing outcompetition. The data confirms a possible ETV5-EBS3 binding. Abbreviations: CCL9, C-C-motif ligand 9; CCR1, C-C-receptor type 1; GCNA, germ cell nuclear antigen 1; Etv5 , Ets variant gene; ETV5 protein, Ets variant protein; B EBS3, biotinylated Ets binding site 3; NB EBS3, nonbiotinylated Ets binding site 3; WT, wild type.

    Article Snippet: Electromobility Shift Assays Electromobility shift assays (EMSAs) were carried out using 3' biotinylated probes (Invitrogen, Carlsbad, CA, http://www.invitrogen.com ) designed to include the three Ets binding sites (EBSs) found in the Ccl9 genomic sequence (Accession number AL596122) and a chemiluminescent kit (Cat. No. 20148, Thermo Scientific, Pittsburgh, PA, http://www.thermo.com ).

    Techniques: Expressing, Immunofluorescence, Staining, Double Staining, Immunohistochemistry, Western Blot, Isolation, Mouse Assay, Electrophoretic Mobility Shift Assay, Binding Assay, Sequencing, Transfection, Construct, Protein Binding, Plasmid Preparation, Incubation, Mutagenesis, Purification, Positron Emission Tomography, Variant Assay

    Localization of 7-Helix-1 in SGs and interaction with translational repressors. (A) Co-localization of 7-Helix-1 with mRNA-aggregates. Mature WF NF54 gametocytes were subjected to mRNA-FISH-IFA and mRNA was labeled with a biotinylated oligo-dT25 probe (red); counterlabeling was performed using mouse anti-7-Helix-1rp2 antisera (green). Nuclei were highlighted by Hoechst33342 nuclear stain (blue). Frame indicates the area chosen for enlargement. DIC, differential interference contrast. Bar, 5 μm; enlargement, 1 μm. (B) Accumulation of 7-Helix-1 in SG fractions. Gametocytes of line 7-Helix-1-HA were stressed by treatment with sodium arsenite for 1 h and a SG core fraction enrichment was conducted. Lysates of 7-Helix-1-HA gametocytes (-) and of enriched SGs (+) were subjected to WB, using mouse antisera directed against Pf39 (~39 kDa) or PfM1-AP (~126 and 68 kDa, black arrows) or rabbit antibodies against HSP70-1 (~70 kDa) or the HA-tag to detect 7-Helix-1-HA (~60 kDa). (C) Co-immunoprecipitation of 7-Helix-1 with CITH, PABP1 and DOZI. Lysates of WT NF54 or 7-Helix-1-HA gametocytes were subjected to co-immunoprecipitation assays using polyclonal mouse anti-7-Helix-1rp2 antisera or polyclonal rabbit anti-DOZI antisera, followed by WB using rabbit anti-CITH, anti-PABP1 and anti-HA antibodies or mouse anti-Pf39 antibody to detect precipitated proteins. Grey arrow indicates the expected running line in the negative control. Asterisk indicates a band corresponding to the precipitation antibody. (D) Co-localization of 7-Helix-1 with CITH, PABP1 and DOZI. WT NF54 gametocytes were immunolabeled with mouse anti-7-Helix-1rp2 antisera (green) and rabbit anti-CITH, anti-PABP1, or anti-DOZI antibodies (red). Nuclei were highlighted by Hoechst33342 nuclear stain (blue). DIC, differential interference contrast. Bar, 5 μm. Results are representative of three independent experiments.

    Journal: PLoS Pathogens

    Article Title: A seven-helix protein constitutes stress granules crucial for regulating translation during human-to-mosquito transmission of Plasmodium falciparum

    doi: 10.1371/journal.ppat.1007249

    Figure Lengend Snippet: Localization of 7-Helix-1 in SGs and interaction with translational repressors. (A) Co-localization of 7-Helix-1 with mRNA-aggregates. Mature WF NF54 gametocytes were subjected to mRNA-FISH-IFA and mRNA was labeled with a biotinylated oligo-dT25 probe (red); counterlabeling was performed using mouse anti-7-Helix-1rp2 antisera (green). Nuclei were highlighted by Hoechst33342 nuclear stain (blue). Frame indicates the area chosen for enlargement. DIC, differential interference contrast. Bar, 5 μm; enlargement, 1 μm. (B) Accumulation of 7-Helix-1 in SG fractions. Gametocytes of line 7-Helix-1-HA were stressed by treatment with sodium arsenite for 1 h and a SG core fraction enrichment was conducted. Lysates of 7-Helix-1-HA gametocytes (-) and of enriched SGs (+) were subjected to WB, using mouse antisera directed against Pf39 (~39 kDa) or PfM1-AP (~126 and 68 kDa, black arrows) or rabbit antibodies against HSP70-1 (~70 kDa) or the HA-tag to detect 7-Helix-1-HA (~60 kDa). (C) Co-immunoprecipitation of 7-Helix-1 with CITH, PABP1 and DOZI. Lysates of WT NF54 or 7-Helix-1-HA gametocytes were subjected to co-immunoprecipitation assays using polyclonal mouse anti-7-Helix-1rp2 antisera or polyclonal rabbit anti-DOZI antisera, followed by WB using rabbit anti-CITH, anti-PABP1 and anti-HA antibodies or mouse anti-Pf39 antibody to detect precipitated proteins. Grey arrow indicates the expected running line in the negative control. Asterisk indicates a band corresponding to the precipitation antibody. (D) Co-localization of 7-Helix-1 with CITH, PABP1 and DOZI. WT NF54 gametocytes were immunolabeled with mouse anti-7-Helix-1rp2 antisera (green) and rabbit anti-CITH, anti-PABP1, or anti-DOZI antibodies (red). Nuclei were highlighted by Hoechst33342 nuclear stain (blue). DIC, differential interference contrast. Bar, 5 μm. Results are representative of three independent experiments.

    Article Snippet: Permeabilization was performed with 0.1% v/v Triton X-100/125 mM glycine (Carl Roth)/PBS at RT for 10 min. After incubation in 2x SSC for 10 min at RT, hybridization was carried out by incubation of the sample with hybridization buffer (50% deionized formamide/200 μM dextran sulfate (MW = 500,000 g/mol) in 20x SSPE buffer) containing 1 μg biotinylated oligo-dT25 probe (Promega) in a humidity chamber overnight at 37°C.

    Techniques: Fluorescence In Situ Hybridization, Immunofluorescence, Labeling, Staining, Western Blot, Immunoprecipitation, Negative Control, Immunolabeling

    Binding of SP1 to MRE1.3, MRE1.3a and MRE1.3c in EMSAs. ( A ) Sequences of MRE1.3 with in silico predicted SP1-binding sites, different MRE1.3 deletion constructs and constructs with mutated SP1-binding site are depicted. ( B ) EMSAs for detection of SP1 binding were performed with biotinylated MRE1.3 (lanes 1–3) or MRE1.3a (lanes 4–6) probe. Probes were either incubated with buffer (probe), 300 ng BSA as control for unspecific protein interactions (BSA) or with 300 ng of rhSP1. ( C ) To identify the relevant SP1-binding site for the interaction, we compared biotinylated MRE1.3c (lanes 1–3) with biotinylated MRE1.3 (lanes 4–6). Probes were either incubated with only buffer (probe), 300 ng of BSA as control for unspecific protein interactions (BSA) or with 300 ng of rhSP1. ( D ) To exclude unspecific SP1-DNA interactions, EMSAs with biotinylated MRE1.3 (lanes 1–3) were compared with EMSAs with biotinylated CRE (cAMP response element) (lanes 4–6) probe. Probes were either incubated with only buffer (probe), 300 ng of BSA as control for unspecific protein interactions (BSA) or with 300 ng of rhSP1 ( N = 6). ( E ) To verify in vivo binding of SP1 to MRE1.3, we analyzed binding of protein from nuclear extracts to MRE1.3 and MRE1.3 with mutations in the SP1-binding sequence, MRE1.3mut1 and MRE1.3mut2. Biotinylated SP1 consensus sequence was used as a positive control. Probes were either incubated with only buffer (probe) or nuclear extracts (NE) ( N = 4).

    Journal: Nucleic Acids Research

    Article Title: Mineralocorticoid receptor interaction with SP1 generates a new response element for pathophysiologically relevant gene expression

    doi: 10.1093/nar/gkt581

    Figure Lengend Snippet: Binding of SP1 to MRE1.3, MRE1.3a and MRE1.3c in EMSAs. ( A ) Sequences of MRE1.3 with in silico predicted SP1-binding sites, different MRE1.3 deletion constructs and constructs with mutated SP1-binding site are depicted. ( B ) EMSAs for detection of SP1 binding were performed with biotinylated MRE1.3 (lanes 1–3) or MRE1.3a (lanes 4–6) probe. Probes were either incubated with buffer (probe), 300 ng BSA as control for unspecific protein interactions (BSA) or with 300 ng of rhSP1. ( C ) To identify the relevant SP1-binding site for the interaction, we compared biotinylated MRE1.3c (lanes 1–3) with biotinylated MRE1.3 (lanes 4–6). Probes were either incubated with only buffer (probe), 300 ng of BSA as control for unspecific protein interactions (BSA) or with 300 ng of rhSP1. ( D ) To exclude unspecific SP1-DNA interactions, EMSAs with biotinylated MRE1.3 (lanes 1–3) were compared with EMSAs with biotinylated CRE (cAMP response element) (lanes 4–6) probe. Probes were either incubated with only buffer (probe), 300 ng of BSA as control for unspecific protein interactions (BSA) or with 300 ng of rhSP1 ( N = 6). ( E ) To verify in vivo binding of SP1 to MRE1.3, we analyzed binding of protein from nuclear extracts to MRE1.3 and MRE1.3 with mutations in the SP1-binding sequence, MRE1.3mut1 and MRE1.3mut2. Biotinylated SP1 consensus sequence was used as a positive control. Probes were either incubated with only buffer (probe) or nuclear extracts (NE) ( N = 4).

    Article Snippet: Biotinylated probes were constructed by hybridization or PCR with bio-dUTP (Roche, Mannheim, Germany) and MRE1-SEAP reporter plasmids as template (Primer see Supplement 1).

    Techniques: Binding Assay, In Silico, Construct, Incubation, In Vivo, Sequencing, Positive Control

    In vitro binding of MR to MRE1 ( A ) In a transcription factor-binding ELISA, nuclear extracts of hMR- and hGR-HEK cells that had been previously stimulated with vehicle, 10 nM aldosterone or 1 µM hydrocortisone, respectively, were tested for binding of hMR or hGR to biotinylated MRE1. ( N = 1–3, n = 4–11, data represented as mean ± SEM, * P ≤ 0.05). ( B ) Binding of in vitro synthesized MR to MRE1 was tested and compared with unspecific binding of MR to DNA (unspecific = binding of MR to DNA probes of exon of eNOS) and binding of MR to a probe containing three classical GREs, which was used as positive control for this experiment ( N = 2–3, n = 4–6, data represented as mean ± SEM, * P ≤ 0.05).

    Journal: Nucleic Acids Research

    Article Title: Mineralocorticoid receptor interaction with SP1 generates a new response element for pathophysiologically relevant gene expression

    doi: 10.1093/nar/gkt581

    Figure Lengend Snippet: In vitro binding of MR to MRE1 ( A ) In a transcription factor-binding ELISA, nuclear extracts of hMR- and hGR-HEK cells that had been previously stimulated with vehicle, 10 nM aldosterone or 1 µM hydrocortisone, respectively, were tested for binding of hMR or hGR to biotinylated MRE1. ( N = 1–3, n = 4–11, data represented as mean ± SEM, * P ≤ 0.05). ( B ) Binding of in vitro synthesized MR to MRE1 was tested and compared with unspecific binding of MR to DNA (unspecific = binding of MR to DNA probes of exon of eNOS) and binding of MR to a probe containing three classical GREs, which was used as positive control for this experiment ( N = 2–3, n = 4–6, data represented as mean ± SEM, * P ≤ 0.05).

    Article Snippet: Biotinylated probes were constructed by hybridization or PCR with bio-dUTP (Roche, Mannheim, Germany) and MRE1-SEAP reporter plasmids as template (Primer see Supplement 1).

    Techniques: In Vitro, Binding Assay, Enzyme-linked Immunosorbent Assay, Synthesized, Positive Control