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rabbit anti sult1a1 antibody  (Bioss)


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    Structured Review

    Bioss rabbit anti sult1a1 antibody
    Sequences of qRT-PCR primers.
    Rabbit Anti Sult1a1 Antibody, supplied by Bioss, used in various techniques. Bioz Stars score: 93/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti sult1a1 antibody/product/Bioss
    Average 93 stars, based on 4 article reviews
    rabbit anti sult1a1 antibody - by Bioz Stars, 2026-03
    93/100 stars

    Images

    1) Product Images from "Excess Folic Acid Supplementation before and during Pregnancy and Lactation Alters Behaviors and Brain Gene Expression in Female Mouse Offspring"

    Article Title: Excess Folic Acid Supplementation before and during Pregnancy and Lactation Alters Behaviors and Brain Gene Expression in Female Mouse Offspring

    Journal: Nutrients

    doi: 10.3390/nu14010066

    Sequences of qRT-PCR primers.
    Figure Legend Snippet: Sequences of qRT-PCR primers.

    Techniques Used: Sequencing, Amplification

    DEGs enriched in the GO category of cellular component were validated by qRT-PCR. The relative mRNA expression level of Tlr1 , Sult1a1 , Tph2 , Acacb , Ppara , Etnppl , Angptl4 and Apold1 genes in control and 2.5 × FA brains ( n = 3) were determined by qRT-PCR. The levels of ribosomal protein S18 (RPS18) mRNA were used for normalization. *, p < 0.05; **, p < 0.01; ***, p < 0.001.
    Figure Legend Snippet: DEGs enriched in the GO category of cellular component were validated by qRT-PCR. The relative mRNA expression level of Tlr1 , Sult1a1 , Tph2 , Acacb , Ppara , Etnppl , Angptl4 and Apold1 genes in control and 2.5 × FA brains ( n = 3) were determined by qRT-PCR. The levels of ribosomal protein S18 (RPS18) mRNA were used for normalization. *, p < 0.05; **, p < 0.01; ***, p < 0.001.

    Techniques Used: Quantitative RT-PCR, Expressing

    The protein levels of Sult1a1 were elevated in 2.5 × FA brains at P21d. ( A ) The brains of control and 2.5 × FA mice were lysed and analyzed by Western blots, comparing anti-Sult1a1 levels ( n = 6). GAPDH was used as a loading control. ( B ) The protein levels of Sult1a1 were calculated by normalizing to GAPDH. ***, p < 0.001.
    Figure Legend Snippet: The protein levels of Sult1a1 were elevated in 2.5 × FA brains at P21d. ( A ) The brains of control and 2.5 × FA mice were lysed and analyzed by Western blots, comparing anti-Sult1a1 levels ( n = 6). GAPDH was used as a loading control. ( B ) The protein levels of Sult1a1 were calculated by normalizing to GAPDH. ***, p < 0.001.

    Techniques Used: Western Blot



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    (A) ICC evaluation of SULT1A1, <t>1C2</t> and 4A1 expression in PBC, UW228-3 and LN-18 cells without (N) and with (R) resveratrol treatment. (B) Western blot analyses of SULT1A1, 1C2 and 4A1 expression in LN-18 cells without (N) and with (R) resveratrol treatment and compared with that in normal control PBCs and resveratrol-sensitive control medulloblastoma UW228-3 cells. β -actin was used as loading control and for calculation of SULT expression levels/densitometry scan of Western blotting results. *Compared with normal cultured LN-18 and UW228-3 cells, respectively; *represents statistical significance ( p <0.05).
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    Astrocytic SULT1A immunoreactivity in the EAE and control white matter spinal cord. Representative stainings for EAE mouse ( a–e ) or control mouse ( f – j and, for non-specific control, k – n ). a , f <t>SULT1A1</t> staining ( green channel ); k non-specific staining (no rabbit primary antibody, green channel ); b , g , l GFAP staining ( red channel ); c , h , m DAPI staining ( blue channel ); d , i , n all channels merged; e , j red and green channels merged. o Schematic representation of the spinal cord section with approximate field ( red square ) used for the pictures. Arrows point to astrocytic (GFAP+) cells (with identified nucleus) in ( e ) or to astrocytic GFAP+ fibers in ( j ). a – n Scale bar, 75 μm
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    Image Search Results


    Sequences of qRT-PCR primers.

    Journal: Nutrients

    Article Title: Excess Folic Acid Supplementation before and during Pregnancy and Lactation Alters Behaviors and Brain Gene Expression in Female Mouse Offspring

    doi: 10.3390/nu14010066

    Figure Lengend Snippet: Sequences of qRT-PCR primers.

    Article Snippet: The membrane was blocked with 5% skim milk in Tris-buffered saline (TBS, 150 mM NaCl, 50 mM Tris-HCl, pH 7.4) for 30 min and incubated with rabbit anti-Sult1a1 antibody (1:500, bs-6283R, Bioss Antibodies, Beijing, China) overnight at room temperature.

    Techniques: Sequencing, Amplification

    DEGs enriched in the GO category of cellular component were validated by qRT-PCR. The relative mRNA expression level of Tlr1 , Sult1a1 , Tph2 , Acacb , Ppara , Etnppl , Angptl4 and Apold1 genes in control and 2.5 × FA brains ( n = 3) were determined by qRT-PCR. The levels of ribosomal protein S18 (RPS18) mRNA were used for normalization. *, p < 0.05; **, p < 0.01; ***, p < 0.001.

    Journal: Nutrients

    Article Title: Excess Folic Acid Supplementation before and during Pregnancy and Lactation Alters Behaviors and Brain Gene Expression in Female Mouse Offspring

    doi: 10.3390/nu14010066

    Figure Lengend Snippet: DEGs enriched in the GO category of cellular component were validated by qRT-PCR. The relative mRNA expression level of Tlr1 , Sult1a1 , Tph2 , Acacb , Ppara , Etnppl , Angptl4 and Apold1 genes in control and 2.5 × FA brains ( n = 3) were determined by qRT-PCR. The levels of ribosomal protein S18 (RPS18) mRNA were used for normalization. *, p < 0.05; **, p < 0.01; ***, p < 0.001.

    Article Snippet: The membrane was blocked with 5% skim milk in Tris-buffered saline (TBS, 150 mM NaCl, 50 mM Tris-HCl, pH 7.4) for 30 min and incubated with rabbit anti-Sult1a1 antibody (1:500, bs-6283R, Bioss Antibodies, Beijing, China) overnight at room temperature.

    Techniques: Quantitative RT-PCR, Expressing

    The protein levels of Sult1a1 were elevated in 2.5 × FA brains at P21d. ( A ) The brains of control and 2.5 × FA mice were lysed and analyzed by Western blots, comparing anti-Sult1a1 levels ( n = 6). GAPDH was used as a loading control. ( B ) The protein levels of Sult1a1 were calculated by normalizing to GAPDH. ***, p < 0.001.

    Journal: Nutrients

    Article Title: Excess Folic Acid Supplementation before and during Pregnancy and Lactation Alters Behaviors and Brain Gene Expression in Female Mouse Offspring

    doi: 10.3390/nu14010066

    Figure Lengend Snippet: The protein levels of Sult1a1 were elevated in 2.5 × FA brains at P21d. ( A ) The brains of control and 2.5 × FA mice were lysed and analyzed by Western blots, comparing anti-Sult1a1 levels ( n = 6). GAPDH was used as a loading control. ( B ) The protein levels of Sult1a1 were calculated by normalizing to GAPDH. ***, p < 0.001.

    Article Snippet: The membrane was blocked with 5% skim milk in Tris-buffered saline (TBS, 150 mM NaCl, 50 mM Tris-HCl, pH 7.4) for 30 min and incubated with rabbit anti-Sult1a1 antibody (1:500, bs-6283R, Bioss Antibodies, Beijing, China) overnight at room temperature.

    Techniques: Western Blot

    (A) ICC evaluation of SULT1A1, 1C2 and 4A1 expression in PBC, UW228-3 and LN-18 cells without (N) and with (R) resveratrol treatment. (B) Western blot analyses of SULT1A1, 1C2 and 4A1 expression in LN-18 cells without (N) and with (R) resveratrol treatment and compared with that in normal control PBCs and resveratrol-sensitive control medulloblastoma UW228-3 cells. β -actin was used as loading control and for calculation of SULT expression levels/densitometry scan of Western blotting results. *Compared with normal cultured LN-18 and UW228-3 cells, respectively; *represents statistical significance ( p <0.05).

    Journal: PLoS ONE

    Article Title: Metabolic Patterns and Biotransformation Activities of Resveratrol in Human Glioblastoma Cells: Relevance with Therapeutic Efficacies

    doi: 10.1371/journal.pone.0027484

    Figure Lengend Snippet: (A) ICC evaluation of SULT1A1, 1C2 and 4A1 expression in PBC, UW228-3 and LN-18 cells without (N) and with (R) resveratrol treatment. (B) Western blot analyses of SULT1A1, 1C2 and 4A1 expression in LN-18 cells without (N) and with (R) resveratrol treatment and compared with that in normal control PBCs and resveratrol-sensitive control medulloblastoma UW228-3 cells. β -actin was used as loading control and for calculation of SULT expression levels/densitometry scan of Western blotting results. *Compared with normal cultured LN-18 and UW228-3 cells, respectively; *represents statistical significance ( p <0.05).

    Article Snippet: ICC staining and Western blot analysis were performed on the samples obtained from each of the experimental groups using the rabbit anti-human SULT1A1, 1C2 and 4A1 antibodies (ProteinTech Group, Inc., Chicago, USA) by the method described elsewhere – .

    Techniques: Expressing, Western Blot, Cell Culture

    Immunohistochemical illustration of differential expression patterns of SULT1A1, 1C2 and 4A1 in two cases of glioblastomas (GM). Medulloblastoma (MB) and its surrounding noncancerous cerebellum tissue (NC) were cited as controls.

    Journal: PLoS ONE

    Article Title: Metabolic Patterns and Biotransformation Activities of Resveratrol in Human Glioblastoma Cells: Relevance with Therapeutic Efficacies

    doi: 10.1371/journal.pone.0027484

    Figure Lengend Snippet: Immunohistochemical illustration of differential expression patterns of SULT1A1, 1C2 and 4A1 in two cases of glioblastomas (GM). Medulloblastoma (MB) and its surrounding noncancerous cerebellum tissue (NC) were cited as controls.

    Article Snippet: ICC staining and Western blot analysis were performed on the samples obtained from each of the experimental groups using the rabbit anti-human SULT1A1, 1C2 and 4A1 antibodies (ProteinTech Group, Inc., Chicago, USA) by the method described elsewhere – .

    Techniques: Immunohistochemical staining, Expressing

    (A) Immunofluorescence illustration of intracellular distribution of STAT3 in LN-18 and PBC cells without (N) and with (AG490) 60 µM AG490 treatment. Arrows indicate the cells shown in the insets in high magnification (X400). (B) Flow cytometry analysis revealed reduction of G1-phase cells, accumulation of S-phase cells and induction of apoptosis (blue peak) in AG490-treated LN-18 cell population. The cell cycle progression was almost unchanged in PBC cells. *, indicates the peak of apoptotic cells. (C) H&E morphologic examination of LN-18 cells under normal culture or incubated with 100 µM trans -resveratrol, 60 µM AG490 or resveratrol/AG490 mixture for 48 hours (Main images). Small images: immunocytochemical illustration of SULT1A1, 1C2 and 4A1 expression in LN-18 cells treated by 60 µM AG490 without/with 100 µM resveratrol supplementation. Normally cultured and 100 µM resveratrol-treated LN-18 cells were cited as controls.

    Journal: PLoS ONE

    Article Title: Metabolic Patterns and Biotransformation Activities of Resveratrol in Human Glioblastoma Cells: Relevance with Therapeutic Efficacies

    doi: 10.1371/journal.pone.0027484

    Figure Lengend Snippet: (A) Immunofluorescence illustration of intracellular distribution of STAT3 in LN-18 and PBC cells without (N) and with (AG490) 60 µM AG490 treatment. Arrows indicate the cells shown in the insets in high magnification (X400). (B) Flow cytometry analysis revealed reduction of G1-phase cells, accumulation of S-phase cells and induction of apoptosis (blue peak) in AG490-treated LN-18 cell population. The cell cycle progression was almost unchanged in PBC cells. *, indicates the peak of apoptotic cells. (C) H&E morphologic examination of LN-18 cells under normal culture or incubated with 100 µM trans -resveratrol, 60 µM AG490 or resveratrol/AG490 mixture for 48 hours (Main images). Small images: immunocytochemical illustration of SULT1A1, 1C2 and 4A1 expression in LN-18 cells treated by 60 µM AG490 without/with 100 µM resveratrol supplementation. Normally cultured and 100 µM resveratrol-treated LN-18 cells were cited as controls.

    Article Snippet: ICC staining and Western blot analysis were performed on the samples obtained from each of the experimental groups using the rabbit anti-human SULT1A1, 1C2 and 4A1 antibodies (ProteinTech Group, Inc., Chicago, USA) by the method described elsewhere – .

    Techniques: Immunofluorescence, Flow Cytometry, Incubation, Expressing, Cell Culture

    Summary of the gene-specific PCR primer sequences, the length of production and the appropriate annealing temperature used in the experiments.

    Journal: Molecular Medicine Reports

    Article Title: Quercetin-3-O-β-D-glucoside decreases the bioavailability of cyclosporin A through regulation of drug metabolizing enzymes, transporters and nuclear receptors in rats

    doi: 10.3892/mmr.2018.9249

    Figure Lengend Snippet: Summary of the gene-specific PCR primer sequences, the length of production and the appropriate annealing temperature used in the experiments.

    Article Snippet: A rabbit anti-SULT1A1 polyclonal antibody (1:1,000; cat. no. bs-6283R) was purchased from Bioss (Beijing, China).

    Techniques:

    Effect of Q3GA on the intestinal and hepatic mRNA expression levels of Cyp3a1, Cyp3a2, Ugt1a1, Sult1a1, Gstm1, Slco2b1, Slco1b2, Mdr1, Bcrp, Mrp2, Pxr, and Car. In rats of the control and Q3GA-L, Q3GA-M, Q3GA-H, KET and VER pretreatment groups, the relative mRNA content was measured by reverse transcription-quantitative polymerase chain reaction. mRNA expression levels of (A) Cyp3a1, (B) Cyp3a2, (C) Ugt1a1, (D) Sult1a1, (E) Gstm1, (F) Slco2b1/Slco1b2, (G) Mdr1, (H) Bcrp, (I) Mrp2, (J) Pxr, and (K) Car were measured in the small intestine and liver of the rats. Values are expressed as the mean ± standard deviation (n=3). aP<0.05, bP<0.01, cP<0.001 vs. the control. dP<0.05, eP<0.01, fP<0.001 vs. the inhibitor group (KET/VER). Q3GA-L, low-dose Q3GA (2.5 mg/kg); Q3GA-M, middle-dose Q3GA (5 mg/kg); Q3GA-H, high-dose Q3GA (10 mg/kg). CsA, cyclosporin A; Q3GA, quercetin-3-O-β-D-glucoside; KET, ketoconazole; VER: Verapamil; Cyp, cytochrome P450; Gstm, glutathione-S-transferase-µ; Q3GA, quercetin-3-O-β-D-glucoside; Slco, solute carrier organic anion transporter family member; Sult, sulfotransferase; Car, constitutive androstane receptor; Mdr1, multidrug resistance protein 1; Mrp2; multidrug resistance protein 2; Pxr, pregnane X receptor; Bcrp, breast cancer resistance protein.

    Journal: Molecular Medicine Reports

    Article Title: Quercetin-3-O-β-D-glucoside decreases the bioavailability of cyclosporin A through regulation of drug metabolizing enzymes, transporters and nuclear receptors in rats

    doi: 10.3892/mmr.2018.9249

    Figure Lengend Snippet: Effect of Q3GA on the intestinal and hepatic mRNA expression levels of Cyp3a1, Cyp3a2, Ugt1a1, Sult1a1, Gstm1, Slco2b1, Slco1b2, Mdr1, Bcrp, Mrp2, Pxr, and Car. In rats of the control and Q3GA-L, Q3GA-M, Q3GA-H, KET and VER pretreatment groups, the relative mRNA content was measured by reverse transcription-quantitative polymerase chain reaction. mRNA expression levels of (A) Cyp3a1, (B) Cyp3a2, (C) Ugt1a1, (D) Sult1a1, (E) Gstm1, (F) Slco2b1/Slco1b2, (G) Mdr1, (H) Bcrp, (I) Mrp2, (J) Pxr, and (K) Car were measured in the small intestine and liver of the rats. Values are expressed as the mean ± standard deviation (n=3). aP<0.05, bP<0.01, cP<0.001 vs. the control. dP<0.05, eP<0.01, fP<0.001 vs. the inhibitor group (KET/VER). Q3GA-L, low-dose Q3GA (2.5 mg/kg); Q3GA-M, middle-dose Q3GA (5 mg/kg); Q3GA-H, high-dose Q3GA (10 mg/kg). CsA, cyclosporin A; Q3GA, quercetin-3-O-β-D-glucoside; KET, ketoconazole; VER: Verapamil; Cyp, cytochrome P450; Gstm, glutathione-S-transferase-µ; Q3GA, quercetin-3-O-β-D-glucoside; Slco, solute carrier organic anion transporter family member; Sult, sulfotransferase; Car, constitutive androstane receptor; Mdr1, multidrug resistance protein 1; Mrp2; multidrug resistance protein 2; Pxr, pregnane X receptor; Bcrp, breast cancer resistance protein.

    Article Snippet: A rabbit anti-SULT1A1 polyclonal antibody (1:1,000; cat. no. bs-6283R) was purchased from Bioss (Beijing, China).

    Techniques: Expressing, Real-time Polymerase Chain Reaction, Standard Deviation

    Effect of Q3GA on the intestinal and hepatic protein expression levels of CYP3A1, CYP3A2, UGT1A1, SULT1A1, GSTM1, OATP2B1, OATP1B2, P-gp, BCRP, MRP2, PXR, and CAR. In rats of the control and Q3GA-L, Q3GA-M, Q3GA-H, KET, VER pretreatment groups, the relative protein contents were assessed by western blotting. Representative western blotting results in (A) liver and (B) in small intestine. Western blotting results of (Aa) UGT1A1, SULT1A1, GSTM1, OATP1B2, BCRP, MRP2, PXR and CAR, (Ab) CYP3A1/2 and (Ac) P-gp in liver. Western blotting results of (Ba) UGT1A1, SULT1A1, GSTM1, OATP2B1, BCRP, MRP2, PXR and CAR, (Bb) CYP3A1/2 and (Bc) P-gp in small intestine. Q3GA-L, low-dose Q3GA (2.5 mg/kg); Q3GA-M, middle-dose Q3GA (5 mg/kg); Q3GA-H, high-dose Q3GA (10 mg/kg). BCRP, breast cancer resistance protein; CAR, constitutive androstane receptor; CsA, cyclosporin A; CYP, cytochrome P450; GSTM, glutathione-S-transferase-µ; KET, ketoconazole; MRP, multidrug resistance-associated protein; OATP1B1, organic anion transporting polypeptide 1B1; P-gp, P-glycoprotein; PXR, pregnane X receptor; Q3GA, quercetin-3-O-β-D-glucoside; SULT, sulfotransferase; UGT, UDP glucuronosyltransferase; VER, verapamil.

    Journal: Molecular Medicine Reports

    Article Title: Quercetin-3-O-β-D-glucoside decreases the bioavailability of cyclosporin A through regulation of drug metabolizing enzymes, transporters and nuclear receptors in rats

    doi: 10.3892/mmr.2018.9249

    Figure Lengend Snippet: Effect of Q3GA on the intestinal and hepatic protein expression levels of CYP3A1, CYP3A2, UGT1A1, SULT1A1, GSTM1, OATP2B1, OATP1B2, P-gp, BCRP, MRP2, PXR, and CAR. In rats of the control and Q3GA-L, Q3GA-M, Q3GA-H, KET, VER pretreatment groups, the relative protein contents were assessed by western blotting. Representative western blotting results in (A) liver and (B) in small intestine. Western blotting results of (Aa) UGT1A1, SULT1A1, GSTM1, OATP1B2, BCRP, MRP2, PXR and CAR, (Ab) CYP3A1/2 and (Ac) P-gp in liver. Western blotting results of (Ba) UGT1A1, SULT1A1, GSTM1, OATP2B1, BCRP, MRP2, PXR and CAR, (Bb) CYP3A1/2 and (Bc) P-gp in small intestine. Q3GA-L, low-dose Q3GA (2.5 mg/kg); Q3GA-M, middle-dose Q3GA (5 mg/kg); Q3GA-H, high-dose Q3GA (10 mg/kg). BCRP, breast cancer resistance protein; CAR, constitutive androstane receptor; CsA, cyclosporin A; CYP, cytochrome P450; GSTM, glutathione-S-transferase-µ; KET, ketoconazole; MRP, multidrug resistance-associated protein; OATP1B1, organic anion transporting polypeptide 1B1; P-gp, P-glycoprotein; PXR, pregnane X receptor; Q3GA, quercetin-3-O-β-D-glucoside; SULT, sulfotransferase; UGT, UDP glucuronosyltransferase; VER, verapamil.

    Article Snippet: A rabbit anti-SULT1A1 polyclonal antibody (1:1,000; cat. no. bs-6283R) was purchased from Bioss (Beijing, China).

    Techniques: Expressing, Western Blot

    Quantification of the effect of Q3GA on the intestinal and hepatic protein levels, assessed by western blotting. Quantification of western blotting results revealed protein expression levels of (A) CYP3A1, (B) CYP3A2, (C) UGT1A1, (D) SULT1A1, (E) GSTM1, (F) OATP2B1/OATP1B2, (G) P-gp, (H) BCRP, (I) MRP2, (J) PXR, and (K) CAR measured in the small intestine and liver of rats. Values are expressed as the mean ± standard deviation (n=3). aP<0.05, bP<0.01, cP<0.001 vs. control; dP<0.05, eP<0.01, fP<0.001 vs. inhibitor group (KET/VER). Q3GA-L, low-dose Q3GA (2.5 mg/kg); Q3GA-M, middle-dose Q3GA (5 mg/kg); Q3GA-H, high-dose Q3GA (10 mg/kg). BCRP, breast cancer resistance protein; CAR, constitutive androstane receptor; CsA, cyclosporin A; CYP, cytochrome P450; GSTM, glutathione-S-transferase-µ; KET, ketoconazole; MRP2 multidrug resistance-associated protein 2; OATP, organic anion transporting polypeptide; P-gp, P-glycoprotein; PXR, pregnane X receptor; Q3GA, quercetin-3-O-β-D-glucoside; SULT, sulfotransferase; UGT, UDP glucuronosyltransferase; VER, verapamil.

    Journal: Molecular Medicine Reports

    Article Title: Quercetin-3-O-β-D-glucoside decreases the bioavailability of cyclosporin A through regulation of drug metabolizing enzymes, transporters and nuclear receptors in rats

    doi: 10.3892/mmr.2018.9249

    Figure Lengend Snippet: Quantification of the effect of Q3GA on the intestinal and hepatic protein levels, assessed by western blotting. Quantification of western blotting results revealed protein expression levels of (A) CYP3A1, (B) CYP3A2, (C) UGT1A1, (D) SULT1A1, (E) GSTM1, (F) OATP2B1/OATP1B2, (G) P-gp, (H) BCRP, (I) MRP2, (J) PXR, and (K) CAR measured in the small intestine and liver of rats. Values are expressed as the mean ± standard deviation (n=3). aP<0.05, bP<0.01, cP<0.001 vs. control; dP<0.05, eP<0.01, fP<0.001 vs. inhibitor group (KET/VER). Q3GA-L, low-dose Q3GA (2.5 mg/kg); Q3GA-M, middle-dose Q3GA (5 mg/kg); Q3GA-H, high-dose Q3GA (10 mg/kg). BCRP, breast cancer resistance protein; CAR, constitutive androstane receptor; CsA, cyclosporin A; CYP, cytochrome P450; GSTM, glutathione-S-transferase-µ; KET, ketoconazole; MRP2 multidrug resistance-associated protein 2; OATP, organic anion transporting polypeptide; P-gp, P-glycoprotein; PXR, pregnane X receptor; Q3GA, quercetin-3-O-β-D-glucoside; SULT, sulfotransferase; UGT, UDP glucuronosyltransferase; VER, verapamil.

    Article Snippet: A rabbit anti-SULT1A1 polyclonal antibody (1:1,000; cat. no. bs-6283R) was purchased from Bioss (Beijing, China).

    Techniques: Western Blot, Expressing, Standard Deviation

    A . Western blots, B . RT-PCR, C . Real-time PCR and D . ICC (100×) all showed that SULT1A1 was upregulated in T24 and EJ cells after resveratrol treatment. Ct, RV represented HBC cells treated without and with 100μM resveratrol incubation for 48h, respectively. * P<0.05, represents statistical significance between RV-treatment HBC cells and the normally cultured HBC cells, respectively.

    Journal: Oncotarget

    Article Title: Differential sensitivities of bladder cancer cell lines to resveratol are unrelated to its metabolic profile

    doi: 10.18632/oncotarget.15041

    Figure Lengend Snippet: A . Western blots, B . RT-PCR, C . Real-time PCR and D . ICC (100×) all showed that SULT1A1 was upregulated in T24 and EJ cells after resveratrol treatment. Ct, RV represented HBC cells treated without and with 100μM resveratrol incubation for 48h, respectively. * P<0.05, represents statistical significance between RV-treatment HBC cells and the normally cultured HBC cells, respectively.

    Article Snippet: The first antibody of rabbit anti-human SULT1A1 (Protein Tech Group, Inc., Chicago, USA) was used in the dilution rates of 1:120.

    Techniques: Western Blot, Reverse Transcription Polymerase Chain Reaction, Real-time Polymerase Chain Reaction, Incubation, Cell Culture

    Astrocytic SULT1A immunoreactivity in the EAE and control white matter spinal cord. Representative stainings for EAE mouse ( a–e ) or control mouse ( f – j and, for non-specific control, k – n ). a , f SULT1A1 staining ( green channel ); k non-specific staining (no rabbit primary antibody, green channel ); b , g , l GFAP staining ( red channel ); c , h , m DAPI staining ( blue channel ); d , i , n all channels merged; e , j red and green channels merged. o Schematic representation of the spinal cord section with approximate field ( red square ) used for the pictures. Arrows point to astrocytic (GFAP+) cells (with identified nucleus) in ( e ) or to astrocytic GFAP+ fibers in ( j ). a – n Scale bar, 75 μm

    Journal: Journal of Neuroinflammation

    Article Title: Transcript analysis of laser capture microdissected white matter astrocytes and higher phenol sulfotransferase 1A1 expression during autoimmune neuroinflammation

    doi: 10.1186/s12974-015-0348-y

    Figure Lengend Snippet: Astrocytic SULT1A immunoreactivity in the EAE and control white matter spinal cord. Representative stainings for EAE mouse ( a–e ) or control mouse ( f – j and, for non-specific control, k – n ). a , f SULT1A1 staining ( green channel ); k non-specific staining (no rabbit primary antibody, green channel ); b , g , l GFAP staining ( red channel ); c , h , m DAPI staining ( blue channel ); d , i , n all channels merged; e , j red and green channels merged. o Schematic representation of the spinal cord section with approximate field ( red square ) used for the pictures. Arrows point to astrocytic (GFAP+) cells (with identified nucleus) in ( e ) or to astrocytic GFAP+ fibers in ( j ). a – n Scale bar, 75 μm

    Article Snippet: Briefly, sections were rehydrated in 0.01 M PBS, incubated with 0.3 % H202 for 20 min, rinsed in PBS, and preincubated in PBS with 25 % Normal Donkey Serum (NDS) and 0.03 % Triton-X100 for 20 min at room temperature, followed by overnight incubation at 4 °C with anti-mouse SULT1A1 rabbit antibody at 1/1000 (Bioss, Woburn, MA, USA) or at 1/400 (Abcam, #38411, Cambridge, MA, USA) or with rabbit anti-GFAP (1/2000, Dako) in PBS and 2.5 % NDS and 0.03 % Triton-X100.

    Techniques: Staining

    List of gene transcripts with their corresponding probes (ID assay)

    Journal: Journal of Neuroinflammation

    Article Title: Transcript analysis of laser capture microdissected white matter astrocytes and higher phenol sulfotransferase 1A1 expression during autoimmune neuroinflammation

    doi: 10.1186/s12974-015-0348-y

    Figure Lengend Snippet: List of gene transcripts with their corresponding probes (ID assay)

    Article Snippet: Briefly, sections were rehydrated in 0.01 M PBS, incubated with 0.3 % H202 for 20 min, rinsed in PBS, and preincubated in PBS with 25 % Normal Donkey Serum (NDS) and 0.03 % Triton-X100 for 20 min at room temperature, followed by overnight incubation at 4 °C with anti-mouse SULT1A1 rabbit antibody at 1/1000 (Bioss, Woburn, MA, USA) or at 1/400 (Abcam, #38411, Cambridge, MA, USA) or with rabbit anti-GFAP (1/2000, Dako) in PBS and 2.5 % NDS and 0.03 % Triton-X100.

    Techniques: Binding Assay

    Summary of TLDA analysis

    Journal: Journal of Neuroinflammation

    Article Title: Transcript analysis of laser capture microdissected white matter astrocytes and higher phenol sulfotransferase 1A1 expression during autoimmune neuroinflammation

    doi: 10.1186/s12974-015-0348-y

    Figure Lengend Snippet: Summary of TLDA analysis

    Article Snippet: Briefly, sections were rehydrated in 0.01 M PBS, incubated with 0.3 % H202 for 20 min, rinsed in PBS, and preincubated in PBS with 25 % Normal Donkey Serum (NDS) and 0.03 % Triton-X100 for 20 min at room temperature, followed by overnight incubation at 4 °C with anti-mouse SULT1A1 rabbit antibody at 1/1000 (Bioss, Woburn, MA, USA) or at 1/400 (Abcam, #38411, Cambridge, MA, USA) or with rabbit anti-GFAP (1/2000, Dako) in PBS and 2.5 % NDS and 0.03 % Triton-X100.

    Techniques:

    Lack of SULT1A1 immunoreactivity in astrocytes of the gray matter spinal cord. Representative stainings for EAE mouse ( a–e ) or control mouse ( f–j ), and for non-specific control ( k–n ). a , f SULT1A1 staining ( green channel ); k , l non-specific staining in absence of rabbit and rat primary antibodies ( k , green channel ; l , red channel ); b , g GFAP staining ( red channel ); c , h , m DAPI staining ( blue channel ); d , i , n all channels merged; e , j red and green channel merged. o Schematic representation of the spinal cord section with approximate field ( red square ) used for the pictures. a – n Scale bar, 75 μm

    Journal: Journal of Neuroinflammation

    Article Title: Transcript analysis of laser capture microdissected white matter astrocytes and higher phenol sulfotransferase 1A1 expression during autoimmune neuroinflammation

    doi: 10.1186/s12974-015-0348-y

    Figure Lengend Snippet: Lack of SULT1A1 immunoreactivity in astrocytes of the gray matter spinal cord. Representative stainings for EAE mouse ( a–e ) or control mouse ( f–j ), and for non-specific control ( k–n ). a , f SULT1A1 staining ( green channel ); k , l non-specific staining in absence of rabbit and rat primary antibodies ( k , green channel ; l , red channel ); b , g GFAP staining ( red channel ); c , h , m DAPI staining ( blue channel ); d , i , n all channels merged; e , j red and green channel merged. o Schematic representation of the spinal cord section with approximate field ( red square ) used for the pictures. a – n Scale bar, 75 μm

    Article Snippet: Briefly, sections were rehydrated in 0.01 M PBS, incubated with 0.3 % H202 for 20 min, rinsed in PBS, and preincubated in PBS with 25 % Normal Donkey Serum (NDS) and 0.03 % Triton-X100 for 20 min at room temperature, followed by overnight incubation at 4 °C with anti-mouse SULT1A1 rabbit antibody at 1/1000 (Bioss, Woburn, MA, USA) or at 1/400 (Abcam, #38411, Cambridge, MA, USA) or with rabbit anti-GFAP (1/2000, Dako) in PBS and 2.5 % NDS and 0.03 % Triton-X100.

    Techniques: Staining