streptavidin biotin blocking solution Search Results


streptavidin biotin horseradish peroxidase hrp complex technique  (Agilent technologies)
99
Agilent technologies streptavidin biotin horseradish peroxidase hrp complex technique
Streptavidin Biotin Horseradish Peroxidase Hrp Complex Technique, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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streptavidin/biotin blocking kit  (Vector Laboratories)
96
Vector Laboratories streptavidin/biotin blocking kit
Streptavidin/Biotin Blocking Kit, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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supersensitive kit  (Biogenex)
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Biogenex supersensitive kit
Supersensitive Kit, supplied by Biogenex, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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streptavidin-biotinylated horseradish peroxidase complex  (Boehringer Mannheim)
90
Boehringer Mannheim streptavidin-biotinylated horseradish peroxidase complex
Streptavidin Biotinylated Horseradish Peroxidase Complex, supplied by Boehringer Mannheim, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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synthetic biotinylated oligonucleotide  (Thermo Fisher)
99
Thermo Fisher synthetic biotinylated oligonucleotide
FIG. 1. Experimental design. A, specific 32P-end labeling of TFIIA. Recombinant TFIIA subunits bearing a heart muscle kinase phospho- rylation site (HMK tag) at one terminus and a His-tag at the other were overexpressed and purified from Escherichia coli by Ni-NTA chroma- tography. The tagged subunits were then joined with a partner lacking the HMK tag and labeled with [g-32P]ATP and heart muscle kinase to generate TFIIA 32P-end-labeled at the HMK tag of one subunit. B, schematic of protease footprinting protocol. To form ternary complexes, recombinant human TBP (the carboxyl-terminal 181 amino acids) and human 32P-end-labeled TFIIA were incubated with a <t>biotinylated</t> oli- gonucleotide containing the TATA box from the adenovirus E4 pro- moter immobilized on streptavidin:magnetic beads. (Binary complexes were assembled by incubating glutathione-agarose-immobilized GST- TBP with human 32P-end-labeled TFIIA, not shown.) The complexes were washed with an excess of binding buffer to remove unbound protein and then digested with limiting amounts of a broad specificity protease. The products were fractionated on high resolution SDS-poly- acrylamide gels and visualized by autoradiography. C, specific ternary complex formation. Increasing amounts of TFIIA end-labeled on the g subunit were incubated with biotinylated TATA box oligonucleotides immobilized on M-280 streptavidin resin with (lanes 3, 5, 7, and 9) or without (lanes 2, 4, 6, and 8) TBP and then washed extensively. The bound fraction was electrophoresed on standard SDS-polyacrylamide gels and autoradiographed. Lane 1 is 3% of the input end-labeled TFIIA for the experiments shown in lanes 8 and 9.
Synthetic Biotinylated Oligonucleotide, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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lsab kit  (Agilent technologies)
90
Agilent technologies lsab kit
FIG. 1. Experimental design. A, specific 32P-end labeling of TFIIA. Recombinant TFIIA subunits bearing a heart muscle kinase phospho- rylation site (HMK tag) at one terminus and a His-tag at the other were overexpressed and purified from Escherichia coli by Ni-NTA chroma- tography. The tagged subunits were then joined with a partner lacking the HMK tag and labeled with [g-32P]ATP and heart muscle kinase to generate TFIIA 32P-end-labeled at the HMK tag of one subunit. B, schematic of protease footprinting protocol. To form ternary complexes, recombinant human TBP (the carboxyl-terminal 181 amino acids) and human 32P-end-labeled TFIIA were incubated with a <t>biotinylated</t> oli- gonucleotide containing the TATA box from the adenovirus E4 pro- moter immobilized on streptavidin:magnetic beads. (Binary complexes were assembled by incubating glutathione-agarose-immobilized GST- TBP with human 32P-end-labeled TFIIA, not shown.) The complexes were washed with an excess of binding buffer to remove unbound protein and then digested with limiting amounts of a broad specificity protease. The products were fractionated on high resolution SDS-poly- acrylamide gels and visualized by autoradiography. C, specific ternary complex formation. Increasing amounts of TFIIA end-labeled on the g subunit were incubated with biotinylated TATA box oligonucleotides immobilized on M-280 streptavidin resin with (lanes 3, 5, 7, and 9) or without (lanes 2, 4, 6, and 8) TBP and then washed extensively. The bound fraction was electrophoresed on standard SDS-polyacrylamide gels and autoradiographed. Lane 1 is 3% of the input end-labeled TFIIA for the experiments shown in lanes 8 and 9.
Lsab Kit, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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biotinylated anti rat igg h l  (Vector Laboratories)
93
Vector Laboratories biotinylated anti rat igg h l
FIG. 1. Experimental design. A, specific 32P-end labeling of TFIIA. Recombinant TFIIA subunits bearing a heart muscle kinase phospho- rylation site (HMK tag) at one terminus and a His-tag at the other were overexpressed and purified from Escherichia coli by Ni-NTA chroma- tography. The tagged subunits were then joined with a partner lacking the HMK tag and labeled with [g-32P]ATP and heart muscle kinase to generate TFIIA 32P-end-labeled at the HMK tag of one subunit. B, schematic of protease footprinting protocol. To form ternary complexes, recombinant human TBP (the carboxyl-terminal 181 amino acids) and human 32P-end-labeled TFIIA were incubated with a <t>biotinylated</t> oli- gonucleotide containing the TATA box from the adenovirus E4 pro- moter immobilized on streptavidin:magnetic beads. (Binary complexes were assembled by incubating glutathione-agarose-immobilized GST- TBP with human 32P-end-labeled TFIIA, not shown.) The complexes were washed with an excess of binding buffer to remove unbound protein and then digested with limiting amounts of a broad specificity protease. The products were fractionated on high resolution SDS-poly- acrylamide gels and visualized by autoradiography. C, specific ternary complex formation. Increasing amounts of TFIIA end-labeled on the g subunit were incubated with biotinylated TATA box oligonucleotides immobilized on M-280 streptavidin resin with (lanes 3, 5, 7, and 9) or without (lanes 2, 4, 6, and 8) TBP and then washed extensively. The bound fraction was electrophoresed on standard SDS-polyacrylamide gels and autoradiographed. Lane 1 is 3% of the input end-labeled TFIIA for the experiments shown in lanes 8 and 9.
Biotinylated Anti Rat Igg H L, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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streptavidin apc prozyme agilent cat  (InvivoGen)
97
InvivoGen streptavidin apc prozyme agilent cat
FIG. 1. Experimental design. A, specific 32P-end labeling of TFIIA. Recombinant TFIIA subunits bearing a heart muscle kinase phospho- rylation site (HMK tag) at one terminus and a His-tag at the other were overexpressed and purified from Escherichia coli by Ni-NTA chroma- tography. The tagged subunits were then joined with a partner lacking the HMK tag and labeled with [g-32P]ATP and heart muscle kinase to generate TFIIA 32P-end-labeled at the HMK tag of one subunit. B, schematic of protease footprinting protocol. To form ternary complexes, recombinant human TBP (the carboxyl-terminal 181 amino acids) and human 32P-end-labeled TFIIA were incubated with a <t>biotinylated</t> oli- gonucleotide containing the TATA box from the adenovirus E4 pro- moter immobilized on streptavidin:magnetic beads. (Binary complexes were assembled by incubating glutathione-agarose-immobilized GST- TBP with human 32P-end-labeled TFIIA, not shown.) The complexes were washed with an excess of binding buffer to remove unbound protein and then digested with limiting amounts of a broad specificity protease. The products were fractionated on high resolution SDS-poly- acrylamide gels and visualized by autoradiography. C, specific ternary complex formation. Increasing amounts of TFIIA end-labeled on the g subunit were incubated with biotinylated TATA box oligonucleotides immobilized on M-280 streptavidin resin with (lanes 3, 5, 7, and 9) or without (lanes 2, 4, 6, and 8) TBP and then washed extensively. The bound fraction was electrophoresed on standard SDS-polyacrylamide gels and autoradiographed. Lane 1 is 3% of the input end-labeled TFIIA for the experiments shown in lanes 8 and 9.
Streptavidin Apc Prozyme Agilent Cat, supplied by InvivoGen, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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alkaline phosphatise conjugated streptavidin biotin abc kit  (Vector Laboratories)
99
Vector Laboratories alkaline phosphatise conjugated streptavidin biotin abc kit
FIG. 1. Experimental design. A, specific 32P-end labeling of TFIIA. Recombinant TFIIA subunits bearing a heart muscle kinase phospho- rylation site (HMK tag) at one terminus and a His-tag at the other were overexpressed and purified from Escherichia coli by Ni-NTA chroma- tography. The tagged subunits were then joined with a partner lacking the HMK tag and labeled with [g-32P]ATP and heart muscle kinase to generate TFIIA 32P-end-labeled at the HMK tag of one subunit. B, schematic of protease footprinting protocol. To form ternary complexes, recombinant human TBP (the carboxyl-terminal 181 amino acids) and human 32P-end-labeled TFIIA were incubated with a <t>biotinylated</t> oli- gonucleotide containing the TATA box from the adenovirus E4 pro- moter immobilized on streptavidin:magnetic beads. (Binary complexes were assembled by incubating glutathione-agarose-immobilized GST- TBP with human 32P-end-labeled TFIIA, not shown.) The complexes were washed with an excess of binding buffer to remove unbound protein and then digested with limiting amounts of a broad specificity protease. The products were fractionated on high resolution SDS-poly- acrylamide gels and visualized by autoradiography. C, specific ternary complex formation. Increasing amounts of TFIIA end-labeled on the g subunit were incubated with biotinylated TATA box oligonucleotides immobilized on M-280 streptavidin resin with (lanes 3, 5, 7, and 9) or without (lanes 2, 4, 6, and 8) TBP and then washed extensively. The bound fraction was electrophoresed on standard SDS-polyacrylamide gels and autoradiographed. Lane 1 is 3% of the input end-labeled TFIIA for the experiments shown in lanes 8 and 9.
Alkaline Phosphatise Conjugated Streptavidin Biotin Abc Kit, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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streptavidin biotin abc elite kit  (Vector Laboratories)
99
Vector Laboratories streptavidin biotin abc elite kit
FIG. 1. Experimental design. A, specific 32P-end labeling of TFIIA. Recombinant TFIIA subunits bearing a heart muscle kinase phospho- rylation site (HMK tag) at one terminus and a His-tag at the other were overexpressed and purified from Escherichia coli by Ni-NTA chroma- tography. The tagged subunits were then joined with a partner lacking the HMK tag and labeled with [g-32P]ATP and heart muscle kinase to generate TFIIA 32P-end-labeled at the HMK tag of one subunit. B, schematic of protease footprinting protocol. To form ternary complexes, recombinant human TBP (the carboxyl-terminal 181 amino acids) and human 32P-end-labeled TFIIA were incubated with a <t>biotinylated</t> oli- gonucleotide containing the TATA box from the adenovirus E4 pro- moter immobilized on streptavidin:magnetic beads. (Binary complexes were assembled by incubating glutathione-agarose-immobilized GST- TBP with human 32P-end-labeled TFIIA, not shown.) The complexes were washed with an excess of binding buffer to remove unbound protein and then digested with limiting amounts of a broad specificity protease. The products were fractionated on high resolution SDS-poly- acrylamide gels and visualized by autoradiography. C, specific ternary complex formation. Increasing amounts of TFIIA end-labeled on the g subunit were incubated with biotinylated TATA box oligonucleotides immobilized on M-280 streptavidin resin with (lanes 3, 5, 7, and 9) or without (lanes 2, 4, 6, and 8) TBP and then washed extensively. The bound fraction was electrophoresed on standard SDS-polyacrylamide gels and autoradiographed. Lane 1 is 3% of the input end-labeled TFIIA for the experiments shown in lanes 8 and 9.
Streptavidin Biotin Abc Elite Kit, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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biotinylated proteins  (Jackson Immuno)
96
Jackson Immuno biotinylated proteins
FIG. 1. Experimental design. A, specific 32P-end labeling of TFIIA. Recombinant TFIIA subunits bearing a heart muscle kinase phospho- rylation site (HMK tag) at one terminus and a His-tag at the other were overexpressed and purified from Escherichia coli by Ni-NTA chroma- tography. The tagged subunits were then joined with a partner lacking the HMK tag and labeled with [g-32P]ATP and heart muscle kinase to generate TFIIA 32P-end-labeled at the HMK tag of one subunit. B, schematic of protease footprinting protocol. To form ternary complexes, recombinant human TBP (the carboxyl-terminal 181 amino acids) and human 32P-end-labeled TFIIA were incubated with a <t>biotinylated</t> oli- gonucleotide containing the TATA box from the adenovirus E4 pro- moter immobilized on streptavidin:magnetic beads. (Binary complexes were assembled by incubating glutathione-agarose-immobilized GST- TBP with human 32P-end-labeled TFIIA, not shown.) The complexes were washed with an excess of binding buffer to remove unbound protein and then digested with limiting amounts of a broad specificity protease. The products were fractionated on high resolution SDS-poly- acrylamide gels and visualized by autoradiography. C, specific ternary complex formation. Increasing amounts of TFIIA end-labeled on the g subunit were incubated with biotinylated TATA box oligonucleotides immobilized on M-280 streptavidin resin with (lanes 3, 5, 7, and 9) or without (lanes 2, 4, 6, and 8) TBP and then washed extensively. The bound fraction was electrophoresed on standard SDS-polyacrylamide gels and autoradiographed. Lane 1 is 3% of the input end-labeled TFIIA for the experiments shown in lanes 8 and 9.
Biotinylated Proteins, supplied by Jackson Immuno, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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anti secondary biotinylated  (Vector Laboratories)
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Vector Laboratories anti secondary biotinylated
FIG. 1. Experimental design. A, specific 32P-end labeling of TFIIA. Recombinant TFIIA subunits bearing a heart muscle kinase phospho- rylation site (HMK tag) at one terminus and a His-tag at the other were overexpressed and purified from Escherichia coli by Ni-NTA chroma- tography. The tagged subunits were then joined with a partner lacking the HMK tag and labeled with [g-32P]ATP and heart muscle kinase to generate TFIIA 32P-end-labeled at the HMK tag of one subunit. B, schematic of protease footprinting protocol. To form ternary complexes, recombinant human TBP (the carboxyl-terminal 181 amino acids) and human 32P-end-labeled TFIIA were incubated with a <t>biotinylated</t> oli- gonucleotide containing the TATA box from the adenovirus E4 pro- moter immobilized on streptavidin:magnetic beads. (Binary complexes were assembled by incubating glutathione-agarose-immobilized GST- TBP with human 32P-end-labeled TFIIA, not shown.) The complexes were washed with an excess of binding buffer to remove unbound protein and then digested with limiting amounts of a broad specificity protease. The products were fractionated on high resolution SDS-poly- acrylamide gels and visualized by autoradiography. C, specific ternary complex formation. Increasing amounts of TFIIA end-labeled on the g subunit were incubated with biotinylated TATA box oligonucleotides immobilized on M-280 streptavidin resin with (lanes 3, 5, 7, and 9) or without (lanes 2, 4, 6, and 8) TBP and then washed extensively. The bound fraction was electrophoresed on standard SDS-polyacrylamide gels and autoradiographed. Lane 1 is 3% of the input end-labeled TFIIA for the experiments shown in lanes 8 and 9.
Anti Secondary Biotinylated, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


FIG. 1. Experimental design. A, specific 32P-end labeling of TFIIA. Recombinant TFIIA subunits bearing a heart muscle kinase phospho- rylation site (HMK tag) at one terminus and a His-tag at the other were overexpressed and purified from Escherichia coli by Ni-NTA chroma- tography. The tagged subunits were then joined with a partner lacking the HMK tag and labeled with [g-32P]ATP and heart muscle kinase to generate TFIIA 32P-end-labeled at the HMK tag of one subunit. B, schematic of protease footprinting protocol. To form ternary complexes, recombinant human TBP (the carboxyl-terminal 181 amino acids) and human 32P-end-labeled TFIIA were incubated with a biotinylated oli- gonucleotide containing the TATA box from the adenovirus E4 pro- moter immobilized on streptavidin:magnetic beads. (Binary complexes were assembled by incubating glutathione-agarose-immobilized GST- TBP with human 32P-end-labeled TFIIA, not shown.) The complexes were washed with an excess of binding buffer to remove unbound protein and then digested with limiting amounts of a broad specificity protease. The products were fractionated on high resolution SDS-poly- acrylamide gels and visualized by autoradiography. C, specific ternary complex formation. Increasing amounts of TFIIA end-labeled on the g subunit were incubated with biotinylated TATA box oligonucleotides immobilized on M-280 streptavidin resin with (lanes 3, 5, 7, and 9) or without (lanes 2, 4, 6, and 8) TBP and then washed extensively. The bound fraction was electrophoresed on standard SDS-polyacrylamide gels and autoradiographed. Lane 1 is 3% of the input end-labeled TFIIA for the experiments shown in lanes 8 and 9.

Journal: The Journal of biological chemistry

Article Title: Protease footprinting analysis of ternary complex formation by human TFIIA.

doi: 10.1074/jbc.272.2.1180

Figure Lengend Snippet: FIG. 1. Experimental design. A, specific 32P-end labeling of TFIIA. Recombinant TFIIA subunits bearing a heart muscle kinase phospho- rylation site (HMK tag) at one terminus and a His-tag at the other were overexpressed and purified from Escherichia coli by Ni-NTA chroma- tography. The tagged subunits were then joined with a partner lacking the HMK tag and labeled with [g-32P]ATP and heart muscle kinase to generate TFIIA 32P-end-labeled at the HMK tag of one subunit. B, schematic of protease footprinting protocol. To form ternary complexes, recombinant human TBP (the carboxyl-terminal 181 amino acids) and human 32P-end-labeled TFIIA were incubated with a biotinylated oli- gonucleotide containing the TATA box from the adenovirus E4 pro- moter immobilized on streptavidin:magnetic beads. (Binary complexes were assembled by incubating glutathione-agarose-immobilized GST- TBP with human 32P-end-labeled TFIIA, not shown.) The complexes were washed with an excess of binding buffer to remove unbound protein and then digested with limiting amounts of a broad specificity protease. The products were fractionated on high resolution SDS-poly- acrylamide gels and visualized by autoradiography. C, specific ternary complex formation. Increasing amounts of TFIIA end-labeled on the g subunit were incubated with biotinylated TATA box oligonucleotides immobilized on M-280 streptavidin resin with (lanes 3, 5, 7, and 9) or without (lanes 2, 4, 6, and 8) TBP and then washed extensively. The bound fraction was electrophoresed on standard SDS-polyacrylamide gels and autoradiographed. Lane 1 is 3% of the input end-labeled TFIIA for the experiments shown in lanes 8 and 9.

Article Snippet: Complex Formation and Proteolysis—TBP-TFIIA-TATA box ternary complexes were formed in a 50-ml mixture containing 3 pmol of biotinylated adenovirus E4 DNA template, a synthetic biotinylated oligonucleotide (biotin-59-GGATCCCCAGTCCTATATATACTCGCTCTGC-39) immobilized on streptavidin-conjugated M-280 magnetic beads (Dynal), with 500 ng of TBP, and 400 ng of 32P-labeled TFIIA.

Techniques: End Labeling, Recombinant, Purification, Labeling, Footprinting, Incubation, Magnetic Beads, Binding Assay, Autoradiography