glutathione sepharose 4 fast flow Ge Healthcare Search Results


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  • 99
    Qiagen ni nta agarose
    Ni Nta Agarose, supplied by Qiagen, used in various techniques. Bioz Stars score: 99/100, based on 22357 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ni nta agarose/product/Qiagen
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    Millipore glutathione
    Glutathione, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 3832 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare glutathione sepharose 4 fast flow
    RUTBC2 is an effector of Rab9A. A , His-Rab2 and His-Rab9A were preloaded with GTPγS and incubated with GST or full-length GST-RUTBC2 and then collected on <t>glutathione-Sepharose.</t> Bound material was eluted in sample buffer and analyzed by immunoblot with anti-His antibodies. Inputs represent 5% of the added His-tagged Rab. B , His-Rab9A and His-Rab6A were preloaded with GTPγS and incubated with full-length GST-RUTBC2 and then collected on glutathione-Sepharose. Bound material was eluted in sample buffer and analyzed by immunoblot with anti-His antibodies. Inputs represent 10% of the added His-tagged Rabs. C , in vitro transcribed/translated 3×Myc-RUTBC2 was incubated with GST-Rab9A or GST-Rab9B preloaded with either GTPγS ( T ) or GDP ( D ) and analyzed as in A. D , purified GST-RUTBC2 and control proteins were incubated with untagged Rab9A loaded with [ 35 S]GTPγS and immobilized using glutathione-Sepharose. Bound Rab was detected by scintillation counting. Error bars represent S.E. from at least two independent experiments. E , His-RUTBC2-N or His-RUTBC2-C was incubated with GST or GST-Rab9A Q66L and then collected on glutathione-Sepharose. Bound material was eluted in sample buffer and analyzed by immunoblot using anti-His antibodies. Inputs represent 5% of the added His-tagged RUTBC2 constructs. F , His-Rab9A was preloaded with GTPγS and incubated with GST, full-length GST-RUTBC2, GST-RUTBC2-N, or GST-RUTBC2-C and then collected on glutathione-Sepharose. Bound material was eluted in sample buffer and analyzed by immunoblot with anti-His antibodies. Inputs represent 5% of the added His-tagged Rab.
    Glutathione Sepharose 4 Fast Flow, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 1796 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    glutathione sepharose 4 fast flow - by Bioz Stars, 2020-01
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    80
    GE Healthcare sepharose glutathione fast flow beads
    RUTBC2 is an effector of Rab9A. A , His-Rab2 and His-Rab9A were preloaded with GTPγS and incubated with GST or full-length GST-RUTBC2 and then collected on <t>glutathione-Sepharose.</t> Bound material was eluted in sample buffer and analyzed by immunoblot with anti-His antibodies. Inputs represent 5% of the added His-tagged Rab. B , His-Rab9A and His-Rab6A were preloaded with GTPγS and incubated with full-length GST-RUTBC2 and then collected on glutathione-Sepharose. Bound material was eluted in sample buffer and analyzed by immunoblot with anti-His antibodies. Inputs represent 10% of the added His-tagged Rabs. C , in vitro transcribed/translated 3×Myc-RUTBC2 was incubated with GST-Rab9A or GST-Rab9B preloaded with either GTPγS ( T ) or GDP ( D ) and analyzed as in A. D , purified GST-RUTBC2 and control proteins were incubated with untagged Rab9A loaded with [ 35 S]GTPγS and immobilized using glutathione-Sepharose. Bound Rab was detected by scintillation counting. Error bars represent S.E. from at least two independent experiments. E , His-RUTBC2-N or His-RUTBC2-C was incubated with GST or GST-Rab9A Q66L and then collected on glutathione-Sepharose. Bound material was eluted in sample buffer and analyzed by immunoblot using anti-His antibodies. Inputs represent 5% of the added His-tagged RUTBC2 constructs. F , His-Rab9A was preloaded with GTPγS and incubated with GST, full-length GST-RUTBC2, GST-RUTBC2-N, or GST-RUTBC2-C and then collected on glutathione-Sepharose. Bound material was eluted in sample buffer and analyzed by immunoblot with anti-His antibodies. Inputs represent 5% of the added His-tagged Rab.
    Sepharose Glutathione Fast Flow Beads, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 80/100, based on 120 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    84
    GE Healthcare glutathione sepharose 4 fast flow gsh sepharose
    RUTBC2 is an effector of Rab9A. A , His-Rab2 and His-Rab9A were preloaded with GTPγS and incubated with GST or full-length GST-RUTBC2 and then collected on <t>glutathione-Sepharose.</t> Bound material was eluted in sample buffer and analyzed by immunoblot with anti-His antibodies. Inputs represent 5% of the added His-tagged Rab. B , His-Rab9A and His-Rab6A were preloaded with GTPγS and incubated with full-length GST-RUTBC2 and then collected on glutathione-Sepharose. Bound material was eluted in sample buffer and analyzed by immunoblot with anti-His antibodies. Inputs represent 10% of the added His-tagged Rabs. C , in vitro transcribed/translated 3×Myc-RUTBC2 was incubated with GST-Rab9A or GST-Rab9B preloaded with either GTPγS ( T ) or GDP ( D ) and analyzed as in A. D , purified GST-RUTBC2 and control proteins were incubated with untagged Rab9A loaded with [ 35 S]GTPγS and immobilized using glutathione-Sepharose. Bound Rab was detected by scintillation counting. Error bars represent S.E. from at least two independent experiments. E , His-RUTBC2-N or His-RUTBC2-C was incubated with GST or GST-Rab9A Q66L and then collected on glutathione-Sepharose. Bound material was eluted in sample buffer and analyzed by immunoblot using anti-His antibodies. Inputs represent 5% of the added His-tagged RUTBC2 constructs. F , His-Rab9A was preloaded with GTPγS and incubated with GST, full-length GST-RUTBC2, GST-RUTBC2-N, or GST-RUTBC2-C and then collected on glutathione-Sepharose. Bound material was eluted in sample buffer and analyzed by immunoblot with anti-His antibodies. Inputs represent 5% of the added His-tagged Rab.
    Glutathione Sepharose 4 Fast Flow Gsh Sepharose, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 84/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare glutathione sepharose 4 fast flow resin
    RUTBC2 is an effector of Rab9A. A , His-Rab2 and His-Rab9A were preloaded with GTPγS and incubated with GST or full-length GST-RUTBC2 and then collected on <t>glutathione-Sepharose.</t> Bound material was eluted in sample buffer and analyzed by immunoblot with anti-His antibodies. Inputs represent 5% of the added His-tagged Rab. B , His-Rab9A and His-Rab6A were preloaded with GTPγS and incubated with full-length GST-RUTBC2 and then collected on glutathione-Sepharose. Bound material was eluted in sample buffer and analyzed by immunoblot with anti-His antibodies. Inputs represent 10% of the added His-tagged Rabs. C , in vitro transcribed/translated 3×Myc-RUTBC2 was incubated with GST-Rab9A or GST-Rab9B preloaded with either GTPγS ( T ) or GDP ( D ) and analyzed as in A. D , purified GST-RUTBC2 and control proteins were incubated with untagged Rab9A loaded with [ 35 S]GTPγS and immobilized using glutathione-Sepharose. Bound Rab was detected by scintillation counting. Error bars represent S.E. from at least two independent experiments. E , His-RUTBC2-N or His-RUTBC2-C was incubated with GST or GST-Rab9A Q66L and then collected on glutathione-Sepharose. Bound material was eluted in sample buffer and analyzed by immunoblot using anti-His antibodies. Inputs represent 5% of the added His-tagged RUTBC2 constructs. F , His-Rab9A was preloaded with GTPγS and incubated with GST, full-length GST-RUTBC2, GST-RUTBC2-N, or GST-RUTBC2-C and then collected on glutathione-Sepharose. Bound material was eluted in sample buffer and analyzed by immunoblot with anti-His antibodies. Inputs represent 5% of the added His-tagged Rab.
    Glutathione Sepharose 4 Fast Flow Resin, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 329 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare glutathione sepharose 4 fast flow column
    RUTBC2 is an effector of Rab9A. A , His-Rab2 and His-Rab9A were preloaded with GTPγS and incubated with GST or full-length GST-RUTBC2 and then collected on <t>glutathione-Sepharose.</t> Bound material was eluted in sample buffer and analyzed by immunoblot with anti-His antibodies. Inputs represent 5% of the added His-tagged Rab. B , His-Rab9A and His-Rab6A were preloaded with GTPγS and incubated with full-length GST-RUTBC2 and then collected on glutathione-Sepharose. Bound material was eluted in sample buffer and analyzed by immunoblot with anti-His antibodies. Inputs represent 10% of the added His-tagged Rabs. C , in vitro transcribed/translated 3×Myc-RUTBC2 was incubated with GST-Rab9A or GST-Rab9B preloaded with either GTPγS ( T ) or GDP ( D ) and analyzed as in A. D , purified GST-RUTBC2 and control proteins were incubated with untagged Rab9A loaded with [ 35 S]GTPγS and immobilized using glutathione-Sepharose. Bound Rab was detected by scintillation counting. Error bars represent S.E. from at least two independent experiments. E , His-RUTBC2-N or His-RUTBC2-C was incubated with GST or GST-Rab9A Q66L and then collected on glutathione-Sepharose. Bound material was eluted in sample buffer and analyzed by immunoblot using anti-His antibodies. Inputs represent 5% of the added His-tagged RUTBC2 constructs. F , His-Rab9A was preloaded with GTPγS and incubated with GST, full-length GST-RUTBC2, GST-RUTBC2-N, or GST-RUTBC2-C and then collected on glutathione-Sepharose. Bound material was eluted in sample buffer and analyzed by immunoblot with anti-His antibodies. Inputs represent 5% of the added His-tagged Rab.
    Glutathione Sepharose 4 Fast Flow Column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 95/100, based on 250 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare glutathione sepharose 4 fast flow system
    RUTBC2 is an effector of Rab9A. A , His-Rab2 and His-Rab9A were preloaded with GTPγS and incubated with GST or full-length GST-RUTBC2 and then collected on <t>glutathione-Sepharose.</t> Bound material was eluted in sample buffer and analyzed by immunoblot with anti-His antibodies. Inputs represent 5% of the added His-tagged Rab. B , His-Rab9A and His-Rab6A were preloaded with GTPγS and incubated with full-length GST-RUTBC2 and then collected on glutathione-Sepharose. Bound material was eluted in sample buffer and analyzed by immunoblot with anti-His antibodies. Inputs represent 10% of the added His-tagged Rabs. C , in vitro transcribed/translated 3×Myc-RUTBC2 was incubated with GST-Rab9A or GST-Rab9B preloaded with either GTPγS ( T ) or GDP ( D ) and analyzed as in A. D , purified GST-RUTBC2 and control proteins were incubated with untagged Rab9A loaded with [ 35 S]GTPγS and immobilized using glutathione-Sepharose. Bound Rab was detected by scintillation counting. Error bars represent S.E. from at least two independent experiments. E , His-RUTBC2-N or His-RUTBC2-C was incubated with GST or GST-Rab9A Q66L and then collected on glutathione-Sepharose. Bound material was eluted in sample buffer and analyzed by immunoblot using anti-His antibodies. Inputs represent 5% of the added His-tagged RUTBC2 constructs. F , His-Rab9A was preloaded with GTPγS and incubated with GST, full-length GST-RUTBC2, GST-RUTBC2-N, or GST-RUTBC2-C and then collected on glutathione-Sepharose. Bound material was eluted in sample buffer and analyzed by immunoblot with anti-His antibodies. Inputs represent 5% of the added His-tagged Rab.
    Glutathione Sepharose 4 Fast Flow System, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 70/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    GE Healthcare glutathione sepharose 4b
    Direct physical interaction between TRF1 and Speedy A a Coomassie blue-stained gels showing the purification of relevant proteins. b Direct physical interaction between TRF1 and Speedy A were determined by GST pull-down assays. GST-TRF1 or GST conjugated <t>sepharose</t> beads were used to pull down His-FLAG-Speedy A. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-GST antibodies. c No direct physical interaction between TRF1 and Cdk2, which was determined by GST pull-down assays. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-MYC and anti-GST antibodies. d Direct physical interaction between CDK2 and Speedy A was determined by GST pull-down assays. GST-CDK2 or GST conjugated sepharose beads were used to pull down purified His-FLAG-Speedy A. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-GST antibodies. e Speedy A-mediated interaction between TRF1 and Cdk2. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-FLAG-Speedy A and (or) His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-FLAG or anti-MYC antibody. Asterisks indicate the bands of Speedy A. Input for His-FLAG-Speedy A and His-MYC-Cdk2 were 10% and 1%, respectively. f TRF1 and Cdk2 do not compete for interaction with Speedy A. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-FLAG-Speedy A in the presence of increasing amounts of His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-MYC antibodies. Asterisks indicate signals of Speedy A.
    Glutathione Sepharose 4b, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 17944 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    84
    GE Healthcare glutathione sepharose 4 fast flow medium
    Direct physical interaction between TRF1 and Speedy A a Coomassie blue-stained gels showing the purification of relevant proteins. b Direct physical interaction between TRF1 and Speedy A were determined by GST pull-down assays. GST-TRF1 or GST conjugated <t>sepharose</t> beads were used to pull down His-FLAG-Speedy A. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-GST antibodies. c No direct physical interaction between TRF1 and Cdk2, which was determined by GST pull-down assays. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-MYC and anti-GST antibodies. d Direct physical interaction between CDK2 and Speedy A was determined by GST pull-down assays. GST-CDK2 or GST conjugated sepharose beads were used to pull down purified His-FLAG-Speedy A. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-GST antibodies. e Speedy A-mediated interaction between TRF1 and Cdk2. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-FLAG-Speedy A and (or) His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-FLAG or anti-MYC antibody. Asterisks indicate the bands of Speedy A. Input for His-FLAG-Speedy A and His-MYC-Cdk2 were 10% and 1%, respectively. f TRF1 and Cdk2 do not compete for interaction with Speedy A. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-FLAG-Speedy A in the presence of increasing amounts of His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-MYC antibodies. Asterisks indicate signals of Speedy A.
    Glutathione Sepharose 4 Fast Flow Medium, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 84/100, based on 60 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    GE Healthcare preequilibrated glutathione sepharose 4 fast flow beads
    Direct physical interaction between TRF1 and Speedy A a Coomassie blue-stained gels showing the purification of relevant proteins. b Direct physical interaction between TRF1 and Speedy A were determined by GST pull-down assays. GST-TRF1 or GST conjugated <t>sepharose</t> beads were used to pull down His-FLAG-Speedy A. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-GST antibodies. c No direct physical interaction between TRF1 and Cdk2, which was determined by GST pull-down assays. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-MYC and anti-GST antibodies. d Direct physical interaction between CDK2 and Speedy A was determined by GST pull-down assays. GST-CDK2 or GST conjugated sepharose beads were used to pull down purified His-FLAG-Speedy A. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-GST antibodies. e Speedy A-mediated interaction between TRF1 and Cdk2. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-FLAG-Speedy A and (or) His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-FLAG or anti-MYC antibody. Asterisks indicate the bands of Speedy A. Input for His-FLAG-Speedy A and His-MYC-Cdk2 were 10% and 1%, respectively. f TRF1 and Cdk2 do not compete for interaction with Speedy A. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-FLAG-Speedy A in the presence of increasing amounts of His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-MYC antibodies. Asterisks indicate signals of Speedy A.
    Preequilibrated Glutathione Sepharose 4 Fast Flow Beads, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 78/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    83
    GE Healthcare glutathione sepharose 4 fast flow resin column
    Direct physical interaction between TRF1 and Speedy A a Coomassie blue-stained gels showing the purification of relevant proteins. b Direct physical interaction between TRF1 and Speedy A were determined by GST pull-down assays. GST-TRF1 or GST conjugated <t>sepharose</t> beads were used to pull down His-FLAG-Speedy A. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-GST antibodies. c No direct physical interaction between TRF1 and Cdk2, which was determined by GST pull-down assays. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-MYC and anti-GST antibodies. d Direct physical interaction between CDK2 and Speedy A was determined by GST pull-down assays. GST-CDK2 or GST conjugated sepharose beads were used to pull down purified His-FLAG-Speedy A. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-GST antibodies. e Speedy A-mediated interaction between TRF1 and Cdk2. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-FLAG-Speedy A and (or) His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-FLAG or anti-MYC antibody. Asterisks indicate the bands of Speedy A. Input for His-FLAG-Speedy A and His-MYC-Cdk2 were 10% and 1%, respectively. f TRF1 and Cdk2 do not compete for interaction with Speedy A. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-FLAG-Speedy A in the presence of increasing amounts of His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-MYC antibodies. Asterisks indicate signals of Speedy A.
    Glutathione Sepharose 4 Fast Flow Resin Column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 83/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    70
    GE Healthcare preequilibrated glutathione sepharose 4 fast flow resin
    Direct physical interaction between TRF1 and Speedy A a Coomassie blue-stained gels showing the purification of relevant proteins. b Direct physical interaction between TRF1 and Speedy A were determined by GST pull-down assays. GST-TRF1 or GST conjugated <t>sepharose</t> beads were used to pull down His-FLAG-Speedy A. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-GST antibodies. c No direct physical interaction between TRF1 and Cdk2, which was determined by GST pull-down assays. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-MYC and anti-GST antibodies. d Direct physical interaction between CDK2 and Speedy A was determined by GST pull-down assays. GST-CDK2 or GST conjugated sepharose beads were used to pull down purified His-FLAG-Speedy A. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-GST antibodies. e Speedy A-mediated interaction between TRF1 and Cdk2. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-FLAG-Speedy A and (or) His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-FLAG or anti-MYC antibody. Asterisks indicate the bands of Speedy A. Input for His-FLAG-Speedy A and His-MYC-Cdk2 were 10% and 1%, respectively. f TRF1 and Cdk2 do not compete for interaction with Speedy A. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-FLAG-Speedy A in the presence of increasing amounts of His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-MYC antibodies. Asterisks indicate signals of Speedy A.
    Preequilibrated Glutathione Sepharose 4 Fast Flow Resin, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 70/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/preequilibrated glutathione sepharose 4 fast flow resin/product/GE Healthcare
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    79
    GE Healthcare glutathione sepharose 4 fast flow beads resin
    Direct physical interaction between TRF1 and Speedy A a Coomassie blue-stained gels showing the purification of relevant proteins. b Direct physical interaction between TRF1 and Speedy A were determined by GST pull-down assays. GST-TRF1 or GST conjugated <t>sepharose</t> beads were used to pull down His-FLAG-Speedy A. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-GST antibodies. c No direct physical interaction between TRF1 and Cdk2, which was determined by GST pull-down assays. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-MYC and anti-GST antibodies. d Direct physical interaction between CDK2 and Speedy A was determined by GST pull-down assays. GST-CDK2 or GST conjugated sepharose beads were used to pull down purified His-FLAG-Speedy A. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-GST antibodies. e Speedy A-mediated interaction between TRF1 and Cdk2. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-FLAG-Speedy A and (or) His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-FLAG or anti-MYC antibody. Asterisks indicate the bands of Speedy A. Input for His-FLAG-Speedy A and His-MYC-Cdk2 were 10% and 1%, respectively. f TRF1 and Cdk2 do not compete for interaction with Speedy A. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-FLAG-Speedy A in the presence of increasing amounts of His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-MYC antibodies. Asterisks indicate signals of Speedy A.
    Glutathione Sepharose 4 Fast Flow Beads Resin, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 79/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    GE Healthcare glutathione sepharose 4 fast flow affinity chromatography
    Direct physical interaction between TRF1 and Speedy A a Coomassie blue-stained gels showing the purification of relevant proteins. b Direct physical interaction between TRF1 and Speedy A were determined by GST pull-down assays. GST-TRF1 or GST conjugated <t>sepharose</t> beads were used to pull down His-FLAG-Speedy A. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-GST antibodies. c No direct physical interaction between TRF1 and Cdk2, which was determined by GST pull-down assays. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-MYC and anti-GST antibodies. d Direct physical interaction between CDK2 and Speedy A was determined by GST pull-down assays. GST-CDK2 or GST conjugated sepharose beads were used to pull down purified His-FLAG-Speedy A. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-GST antibodies. e Speedy A-mediated interaction between TRF1 and Cdk2. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-FLAG-Speedy A and (or) His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-FLAG or anti-MYC antibody. Asterisks indicate the bands of Speedy A. Input for His-FLAG-Speedy A and His-MYC-Cdk2 were 10% and 1%, respectively. f TRF1 and Cdk2 do not compete for interaction with Speedy A. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-FLAG-Speedy A in the presence of increasing amounts of His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-MYC antibodies. Asterisks indicate signals of Speedy A.
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    GE Healthcare gst coupled glutathione sepharose 4 fast flow beads
    Direct physical interaction between TRF1 and Speedy A a Coomassie blue-stained gels showing the purification of relevant proteins. b Direct physical interaction between TRF1 and Speedy A were determined by GST pull-down assays. GST-TRF1 or GST conjugated <t>sepharose</t> beads were used to pull down His-FLAG-Speedy A. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-GST antibodies. c No direct physical interaction between TRF1 and Cdk2, which was determined by GST pull-down assays. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-MYC and anti-GST antibodies. d Direct physical interaction between CDK2 and Speedy A was determined by GST pull-down assays. GST-CDK2 or GST conjugated sepharose beads were used to pull down purified His-FLAG-Speedy A. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-GST antibodies. e Speedy A-mediated interaction between TRF1 and Cdk2. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-FLAG-Speedy A and (or) His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-FLAG or anti-MYC antibody. Asterisks indicate the bands of Speedy A. Input for His-FLAG-Speedy A and His-MYC-Cdk2 were 10% and 1%, respectively. f TRF1 and Cdk2 do not compete for interaction with Speedy A. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-FLAG-Speedy A in the presence of increasing amounts of His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-MYC antibodies. Asterisks indicate signals of Speedy A.
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    Direct physical interaction between TRF1 and Speedy A a Coomassie blue-stained gels showing the purification of relevant proteins. b Direct physical interaction between TRF1 and Speedy A were determined by GST pull-down assays. GST-TRF1 or GST conjugated <t>sepharose</t> beads were used to pull down His-FLAG-Speedy A. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-GST antibodies. c No direct physical interaction between TRF1 and Cdk2, which was determined by GST pull-down assays. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-MYC and anti-GST antibodies. d Direct physical interaction between CDK2 and Speedy A was determined by GST pull-down assays. GST-CDK2 or GST conjugated sepharose beads were used to pull down purified His-FLAG-Speedy A. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-GST antibodies. e Speedy A-mediated interaction between TRF1 and Cdk2. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-FLAG-Speedy A and (or) His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-FLAG or anti-MYC antibody. Asterisks indicate the bands of Speedy A. Input for His-FLAG-Speedy A and His-MYC-Cdk2 were 10% and 1%, respectively. f TRF1 and Cdk2 do not compete for interaction with Speedy A. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-FLAG-Speedy A in the presence of increasing amounts of His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-MYC antibodies. Asterisks indicate signals of Speedy A.
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    GE Healthcare glutathione sepharose 4 fast flow one step protocol
    Direct physical interaction between TRF1 and Speedy A a Coomassie blue-stained gels showing the purification of relevant proteins. b Direct physical interaction between TRF1 and Speedy A were determined by GST pull-down assays. GST-TRF1 or GST conjugated <t>sepharose</t> beads were used to pull down His-FLAG-Speedy A. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-GST antibodies. c No direct physical interaction between TRF1 and Cdk2, which was determined by GST pull-down assays. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-MYC and anti-GST antibodies. d Direct physical interaction between CDK2 and Speedy A was determined by GST pull-down assays. GST-CDK2 or GST conjugated sepharose beads were used to pull down purified His-FLAG-Speedy A. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-GST antibodies. e Speedy A-mediated interaction between TRF1 and Cdk2. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-FLAG-Speedy A and (or) His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-FLAG or anti-MYC antibody. Asterisks indicate the bands of Speedy A. Input for His-FLAG-Speedy A and His-MYC-Cdk2 were 10% and 1%, respectively. f TRF1 and Cdk2 do not compete for interaction with Speedy A. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-FLAG-Speedy A in the presence of increasing amounts of His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-MYC antibodies. Asterisks indicate signals of Speedy A.
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    GE Healthcare glutathione sepharose 4 fast flow matrix
    Direct physical interaction between TRF1 and Speedy A a Coomassie blue-stained gels showing the purification of relevant proteins. b Direct physical interaction between TRF1 and Speedy A were determined by GST pull-down assays. GST-TRF1 or GST conjugated <t>sepharose</t> beads were used to pull down His-FLAG-Speedy A. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-GST antibodies. c No direct physical interaction between TRF1 and Cdk2, which was determined by GST pull-down assays. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-MYC and anti-GST antibodies. d Direct physical interaction between CDK2 and Speedy A was determined by GST pull-down assays. GST-CDK2 or GST conjugated sepharose beads were used to pull down purified His-FLAG-Speedy A. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-GST antibodies. e Speedy A-mediated interaction between TRF1 and Cdk2. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-FLAG-Speedy A and (or) His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-FLAG or anti-MYC antibody. Asterisks indicate the bands of Speedy A. Input for His-FLAG-Speedy A and His-MYC-Cdk2 were 10% and 1%, respectively. f TRF1 and Cdk2 do not compete for interaction with Speedy A. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-FLAG-Speedy A in the presence of increasing amounts of His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-MYC antibodies. Asterisks indicate signals of Speedy A.
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    GE Healthcare glutathion sepharose fast flow
    Direct physical interaction between TRF1 and Speedy A a Coomassie blue-stained gels showing the purification of relevant proteins. b Direct physical interaction between TRF1 and Speedy A were determined by GST pull-down assays. GST-TRF1 or GST conjugated <t>sepharose</t> beads were used to pull down His-FLAG-Speedy A. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-GST antibodies. c No direct physical interaction between TRF1 and Cdk2, which was determined by GST pull-down assays. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-MYC and anti-GST antibodies. d Direct physical interaction between CDK2 and Speedy A was determined by GST pull-down assays. GST-CDK2 or GST conjugated sepharose beads were used to pull down purified His-FLAG-Speedy A. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-GST antibodies. e Speedy A-mediated interaction between TRF1 and Cdk2. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-FLAG-Speedy A and (or) His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-FLAG or anti-MYC antibody. Asterisks indicate the bands of Speedy A. Input for His-FLAG-Speedy A and His-MYC-Cdk2 were 10% and 1%, respectively. f TRF1 and Cdk2 do not compete for interaction with Speedy A. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-FLAG-Speedy A in the presence of increasing amounts of His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-MYC antibodies. Asterisks indicate signals of Speedy A.
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    Simultaneous recognition of PTEN peptide by aptamers and antibodies. The results of precipitation are shown in terms of net amounts of molecules acquired through extrapolations from the standard curve of quantification. The backgrounds considered (PTENz7 and PTENz14) were attained through incubation and co-purification of the aptamers and antibodies in the absence of peptides. Quadruplicate samples showed the positive binding of PTENz14 to the peptide (PTENz14+Peptide). Findings also confirmed the blockade of PTENz7 recognition by the antibodies (PTENz7+Peptide). Extrapolations from the standard curve of quantification show 1.8×10 11 molecules of PTENz14 aptamer were bound to the peptide and co-precipitated with the antibodies attached to <t>Sepharose</t> – nearly a 20-fold increase with respect to the background (P
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    Simultaneous recognition of PTEN peptide by aptamers and antibodies. The results of precipitation are shown in terms of net amounts of molecules acquired through extrapolations from the standard curve of quantification. The backgrounds considered (PTENz7 and PTENz14) were attained through incubation and co-purification of the aptamers and antibodies in the absence of peptides. Quadruplicate samples showed the positive binding of PTENz14 to the peptide (PTENz14+Peptide). Findings also confirmed the blockade of PTENz7 recognition by the antibodies (PTENz7+Peptide). Extrapolations from the standard curve of quantification show 1.8×10 11 molecules of PTENz14 aptamer were bound to the peptide and co-precipitated with the antibodies attached to <t>Sepharose</t> – nearly a 20-fold increase with respect to the background (P
    Glutathione Sepharose Beads, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 14446 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare glutathione sepharose 4
    Simultaneous recognition of PTEN peptide by aptamers and antibodies. The results of precipitation are shown in terms of net amounts of molecules acquired through extrapolations from the standard curve of quantification. The backgrounds considered (PTENz7 and PTENz14) were attained through incubation and co-purification of the aptamers and antibodies in the absence of peptides. Quadruplicate samples showed the positive binding of PTENz14 to the peptide (PTENz14+Peptide). Findings also confirmed the blockade of PTENz7 recognition by the antibodies (PTENz7+Peptide). Extrapolations from the standard curve of quantification show 1.8×10 11 molecules of PTENz14 aptamer were bound to the peptide and co-precipitated with the antibodies attached to <t>Sepharose</t> – nearly a 20-fold increase with respect to the background (P
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    Simultaneous recognition of PTEN peptide by aptamers and antibodies. The results of precipitation are shown in terms of net amounts of molecules acquired through extrapolations from the standard curve of quantification. The backgrounds considered (PTENz7 and PTENz14) were attained through incubation and co-purification of the aptamers and antibodies in the absence of peptides. Quadruplicate samples showed the positive binding of PTENz14 to the peptide (PTENz14+Peptide). Findings also confirmed the blockade of PTENz7 recognition by the antibodies (PTENz7+Peptide). Extrapolations from the standard curve of quantification show 1.8×10 11 molecules of PTENz14 aptamer were bound to the peptide and co-precipitated with the antibodies attached to <t>Sepharose</t> – nearly a 20-fold increase with respect to the background (P
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    Simultaneous recognition of PTEN peptide by aptamers and antibodies. The results of precipitation are shown in terms of net amounts of molecules acquired through extrapolations from the standard curve of quantification. The backgrounds considered (PTENz7 and PTENz14) were attained through incubation and co-purification of the aptamers and antibodies in the absence of peptides. Quadruplicate samples showed the positive binding of PTENz14 to the peptide (PTENz14+Peptide). Findings also confirmed the blockade of PTENz7 recognition by the antibodies (PTENz7+Peptide). Extrapolations from the standard curve of quantification show 1.8×10 11 molecules of PTENz14 aptamer were bound to the peptide and co-precipitated with the antibodies attached to <t>Sepharose</t> – nearly a 20-fold increase with respect to the background (P
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    Simultaneous recognition of PTEN peptide by aptamers and antibodies. The results of precipitation are shown in terms of net amounts of molecules acquired through extrapolations from the standard curve of quantification. The backgrounds considered (PTENz7 and PTENz14) were attained through incubation and co-purification of the aptamers and antibodies in the absence of peptides. Quadruplicate samples showed the positive binding of PTENz14 to the peptide (PTENz14+Peptide). Findings also confirmed the blockade of PTENz7 recognition by the antibodies (PTENz7+Peptide). Extrapolations from the standard curve of quantification show 1.8×10 11 molecules of PTENz14 aptamer were bound to the peptide and co-precipitated with the antibodies attached to <t>Sepharose</t> – nearly a 20-fold increase with respect to the background (P
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    Simultaneous recognition of PTEN peptide by aptamers and antibodies. The results of precipitation are shown in terms of net amounts of molecules acquired through extrapolations from the standard curve of quantification. The backgrounds considered (PTENz7 and PTENz14) were attained through incubation and co-purification of the aptamers and antibodies in the absence of peptides. Quadruplicate samples showed the positive binding of PTENz14 to the peptide (PTENz14+Peptide). Findings also confirmed the blockade of PTENz7 recognition by the antibodies (PTENz7+Peptide). Extrapolations from the standard curve of quantification show 1.8×10 11 molecules of PTENz14 aptamer were bound to the peptide and co-precipitated with the antibodies attached to <t>Sepharose</t> – nearly a 20-fold increase with respect to the background (P
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    Simultaneous recognition of PTEN peptide by aptamers and antibodies. The results of precipitation are shown in terms of net amounts of molecules acquired through extrapolations from the standard curve of quantification. The backgrounds considered (PTENz7 and PTENz14) were attained through incubation and co-purification of the aptamers and antibodies in the absence of peptides. Quadruplicate samples showed the positive binding of PTENz14 to the peptide (PTENz14+Peptide). Findings also confirmed the blockade of PTENz7 recognition by the antibodies (PTENz7+Peptide). Extrapolations from the standard curve of quantification show 1.8×10 11 molecules of PTENz14 aptamer were bound to the peptide and co-precipitated with the antibodies attached to <t>Sepharose</t> – nearly a 20-fold increase with respect to the background (P
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    Simultaneous recognition of PTEN peptide by aptamers and antibodies. The results of precipitation are shown in terms of net amounts of molecules acquired through extrapolations from the standard curve of quantification. The backgrounds considered (PTENz7 and PTENz14) were attained through incubation and co-purification of the aptamers and antibodies in the absence of peptides. Quadruplicate samples showed the positive binding of PTENz14 to the peptide (PTENz14+Peptide). Findings also confirmed the blockade of PTENz7 recognition by the antibodies (PTENz7+Peptide). Extrapolations from the standard curve of quantification show 1.8×10 11 molecules of PTENz14 aptamer were bound to the peptide and co-precipitated with the antibodies attached to <t>Sepharose</t> – nearly a 20-fold increase with respect to the background (P
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    Simultaneous recognition of PTEN peptide by aptamers and antibodies. The results of precipitation are shown in terms of net amounts of molecules acquired through extrapolations from the standard curve of quantification. The backgrounds considered (PTENz7 and PTENz14) were attained through incubation and co-purification of the aptamers and antibodies in the absence of peptides. Quadruplicate samples showed the positive binding of PTENz14 to the peptide (PTENz14+Peptide). Findings also confirmed the blockade of PTENz7 recognition by the antibodies (PTENz7+Peptide). Extrapolations from the standard curve of quantification show 1.8×10 11 molecules of PTENz14 aptamer were bound to the peptide and co-precipitated with the antibodies attached to <t>Sepharose</t> – nearly a 20-fold increase with respect to the background (P
    Glutathione Sepharose 4 Fast Flow Gst Affinity Resin, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 88/100, based on 24 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Simultaneous recognition of PTEN peptide by aptamers and antibodies. The results of precipitation are shown in terms of net amounts of molecules acquired through extrapolations from the standard curve of quantification. The backgrounds considered (PTENz7 and PTENz14) were attained through incubation and co-purification of the aptamers and antibodies in the absence of peptides. Quadruplicate samples showed the positive binding of PTENz14 to the peptide (PTENz14+Peptide). Findings also confirmed the blockade of PTENz7 recognition by the antibodies (PTENz7+Peptide). Extrapolations from the standard curve of quantification show 1.8×10 11 molecules of PTENz14 aptamer were bound to the peptide and co-precipitated with the antibodies attached to <t>Sepharose</t> – nearly a 20-fold increase with respect to the background (P
    Amylose Resin High Flow, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 91/100, based on 88 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare hpol κ glutathione sepharose 4 fast flow beads
    Simultaneous recognition of PTEN peptide by aptamers and antibodies. The results of precipitation are shown in terms of net amounts of molecules acquired through extrapolations from the standard curve of quantification. The backgrounds considered (PTENz7 and PTENz14) were attained through incubation and co-purification of the aptamers and antibodies in the absence of peptides. Quadruplicate samples showed the positive binding of PTENz14 to the peptide (PTENz14+Peptide). Findings also confirmed the blockade of PTENz7 recognition by the antibodies (PTENz7+Peptide). Extrapolations from the standard curve of quantification show 1.8×10 11 molecules of PTENz14 aptamer were bound to the peptide and co-precipitated with the antibodies attached to <t>Sepharose</t> – nearly a 20-fold increase with respect to the background (P
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    RUTBC2 is an effector of Rab9A. A , His-Rab2 and His-Rab9A were preloaded with GTPγS and incubated with GST or full-length GST-RUTBC2 and then collected on glutathione-Sepharose. Bound material was eluted in sample buffer and analyzed by immunoblot with anti-His antibodies. Inputs represent 5% of the added His-tagged Rab. B , His-Rab9A and His-Rab6A were preloaded with GTPγS and incubated with full-length GST-RUTBC2 and then collected on glutathione-Sepharose. Bound material was eluted in sample buffer and analyzed by immunoblot with anti-His antibodies. Inputs represent 10% of the added His-tagged Rabs. C , in vitro transcribed/translated 3×Myc-RUTBC2 was incubated with GST-Rab9A or GST-Rab9B preloaded with either GTPγS ( T ) or GDP ( D ) and analyzed as in A. D , purified GST-RUTBC2 and control proteins were incubated with untagged Rab9A loaded with [ 35 S]GTPγS and immobilized using glutathione-Sepharose. Bound Rab was detected by scintillation counting. Error bars represent S.E. from at least two independent experiments. E , His-RUTBC2-N or His-RUTBC2-C was incubated with GST or GST-Rab9A Q66L and then collected on glutathione-Sepharose. Bound material was eluted in sample buffer and analyzed by immunoblot using anti-His antibodies. Inputs represent 5% of the added His-tagged RUTBC2 constructs. F , His-Rab9A was preloaded with GTPγS and incubated with GST, full-length GST-RUTBC2, GST-RUTBC2-N, or GST-RUTBC2-C and then collected on glutathione-Sepharose. Bound material was eluted in sample buffer and analyzed by immunoblot with anti-His antibodies. Inputs represent 5% of the added His-tagged Rab.

    Journal: The Journal of Biological Chemistry

    Article Title: RUTBC2 Protein, a Rab9A Effector and GTPase-activating Protein for Rab36 *

    doi: 10.1074/jbc.M112.362558

    Figure Lengend Snippet: RUTBC2 is an effector of Rab9A. A , His-Rab2 and His-Rab9A were preloaded with GTPγS and incubated with GST or full-length GST-RUTBC2 and then collected on glutathione-Sepharose. Bound material was eluted in sample buffer and analyzed by immunoblot with anti-His antibodies. Inputs represent 5% of the added His-tagged Rab. B , His-Rab9A and His-Rab6A were preloaded with GTPγS and incubated with full-length GST-RUTBC2 and then collected on glutathione-Sepharose. Bound material was eluted in sample buffer and analyzed by immunoblot with anti-His antibodies. Inputs represent 10% of the added His-tagged Rabs. C , in vitro transcribed/translated 3×Myc-RUTBC2 was incubated with GST-Rab9A or GST-Rab9B preloaded with either GTPγS ( T ) or GDP ( D ) and analyzed as in A. D , purified GST-RUTBC2 and control proteins were incubated with untagged Rab9A loaded with [ 35 S]GTPγS and immobilized using glutathione-Sepharose. Bound Rab was detected by scintillation counting. Error bars represent S.E. from at least two independent experiments. E , His-RUTBC2-N or His-RUTBC2-C was incubated with GST or GST-Rab9A Q66L and then collected on glutathione-Sepharose. Bound material was eluted in sample buffer and analyzed by immunoblot using anti-His antibodies. Inputs represent 5% of the added His-tagged RUTBC2 constructs. F , His-Rab9A was preloaded with GTPγS and incubated with GST, full-length GST-RUTBC2, GST-RUTBC2-N, or GST-RUTBC2-C and then collected on glutathione-Sepharose. Bound material was eluted in sample buffer and analyzed by immunoblot with anti-His antibodies. Inputs represent 5% of the added His-tagged Rab.

    Article Snippet: Cleared lysates (19,000 rpm for 30 min at 4 °C in a JA-20 rotor; Beckman Coulter) were incubated with glutathione-Sepharose Fast Flow (GE Healthcare) for 1.5 h at 4 °C.

    Techniques: Incubation, In Vitro, Purification, Construct

    RUTBC2 binds to, but is not a GAP for Rab9A in cells. A , HEK293T cells were transfected with 3×Myc-RUTBC2 and GFP or GFP-Rab9A for 24 h, and GFP was immunoprecipitated with GFP-binding protein-conjugated Sepharose and immunoblotted with anti-Myc antibodies ( top panel ) and anti-GFP antibodies ( bottom panel ). Input represents 2% of the lysate subjected to immunoprecipitation. B , COS-1 cells were transfected with 3×Myc-RUTBC2 for 48 h, and total cell extracts were immunoblotted with anti-CI-MPR antibodies. AU , arbitrary units. C , quantitation of CI-MPR half-life measured from pulse-chase analysis of HeLa cells transfected with 3×Myc-RUTBC2 for 48 h. Extracts were immunoprecipitated with anti-CI-MPR antibodies and exposed to a phosphor screen. D , HEK293T cells transfected with 3×Myc-RUTBC2 wild type or R829A for 24 h were assayed for secreted and intracellular hexosaminidase activity. Error bars in panels B–D represent S.E. from at least two independent experiments.

    Journal: The Journal of Biological Chemistry

    Article Title: RUTBC2 Protein, a Rab9A Effector and GTPase-activating Protein for Rab36 *

    doi: 10.1074/jbc.M112.362558

    Figure Lengend Snippet: RUTBC2 binds to, but is not a GAP for Rab9A in cells. A , HEK293T cells were transfected with 3×Myc-RUTBC2 and GFP or GFP-Rab9A for 24 h, and GFP was immunoprecipitated with GFP-binding protein-conjugated Sepharose and immunoblotted with anti-Myc antibodies ( top panel ) and anti-GFP antibodies ( bottom panel ). Input represents 2% of the lysate subjected to immunoprecipitation. B , COS-1 cells were transfected with 3×Myc-RUTBC2 for 48 h, and total cell extracts were immunoblotted with anti-CI-MPR antibodies. AU , arbitrary units. C , quantitation of CI-MPR half-life measured from pulse-chase analysis of HeLa cells transfected with 3×Myc-RUTBC2 for 48 h. Extracts were immunoprecipitated with anti-CI-MPR antibodies and exposed to a phosphor screen. D , HEK293T cells transfected with 3×Myc-RUTBC2 wild type or R829A for 24 h were assayed for secreted and intracellular hexosaminidase activity. Error bars in panels B–D represent S.E. from at least two independent experiments.

    Article Snippet: Cleared lysates (19,000 rpm for 30 min at 4 °C in a JA-20 rotor; Beckman Coulter) were incubated with glutathione-Sepharose Fast Flow (GE Healthcare) for 1.5 h at 4 °C.

    Techniques: Transfection, Immunoprecipitation, Binding Assay, Quantitation Assay, Pulse Chase, Activity Assay

    Direct physical interaction between TRF1 and Speedy A a Coomassie blue-stained gels showing the purification of relevant proteins. b Direct physical interaction between TRF1 and Speedy A were determined by GST pull-down assays. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-FLAG-Speedy A. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-GST antibodies. c No direct physical interaction between TRF1 and Cdk2, which was determined by GST pull-down assays. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-MYC and anti-GST antibodies. d Direct physical interaction between CDK2 and Speedy A was determined by GST pull-down assays. GST-CDK2 or GST conjugated sepharose beads were used to pull down purified His-FLAG-Speedy A. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-GST antibodies. e Speedy A-mediated interaction between TRF1 and Cdk2. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-FLAG-Speedy A and (or) His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-FLAG or anti-MYC antibody. Asterisks indicate the bands of Speedy A. Input for His-FLAG-Speedy A and His-MYC-Cdk2 were 10% and 1%, respectively. f TRF1 and Cdk2 do not compete for interaction with Speedy A. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-FLAG-Speedy A in the presence of increasing amounts of His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-MYC antibodies. Asterisks indicate signals of Speedy A.

    Journal: Cell Death and Differentiation

    Article Title: Dual roles of TRF1 in tethering telomeres to the nuclear envelope and protecting them from fusion during meiosis

    doi: 10.1038/s41418-017-0037-8

    Figure Lengend Snippet: Direct physical interaction between TRF1 and Speedy A a Coomassie blue-stained gels showing the purification of relevant proteins. b Direct physical interaction between TRF1 and Speedy A were determined by GST pull-down assays. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-FLAG-Speedy A. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-GST antibodies. c No direct physical interaction between TRF1 and Cdk2, which was determined by GST pull-down assays. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-MYC and anti-GST antibodies. d Direct physical interaction between CDK2 and Speedy A was determined by GST pull-down assays. GST-CDK2 or GST conjugated sepharose beads were used to pull down purified His-FLAG-Speedy A. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-GST antibodies. e Speedy A-mediated interaction between TRF1 and Cdk2. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-FLAG-Speedy A and (or) His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-FLAG or anti-MYC antibody. Asterisks indicate the bands of Speedy A. Input for His-FLAG-Speedy A and His-MYC-Cdk2 were 10% and 1%, respectively. f TRF1 and Cdk2 do not compete for interaction with Speedy A. GST-TRF1 or GST conjugated sepharose beads were used to pull down His-FLAG-Speedy A in the presence of increasing amounts of His-MYC-Cdk2. Bound proteins were detected by immunoblotting analysis with anti-FLAG and anti-MYC antibodies. Asterisks indicate signals of Speedy A.

    Article Snippet: Then we collected the supernatant by high-speed centrifugation, and incubated them with Ni Sepharose 6 Fast Flow (GE Healthcare, Marlborough, MA) or Glutathione Sepharose 4B (GE Healthcare, Marlborough, MA) for 2 h at 4 °C.

    Techniques: Staining, Purification

    Simultaneous recognition of PTEN peptide by aptamers and antibodies. The results of precipitation are shown in terms of net amounts of molecules acquired through extrapolations from the standard curve of quantification. The backgrounds considered (PTENz7 and PTENz14) were attained through incubation and co-purification of the aptamers and antibodies in the absence of peptides. Quadruplicate samples showed the positive binding of PTENz14 to the peptide (PTENz14+Peptide). Findings also confirmed the blockade of PTENz7 recognition by the antibodies (PTENz7+Peptide). Extrapolations from the standard curve of quantification show 1.8×10 11 molecules of PTENz14 aptamer were bound to the peptide and co-precipitated with the antibodies attached to Sepharose – nearly a 20-fold increase with respect to the background (P

    Journal: PLoS ONE

    Article Title: Different Conformations of Phosphatase and Tensin Homolog, Deleted on Chromosome 10 (PTEN) Protein within the Nucleus and Cytoplasm of Neurons

    doi: 10.1371/journal.pone.0018857

    Figure Lengend Snippet: Simultaneous recognition of PTEN peptide by aptamers and antibodies. The results of precipitation are shown in terms of net amounts of molecules acquired through extrapolations from the standard curve of quantification. The backgrounds considered (PTENz7 and PTENz14) were attained through incubation and co-purification of the aptamers and antibodies in the absence of peptides. Quadruplicate samples showed the positive binding of PTENz14 to the peptide (PTENz14+Peptide). Findings also confirmed the blockade of PTENz7 recognition by the antibodies (PTENz7+Peptide). Extrapolations from the standard curve of quantification show 1.8×10 11 molecules of PTENz14 aptamer were bound to the peptide and co-precipitated with the antibodies attached to Sepharose – nearly a 20-fold increase with respect to the background (P

    Article Snippet: Pure proteins were obtained using a glutathione-Sepharose column (Glutathione Sepharose-4 fast-flow, Amersham Biosciences, Uppsala, Sweden).

    Techniques: Incubation, Copurification, Binding Assay