human mcl 1l isoform Search Results


tl100 image analysis software  (TotalLab Ltd)
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d4004 1 l qubit 13 dsdna hs assay thermo fisher q33230 bioanalyzer high sensitivity dna kit agilent  (Thermo Fisher)
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bovine serum albumin  (Santa Cruz Biotechnology)
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tbs t  (Santa Cruz Biotechnology)
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mmol l 1 l glutamine  (GE Healthcare)
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saline tween tbs t  (Santa Cruz Biotechnology)
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antibody against fxr  (Santa Cruz Biotechnology)
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Santa Cruz Biotechnology antibody against fxr
Fig. <t>7.</t> <t>FXR/RXR</t> heterodimer binds to the IR1 element of human ALAS1. Electromobility shift assays were performed using the radiolabeled probes of human ALAS1 (huA IR1) [lanes 1-14 in (A) and lanes 1-3 in (B)] or a perfect IR1 (per IR1) (lanes 15-16). The sequences of the wild-type and mutated probes are listed in Table 1. (A) FXR/RXR heterodimer binds to huA IR1 with high affinity (lane 4). The protein DNA complex disappears with increasing doses of competing wild-type unlabeled probe (lanes 5-8) or unlabeled perfect IR1 (lane 10-13), but not with mutated huA IR1 (lane 9). An antibody against human FXR blocks the formation of an FXR/RXR DNA complex at huA IR1 and at per IR1 [lanes 14 and 16 in (A) and lane 3 in (B)]. The FXR/RXR complex is successfully supershifted by an antibody against RXR [lane 2 in (B)].
Antibody Against Fxr, supplied by Santa Cruz Biotechnology, 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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pcmv6 lgals1 myc ddk origene cat  (OriGene)
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OriGene pcmv6 lgals1 myc ddk origene cat
Fig. <t>7.</t> <t>FXR/RXR</t> heterodimer binds to the IR1 element of human ALAS1. Electromobility shift assays were performed using the radiolabeled probes of human ALAS1 (huA IR1) [lanes 1-14 in (A) and lanes 1-3 in (B)] or a perfect IR1 (per IR1) (lanes 15-16). The sequences of the wild-type and mutated probes are listed in Table 1. (A) FXR/RXR heterodimer binds to huA IR1 with high affinity (lane 4). The protein DNA complex disappears with increasing doses of competing wild-type unlabeled probe (lanes 5-8) or unlabeled perfect IR1 (lane 10-13), but not with mutated huA IR1 (lane 9). An antibody against human FXR blocks the formation of an FXR/RXR DNA complex at huA IR1 and at per IR1 [lanes 14 and 16 in (A) and lane 3 in (B)]. The FXR/RXR complex is successfully supershifted by an antibody against RXR [lane 2 in (B)].
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recombinant human interleukin-1l (il-1l)  (Genzyme)
90
Genzyme recombinant human interleukin-1l (il-1l)
Fig. <t>7.</t> <t>FXR/RXR</t> heterodimer binds to the IR1 element of human ALAS1. Electromobility shift assays were performed using the radiolabeled probes of human ALAS1 (huA IR1) [lanes 1-14 in (A) and lanes 1-3 in (B)] or a perfect IR1 (per IR1) (lanes 15-16). The sequences of the wild-type and mutated probes are listed in Table 1. (A) FXR/RXR heterodimer binds to huA IR1 with high affinity (lane 4). The protein DNA complex disappears with increasing doses of competing wild-type unlabeled probe (lanes 5-8) or unlabeled perfect IR1 (lane 10-13), but not with mutated huA IR1 (lane 9). An antibody against human FXR blocks the formation of an FXR/RXR DNA complex at huA IR1 and at per IR1 [lanes 14 and 16 in (A) and lane 3 in (B)]. The FXR/RXR complex is successfully supershifted by an antibody against RXR [lane 2 in (B)].
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goat f(ab )2 anti-human igg (fc specific  (Thermo Fisher)
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Thermo Fisher goat f(ab )2 anti-human igg (fc specific
Fig. <t>7.</t> <t>FXR/RXR</t> heterodimer binds to the IR1 element of human ALAS1. Electromobility shift assays were performed using the radiolabeled probes of human ALAS1 (huA IR1) [lanes 1-14 in (A) and lanes 1-3 in (B)] or a perfect IR1 (per IR1) (lanes 15-16). The sequences of the wild-type and mutated probes are listed in Table 1. (A) FXR/RXR heterodimer binds to huA IR1 with high affinity (lane 4). The protein DNA complex disappears with increasing doses of competing wild-type unlabeled probe (lanes 5-8) or unlabeled perfect IR1 (lane 10-13), but not with mutated huA IR1 (lane 9). An antibody against human FXR blocks the formation of an FXR/RXR DNA complex at huA IR1 and at per IR1 [lanes 14 and 16 in (A) and lane 3 in (B)]. The FXR/RXR complex is successfully supershifted by an antibody against RXR [lane 2 in (B)].
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phosphate buffered saline pbs  (Santa Cruz Biotechnology)
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Santa Cruz Biotechnology phosphate buffered saline pbs
Fig. <t>7.</t> <t>FXR/RXR</t> heterodimer binds to the IR1 element of human ALAS1. Electromobility shift assays were performed using the radiolabeled probes of human ALAS1 (huA IR1) [lanes 1-14 in (A) and lanes 1-3 in (B)] or a perfect IR1 (per IR1) (lanes 15-16). The sequences of the wild-type and mutated probes are listed in Table 1. (A) FXR/RXR heterodimer binds to huA IR1 with high affinity (lane 4). The protein DNA complex disappears with increasing doses of competing wild-type unlabeled probe (lanes 5-8) or unlabeled perfect IR1 (lane 10-13), but not with mutated huA IR1 (lane 9). An antibody against human FXR blocks the formation of an FXR/RXR DNA complex at huA IR1 and at per IR1 [lanes 14 and 16 in (A) and lane 3 in (B)]. The FXR/RXR complex is successfully supershifted by an antibody against RXR [lane 2 in (B)].
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rbc lysis buffer  (Thermo Fisher)
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Thermo Fisher rbc lysis buffer
Fig. <t>7.</t> <t>FXR/RXR</t> heterodimer binds to the IR1 element of human ALAS1. Electromobility shift assays were performed using the radiolabeled probes of human ALAS1 (huA IR1) [lanes 1-14 in (A) and lanes 1-3 in (B)] or a perfect IR1 (per IR1) (lanes 15-16). The sequences of the wild-type and mutated probes are listed in Table 1. (A) FXR/RXR heterodimer binds to huA IR1 with high affinity (lane 4). The protein DNA complex disappears with increasing doses of competing wild-type unlabeled probe (lanes 5-8) or unlabeled perfect IR1 (lane 10-13), but not with mutated huA IR1 (lane 9). An antibody against human FXR blocks the formation of an FXR/RXR DNA complex at huA IR1 and at per IR1 [lanes 14 and 16 in (A) and lane 3 in (B)]. The FXR/RXR complex is successfully supershifted by an antibody against RXR [lane 2 in (B)].
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Image Search Results


Fig. 7. FXR/RXR heterodimer binds to the IR1 element of human ALAS1. Electromobility shift assays were performed using the radiolabeled probes of human ALAS1 (huA IR1) [lanes 1-14 in (A) and lanes 1-3 in (B)] or a perfect IR1 (per IR1) (lanes 15-16). The sequences of the wild-type and mutated probes are listed in Table 1. (A) FXR/RXR heterodimer binds to huA IR1 with high affinity (lane 4). The protein DNA complex disappears with increasing doses of competing wild-type unlabeled probe (lanes 5-8) or unlabeled perfect IR1 (lane 10-13), but not with mutated huA IR1 (lane 9). An antibody against human FXR blocks the formation of an FXR/RXR DNA complex at huA IR1 and at per IR1 [lanes 14 and 16 in (A) and lane 3 in (B)]. The FXR/RXR complex is successfully supershifted by an antibody against RXR [lane 2 in (B)].

Journal: Hepatology (Baltimore, Md.)

Article Title: Regulation of human liver delta-aminolevulinic acid synthase by bile acids.

doi: 10.1002/hep.21879

Figure Lengend Snippet: Fig. 7. FXR/RXR heterodimer binds to the IR1 element of human ALAS1. Electromobility shift assays were performed using the radiolabeled probes of human ALAS1 (huA IR1) [lanes 1-14 in (A) and lanes 1-3 in (B)] or a perfect IR1 (per IR1) (lanes 15-16). The sequences of the wild-type and mutated probes are listed in Table 1. (A) FXR/RXR heterodimer binds to huA IR1 with high affinity (lane 4). The protein DNA complex disappears with increasing doses of competing wild-type unlabeled probe (lanes 5-8) or unlabeled perfect IR1 (lane 10-13), but not with mutated huA IR1 (lane 9). An antibody against human FXR blocks the formation of an FXR/RXR DNA complex at huA IR1 and at per IR1 [lanes 14 and 16 in (A) and lane 3 in (B)]. The FXR/RXR complex is successfully supershifted by an antibody against RXR [lane 2 in (B)].

Article Snippet: Electromobility shift assays were performed as previously described.22 For supershift experiments, 1 L of antibody against FXR (Santa Cruz Biotechnology; sc-13063) or 0.5 L of monoclonal anti-mouse–RXR rabbit antibody (kindly provided by P. Chambon, Institut de Génétique et de Biologie Moléculaire et Cellulaire, Université Louis Pasteur, Illkirch, France) was used.

Techniques: