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rabbit anti phospho stat5  (Bioss)


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    Structured Review

    Bioss rabbit anti phospho stat5
    Rabbit Anti Phospho Stat5, supplied by Bioss, used in various techniques. Bioz Stars score: 94/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti phospho stat5/product/Bioss
    Average 94 stars, based on 14 article reviews
    rabbit anti phospho stat5 - by Bioz Stars, 2026-03
    94/100 stars

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    Silencing of MRCKα inhibits the stimulatory effects of Met and Leu on mRNA abundance of genes related to milk protein synthesis in bovine mammary epithelial cells. Cells were transfected with scrambled siRNA (control, SC) or MRCKα siRNA (SI) and stimulated simultaneously with control (B, basal medium), additional Met (M, Met = 0.6 mM) or Leu (L, Leu = 0.6 mM). After 24 h, cells were collected and isolated for RT-qPCR analysis. Values are presented as mean ± SEM for three independent experiments. P AA , P -value of amino acid addition (AA); P SI , P -value of silencing of MRCKα (SI); P AA×SI , P -value of AA × SI interaction. CSN2 = β-casein; CSN1S1 = αS1-casein; CSN3 = κ-casein; LALBA = lactalbumin α; MRCKα = myotonic dystrophy-related CDC42-binding kinase alpha; mTOR = mechanistic target of rapamycin; JAK2 = Janus kinase 2; <t>STAT5</t> = signal transducers and activators of transcription 5.
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    Silencing of MRCKα inhibits the stimulatory effects of Met and Leu on mRNA abundance of genes related to milk protein synthesis in bovine mammary epithelial cells. Cells were transfected with scrambled siRNA (control, SC) or MRCKα siRNA (SI) and stimulated simultaneously with control (B, basal medium), additional Met (M, Met = 0.6 mM) or Leu (L, Leu = 0.6 mM). After 24 h, cells were collected and isolated for RT-qPCR analysis. Values are presented as mean ± SEM for three independent experiments. P AA , P -value of amino acid addition (AA); P SI , P -value of silencing of MRCKα (SI); P AA×SI , P -value of AA × SI interaction. CSN2 = β-casein; CSN1S1 = αS1-casein; CSN3 = κ-casein; LALBA = lactalbumin α; MRCKα = myotonic dystrophy-related CDC42-binding kinase alpha; mTOR = mechanistic target of rapamycin; JAK2 = Janus kinase 2; <t>STAT5</t> = signal transducers and activators of transcription 5.
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    Silencing of MRCKα inhibits the stimulatory effects of Met and Leu on mRNA abundance of genes related to milk protein synthesis in bovine mammary epithelial cells. Cells were transfected with scrambled siRNA (control, SC) or MRCKα siRNA (SI) and stimulated simultaneously with control (B, basal medium), additional Met (M, Met = 0.6 mM) or Leu (L, Leu = 0.6 mM). After 24 h, cells were collected and isolated for RT-qPCR analysis. Values are presented as mean ± SEM for three independent experiments. P AA , P -value of amino acid addition (AA); P SI , P -value of silencing of MRCKα (SI); P AA×SI , P -value of AA × SI interaction. CSN2 = β-casein; CSN1S1 = αS1-casein; CSN3 = κ-casein; LALBA = lactalbumin α; MRCKα = myotonic dystrophy-related CDC42-binding kinase alpha; mTOR = mechanistic target of rapamycin; JAK2 = Janus kinase 2; <t>STAT5</t> = signal transducers and activators of transcription 5.
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    Gαi1/3 knockdown inhibits <t>STAT5</t> activation, differentiation and growth by IL-5 in EoL-1 cells. Stable EoL-1 cells, expressing the scramble control shRNA (“C-shRNA”), Gαi1 shRNA and Gαi3 shRNA, were treated with GM-CSF (50 ng/mL) and IL-5 (50 ng/mL) for 24 hours, and were tested by Western blotting of listed proteins (A, E) . Relative expression of listed genes (24 hours after GM-CSF and IL-5 treatment) was shown (B, C) ; In each experiment, n=3 (three replicated wells). Cells were further cultured for the times indicated, cell proliferation were tested (F, G) , with cell viability tested by CCK-8 assay (D) . Bar = 100 μm. Blotting quantification was performed from five replicate blot data, data of all repeated experiments were pulled together to calculate mean ± SD. *P <0.05 (B, E, G) . *P <0.05 vs. “Control” treatment in “C-shRNA” EoL-1 cells (C) . # P <0.05 vs. GM-CSF and IL-5 treatment in “C-shRNA” EoL-1 cells (C) . *P <0.05 vs. “Control” treatment in “Gαi1/3-shRNA” EoL-1 cells (D) . #P <0.05 vs. GM-CSF and IL-5 treatment in “Gαi1/3-shRNA” EoL-1 cells (D) .
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    Santa Cruz Biotechnology rabbit polyclonal stat5 antibody
    (A) Western blot analyses of JAK1, JAK2, as well as tyrosine phosphorylated STAT proteins in human pancreatic cancer cell lines ( n = 9) and untransformed pancreatic cells (HPNE). Beta-actin (ACTB) and GAPDH served as loading controls; mouse pancreatic tumor cells treated with human growth hormone (hGH) and IL-4 served as controls for the activation of <t>STAT5</t> and STAT6, respectively (b and c). Western blots are representative of three experimental replicates used for quantitative analysis in . (B) Quantitative analysis of nuclear STAT3 expression in primary human pancreatic cancers ( n = 28) and normal tissues ( n = 17). The right panel shows representative immunofluorescent (IF) images of normal and tumor tissues co-stained for tyrosine phosphorylated STAT3 (pSTAT3) and pan-cytokeratin (panCK). Slides were counterstained with DAPI; bars, 40 μm.
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    Cell Signaling Technology Inc phospho stat5 polyclonal antibody
    (A) Western blot analyses of JAK1, JAK2, as well as tyrosine phosphorylated STAT proteins in human pancreatic cancer cell lines ( n = 9) and untransformed pancreatic cells (HPNE). Beta-actin (ACTB) and GAPDH served as loading controls; mouse pancreatic tumor cells treated with human growth hormone (hGH) and IL-4 served as controls for the activation of <t>STAT5</t> and STAT6, respectively (b and c). Western blots are representative of three experimental replicates used for quantitative analysis in . (B) Quantitative analysis of nuclear STAT3 expression in primary human pancreatic cancers ( n = 28) and normal tissues ( n = 17). The right panel shows representative immunofluorescent (IF) images of normal and tumor tissues co-stained for tyrosine phosphorylated STAT3 (pSTAT3) and pan-cytokeratin (panCK). Slides were counterstained with DAPI; bars, 40 μm.
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    Image Search Results


    Silencing of MRCKα inhibits the stimulatory effects of Met and Leu on mRNA abundance of genes related to milk protein synthesis in bovine mammary epithelial cells. Cells were transfected with scrambled siRNA (control, SC) or MRCKα siRNA (SI) and stimulated simultaneously with control (B, basal medium), additional Met (M, Met = 0.6 mM) or Leu (L, Leu = 0.6 mM). After 24 h, cells were collected and isolated for RT-qPCR analysis. Values are presented as mean ± SEM for three independent experiments. P AA , P -value of amino acid addition (AA); P SI , P -value of silencing of MRCKα (SI); P AA×SI , P -value of AA × SI interaction. CSN2 = β-casein; CSN1S1 = αS1-casein; CSN3 = κ-casein; LALBA = lactalbumin α; MRCKα = myotonic dystrophy-related CDC42-binding kinase alpha; mTOR = mechanistic target of rapamycin; JAK2 = Janus kinase 2; STAT5 = signal transducers and activators of transcription 5.

    Journal: Animal Nutrition

    Article Title: Myotonic dystrophy-related CDC42-binding kinase alpha (MRCKα) mediates methionine- and leucine-stimulated β-casein synthesis in bovine mammary epithelial cells via targeting mTOR

    doi: 10.1016/j.aninu.2025.01.003

    Figure Lengend Snippet: Silencing of MRCKα inhibits the stimulatory effects of Met and Leu on mRNA abundance of genes related to milk protein synthesis in bovine mammary epithelial cells. Cells were transfected with scrambled siRNA (control, SC) or MRCKα siRNA (SI) and stimulated simultaneously with control (B, basal medium), additional Met (M, Met = 0.6 mM) or Leu (L, Leu = 0.6 mM). After 24 h, cells were collected and isolated for RT-qPCR analysis. Values are presented as mean ± SEM for three independent experiments. P AA , P -value of amino acid addition (AA); P SI , P -value of silencing of MRCKα (SI); P AA×SI , P -value of AA × SI interaction. CSN2 = β-casein; CSN1S1 = αS1-casein; CSN3 = κ-casein; LALBA = lactalbumin α; MRCKα = myotonic dystrophy-related CDC42-binding kinase alpha; mTOR = mechanistic target of rapamycin; JAK2 = Janus kinase 2; STAT5 = signal transducers and activators of transcription 5.

    Article Snippet: Rabbit polyclonal anti-human signal transducer and activator of transcription 5 (STAT5) antibody, rabbit polyclonal anti-human phosphorylated STAT5 (Tyr 694 ) antibody, rabbit polyclonal anti-human PI3K antibody and rabbit polyclonal anti-human phosphorylated PI3K (Tyr 317 ) antibody were purchased from Bioss antibodies (Beijing, China).

    Techniques: Transfection, Control, Isolation, Quantitative RT-PCR, Binding Assay

    Silencing of MRCKα inhibits the stimulatory effects of Met and Leu on mRNA abundance of genes related to milk protein synthesis in bovine mammary epithelial cells. Cells were transfected with scrambled siRNA (control, SC) or MRCKα siRNA (SI) and stimulated simultaneously with control (B, basal medium), additional Met (M, Met = 0.6 mM) or Leu (L, Leu = 0.6 mM). After 24 h, cells were collected and isolated for RT-qPCR analysis. Values are presented as mean ± SEM for three independent experiments. P AA , P -value of amino acid addition (AA); P SI , P -value of silencing of MRCKα (SI); P AA×SI , P -value of AA × SI interaction. CSN2 = β-casein; CSN1S1 = αS1-casein; CSN3 = κ-casein; LALBA = lactalbumin α; MRCKα = myotonic dystrophy-related CDC42-binding kinase alpha; mTOR = mechanistic target of rapamycin; JAK2 = Janus kinase 2; STAT5 = signal transducers and activators of transcription 5.

    Journal: Animal Nutrition

    Article Title: Myotonic dystrophy-related CDC42-binding kinase alpha (MRCKα) mediates methionine- and leucine-stimulated β-casein synthesis in bovine mammary epithelial cells via targeting mTOR

    doi: 10.1016/j.aninu.2025.01.003

    Figure Lengend Snippet: Silencing of MRCKα inhibits the stimulatory effects of Met and Leu on mRNA abundance of genes related to milk protein synthesis in bovine mammary epithelial cells. Cells were transfected with scrambled siRNA (control, SC) or MRCKα siRNA (SI) and stimulated simultaneously with control (B, basal medium), additional Met (M, Met = 0.6 mM) or Leu (L, Leu = 0.6 mM). After 24 h, cells were collected and isolated for RT-qPCR analysis. Values are presented as mean ± SEM for three independent experiments. P AA , P -value of amino acid addition (AA); P SI , P -value of silencing of MRCKα (SI); P AA×SI , P -value of AA × SI interaction. CSN2 = β-casein; CSN1S1 = αS1-casein; CSN3 = κ-casein; LALBA = lactalbumin α; MRCKα = myotonic dystrophy-related CDC42-binding kinase alpha; mTOR = mechanistic target of rapamycin; JAK2 = Janus kinase 2; STAT5 = signal transducers and activators of transcription 5.

    Article Snippet: Rabbit polyclonal anti-human signal transducer and activator of transcription 5 (STAT5) antibody, rabbit polyclonal anti-human phosphorylated STAT5 (Tyr 694 ) antibody, rabbit polyclonal anti-human PI3K antibody and rabbit polyclonal anti-human phosphorylated PI3K (Tyr 317 ) antibody were purchased from Bioss antibodies (Beijing, China).

    Techniques: Transfection, Control, Isolation, Quantitative RT-PCR, Binding Assay

    Gαi1/3 knockdown inhibits STAT5 activation, differentiation and growth by IL-5 in EoL-1 cells. Stable EoL-1 cells, expressing the scramble control shRNA (“C-shRNA”), Gαi1 shRNA and Gαi3 shRNA, were treated with GM-CSF (50 ng/mL) and IL-5 (50 ng/mL) for 24 hours, and were tested by Western blotting of listed proteins (A, E) . Relative expression of listed genes (24 hours after GM-CSF and IL-5 treatment) was shown (B, C) ; In each experiment, n=3 (three replicated wells). Cells were further cultured for the times indicated, cell proliferation were tested (F, G) , with cell viability tested by CCK-8 assay (D) . Bar = 100 μm. Blotting quantification was performed from five replicate blot data, data of all repeated experiments were pulled together to calculate mean ± SD. *P <0.05 (B, E, G) . *P <0.05 vs. “Control” treatment in “C-shRNA” EoL-1 cells (C) . # P <0.05 vs. GM-CSF and IL-5 treatment in “C-shRNA” EoL-1 cells (C) . *P <0.05 vs. “Control” treatment in “Gαi1/3-shRNA” EoL-1 cells (D) . #P <0.05 vs. GM-CSF and IL-5 treatment in “Gαi1/3-shRNA” EoL-1 cells (D) .

    Journal: Frontiers in Immunology

    Article Title: Gαi1/3 signaling mediates IL-5-induced eosinophil activation and type 2 inflammation in eosinophilic chronic rhinosinusitis

    doi: 10.3389/fimmu.2024.1460104

    Figure Lengend Snippet: Gαi1/3 knockdown inhibits STAT5 activation, differentiation and growth by IL-5 in EoL-1 cells. Stable EoL-1 cells, expressing the scramble control shRNA (“C-shRNA”), Gαi1 shRNA and Gαi3 shRNA, were treated with GM-CSF (50 ng/mL) and IL-5 (50 ng/mL) for 24 hours, and were tested by Western blotting of listed proteins (A, E) . Relative expression of listed genes (24 hours after GM-CSF and IL-5 treatment) was shown (B, C) ; In each experiment, n=3 (three replicated wells). Cells were further cultured for the times indicated, cell proliferation were tested (F, G) , with cell viability tested by CCK-8 assay (D) . Bar = 100 μm. Blotting quantification was performed from five replicate blot data, data of all repeated experiments were pulled together to calculate mean ± SD. *P <0.05 (B, E, G) . *P <0.05 vs. “Control” treatment in “C-shRNA” EoL-1 cells (C) . # P <0.05 vs. GM-CSF and IL-5 treatment in “C-shRNA” EoL-1 cells (C) . *P <0.05 vs. “Control” treatment in “Gαi1/3-shRNA” EoL-1 cells (D) . #P <0.05 vs. GM-CSF and IL-5 treatment in “Gαi1/3-shRNA” EoL-1 cells (D) .

    Article Snippet: Antibodies against Gαi1 (sc-13533), Gαi2 (sc-13534), Gαi3 (sc-365422), Gab1 (sc-133191), Akt (sc-81434), Erk1/2 (sc-514302), S6K (sc-8418), p-Gab1 (AP0256), p-Akt s473 (sc-101629), p-Erk1/2 (sc-136521), p-S6K (sc-8416), STAT5 (sc-74442), p-STAT5 (AP-0887), IL-5Rα (bs-2601R-100ul), IgE (ab75673), and tryptase (ab2378) were purchased from Bioss (Woburn, MA, USA), ABcolnal (Wuhan, China), Abcam (Cambridge, MA, USA), and Santa Cruz Biotechnology (Santa Cruz, CA, USA).

    Techniques: Knockdown, Activation Assay, Expressing, Control, shRNA, Western Blot, Cell Culture, CCK-8 Assay

    (A) Western blot analyses of JAK1, JAK2, as well as tyrosine phosphorylated STAT proteins in human pancreatic cancer cell lines ( n = 9) and untransformed pancreatic cells (HPNE). Beta-actin (ACTB) and GAPDH served as loading controls; mouse pancreatic tumor cells treated with human growth hormone (hGH) and IL-4 served as controls for the activation of STAT5 and STAT6, respectively (b and c). Western blots are representative of three experimental replicates used for quantitative analysis in . (B) Quantitative analysis of nuclear STAT3 expression in primary human pancreatic cancers ( n = 28) and normal tissues ( n = 17). The right panel shows representative immunofluorescent (IF) images of normal and tumor tissues co-stained for tyrosine phosphorylated STAT3 (pSTAT3) and pan-cytokeratin (panCK). Slides were counterstained with DAPI; bars, 40 μm.

    Journal: Cell reports

    Article Title: The Janus kinase 1 is critical for pancreatic cancer initiation and progression

    doi: 10.1016/j.celrep.2024.114202

    Figure Lengend Snippet: (A) Western blot analyses of JAK1, JAK2, as well as tyrosine phosphorylated STAT proteins in human pancreatic cancer cell lines ( n = 9) and untransformed pancreatic cells (HPNE). Beta-actin (ACTB) and GAPDH served as loading controls; mouse pancreatic tumor cells treated with human growth hormone (hGH) and IL-4 served as controls for the activation of STAT5 and STAT6, respectively (b and c). Western blots are representative of three experimental replicates used for quantitative analysis in . (B) Quantitative analysis of nuclear STAT3 expression in primary human pancreatic cancers ( n = 28) and normal tissues ( n = 17). The right panel shows representative immunofluorescent (IF) images of normal and tumor tissues co-stained for tyrosine phosphorylated STAT3 (pSTAT3) and pan-cytokeratin (panCK). Slides were counterstained with DAPI; bars, 40 μm.

    Article Snippet: Rabbit polyclonal, STAT5 , Santa Cruz , Cat#sc-836; RRID:AB_632445.

    Techniques: Western Blot, Activation Assay, Expressing, Staining

    KEY RESOURCES TABLE

    Journal: Cell reports

    Article Title: The Janus kinase 1 is critical for pancreatic cancer initiation and progression

    doi: 10.1016/j.celrep.2024.114202

    Figure Lengend Snippet: KEY RESOURCES TABLE

    Article Snippet: Rabbit polyclonal, STAT5 , Santa Cruz , Cat#sc-836; RRID:AB_632445.

    Techniques: Recombinant, Transduction, Polymer, Virus, Western Blot, Software