pab goat anti ent1 n 12 Search Results


pab goat anti ent1 n 12  (Santa Cruz Biotechnology)
93
Santa Cruz Biotechnology pab goat anti ent1 n 12
Pab Goat Anti Ent1 N 12, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/pab+goat+anti+ent1+n+12/ENT1+Antibody/pm24870236-246-41-45
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ugt2b pan antibody  (Santa Cruz Biotechnology)
93
Santa Cruz Biotechnology ugt2b pan antibody
Effects of modulation of Gli1 levels on UGT1A A. Effects of the direct Gli1 inhibitor GANT-61 on restoring ribavirin sensitivity (20 uM) in FRII cells. Effects are dependent on GANT-61 dose. B–D. Controls for eIF4E-ribavirin immunoprecipitations (IP) shown in and . Inputs, supernatants (Sn) and IP controls for 3 H ribavirin anti-eIF4E IPs are shown for GDC-0449 treated cells ( B ), FRII and FRI cells ( C ), and RNAi mediated knockdown of Gli1 ( D ). E–G. qPCR analysis of Gli1 ( E ) and UGT1A ( F ) using a pan-UGT1A primer or primers for specific UGT1As ( G ). mRNA levels were normalized to RNA Polymerase IIa. These findings are consistent with which indicates lower levels of UGT1A mRNA levels. Further, UGT1A3 and UGT1A8 decreased similarly (data not shown). Experiments were carried out in triplicate, at least three independent times. Average values are reported and error bars indicate standard deviations. These findings, that Gli1 elevation leads to reduce mRNA levels but increased protein levels are counter-intuitive. We hypothesize that Gli1 elevation increases protein stability of UGT1As (see below) and this leads to some sort of feedback mechanism leading to reduced UGT1As. Other scenarios are possible but the main point that Gli1 elevation leads to increased UGT1A protein production is clear. G. Gli1 increases UGT1A protein stability as shown by studies with the proteasomal inhibitor MG132 and a pan-UGT1A antibody. Here, MG132 addition stabilizes levels of UGT1A in parental cells, but in FRII cells where levels are already increased, there is no further increase with MG132. This indicates that UGT1A proteins are already stabilized in the FRII cells. All results are representative of three independent experiments. H. Western blot analysis with a <t>pan-UGT2B</t> antibody indicates that UGT2B levels are unchanged in FRII relative to FaDu cells suggesting the glucuronidation effects are mediated mostly through the UGT1A family. Tubulin provides a loading control.
Ugt2b Pan Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/pab+goat+anti+ent1+n+12/UGT2B+Antibody/pmc04138053-33-131-134
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mab rabbit anti shh  (Cell Signaling Technology Inc)
95
Cell Signaling Technology Inc mab rabbit anti shh
Effects of modulation of Gli1 levels on UGT1A A. Effects of the direct Gli1 inhibitor GANT-61 on restoring ribavirin sensitivity (20 uM) in FRII cells. Effects are dependent on GANT-61 dose. B–D. Controls for eIF4E-ribavirin immunoprecipitations (IP) shown in and . Inputs, supernatants (Sn) and IP controls for 3 H ribavirin anti-eIF4E IPs are shown for GDC-0449 treated cells ( B ), FRII and FRI cells ( C ), and RNAi mediated knockdown of Gli1 ( D ). E–G. qPCR analysis of Gli1 ( E ) and UGT1A ( F ) using a pan-UGT1A primer or primers for specific UGT1As ( G ). mRNA levels were normalized to RNA Polymerase IIa. These findings are consistent with which indicates lower levels of UGT1A mRNA levels. Further, UGT1A3 and UGT1A8 decreased similarly (data not shown). Experiments were carried out in triplicate, at least three independent times. Average values are reported and error bars indicate standard deviations. These findings, that Gli1 elevation leads to reduce mRNA levels but increased protein levels are counter-intuitive. We hypothesize that Gli1 elevation increases protein stability of UGT1As (see below) and this leads to some sort of feedback mechanism leading to reduced UGT1As. Other scenarios are possible but the main point that Gli1 elevation leads to increased UGT1A protein production is clear. G. Gli1 increases UGT1A protein stability as shown by studies with the proteasomal inhibitor MG132 and a pan-UGT1A antibody. Here, MG132 addition stabilizes levels of UGT1A in parental cells, but in FRII cells where levels are already increased, there is no further increase with MG132. This indicates that UGT1A proteins are already stabilized in the FRII cells. All results are representative of three independent experiments. H. Western blot analysis with a <t>pan-UGT2B</t> antibody indicates that UGT2B levels are unchanged in FRII relative to FaDu cells suggesting the glucuronidation effects are mediated mostly through the UGT1A family. Tubulin provides a loading control.
Mab Rabbit Anti Shh, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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mab mouse anti smo  (Santa Cruz Biotechnology)
95
Santa Cruz Biotechnology mab mouse anti smo
Effects of modulation of Gli1 levels on UGT1A A. Effects of the direct Gli1 inhibitor GANT-61 on restoring ribavirin sensitivity (20 uM) in FRII cells. Effects are dependent on GANT-61 dose. B–D. Controls for eIF4E-ribavirin immunoprecipitations (IP) shown in and . Inputs, supernatants (Sn) and IP controls for 3 H ribavirin anti-eIF4E IPs are shown for GDC-0449 treated cells ( B ), FRII and FRI cells ( C ), and RNAi mediated knockdown of Gli1 ( D ). E–G. qPCR analysis of Gli1 ( E ) and UGT1A ( F ) using a pan-UGT1A primer or primers for specific UGT1As ( G ). mRNA levels were normalized to RNA Polymerase IIa. These findings are consistent with which indicates lower levels of UGT1A mRNA levels. Further, UGT1A3 and UGT1A8 decreased similarly (data not shown). Experiments were carried out in triplicate, at least three independent times. Average values are reported and error bars indicate standard deviations. These findings, that Gli1 elevation leads to reduce mRNA levels but increased protein levels are counter-intuitive. We hypothesize that Gli1 elevation increases protein stability of UGT1As (see below) and this leads to some sort of feedback mechanism leading to reduced UGT1As. Other scenarios are possible but the main point that Gli1 elevation leads to increased UGT1A protein production is clear. G. Gli1 increases UGT1A protein stability as shown by studies with the proteasomal inhibitor MG132 and a pan-UGT1A antibody. Here, MG132 addition stabilizes levels of UGT1A in parental cells, but in FRII cells where levels are already increased, there is no further increase with MG132. This indicates that UGT1A proteins are already stabilized in the FRII cells. All results are representative of three independent experiments. H. Western blot analysis with a <t>pan-UGT2B</t> antibody indicates that UGT2B levels are unchanged in FRII relative to FaDu cells suggesting the glucuronidation effects are mediated mostly through the UGT1A family. Tubulin provides a loading control.
Mab Mouse Anti Smo, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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mab mouse anti hsp 90α β f 8  (Santa Cruz Biotechnology)
96
Santa Cruz Biotechnology mab mouse anti hsp 90α β f 8
Effects of modulation of Gli1 levels on UGT1A A. Effects of the direct Gli1 inhibitor GANT-61 on restoring ribavirin sensitivity (20 uM) in FRII cells. Effects are dependent on GANT-61 dose. B–D. Controls for eIF4E-ribavirin immunoprecipitations (IP) shown in and . Inputs, supernatants (Sn) and IP controls for 3 H ribavirin anti-eIF4E IPs are shown for GDC-0449 treated cells ( B ), FRII and FRI cells ( C ), and RNAi mediated knockdown of Gli1 ( D ). E–G. qPCR analysis of Gli1 ( E ) and UGT1A ( F ) using a pan-UGT1A primer or primers for specific UGT1As ( G ). mRNA levels were normalized to RNA Polymerase IIa. These findings are consistent with which indicates lower levels of UGT1A mRNA levels. Further, UGT1A3 and UGT1A8 decreased similarly (data not shown). Experiments were carried out in triplicate, at least three independent times. Average values are reported and error bars indicate standard deviations. These findings, that Gli1 elevation leads to reduce mRNA levels but increased protein levels are counter-intuitive. We hypothesize that Gli1 elevation increases protein stability of UGT1As (see below) and this leads to some sort of feedback mechanism leading to reduced UGT1As. Other scenarios are possible but the main point that Gli1 elevation leads to increased UGT1A protein production is clear. G. Gli1 increases UGT1A protein stability as shown by studies with the proteasomal inhibitor MG132 and a pan-UGT1A antibody. Here, MG132 addition stabilizes levels of UGT1A in parental cells, but in FRII cells where levels are already increased, there is no further increase with MG132. This indicates that UGT1A proteins are already stabilized in the FRII cells. All results are representative of three independent experiments. H. Western blot analysis with a <t>pan-UGT2B</t> antibody indicates that UGT2B levels are unchanged in FRII relative to FaDu cells suggesting the glucuronidation effects are mediated mostly through the UGT1A family. Tubulin provides a loading control.
Mab Mouse Anti Hsp 90α β F 8, supplied by Santa Cruz Biotechnology, 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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pab rabbit anti ugt1a  (Cell Signaling Technology Inc)
94
Cell Signaling Technology Inc pab rabbit anti ugt1a
Effects of modulation of Gli1 levels on UGT1A A. Effects of the direct Gli1 inhibitor GANT-61 on restoring ribavirin sensitivity (20 uM) in FRII cells. Effects are dependent on GANT-61 dose. B–D. Controls for eIF4E-ribavirin immunoprecipitations (IP) shown in and . Inputs, supernatants (Sn) and IP controls for 3 H ribavirin anti-eIF4E IPs are shown for GDC-0449 treated cells ( B ), FRII and FRI cells ( C ), and RNAi mediated knockdown of Gli1 ( D ). E–G. qPCR analysis of Gli1 ( E ) and UGT1A ( F ) using a pan-UGT1A primer or primers for specific UGT1As ( G ). mRNA levels were normalized to RNA Polymerase IIa. These findings are consistent with which indicates lower levels of UGT1A mRNA levels. Further, UGT1A3 and UGT1A8 decreased similarly (data not shown). Experiments were carried out in triplicate, at least three independent times. Average values are reported and error bars indicate standard deviations. These findings, that Gli1 elevation leads to reduce mRNA levels but increased protein levels are counter-intuitive. We hypothesize that Gli1 elevation increases protein stability of UGT1As (see below) and this leads to some sort of feedback mechanism leading to reduced UGT1As. Other scenarios are possible but the main point that Gli1 elevation leads to increased UGT1A protein production is clear. G. Gli1 increases UGT1A protein stability as shown by studies with the proteasomal inhibitor MG132 and a pan-UGT1A antibody. Here, MG132 addition stabilizes levels of UGT1A in parental cells, but in FRII cells where levels are already increased, there is no further increase with MG132. This indicates that UGT1A proteins are already stabilized in the FRII cells. All results are representative of three independent experiments. H. Western blot analysis with a <t>pan-UGT2B</t> antibody indicates that UGT2B levels are unchanged in FRII relative to FaDu cells suggesting the glucuronidation effects are mediated mostly through the UGT1A family. Tubulin provides a loading control.
Pab Rabbit Anti Ugt1a, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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mab rabbit anti snail c15d3  (Cell Signaling Technology Inc)
93
Cell Signaling Technology Inc mab rabbit anti snail c15d3
Effects of modulation of Gli1 levels on UGT1A A. Effects of the direct Gli1 inhibitor GANT-61 on restoring ribavirin sensitivity (20 uM) in FRII cells. Effects are dependent on GANT-61 dose. B–D. Controls for eIF4E-ribavirin immunoprecipitations (IP) shown in and . Inputs, supernatants (Sn) and IP controls for 3 H ribavirin anti-eIF4E IPs are shown for GDC-0449 treated cells ( B ), FRII and FRI cells ( C ), and RNAi mediated knockdown of Gli1 ( D ). E–G. qPCR analysis of Gli1 ( E ) and UGT1A ( F ) using a pan-UGT1A primer or primers for specific UGT1As ( G ). mRNA levels were normalized to RNA Polymerase IIa. These findings are consistent with which indicates lower levels of UGT1A mRNA levels. Further, UGT1A3 and UGT1A8 decreased similarly (data not shown). Experiments were carried out in triplicate, at least three independent times. Average values are reported and error bars indicate standard deviations. These findings, that Gli1 elevation leads to reduce mRNA levels but increased protein levels are counter-intuitive. We hypothesize that Gli1 elevation increases protein stability of UGT1As (see below) and this leads to some sort of feedback mechanism leading to reduced UGT1As. Other scenarios are possible but the main point that Gli1 elevation leads to increased UGT1A protein production is clear. G. Gli1 increases UGT1A protein stability as shown by studies with the proteasomal inhibitor MG132 and a pan-UGT1A antibody. Here, MG132 addition stabilizes levels of UGT1A in parental cells, but in FRII cells where levels are already increased, there is no further increase with MG132. This indicates that UGT1A proteins are already stabilized in the FRII cells. All results are representative of three independent experiments. H. Western blot analysis with a <t>pan-UGT2B</t> antibody indicates that UGT2B levels are unchanged in FRII relative to FaDu cells suggesting the glucuronidation effects are mediated mostly through the UGT1A family. Tubulin provides a loading control.
Mab Rabbit Anti Snail C15d3, supplied by Cell Signaling Technology Inc, 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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mab rabbit anti gli1 c68h3  (Cell Signaling Technology Inc)
95
Cell Signaling Technology Inc mab rabbit anti gli1 c68h3
Effects of modulation of Gli1 levels on UGT1A A. Effects of the direct Gli1 inhibitor GANT-61 on restoring ribavirin sensitivity (20 uM) in FRII cells. Effects are dependent on GANT-61 dose. B–D. Controls for eIF4E-ribavirin immunoprecipitations (IP) shown in and . Inputs, supernatants (Sn) and IP controls for 3 H ribavirin anti-eIF4E IPs are shown for GDC-0449 treated cells ( B ), FRII and FRI cells ( C ), and RNAi mediated knockdown of Gli1 ( D ). E–G. qPCR analysis of Gli1 ( E ) and UGT1A ( F ) using a pan-UGT1A primer or primers for specific UGT1As ( G ). mRNA levels were normalized to RNA Polymerase IIa. These findings are consistent with which indicates lower levels of UGT1A mRNA levels. Further, UGT1A3 and UGT1A8 decreased similarly (data not shown). Experiments were carried out in triplicate, at least three independent times. Average values are reported and error bars indicate standard deviations. These findings, that Gli1 elevation leads to reduce mRNA levels but increased protein levels are counter-intuitive. We hypothesize that Gli1 elevation increases protein stability of UGT1As (see below) and this leads to some sort of feedback mechanism leading to reduced UGT1As. Other scenarios are possible but the main point that Gli1 elevation leads to increased UGT1A protein production is clear. G. Gli1 increases UGT1A protein stability as shown by studies with the proteasomal inhibitor MG132 and a pan-UGT1A antibody. Here, MG132 addition stabilizes levels of UGT1A in parental cells, but in FRII cells where levels are already increased, there is no further increase with MG132. This indicates that UGT1A proteins are already stabilized in the FRII cells. All results are representative of three independent experiments. H. Western blot analysis with a <t>pan-UGT2B</t> antibody indicates that UGT2B levels are unchanged in FRII relative to FaDu cells suggesting the glucuronidation effects are mediated mostly through the UGT1A family. Tubulin provides a loading control.
Mab Rabbit Anti Gli1 C68h3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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mab mouse anti eif4g a 10  (Santa Cruz Biotechnology)
95
Santa Cruz Biotechnology mab mouse anti eif4g a 10
Effects of modulation of Gli1 levels on UGT1A A. Effects of the direct Gli1 inhibitor GANT-61 on restoring ribavirin sensitivity (20 uM) in FRII cells. Effects are dependent on GANT-61 dose. B–D. Controls for eIF4E-ribavirin immunoprecipitations (IP) shown in and . Inputs, supernatants (Sn) and IP controls for 3 H ribavirin anti-eIF4E IPs are shown for GDC-0449 treated cells ( B ), FRII and FRI cells ( C ), and RNAi mediated knockdown of Gli1 ( D ). E–G. qPCR analysis of Gli1 ( E ) and UGT1A ( F ) using a pan-UGT1A primer or primers for specific UGT1As ( G ). mRNA levels were normalized to RNA Polymerase IIa. These findings are consistent with which indicates lower levels of UGT1A mRNA levels. Further, UGT1A3 and UGT1A8 decreased similarly (data not shown). Experiments were carried out in triplicate, at least three independent times. Average values are reported and error bars indicate standard deviations. These findings, that Gli1 elevation leads to reduce mRNA levels but increased protein levels are counter-intuitive. We hypothesize that Gli1 elevation increases protein stability of UGT1As (see below) and this leads to some sort of feedback mechanism leading to reduced UGT1As. Other scenarios are possible but the main point that Gli1 elevation leads to increased UGT1A protein production is clear. G. Gli1 increases UGT1A protein stability as shown by studies with the proteasomal inhibitor MG132 and a pan-UGT1A antibody. Here, MG132 addition stabilizes levels of UGT1A in parental cells, but in FRII cells where levels are already increased, there is no further increase with MG132. This indicates that UGT1A proteins are already stabilized in the FRII cells. All results are representative of three independent experiments. H. Western blot analysis with a <t>pan-UGT2B</t> antibody indicates that UGT2B levels are unchanged in FRII relative to FaDu cells suggesting the glucuronidation effects are mediated mostly through the UGT1A family. Tubulin provides a loading control.
Mab Mouse Anti Eif4g A 10, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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mab rabbit anti 4e bp1 53h11  (Cell Signaling Technology Inc)
96
Cell Signaling Technology Inc mab rabbit anti 4e bp1 53h11
Effects of modulation of Gli1 levels on UGT1A A. Effects of the direct Gli1 inhibitor GANT-61 on restoring ribavirin sensitivity (20 uM) in FRII cells. Effects are dependent on GANT-61 dose. B–D. Controls for eIF4E-ribavirin immunoprecipitations (IP) shown in and . Inputs, supernatants (Sn) and IP controls for 3 H ribavirin anti-eIF4E IPs are shown for GDC-0449 treated cells ( B ), FRII and FRI cells ( C ), and RNAi mediated knockdown of Gli1 ( D ). E–G. qPCR analysis of Gli1 ( E ) and UGT1A ( F ) using a pan-UGT1A primer or primers for specific UGT1As ( G ). mRNA levels were normalized to RNA Polymerase IIa. These findings are consistent with which indicates lower levels of UGT1A mRNA levels. Further, UGT1A3 and UGT1A8 decreased similarly (data not shown). Experiments were carried out in triplicate, at least three independent times. Average values are reported and error bars indicate standard deviations. These findings, that Gli1 elevation leads to reduce mRNA levels but increased protein levels are counter-intuitive. We hypothesize that Gli1 elevation increases protein stability of UGT1As (see below) and this leads to some sort of feedback mechanism leading to reduced UGT1As. Other scenarios are possible but the main point that Gli1 elevation leads to increased UGT1A protein production is clear. G. Gli1 increases UGT1A protein stability as shown by studies with the proteasomal inhibitor MG132 and a pan-UGT1A antibody. Here, MG132 addition stabilizes levels of UGT1A in parental cells, but in FRII cells where levels are already increased, there is no further increase with MG132. This indicates that UGT1A proteins are already stabilized in the FRII cells. All results are representative of three independent experiments. H. Western blot analysis with a <t>pan-UGT2B</t> antibody indicates that UGT2B levels are unchanged in FRII relative to FaDu cells suggesting the glucuronidation effects are mediated mostly through the UGT1A family. Tubulin provides a loading control.
Mab Rabbit Anti 4e Bp1 53h11, supplied by Cell Signaling Technology Inc, 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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mab mouse anti c myc 9e10  (Santa Cruz Biotechnology)
96
Santa Cruz Biotechnology mab mouse anti c myc 9e10
Effects of modulation of Gli1 levels on UGT1A A. Effects of the direct Gli1 inhibitor GANT-61 on restoring ribavirin sensitivity (20 uM) in FRII cells. Effects are dependent on GANT-61 dose. B–D. Controls for eIF4E-ribavirin immunoprecipitations (IP) shown in and . Inputs, supernatants (Sn) and IP controls for 3 H ribavirin anti-eIF4E IPs are shown for GDC-0449 treated cells ( B ), FRII and FRI cells ( C ), and RNAi mediated knockdown of Gli1 ( D ). E–G. qPCR analysis of Gli1 ( E ) and UGT1A ( F ) using a pan-UGT1A primer or primers for specific UGT1As ( G ). mRNA levels were normalized to RNA Polymerase IIa. These findings are consistent with which indicates lower levels of UGT1A mRNA levels. Further, UGT1A3 and UGT1A8 decreased similarly (data not shown). Experiments were carried out in triplicate, at least three independent times. Average values are reported and error bars indicate standard deviations. These findings, that Gli1 elevation leads to reduce mRNA levels but increased protein levels are counter-intuitive. We hypothesize that Gli1 elevation increases protein stability of UGT1As (see below) and this leads to some sort of feedback mechanism leading to reduced UGT1As. Other scenarios are possible but the main point that Gli1 elevation leads to increased UGT1A protein production is clear. G. Gli1 increases UGT1A protein stability as shown by studies with the proteasomal inhibitor MG132 and a pan-UGT1A antibody. Here, MG132 addition stabilizes levels of UGT1A in parental cells, but in FRII cells where levels are already increased, there is no further increase with MG132. This indicates that UGT1A proteins are already stabilized in the FRII cells. All results are representative of three independent experiments. H. Western blot analysis with a <t>pan-UGT2B</t> antibody indicates that UGT2B levels are unchanged in FRII relative to FaDu cells suggesting the glucuronidation effects are mediated mostly through the UGT1A family. Tubulin provides a loading control.
Mab Mouse Anti C Myc 9e10, supplied by Santa Cruz Biotechnology, 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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Effects of modulation of Gli1 levels on UGT1A A. Effects of the direct Gli1 inhibitor GANT-61 on restoring ribavirin sensitivity (20 uM) in FRII cells. Effects are dependent on GANT-61 dose. B–D. Controls for eIF4E-ribavirin immunoprecipitations (IP) shown in and . Inputs, supernatants (Sn) and IP controls for 3 H ribavirin anti-eIF4E IPs are shown for GDC-0449 treated cells ( B ), FRII and FRI cells ( C ), and RNAi mediated knockdown of Gli1 ( D ). E–G. qPCR analysis of Gli1 ( E ) and UGT1A ( F ) using a pan-UGT1A primer or primers for specific UGT1As ( G ). mRNA levels were normalized to RNA Polymerase IIa. These findings are consistent with which indicates lower levels of UGT1A mRNA levels. Further, UGT1A3 and UGT1A8 decreased similarly (data not shown). Experiments were carried out in triplicate, at least three independent times. Average values are reported and error bars indicate standard deviations. These findings, that Gli1 elevation leads to reduce mRNA levels but increased protein levels are counter-intuitive. We hypothesize that Gli1 elevation increases protein stability of UGT1As (see below) and this leads to some sort of feedback mechanism leading to reduced UGT1As. Other scenarios are possible but the main point that Gli1 elevation leads to increased UGT1A protein production is clear. G. Gli1 increases UGT1A protein stability as shown by studies with the proteasomal inhibitor MG132 and a pan-UGT1A antibody. Here, MG132 addition stabilizes levels of UGT1A in parental cells, but in FRII cells where levels are already increased, there is no further increase with MG132. This indicates that UGT1A proteins are already stabilized in the FRII cells. All results are representative of three independent experiments. H. Western blot analysis with a pan-UGT2B antibody indicates that UGT2B levels are unchanged in FRII relative to FaDu cells suggesting the glucuronidation effects are mediated mostly through the UGT1A family. Tubulin provides a loading control.

Journal: Nature

Article Title: The sonic hedgehog factor Gli1 imparts drug resistance through inducible glucuronidation

doi: 10.1038/nature13283

Figure Lengend Snippet: Effects of modulation of Gli1 levels on UGT1A A. Effects of the direct Gli1 inhibitor GANT-61 on restoring ribavirin sensitivity (20 uM) in FRII cells. Effects are dependent on GANT-61 dose. B–D. Controls for eIF4E-ribavirin immunoprecipitations (IP) shown in and . Inputs, supernatants (Sn) and IP controls for 3 H ribavirin anti-eIF4E IPs are shown for GDC-0449 treated cells ( B ), FRII and FRI cells ( C ), and RNAi mediated knockdown of Gli1 ( D ). E–G. qPCR analysis of Gli1 ( E ) and UGT1A ( F ) using a pan-UGT1A primer or primers for specific UGT1As ( G ). mRNA levels were normalized to RNA Polymerase IIa. These findings are consistent with which indicates lower levels of UGT1A mRNA levels. Further, UGT1A3 and UGT1A8 decreased similarly (data not shown). Experiments were carried out in triplicate, at least three independent times. Average values are reported and error bars indicate standard deviations. These findings, that Gli1 elevation leads to reduce mRNA levels but increased protein levels are counter-intuitive. We hypothesize that Gli1 elevation increases protein stability of UGT1As (see below) and this leads to some sort of feedback mechanism leading to reduced UGT1As. Other scenarios are possible but the main point that Gli1 elevation leads to increased UGT1A protein production is clear. G. Gli1 increases UGT1A protein stability as shown by studies with the proteasomal inhibitor MG132 and a pan-UGT1A antibody. Here, MG132 addition stabilizes levels of UGT1A in parental cells, but in FRII cells where levels are already increased, there is no further increase with MG132. This indicates that UGT1A proteins are already stabilized in the FRII cells. All results are representative of three independent experiments. H. Western blot analysis with a pan-UGT2B antibody indicates that UGT2B levels are unchanged in FRII relative to FaDu cells suggesting the glucuronidation effects are mediated mostly through the UGT1A family. Tubulin provides a loading control.

Article Snippet: Antibodies for immunoblotting were as follows: mAb mouse anti-eIF4E (BD PharMingen, 610270), pAb rabbit anti-eIF4E (Sigma Aldrich, E5906), mAb mouse anti-β-Actin (Sigma Aldrich, A5441), mAb mouse anti-α-Tubulin (Sigma Aldrich, T5168), pAb goat anti-ADK (D-21) (Santa Cruz, sc-23360), pAb goat anti-ENT1 (N-12) (Santa Cruz, sc-45489), pAb rabbit anti-Mcl-I (S-19) (Santa Cruz, sc-819), mAb mouse anti-c-myc (9E10) (Santa Cruz, sc-40), mAb mouse anti-HSP 90α/β (F-8) (Santa Cruz, sc-13119), mAb mouse anti-eIF4G (A-10) (Santa Cruz, sc-133155), mAb rabbit anti-Gli1 (C68H3) (Cell Signaling, 3538), pAb rabbit anti-UGT1A (Cell Signaling, 4371S), mAb rabbit anti-Snail (C15D3) (Cell Signaling, 2522S), mAb rabbit anti-4E-BP1 (53H11) (Cell Signaling, 9644), mAb rabbit anti-IHH (Indian hedgehog; EP1192Y) (Abcam, ab52919), mAb rabbit anti-SHH (sonic hedgehog; C9C5) (Cell Signaling, 2207S), pAb anti-PTCH1 (H-267) (Santa Cruz, sc-9016), mAb mouse anti-Smo (Smoothened; E-5) (Santa Cruz, sc-166685), UGT2B pan antibody (Santa Cruz, sc-50386).

Techniques: Knockdown, Western Blot, Control