consensus stat 1 sequence Search Results


94
Santa Cruz Biotechnology consensus stat 1 sequence
Consensus Stat 1 Sequence, 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/consensus stat 1 sequence/product/Santa Cruz Biotechnology
Average 94 stars, based on 1 article reviews
consensus stat 1 sequence - by Bioz Stars, 2026-05
94/100 stars
  Buy from Supplier

96
Santa Cruz Biotechnology stat1
Gestational MZD affects phosphorylations of <t>STAT1</t> and STAT3 in E19 brain total fractions. From gestation day 0 through 19, dams were fed ad libitum control (C) or MZD diets. STAT1 and STAT3 contents and phosphorylations in E19 brain total homogenates were measured by Western blot. (A) Representative images for pY 701 -STAT1, pS 727 -STAT1, STAT1, and β-actin (top); and band quantifications expressed as pY 701 -STAT1/STAT1, pS 727 -STAT1/STAT1 and total STAT1/β-actin (bottom). (B) Representative images for pY 705 -STAT3, pS 727 -STAT3, STAT3, and β-actin (top), and band quantifications expressed as pY 705 -STAT3/STAT3, pS 727 -STAT3/STAT3 and STAT3/β-actin (bottom). Results were normalized to control values and are shown as means±S.E.M. of 6 animals per group. *, ** Significantly different compared to C groups ( P <0.05 and P <0.01, respectively, one-way ANOVA).
Stat1, 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/stat1/product/Santa Cruz Biotechnology
Average 96 stars, based on 1 article reviews
stat1 - by Bioz Stars, 2026-05
96/100 stars
  Buy from Supplier

Image Search Results


Gestational MZD affects phosphorylations of STAT1 and STAT3 in E19 brain total fractions. From gestation day 0 through 19, dams were fed ad libitum control (C) or MZD diets. STAT1 and STAT3 contents and phosphorylations in E19 brain total homogenates were measured by Western blot. (A) Representative images for pY 701 -STAT1, pS 727 -STAT1, STAT1, and β-actin (top); and band quantifications expressed as pY 701 -STAT1/STAT1, pS 727 -STAT1/STAT1 and total STAT1/β-actin (bottom). (B) Representative images for pY 705 -STAT3, pS 727 -STAT3, STAT3, and β-actin (top), and band quantifications expressed as pY 705 -STAT3/STAT3, pS 727 -STAT3/STAT3 and STAT3/β-actin (bottom). Results were normalized to control values and are shown as means±S.E.M. of 6 animals per group. *, ** Significantly different compared to C groups ( P <0.05 and P <0.01, respectively, one-way ANOVA).

Journal: Redox Biology

Article Title: Zinc deficiency affects the STAT1/3 signaling pathways in part through redox-mediated mechanisms

doi: 10.1016/j.redox.2016.12.027

Figure Lengend Snippet: Gestational MZD affects phosphorylations of STAT1 and STAT3 in E19 brain total fractions. From gestation day 0 through 19, dams were fed ad libitum control (C) or MZD diets. STAT1 and STAT3 contents and phosphorylations in E19 brain total homogenates were measured by Western blot. (A) Representative images for pY 701 -STAT1, pS 727 -STAT1, STAT1, and β-actin (top); and band quantifications expressed as pY 701 -STAT1/STAT1, pS 727 -STAT1/STAT1 and total STAT1/β-actin (bottom). (B) Representative images for pY 705 -STAT3, pS 727 -STAT3, STAT3, and β-actin (top), and band quantifications expressed as pY 705 -STAT3/STAT3, pS 727 -STAT3/STAT3 and STAT3/β-actin (bottom). Results were normalized to control values and are shown as means±S.E.M. of 6 animals per group. *, ** Significantly different compared to C groups ( P <0.05 and P <0.01, respectively, one-way ANOVA).

Article Snippet: Antibodies for STAT1, STAT3, β-actin, α-tubulin, β-tubulin and heterogeneous nuclear ribonucleoprotein A1 (hnRNP), and the oligonucleotides containing the consensus sequence for STAT1 and STAT3 were obtained from Santa Cruz Biotechnology (Santa Cruz, CA).

Techniques: Western Blot

Gestational MZD affects DNA binding and content of STAT1 and STAT3 in nuclear fractions isolated from E19 brains. From gestation day 0 through 19, dams were fed ad libitum control (C) or MZD diets. Nuclear and cytosolic fractions were prepared from E19 brains as described in the Materials and Methods section. (A) EMSA for STAT1 and STAT3 in nuclear and cytosolic fractions. To determine the specificity of each transcription factor-DNA complex, a control nuclear fraction was incubated in the presence of a 100-fold molar excess of unlabeled oligonucleotide containing the consensus sequence for either the specific (S) or an unspecific (U) transcription factor before the binding assay. Bands were quantified and the ratio nuclear/cytosolic DNA binding (NF/CF) was calculated. (B) Western blots for pY 701 -STAT1, pS 727 -STAT1, and STAT1 (left); and pY 705 -STAT3, pS 727 -STAT3, and STAT3 (right); and hnRNP as the nuclear housekeeping protein. After quantification, results were expressed as pY 701 -STAT1/STAT1, pS 727 -STAT1/STAT1 and STAT1/hnRNP (bottom left), or pY 705 -STAT3/STAT3, pS 727 -STAT3/STAT3, and STAT3/hnRNP (bottom right). Results were normalized to control values and are shown as means±S.E.M. of 6 animals per group. *, ** Significantly different compared to C groups ( P <0.05 and P <0.01, respectively, one-way ANOVA).

Journal: Redox Biology

Article Title: Zinc deficiency affects the STAT1/3 signaling pathways in part through redox-mediated mechanisms

doi: 10.1016/j.redox.2016.12.027

Figure Lengend Snippet: Gestational MZD affects DNA binding and content of STAT1 and STAT3 in nuclear fractions isolated from E19 brains. From gestation day 0 through 19, dams were fed ad libitum control (C) or MZD diets. Nuclear and cytosolic fractions were prepared from E19 brains as described in the Materials and Methods section. (A) EMSA for STAT1 and STAT3 in nuclear and cytosolic fractions. To determine the specificity of each transcription factor-DNA complex, a control nuclear fraction was incubated in the presence of a 100-fold molar excess of unlabeled oligonucleotide containing the consensus sequence for either the specific (S) or an unspecific (U) transcription factor before the binding assay. Bands were quantified and the ratio nuclear/cytosolic DNA binding (NF/CF) was calculated. (B) Western blots for pY 701 -STAT1, pS 727 -STAT1, and STAT1 (left); and pY 705 -STAT3, pS 727 -STAT3, and STAT3 (right); and hnRNP as the nuclear housekeeping protein. After quantification, results were expressed as pY 701 -STAT1/STAT1, pS 727 -STAT1/STAT1 and STAT1/hnRNP (bottom left), or pY 705 -STAT3/STAT3, pS 727 -STAT3/STAT3, and STAT3/hnRNP (bottom right). Results were normalized to control values and are shown as means±S.E.M. of 6 animals per group. *, ** Significantly different compared to C groups ( P <0.05 and P <0.01, respectively, one-way ANOVA).

Article Snippet: Antibodies for STAT1, STAT3, β-actin, α-tubulin, β-tubulin and heterogeneous nuclear ribonucleoprotein A1 (hnRNP), and the oligonucleotides containing the consensus sequence for STAT1 and STAT3 were obtained from Santa Cruz Biotechnology (Santa Cruz, CA).

Techniques: Binding Assay, Isolation, Incubation, Sequencing, Western Blot

Zinc deficiency affects total protein content and phosphorylation patterns of STAT1 and STAT3 in IMR-32 total fractions. Total cell fractions were isolated from IMR-32 cells incubated for 24 h in control (C) or zinc -depleted (1.5 μM zinc (1.5Zn)) medium. STAT1 and STAT3 contents and phosphorylations were measured by Western blot. (A) Representative images for pY 701 -STAT1, pS 727 -STAT1, STAT1, and β-tubulin as the housekeeping protein (top), and their quantification expressed as pY 701 -STAT1/STAT1, pS 727 -STAT1/STAT1 and STAT1/β-tubulin (bottom). (B) Representative images for pY 705 -STAT3, pS 727 -STAT3, STAT3, and β-tubulin (top), and their quantification expressed as pY 705 -STAT3/STAT3, pS 727 -STAT3/STAT3, and STAT3/β-tubulin (bottom). Results were normalized to control values (dotted lined) and shown as means±S.E.M. of four independent experiments. *, ** Significantly different compared to C groups ( P <0.05 and P <0.01, respectively, one-way ANOVA).

Journal: Redox Biology

Article Title: Zinc deficiency affects the STAT1/3 signaling pathways in part through redox-mediated mechanisms

doi: 10.1016/j.redox.2016.12.027

Figure Lengend Snippet: Zinc deficiency affects total protein content and phosphorylation patterns of STAT1 and STAT3 in IMR-32 total fractions. Total cell fractions were isolated from IMR-32 cells incubated for 24 h in control (C) or zinc -depleted (1.5 μM zinc (1.5Zn)) medium. STAT1 and STAT3 contents and phosphorylations were measured by Western blot. (A) Representative images for pY 701 -STAT1, pS 727 -STAT1, STAT1, and β-tubulin as the housekeeping protein (top), and their quantification expressed as pY 701 -STAT1/STAT1, pS 727 -STAT1/STAT1 and STAT1/β-tubulin (bottom). (B) Representative images for pY 705 -STAT3, pS 727 -STAT3, STAT3, and β-tubulin (top), and their quantification expressed as pY 705 -STAT3/STAT3, pS 727 -STAT3/STAT3, and STAT3/β-tubulin (bottom). Results were normalized to control values (dotted lined) and shown as means±S.E.M. of four independent experiments. *, ** Significantly different compared to C groups ( P <0.05 and P <0.01, respectively, one-way ANOVA).

Article Snippet: Antibodies for STAT1, STAT3, β-actin, α-tubulin, β-tubulin and heterogeneous nuclear ribonucleoprotein A1 (hnRNP), and the oligonucleotides containing the consensus sequence for STAT1 and STAT3 were obtained from Santa Cruz Biotechnology (Santa Cruz, CA).

Techniques: Isolation, Incubation, Western Blot

Zinc deficiency affects nuclear STAT1- and STAT3-DNA binding, and transactivation of STAT1 and STAT3-dependent genes in IMR-32 cells . Nuclear and total cell fractions were isolated after incubating IMR-32 cells for 24 h in control medium (C), or in chelated medium containing 1.5 μM zinc (1.5Zn), or 15 μM zinc (15Zn). (A) Representative image of an EMSA for STAT1 and STAT3 in nuclear fractions (top). A control nuclear fraction was incubated in the presence of a 100-fold molar excess of unlabeled oligonucleotide containing the consensus sequence for aspecific (S) transcription factor before the binding assay. Bands were quantified, results expressed as the ratio nuclear/total fraction binding (NF/TF) for STAT1 (white bars) and STAT3 (grey bars), and normalized to control values. Results are shown as means±S.E.M. of three independent experiments. (B) Transactivation of STAT1- and STAT3-driven luciferase was measured as described in Materials and Methods in cells incubated for 24 h in control, 1.5Zn or 15Zn medium. Data are expressed as the ratio luciferase activity/β-galactosidase activity. Results are shown as means±S.E.M of three independent experiments. *Significantly different compared to the C groups ( P <0.05, one-way ANOVA).

Journal: Redox Biology

Article Title: Zinc deficiency affects the STAT1/3 signaling pathways in part through redox-mediated mechanisms

doi: 10.1016/j.redox.2016.12.027

Figure Lengend Snippet: Zinc deficiency affects nuclear STAT1- and STAT3-DNA binding, and transactivation of STAT1 and STAT3-dependent genes in IMR-32 cells . Nuclear and total cell fractions were isolated after incubating IMR-32 cells for 24 h in control medium (C), or in chelated medium containing 1.5 μM zinc (1.5Zn), or 15 μM zinc (15Zn). (A) Representative image of an EMSA for STAT1 and STAT3 in nuclear fractions (top). A control nuclear fraction was incubated in the presence of a 100-fold molar excess of unlabeled oligonucleotide containing the consensus sequence for aspecific (S) transcription factor before the binding assay. Bands were quantified, results expressed as the ratio nuclear/total fraction binding (NF/TF) for STAT1 (white bars) and STAT3 (grey bars), and normalized to control values. Results are shown as means±S.E.M. of three independent experiments. (B) Transactivation of STAT1- and STAT3-driven luciferase was measured as described in Materials and Methods in cells incubated for 24 h in control, 1.5Zn or 15Zn medium. Data are expressed as the ratio luciferase activity/β-galactosidase activity. Results are shown as means±S.E.M of three independent experiments. *Significantly different compared to the C groups ( P <0.05, one-way ANOVA).

Article Snippet: Antibodies for STAT1, STAT3, β-actin, α-tubulin, β-tubulin and heterogeneous nuclear ribonucleoprotein A1 (hnRNP), and the oligonucleotides containing the consensus sequence for STAT1 and STAT3 were obtained from Santa Cruz Biotechnology (Santa Cruz, CA).

Techniques: Binding Assay, Isolation, Incubation, Sequencing, Luciferase, Activity Assay

Zinc deficiency affects total protein content and phosphorylation patterns of STAT1 and STAT3 in IMR-32 cell nuclear fractions. Nuclear fractions were isolated from IMR-32 cells incubated for 24 h in control (C) or 1.5Zn medium. STAT1 and STAT3 content and phosphorylations were measured by Western blot. (A) Representative images for pY 701 -STAT1, pS 727 -STAT1, STAT1, and hnRNP as the nuclear housekeeping protein (top), and their quantification expressed as pY 701 -STAT1/STAT1, pS 727 -STAT1/STAT1 and STAT1/hnRNP (bottom). (B) Representative images for pY 705 -STAT3, pS 727 -STAT3, STAT3, and hnRNP (top), and their quantification expressed as pY 705 -STAT3/STAT3, pS 727 -STAT3/STAT3, and STAT3/hnRNP (bottom). Results were normalized to control values (dotted lined) and shown as means±S.E.M. of four independent experiments. *, ** Significantly different compared to C groups ( P <0.05 and P <0.01, respectively, one-way ANOVA).

Journal: Redox Biology

Article Title: Zinc deficiency affects the STAT1/3 signaling pathways in part through redox-mediated mechanisms

doi: 10.1016/j.redox.2016.12.027

Figure Lengend Snippet: Zinc deficiency affects total protein content and phosphorylation patterns of STAT1 and STAT3 in IMR-32 cell nuclear fractions. Nuclear fractions were isolated from IMR-32 cells incubated for 24 h in control (C) or 1.5Zn medium. STAT1 and STAT3 content and phosphorylations were measured by Western blot. (A) Representative images for pY 701 -STAT1, pS 727 -STAT1, STAT1, and hnRNP as the nuclear housekeeping protein (top), and their quantification expressed as pY 701 -STAT1/STAT1, pS 727 -STAT1/STAT1 and STAT1/hnRNP (bottom). (B) Representative images for pY 705 -STAT3, pS 727 -STAT3, STAT3, and hnRNP (top), and their quantification expressed as pY 705 -STAT3/STAT3, pS 727 -STAT3/STAT3, and STAT3/hnRNP (bottom). Results were normalized to control values (dotted lined) and shown as means±S.E.M. of four independent experiments. *, ** Significantly different compared to C groups ( P <0.05 and P <0.01, respectively, one-way ANOVA).

Article Snippet: Antibodies for STAT1, STAT3, β-actin, α-tubulin, β-tubulin and heterogeneous nuclear ribonucleoprotein A1 (hnRNP), and the oligonucleotides containing the consensus sequence for STAT1 and STAT3 were obtained from Santa Cruz Biotechnology (Santa Cruz, CA).

Techniques: Isolation, Incubation, Western Blot

α-Lipoic acid prevents zinc deficiency-induced impaired STAT1 and STAT3 nuclear import. Nuclear fraction and cytosolic fraction were isolated from IMR-32 cells incubated for 24 h in control (C), or zinc depleted (1.5Zn) medium with or without supplementation with 0.5mM α-lipoic acid (LA). Western blots for: (A) STAT1 and hnRNP as housekeeping protein in the nuclear fraction (top left), and STAT1 and β-actin as housekeeping protein in the cytosolic fraction (top right), and band quantification expressed as the ratio of total STAT1 nuclear/cytosolic (bottom); (B) STAT3 and hnRNP in the nuclear fraction (top left) and STAT3 and β-actin in the cytosolic fraction (top right), and band quantification expressed as the ratio total STAT3 nuclear/cytosolic fractions (bottom). Results were normalized to controls values, and shown as means±S.E.M. of three independent experiments. *, ** Significantly different compared to C groups ( P <0.05 and P <0.01, respectively, one-way ANOVA).

Journal: Redox Biology

Article Title: Zinc deficiency affects the STAT1/3 signaling pathways in part through redox-mediated mechanisms

doi: 10.1016/j.redox.2016.12.027

Figure Lengend Snippet: α-Lipoic acid prevents zinc deficiency-induced impaired STAT1 and STAT3 nuclear import. Nuclear fraction and cytosolic fraction were isolated from IMR-32 cells incubated for 24 h in control (C), or zinc depleted (1.5Zn) medium with or without supplementation with 0.5mM α-lipoic acid (LA). Western blots for: (A) STAT1 and hnRNP as housekeeping protein in the nuclear fraction (top left), and STAT1 and β-actin as housekeeping protein in the cytosolic fraction (top right), and band quantification expressed as the ratio of total STAT1 nuclear/cytosolic (bottom); (B) STAT3 and hnRNP in the nuclear fraction (top left) and STAT3 and β-actin in the cytosolic fraction (top right), and band quantification expressed as the ratio total STAT3 nuclear/cytosolic fractions (bottom). Results were normalized to controls values, and shown as means±S.E.M. of three independent experiments. *, ** Significantly different compared to C groups ( P <0.05 and P <0.01, respectively, one-way ANOVA).

Article Snippet: Antibodies for STAT1, STAT3, β-actin, α-tubulin, β-tubulin and heterogeneous nuclear ribonucleoprotein A1 (hnRNP), and the oligonucleotides containing the consensus sequence for STAT1 and STAT3 were obtained from Santa Cruz Biotechnology (Santa Cruz, CA).

Techniques: Isolation, Incubation, Western Blot

STAT1 and STAT3 require a functional cytoskeleton for nuclear translocation in IMR-32 cells. Nuclear fractions and total fractions were prepared from IMR-32 cells incubated for 24 h in control medium (C) with or without the addition of 0.5 μM vinblastine (Vb), 0.5 μM colchicine (Col), or 0.5 μM cytochalasin D (Cyt D). (A) EMSA for STAT1 in nuclear and total fractions (top), and band quantifications (bottom). (B) EMSA for STAT3 in nuclear and total fractions (top), and band quantifications (bottom). Results were expressed as the ratio nuclear/total fractions of DNA binding (NF/TF) and normalized to their control levels. Results are shown as means±S.E.M. of three independent experiments. *Significantly different compared to C without inhibitors ( P <0.05, one-way ANOVA).

Journal: Redox Biology

Article Title: Zinc deficiency affects the STAT1/3 signaling pathways in part through redox-mediated mechanisms

doi: 10.1016/j.redox.2016.12.027

Figure Lengend Snippet: STAT1 and STAT3 require a functional cytoskeleton for nuclear translocation in IMR-32 cells. Nuclear fractions and total fractions were prepared from IMR-32 cells incubated for 24 h in control medium (C) with or without the addition of 0.5 μM vinblastine (Vb), 0.5 μM colchicine (Col), or 0.5 μM cytochalasin D (Cyt D). (A) EMSA for STAT1 in nuclear and total fractions (top), and band quantifications (bottom). (B) EMSA for STAT3 in nuclear and total fractions (top), and band quantifications (bottom). Results were expressed as the ratio nuclear/total fractions of DNA binding (NF/TF) and normalized to their control levels. Results are shown as means±S.E.M. of three independent experiments. *Significantly different compared to C without inhibitors ( P <0.05, one-way ANOVA).

Article Snippet: Antibodies for STAT1, STAT3, β-actin, α-tubulin, β-tubulin and heterogeneous nuclear ribonucleoprotein A1 (hnRNP), and the oligonucleotides containing the consensus sequence for STAT1 and STAT3 were obtained from Santa Cruz Biotechnology (Santa Cruz, CA).

Techniques: Functional Assay, Translocation Assay, Incubation, Binding Assay

α-Lipoic acid differentially affects STAT1 and STAT3 phosphorylation in zinc deficient IMR-32 cells. Total fractions were prepared from IMR-32 cells incubated for 24 h in control (C), or zinc deficient (1.5Zn) medium with or without supplementation with 0.5mM α-lipoic acid (LA). STAT1 and STAT3 content and phosphorylation were measured by Western blot. (A) Representative images for pY 701 -STAT1, pS 727 -STAT1, STAT1, and β-actin and their quantification expressed as pY 701 -STAT1/STAT1, pS 727 -STAT1/STAT1, and STAT1/β-actin (bottom). (B) Representative images for pY 705 -STAT3, STAT3 and β-actin, and their quantification expressed as pY 705 -STAT3/STAT3, and STAT3/β-actin. Results were normalized to control values and shown as means±S.E.M. of four independent experiments. *, **, *** Significantly different compared to C groups ( P <0.05, P <0.01, and P <0.001, respectively, one-way ANOVA).

Journal: Redox Biology

Article Title: Zinc deficiency affects the STAT1/3 signaling pathways in part through redox-mediated mechanisms

doi: 10.1016/j.redox.2016.12.027

Figure Lengend Snippet: α-Lipoic acid differentially affects STAT1 and STAT3 phosphorylation in zinc deficient IMR-32 cells. Total fractions were prepared from IMR-32 cells incubated for 24 h in control (C), or zinc deficient (1.5Zn) medium with or without supplementation with 0.5mM α-lipoic acid (LA). STAT1 and STAT3 content and phosphorylation were measured by Western blot. (A) Representative images for pY 701 -STAT1, pS 727 -STAT1, STAT1, and β-actin and their quantification expressed as pY 701 -STAT1/STAT1, pS 727 -STAT1/STAT1, and STAT1/β-actin (bottom). (B) Representative images for pY 705 -STAT3, STAT3 and β-actin, and their quantification expressed as pY 705 -STAT3/STAT3, and STAT3/β-actin. Results were normalized to control values and shown as means±S.E.M. of four independent experiments. *, **, *** Significantly different compared to C groups ( P <0.05, P <0.01, and P <0.001, respectively, one-way ANOVA).

Article Snippet: Antibodies for STAT1, STAT3, β-actin, α-tubulin, β-tubulin and heterogeneous nuclear ribonucleoprotein A1 (hnRNP), and the oligonucleotides containing the consensus sequence for STAT1 and STAT3 were obtained from Santa Cruz Biotechnology (Santa Cruz, CA).

Techniques: Incubation, Western Blot