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k 4700 1kit  (Echelon Biosciences)


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    Structured Review

    Echelon Biosciences k 4700 1kit
    K 4700 1kit, supplied by Echelon Biosciences, 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/k 4700 1kit/product/Echelon Biosciences
    Average 94 stars, based on 1 article reviews
    k 4700 1kit - by Bioz Stars, 2025-02
    94/100 stars

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    Echelon Biosciences pten activity
    <t>PTEN</t> <t>phosphatase</t> activity by measurement of phosphate production for the assessment of the interaction between myo‐inositol derivative and PTEN. (A) Dose–response curve for phosphate concentration measured by absorbance at 620 nm of molybdate green/orthophosphate complex formation. (B) Soluble PIP3 (125 × 10 −6 M) hydrolysis by PTEN (25 × 10 −6 to 100 × 10 −6 M) performed in the presence of variable concentrations (12.5 × 10 −3 to 50.0 × 10 −3 M) of ITPP. (C) Myo‐inositol derivative relative reactivity with PTEN. Soluble PIP3 (200 × 10 −6 M) hydrolysis by PTEN (50 × 10 −6 M) in the presence of variable concentrations (2.5 × 10 −3 to 40.0 × 10 −3 M) of ITPP, BPBPP or IHP. The data are the means of three separate experiments in triplicate. The data are the means ± SD of three separate experiments in triplicate, * p < 0.05, ** p < 0.01.
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    <t>PTEN</t> <t>phosphatase</t> activity by measurement of phosphate production for the assessment of the interaction between myo‐inositol derivative and PTEN. (A) Dose–response curve for phosphate concentration measured by absorbance at 620 nm of molybdate green/orthophosphate complex formation. (B) Soluble PIP3 (125 × 10 −6 M) hydrolysis by PTEN (25 × 10 −6 to 100 × 10 −6 M) performed in the presence of variable concentrations (12.5 × 10 −3 to 50.0 × 10 −3 M) of ITPP. (C) Myo‐inositol derivative relative reactivity with PTEN. Soluble PIP3 (200 × 10 −6 M) hydrolysis by PTEN (50 × 10 −6 M) in the presence of variable concentrations (2.5 × 10 −3 to 40.0 × 10 −3 M) of ITPP, BPBPP or IHP. The data are the means of three separate experiments in triplicate. The data are the means ± SD of three separate experiments in triplicate, * p < 0.05, ** p < 0.01.
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    <t>PTEN</t> <t>phosphatase</t> activity by measurement of phosphate production for the assessment of the interaction between myo‐inositol derivative and PTEN. (A) Dose–response curve for phosphate concentration measured by absorbance at 620 nm of molybdate green/orthophosphate complex formation. (B) Soluble PIP3 (125 × 10 −6 M) hydrolysis by PTEN (25 × 10 −6 to 100 × 10 −6 M) performed in the presence of variable concentrations (12.5 × 10 −3 to 50.0 × 10 −3 M) of ITPP. (C) Myo‐inositol derivative relative reactivity with PTEN. Soluble PIP3 (200 × 10 −6 M) hydrolysis by PTEN (50 × 10 −6 M) in the presence of variable concentrations (2.5 × 10 −3 to 40.0 × 10 −3 M) of ITPP, BPBPP or IHP. The data are the means of three separate experiments in triplicate. The data are the means ± SD of three separate experiments in triplicate, * p < 0.05, ** p < 0.01.
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    Echelon Biosciences elisa kit
    <t>PTEN</t> <t>phosphatase</t> activity by measurement of phosphate production for the assessment of the interaction between myo‐inositol derivative and PTEN. (A) Dose–response curve for phosphate concentration measured by absorbance at 620 nm of molybdate green/orthophosphate complex formation. (B) Soluble PIP3 (125 × 10 −6 M) hydrolysis by PTEN (25 × 10 −6 to 100 × 10 −6 M) performed in the presence of variable concentrations (12.5 × 10 −3 to 50.0 × 10 −3 M) of ITPP. (C) Myo‐inositol derivative relative reactivity with PTEN. Soluble PIP3 (200 × 10 −6 M) hydrolysis by PTEN (50 × 10 −6 M) in the presence of variable concentrations (2.5 × 10 −3 to 40.0 × 10 −3 M) of ITPP, BPBPP or IHP. The data are the means of three separate experiments in triplicate. The data are the means ± SD of three separate experiments in triplicate, * p < 0.05, ** p < 0.01.
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    PTEN phosphatase activity by measurement of phosphate production for the assessment of the interaction between myo‐inositol derivative and PTEN. (A) Dose–response curve for phosphate concentration measured by absorbance at 620 nm of molybdate green/orthophosphate complex formation. (B) Soluble PIP3 (125 × 10 −6 M) hydrolysis by PTEN (25 × 10 −6 to 100 × 10 −6 M) performed in the presence of variable concentrations (12.5 × 10 −3 to 50.0 × 10 −3 M) of ITPP. (C) Myo‐inositol derivative relative reactivity with PTEN. Soluble PIP3 (200 × 10 −6 M) hydrolysis by PTEN (50 × 10 −6 M) in the presence of variable concentrations (2.5 × 10 −3 to 40.0 × 10 −3 M) of ITPP, BPBPP or IHP. The data are the means of three separate experiments in triplicate. The data are the means ± SD of three separate experiments in triplicate, * p < 0.05, ** p < 0.01.

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: Tumour suppressor PTEN activity is differentially inducible by myo‐inositol phosphates

    doi: 10.1111/jcmm.17699

    Figure Lengend Snippet: PTEN phosphatase activity by measurement of phosphate production for the assessment of the interaction between myo‐inositol derivative and PTEN. (A) Dose–response curve for phosphate concentration measured by absorbance at 620 nm of molybdate green/orthophosphate complex formation. (B) Soluble PIP3 (125 × 10 −6 M) hydrolysis by PTEN (25 × 10 −6 to 100 × 10 −6 M) performed in the presence of variable concentrations (12.5 × 10 −3 to 50.0 × 10 −3 M) of ITPP. (C) Myo‐inositol derivative relative reactivity with PTEN. Soluble PIP3 (200 × 10 −6 M) hydrolysis by PTEN (50 × 10 −6 M) in the presence of variable concentrations (2.5 × 10 −3 to 40.0 × 10 −3 M) of ITPP, BPBPP or IHP. The data are the means of three separate experiments in triplicate. The data are the means ± SD of three separate experiments in triplicate, * p < 0.05, ** p < 0.01.

    Article Snippet: PTEN biochemical activity towards ITPP, BPBPP and IHP was assessed by an ELISA competition assay using the lipid Phosphatase Activity Assay to quantify PTEN activity (ELISA kit K‐4700, Echelon Biosciences, Salt Lake City, UT) following the manufacturer's protocol, designed to quantify the phosphatase activity of PTEN by the detection of the enzyme product, PI(4,5)P 2 .

    Techniques: Activity Assay, Concentration Assay

    (A, B) Effect of ITPP and BPBPP on PTEN phosphatase activity on PIP3 by measurement of PIP2 production. (A) Soluble PIP3 (5.0 × 10 −6 M) hydrolysis by PTEN (0.5 × 10 −6 M), performed in the presence of variable concentrations (0.1 × 10 −6 to 100.0 × 10 −6 M) of ITPP measured by anti‐PIP2 antibodies binding competition. (B) Soluble PIP3 (5.0 × 10 −6 M) hydrolysis by PTEN (0.5 × 10 −6 M) performed in the presence of variable concentrations (0.1 × 10 −6 to 100.0 × 10 −6 M) of BPBPP measured by anti‐PIP2 antibodies binding competition. The data are the means of three separate experiments in triplicate. The data are the means ± SD of three separate experiments in triplicate (* p < 0.05, ** p < 0.01). (C, D) Effect of ITPP and BPBPP on the activity of PI3‐Kinase on PIP2 by measuring PIP3 production. (C) Soluble PIP2 (5.0 × 10 −6 M) phosphorylation by PI3K (0.5 × 10 −6 M) was performed in the presence of variable concentrations (0.1 × 10 −6 to 100.0 × 10 −6 M) of ITPP measured by anti‐PIP3 antibodies binding competition. (D) Soluble PIP2 (5.0 × 10 −6 M) phosphorylation by PI3K (0.5 × 10 −6 M) performed in the presence of variable concentrations (0.1 × 10 −6 to 100.0 × 10 −6 M) of BPBPP measured by anti‐PIP3 antibodies binding competition. The data are the means of three separate experiments in triplicate.

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: Tumour suppressor PTEN activity is differentially inducible by myo‐inositol phosphates

    doi: 10.1111/jcmm.17699

    Figure Lengend Snippet: (A, B) Effect of ITPP and BPBPP on PTEN phosphatase activity on PIP3 by measurement of PIP2 production. (A) Soluble PIP3 (5.0 × 10 −6 M) hydrolysis by PTEN (0.5 × 10 −6 M), performed in the presence of variable concentrations (0.1 × 10 −6 to 100.0 × 10 −6 M) of ITPP measured by anti‐PIP2 antibodies binding competition. (B) Soluble PIP3 (5.0 × 10 −6 M) hydrolysis by PTEN (0.5 × 10 −6 M) performed in the presence of variable concentrations (0.1 × 10 −6 to 100.0 × 10 −6 M) of BPBPP measured by anti‐PIP2 antibodies binding competition. The data are the means of three separate experiments in triplicate. The data are the means ± SD of three separate experiments in triplicate (* p < 0.05, ** p < 0.01). (C, D) Effect of ITPP and BPBPP on the activity of PI3‐Kinase on PIP2 by measuring PIP3 production. (C) Soluble PIP2 (5.0 × 10 −6 M) phosphorylation by PI3K (0.5 × 10 −6 M) was performed in the presence of variable concentrations (0.1 × 10 −6 to 100.0 × 10 −6 M) of ITPP measured by anti‐PIP3 antibodies binding competition. (D) Soluble PIP2 (5.0 × 10 −6 M) phosphorylation by PI3K (0.5 × 10 −6 M) performed in the presence of variable concentrations (0.1 × 10 −6 to 100.0 × 10 −6 M) of BPBPP measured by anti‐PIP3 antibodies binding competition. The data are the means of three separate experiments in triplicate.

    Article Snippet: PTEN biochemical activity towards ITPP, BPBPP and IHP was assessed by an ELISA competition assay using the lipid Phosphatase Activity Assay to quantify PTEN activity (ELISA kit K‐4700, Echelon Biosciences, Salt Lake City, UT) following the manufacturer's protocol, designed to quantify the phosphatase activity of PTEN by the detection of the enzyme product, PI(4,5)P 2 .

    Techniques: Activity Assay, Binding Assay