mouse anti xod Search Results


mouse anti xod  (Santa Cruz Biotechnology)
94
Santa Cruz Biotechnology mouse anti xod
Mouse Anti Xod, 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
https://www.bioz.com/result/mouse anti xod/product/Santa Cruz Biotechnology
Average 94 stars, based on 1 article reviews
mouse anti xod - by Bioz Stars, 2026-03
94/100 stars
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antibodies against xod  (Santa Cruz Biotechnology)
94
Santa Cruz Biotechnology antibodies against xod
Figure 1 Transcriptional regulation of the mouse <t>XOD</t> gene <t>by</t> <t>PPARα.</t> (A) Closed boxes indicate the sites that match the consensus PPAR response element (PPRE) in the mouse XOD gene. The numbers of nucleotide residues indicate the distance from the transcription start site. (B) Hepa1-6 cells were treated with 30 µM bezafibrate for 4 h in the presence or absence of GW6471. In plots of intensity, the mean value of vehicle-treated cells (control) was set at 1.0. Each value represents the mean with S.D. (N = 3). *P < 0.05 significant difference between the groups (F4,10 = 10.404, P = 0.007; ANOVA with the Tukey-Kramer post hoc test). (C) Hepa1-6 cells were transfected with XOD reporter constructs (XOD (-1848)::Luc) in the absence or presence of expression plasmids encoding CLOCK, BMAL1, RORα, ATF4, PPARα, and RXRα. Luciferase activity was measured 24 hours after transfection. In plots of intensity, the mean value of the control (pcDNA3.1) was set at 1.0. Each value represents the mean with S.D. (N = 3). *P < 0.05 significant difference from the control group (F4,10 = 64.715, P < 0.001; ANOVA with the Dunnett’s post hoc test). (D) Hepa1-6 cells were transfected with luciferase reporter constructs containing various lengths of the 5’-flanking region of the XOD gene in the absence or presence of expression plasmids encoding PPARα and RXRα. In plots of intensity, the mean value of the control (pcDNA3.1) was set at 1.0. Each value represents the mean with S.D. (N = 3). **P<0.001 significant difference from the control group (F5,12 = 113.652, P < 0.001; ANOVA with the Tukey-Kramer post hoc test).
Antibodies Against Xod, 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
https://www.bioz.com/result/antibodies against xod/product/Santa Cruz Biotechnology
Average 94 stars, based on 1 article reviews
antibodies against xod - by Bioz Stars, 2026-03
94/100 stars
  Buy from Supplier
rabbit anti mouse xod  (Santa Cruz Biotechnology)
96
Santa Cruz Biotechnology rabbit anti mouse xod
Figure 1 Transcriptional regulation of the mouse <t>XOD</t> gene <t>by</t> <t>PPARα.</t> (A) Closed boxes indicate the sites that match the consensus PPAR response element (PPRE) in the mouse XOD gene. The numbers of nucleotide residues indicate the distance from the transcription start site. (B) Hepa1-6 cells were treated with 30 µM bezafibrate for 4 h in the presence or absence of GW6471. In plots of intensity, the mean value of vehicle-treated cells (control) was set at 1.0. Each value represents the mean with S.D. (N = 3). *P < 0.05 significant difference between the groups (F4,10 = 10.404, P = 0.007; ANOVA with the Tukey-Kramer post hoc test). (C) Hepa1-6 cells were transfected with XOD reporter constructs (XOD (-1848)::Luc) in the absence or presence of expression plasmids encoding CLOCK, BMAL1, RORα, ATF4, PPARα, and RXRα. Luciferase activity was measured 24 hours after transfection. In plots of intensity, the mean value of the control (pcDNA3.1) was set at 1.0. Each value represents the mean with S.D. (N = 3). *P < 0.05 significant difference from the control group (F4,10 = 64.715, P < 0.001; ANOVA with the Dunnett’s post hoc test). (D) Hepa1-6 cells were transfected with luciferase reporter constructs containing various lengths of the 5’-flanking region of the XOD gene in the absence or presence of expression plasmids encoding PPARα and RXRα. In plots of intensity, the mean value of the control (pcDNA3.1) was set at 1.0. Each value represents the mean with S.D. (N = 3). **P<0.001 significant difference from the control group (F5,12 = 113.652, P < 0.001; ANOVA with the Tukey-Kramer post hoc test).
Rabbit Anti Mouse Xod, 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
https://www.bioz.com/result/rabbit anti mouse xod/product/Santa Cruz Biotechnology
Average 96 stars, based on 1 article reviews
rabbit anti mouse xod - by Bioz Stars, 2026-03
96/100 stars
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exod1 antibody n terminal region arp52508 p050  (Aviva Systems)
N/A
This is a rabbit polyclonal antibody against EXOD1 It was validated on Western Blot by Aviva Systems Biology At Aviva Systems Biology we manufacture rabbit polyclonal antibodies on a large scale 200 1000 products month
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rabbit anti mouse exodus 2  (Bio-Rad)
N/A
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exod1 antibody  (biorbyt)
N/A
Rabbit polyclonal antibody to EXOD1 Isotype Note IgG Host Note Rabbit Conjugation Note Unconjugated Reactivity Note Human Mouse Rat Guinea Pig Application Note WB IHC P P ELISA
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exod1 antibody fitc  (biorbyt)
N/A
Rabbit polyclonal antibody against EXOD1 conjugated to FITC Isotype Note IgG Host Note Rabbit Conjugation Note FITC Reactivity Note Human Mouse Rat Guinea Pig Application Note IF ICC
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exod1 antibody  (ProSci Incorporated)
N/A
EXOD1 Antibody raised in Rabbit validated in E WB in Human Mouse
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Image Search Results


Figure 1 Transcriptional regulation of the mouse XOD gene by PPARα. (A) Closed boxes indicate the sites that match the consensus PPAR response element (PPRE) in the mouse XOD gene. The numbers of nucleotide residues indicate the distance from the transcription start site. (B) Hepa1-6 cells were treated with 30 µM bezafibrate for 4 h in the presence or absence of GW6471. In plots of intensity, the mean value of vehicle-treated cells (control) was set at 1.0. Each value represents the mean with S.D. (N = 3). *P < 0.05 significant difference between the groups (F4,10 = 10.404, P = 0.007; ANOVA with the Tukey-Kramer post hoc test). (C) Hepa1-6 cells were transfected with XOD reporter constructs (XOD (-1848)::Luc) in the absence or presence of expression plasmids encoding CLOCK, BMAL1, RORα, ATF4, PPARα, and RXRα. Luciferase activity was measured 24 hours after transfection. In plots of intensity, the mean value of the control (pcDNA3.1) was set at 1.0. Each value represents the mean with S.D. (N = 3). *P < 0.05 significant difference from the control group (F4,10 = 64.715, P < 0.001; ANOVA with the Dunnett’s post hoc test). (D) Hepa1-6 cells were transfected with luciferase reporter constructs containing various lengths of the 5’-flanking region of the XOD gene in the absence or presence of expression plasmids encoding PPARα and RXRα. In plots of intensity, the mean value of the control (pcDNA3.1) was set at 1.0. Each value represents the mean with S.D. (N = 3). **P<0.001 significant difference from the control group (F5,12 = 113.652, P < 0.001; ANOVA with the Tukey-Kramer post hoc test).

Journal: Journal of Biological Chemistry

Article Title: Periodic variation in bile acids controls circadian changes in uric acid via regulation of xanthine oxidase by the orphan nuclear receptor PPARα

doi: 10.1074/jbc.m117.791285

Figure Lengend Snippet: Figure 1 Transcriptional regulation of the mouse XOD gene by PPARα. (A) Closed boxes indicate the sites that match the consensus PPAR response element (PPRE) in the mouse XOD gene. The numbers of nucleotide residues indicate the distance from the transcription start site. (B) Hepa1-6 cells were treated with 30 µM bezafibrate for 4 h in the presence or absence of GW6471. In plots of intensity, the mean value of vehicle-treated cells (control) was set at 1.0. Each value represents the mean with S.D. (N = 3). *P < 0.05 significant difference between the groups (F4,10 = 10.404, P = 0.007; ANOVA with the Tukey-Kramer post hoc test). (C) Hepa1-6 cells were transfected with XOD reporter constructs (XOD (-1848)::Luc) in the absence or presence of expression plasmids encoding CLOCK, BMAL1, RORα, ATF4, PPARα, and RXRα. Luciferase activity was measured 24 hours after transfection. In plots of intensity, the mean value of the control (pcDNA3.1) was set at 1.0. Each value represents the mean with S.D. (N = 3). *P < 0.05 significant difference from the control group (F4,10 = 64.715, P < 0.001; ANOVA with the Dunnett’s post hoc test). (D) Hepa1-6 cells were transfected with luciferase reporter constructs containing various lengths of the 5’-flanking region of the XOD gene in the absence or presence of expression plasmids encoding PPARα and RXRα. In plots of intensity, the mean value of the control (pcDNA3.1) was set at 1.0. Each value represents the mean with S.D. (N = 3). **P<0.001 significant difference from the control group (F5,12 = 113.652, P < 0.001; ANOVA with the Tukey-Kramer post hoc test).

Article Snippet: The membranes were reacted with antibodies against XOD (sc-20991; Santa Cruz Biotechnology, Santa Cruz, CA), PPARα (sc-9000; Santa Cruz Biotechnology), RXRα (sc-553, Santa Cruz Biotechnology), p300 (sc-584, Santa Cruz Biotechnology), β-ACTIN (sc-1616; Santa Cruz Biotechnology), or TATA-binding protein TBP (1:1000; ab51841; Abcam).

Techniques: Control, Transfection, Construct, Expressing, Luciferase, Activity Assay

Figure 2 Disrupted rhythms in the expression of XOD and its enzymatic activity in livers of PPARα-null mice. (A) Temporal expression profiles of XOD mRNA in the livers of wild-type and PPARα-null mice. Each value represents the mean with S.D. (N = 3-6). There was a significant time-dependent variation in mRNA levels in wild-type mice (F5,30=3.743, P < 0.001; ANOVA). **P < 0.01, *P <0.05, significant difference from wild-type mice at the corresponding time points (F11,42 = 5.932, P < 0.001; ANOVA with the Tukey-Kramer post hoc test). (B) Temporal expression profiles of the XOD protein in the livers of wild-type and PPARα-null mice. The left panel shows representative immunoblots of the XOD protein in the livers of mice. Each value represents the mean with S.D. (N=3). There was a significant time-dependent variation in protein levels in wild-type mice (F5,18=3.934, P = 0.014; ANOVA). **P < 0.01, significant difference from wild-type mice at the corresponding time point (F11,35= 9.234, P < 0.001; ANOVA with the Tukey-Kramer post hoc test). (C) Temporal profiles of XOD activity in the livers of wild-type and PPARα-null mice. Each value represents the mean with S.D. (N =3-4). *P < 0.05, significant difference from wild-type mice at the corresponding time point (F11,29 = 3.006, P = 0.009; ANOVA with the Tukey-Kramer post hoc test). (D) Temporal profiles of uric acid contents in the livers of wild-type and PPARα-null mice. Each value represents the mean with S.D. (N=3). There was a significant time-dependent variation in the hepatic contents of uric acid in wild-type mice (F5,12 = 6.884, P = 0.003; ANOVA). **P < 0.01; *P < 0.05, significant difference from wild-type mice at the corresponding time point (F11,24 = 6.399, P < 0.001; ANOVA with the Tukey-Kramer post hoc test). (E) Temporal profiles of serum uric acid concentrations in wild-type and PPARα-null mice. Each value represents the mean with S.D. (N=3). There was a significant time-dependent variation in serum uric acid levels in wild-type mice (F5,12 = 3.748, P = 0.028; ANOVA). *P < 0.05, significant difference from wild-type mice at the corresponding time point (F11,24 = 5.562, P < 0.001; ANOVA with the Tukey-Kramer post hoc test).

Journal: Journal of Biological Chemistry

Article Title: Periodic variation in bile acids controls circadian changes in uric acid via regulation of xanthine oxidase by the orphan nuclear receptor PPARα

doi: 10.1074/jbc.m117.791285

Figure Lengend Snippet: Figure 2 Disrupted rhythms in the expression of XOD and its enzymatic activity in livers of PPARα-null mice. (A) Temporal expression profiles of XOD mRNA in the livers of wild-type and PPARα-null mice. Each value represents the mean with S.D. (N = 3-6). There was a significant time-dependent variation in mRNA levels in wild-type mice (F5,30=3.743, P < 0.001; ANOVA). **P < 0.01, *P <0.05, significant difference from wild-type mice at the corresponding time points (F11,42 = 5.932, P < 0.001; ANOVA with the Tukey-Kramer post hoc test). (B) Temporal expression profiles of the XOD protein in the livers of wild-type and PPARα-null mice. The left panel shows representative immunoblots of the XOD protein in the livers of mice. Each value represents the mean with S.D. (N=3). There was a significant time-dependent variation in protein levels in wild-type mice (F5,18=3.934, P = 0.014; ANOVA). **P < 0.01, significant difference from wild-type mice at the corresponding time point (F11,35= 9.234, P < 0.001; ANOVA with the Tukey-Kramer post hoc test). (C) Temporal profiles of XOD activity in the livers of wild-type and PPARα-null mice. Each value represents the mean with S.D. (N =3-4). *P < 0.05, significant difference from wild-type mice at the corresponding time point (F11,29 = 3.006, P = 0.009; ANOVA with the Tukey-Kramer post hoc test). (D) Temporal profiles of uric acid contents in the livers of wild-type and PPARα-null mice. Each value represents the mean with S.D. (N=3). There was a significant time-dependent variation in the hepatic contents of uric acid in wild-type mice (F5,12 = 6.884, P = 0.003; ANOVA). **P < 0.01; *P < 0.05, significant difference from wild-type mice at the corresponding time point (F11,24 = 6.399, P < 0.001; ANOVA with the Tukey-Kramer post hoc test). (E) Temporal profiles of serum uric acid concentrations in wild-type and PPARα-null mice. Each value represents the mean with S.D. (N=3). There was a significant time-dependent variation in serum uric acid levels in wild-type mice (F5,12 = 3.748, P = 0.028; ANOVA). *P < 0.05, significant difference from wild-type mice at the corresponding time point (F11,24 = 5.562, P < 0.001; ANOVA with the Tukey-Kramer post hoc test).

Article Snippet: The membranes were reacted with antibodies against XOD (sc-20991; Santa Cruz Biotechnology, Santa Cruz, CA), PPARα (sc-9000; Santa Cruz Biotechnology), RXRα (sc-553, Santa Cruz Biotechnology), p300 (sc-584, Santa Cruz Biotechnology), β-ACTIN (sc-1616; Santa Cruz Biotechnology), or TATA-binding protein TBP (1:1000; ab51841; Abcam).

Techniques: Expressing, Activity Assay, Western Blot

Figure 3 Repression of PPARα-mediated transactivation of the mouse XOD gene by bile acids. (A) Temporal expression profiles for PPARα, RXRα, and the p300 protein in the livers of wild-type mice. The left panel shows representative immunoblots of PPARα, RXRα, and the p300 protein in the livers of mice. Protein band intensity was normalized to TBP and converted to a ratio to maximal levels (set as 1.00). Each value represents the mean with S.D. (N=3). (B) Cross-linked chromatin was prepared from wild-type mice and subjected to PCR using primers surrounding the PPRE (from bp –174 to –163) in the 5’-flanking region of the mouse XOD gene. Solid arrows indicate the primer sets for the amplification area by PCR. In the right panel, the peak amounts of binding of PPARα, RXRα, and p300 were set at 100. Values shown are the mean ± S.D. (N = 4). There was a significant time-dependent variation in the amount of p300 binding (F5,12 = 10.916, P < 0.001; ANOVA). (C) Influence of cholic acid (CA) on the PPARα/RXRα-mediated expression of XOD mRNA in Hepa1-6 cells. Twenty-four hours after the co-transfection of PPARα and PXRα expression vectors, Hepa1-6 cells were treated with CA or GW6471 (applied as a positive control) for 4 hours. Each value represents the mean with S.D. (N = 4). **P<0.01, significant difference between the two groups (F5,23 = 20.252, P < 0.001; ANOVA with the Tukey-Kramer post hoc test). (D) Suppression effects of CA on the recruitment of p300 on the PPRE in the mouse XOD gene. Hepa1-6 cells were treated with 100 and 250 µM CA or vehicle for 4 hours. Cross-linked chromatin was subjected to PCR using primers surrounding the PPRE of the mouse XOD gene. Values shown are the mean ± S.D. (N = 4). **P<0.01, *P<0.05 significant decrease in the amount of p300 binding from that in the vehicle-treated group (F2,9 = 16.459, P < 0.001; ANOVA with the Tukey-Kramer post hoc test). (E) Suppressive effects of CA on the protein expression of XOD and its activity in Hepa1-6 cells. The upper panel shows representative immunoblots of the XOD protein in Hepa1-6 cells treated with 250 µM CA or vehicle. Data were confirmed in more than three experiments in each group. The lower panel shows XOD activity in Hepa1-6 cells treated with 250 µM CA or vehicle. Each value represents the mean with S.D. (N=6). *P < 0.05, significant difference between the two groups (t8 = 2.919, P = 0.015, unpaired t-test, two-sided). (F) Temporal profile of the accumulation of bile acids in the livers of wild-type mice. Each value represents the mean with S.D. (N = 4). There was a significant time-dependent variation in bile acid accumulation (F5,18= 3.519, P = 0.022; ANOVA).

Journal: Journal of Biological Chemistry

Article Title: Periodic variation in bile acids controls circadian changes in uric acid via regulation of xanthine oxidase by the orphan nuclear receptor PPARα

doi: 10.1074/jbc.m117.791285

Figure Lengend Snippet: Figure 3 Repression of PPARα-mediated transactivation of the mouse XOD gene by bile acids. (A) Temporal expression profiles for PPARα, RXRα, and the p300 protein in the livers of wild-type mice. The left panel shows representative immunoblots of PPARα, RXRα, and the p300 protein in the livers of mice. Protein band intensity was normalized to TBP and converted to a ratio to maximal levels (set as 1.00). Each value represents the mean with S.D. (N=3). (B) Cross-linked chromatin was prepared from wild-type mice and subjected to PCR using primers surrounding the PPRE (from bp –174 to –163) in the 5’-flanking region of the mouse XOD gene. Solid arrows indicate the primer sets for the amplification area by PCR. In the right panel, the peak amounts of binding of PPARα, RXRα, and p300 were set at 100. Values shown are the mean ± S.D. (N = 4). There was a significant time-dependent variation in the amount of p300 binding (F5,12 = 10.916, P < 0.001; ANOVA). (C) Influence of cholic acid (CA) on the PPARα/RXRα-mediated expression of XOD mRNA in Hepa1-6 cells. Twenty-four hours after the co-transfection of PPARα and PXRα expression vectors, Hepa1-6 cells were treated with CA or GW6471 (applied as a positive control) for 4 hours. Each value represents the mean with S.D. (N = 4). **P<0.01, significant difference between the two groups (F5,23 = 20.252, P < 0.001; ANOVA with the Tukey-Kramer post hoc test). (D) Suppression effects of CA on the recruitment of p300 on the PPRE in the mouse XOD gene. Hepa1-6 cells were treated with 100 and 250 µM CA or vehicle for 4 hours. Cross-linked chromatin was subjected to PCR using primers surrounding the PPRE of the mouse XOD gene. Values shown are the mean ± S.D. (N = 4). **P<0.01, *P<0.05 significant decrease in the amount of p300 binding from that in the vehicle-treated group (F2,9 = 16.459, P < 0.001; ANOVA with the Tukey-Kramer post hoc test). (E) Suppressive effects of CA on the protein expression of XOD and its activity in Hepa1-6 cells. The upper panel shows representative immunoblots of the XOD protein in Hepa1-6 cells treated with 250 µM CA or vehicle. Data were confirmed in more than three experiments in each group. The lower panel shows XOD activity in Hepa1-6 cells treated with 250 µM CA or vehicle. Each value represents the mean with S.D. (N=6). *P < 0.05, significant difference between the two groups (t8 = 2.919, P = 0.015, unpaired t-test, two-sided). (F) Temporal profile of the accumulation of bile acids in the livers of wild-type mice. Each value represents the mean with S.D. (N = 4). There was a significant time-dependent variation in bile acid accumulation (F5,18= 3.519, P = 0.022; ANOVA).

Article Snippet: The membranes were reacted with antibodies against XOD (sc-20991; Santa Cruz Biotechnology, Santa Cruz, CA), PPARα (sc-9000; Santa Cruz Biotechnology), RXRα (sc-553, Santa Cruz Biotechnology), p300 (sc-584, Santa Cruz Biotechnology), β-ACTIN (sc-1616; Santa Cruz Biotechnology), or TATA-binding protein TBP (1:1000; ab51841; Abcam).

Techniques: Expressing, Western Blot, Amplification, Binding Assay, Cotransfection, Positive Control, Activity Assay