yeast adh  (Worthington Biochemical)


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    Worthington Biochemical yeast adh
    Yeast Adh, supplied by Worthington Biochemical, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    yeast adh  (Worthington Biochemical)


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    Worthington Biochemical yeast adh
    Yeast Adh, supplied by Worthington Biochemical, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 93 stars, based on 1 article reviews
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    yeast adh  (Worthington Biochemical)


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    Worthington Biochemical yeast adh
    Yeast Adh, supplied by Worthington Biochemical, 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/yeast adh/product/Worthington Biochemical
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    adh  (Worthington Biochemical)


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    Worthington Biochemical adh
    Adh, supplied by Worthington Biochemical, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    alcohol dehydrogenase adh  (Worthington Biochemical)


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    Worthington Biochemical alcohol dehydrogenase adh
    Alcohol Dehydrogenase Adh, supplied by Worthington Biochemical, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    alcohol dehydrogenase adh  (Worthington Biochemical)


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    Worthington Biochemical alcohol dehydrogenase adh
    Alcohol Dehydrogenase Adh, supplied by Worthington Biochemical, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/alcohol dehydrogenase adh/product/Worthington Biochemical
    Average 93 stars, based on 1 article reviews
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    adh assay  (Worthington Biochemical)


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    Worthington Biochemical adh assay
    Adh Assay, supplied by Worthington Biochemical, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/adh assay/product/Worthington Biochemical
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
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    adh assay  (Worthington Biochemical)


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    Worthington Biochemical adh assay
    Validation of LC-MSE identified PRPs by Western blotting. Protein lysate of Control (CK) and diabetic (DK) rat kidney was digested with trypsin, and separated on SDS-PAGE, followed by immunoblotting with antibodies against GAPDH, HSP <t>60,</t> <t>SOD,</t> GST, LDH, and <t>ADH.</t> Presence of these proteins in DK after trypsin digestion confirmed the identification of PRPs by mass spectrometry. The experiment was repeated independently three times.
    Adh Assay, supplied by Worthington Biochemical, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/adh assay/product/Worthington Biochemical
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    adh assay - by Bioz Stars, 2023-03
    86/100 stars

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    1) Product Images from "Proteomic Analysis of Protease Resistant Proteins in the Diabetic Rat Kidney "

    Article Title: Proteomic Analysis of Protease Resistant Proteins in the Diabetic Rat Kidney

    Journal: Molecular & Cellular Proteomics : MCP

    doi: 10.1074/mcp.M112.020651

    Validation of LC-MSE identified PRPs by Western blotting. Protein lysate of Control (CK) and diabetic (DK) rat kidney was digested with trypsin, and separated on SDS-PAGE, followed by immunoblotting with antibodies against GAPDH, HSP 60, SOD, GST, LDH, and ADH. Presence of these proteins in DK after trypsin digestion confirmed the identification of PRPs by mass spectrometry. The experiment was repeated independently three times.
    Figure Legend Snippet: Validation of LC-MSE identified PRPs by Western blotting. Protein lysate of Control (CK) and diabetic (DK) rat kidney was digested with trypsin, and separated on SDS-PAGE, followed by immunoblotting with antibodies against GAPDH, HSP 60, SOD, GST, LDH, and ADH. Presence of these proteins in DK after trypsin digestion confirmed the identification of PRPs by mass spectrometry. The experiment was repeated independently three times.

    Techniques Used: Western Blot, SDS Page, Mass Spectrometry

    Functional assays of identified PRPs. The enzymatic activities of A, SOD, B, LDH, C, ADH, and D, GST were analyzed for control (CK) and diabetic (DK) rat kidney protein lysate using protocols described in supplemental method S1. In DK, significant reduction in enzymatic activity was observed. Bars represent means ± S.E. from three independent experiments. *p < 0.05.
    Figure Legend Snippet: Functional assays of identified PRPs. The enzymatic activities of A, SOD, B, LDH, C, ADH, and D, GST were analyzed for control (CK) and diabetic (DK) rat kidney protein lysate using protocols described in supplemental method S1. In DK, significant reduction in enzymatic activity was observed. Bars represent means ± S.E. from three independent experiments. *p < 0.05.

    Techniques Used: Functional Assay, Activity Assay

    Prediction of aggregation prone regions. Protein structures of rat GAPDH, HSP 60, SOD, GST, LDH and ADH were modeled by CPH 3.0 model server and analyzed using PyMol. Aggregation prone regions in these proteins were predicted in silico using Aggrescan, Tango, PASTA, and Waltz web servers (blue color). The regions common to aggregation prone sequences and glycation sites were highlighted in the red color, indicating that most of the glycation sites were overlapping with predicted aggregation hotspots.
    Figure Legend Snippet: Prediction of aggregation prone regions. Protein structures of rat GAPDH, HSP 60, SOD, GST, LDH and ADH were modeled by CPH 3.0 model server and analyzed using PyMol. Aggregation prone regions in these proteins were predicted in silico using Aggrescan, Tango, PASTA, and Waltz web servers (blue color). The regions common to aggregation prone sequences and glycation sites were highlighted in the red color, indicating that most of the glycation sites were overlapping with predicted aggregation hotspots.

    Techniques Used: In Silico

    Expression analysis of PRPs. A, Protein expression of GAPDH, HSP 60, SOD, GST, LDH, and ADH in control (CK) and diabetic (DK) rat kidney was measured by the Western blot analysis. B, The same proteins were analyzed at the transcript level by performing semi-quantitative RT-PCR using total RNA isolated from control and diabetic rat kidney tissues. All samples were analyzed on 2% agarose gels containing gel red. Both analyses showed up-regulation of PRPs in diabetic condition. Results shown are representative of three independent experiments.
    Figure Legend Snippet: Expression analysis of PRPs. A, Protein expression of GAPDH, HSP 60, SOD, GST, LDH, and ADH in control (CK) and diabetic (DK) rat kidney was measured by the Western blot analysis. B, The same proteins were analyzed at the transcript level by performing semi-quantitative RT-PCR using total RNA isolated from control and diabetic rat kidney tissues. All samples were analyzed on 2% agarose gels containing gel red. Both analyses showed up-regulation of PRPs in diabetic condition. Results shown are representative of three independent experiments.

    Techniques Used: Expressing, Western Blot, Quantitative RT-PCR, Isolation

    adh assay  (Worthington Biochemical)


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    Worthington Biochemical adh assay
    Validation of LC-MSE identified PRPs by Western blotting. Protein lysate of Control (CK) and diabetic (DK) rat kidney was digested with trypsin, and separated on SDS-PAGE, followed by immunoblotting with antibodies against GAPDH, HSP <t>60,</t> <t>SOD,</t> GST, LDH, and <t>ADH.</t> Presence of these proteins in DK after trypsin digestion confirmed the identification of PRPs by mass spectrometry. The experiment was repeated independently three times.
    Adh Assay, supplied by Worthington Biochemical, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/adh assay/product/Worthington Biochemical
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    adh assay - by Bioz Stars, 2023-03
    86/100 stars

    Images

    1) Product Images from "Proteomic Analysis of Protease Resistant Proteins in the Diabetic Rat Kidney "

    Article Title: Proteomic Analysis of Protease Resistant Proteins in the Diabetic Rat Kidney

    Journal: Molecular & Cellular Proteomics : MCP

    doi: 10.1074/mcp.M112.020651

    Validation of LC-MSE identified PRPs by Western blotting. Protein lysate of Control (CK) and diabetic (DK) rat kidney was digested with trypsin, and separated on SDS-PAGE, followed by immunoblotting with antibodies against GAPDH, HSP 60, SOD, GST, LDH, and ADH. Presence of these proteins in DK after trypsin digestion confirmed the identification of PRPs by mass spectrometry. The experiment was repeated independently three times.
    Figure Legend Snippet: Validation of LC-MSE identified PRPs by Western blotting. Protein lysate of Control (CK) and diabetic (DK) rat kidney was digested with trypsin, and separated on SDS-PAGE, followed by immunoblotting with antibodies against GAPDH, HSP 60, SOD, GST, LDH, and ADH. Presence of these proteins in DK after trypsin digestion confirmed the identification of PRPs by mass spectrometry. The experiment was repeated independently three times.

    Techniques Used: Western Blot, SDS Page, Mass Spectrometry

    Functional assays of identified PRPs. The enzymatic activities of A, SOD, B, LDH, C, ADH, and D, GST were analyzed for control (CK) and diabetic (DK) rat kidney protein lysate using protocols described in supplemental method S1. In DK, significant reduction in enzymatic activity was observed. Bars represent means ± S.E. from three independent experiments. *p < 0.05.
    Figure Legend Snippet: Functional assays of identified PRPs. The enzymatic activities of A, SOD, B, LDH, C, ADH, and D, GST were analyzed for control (CK) and diabetic (DK) rat kidney protein lysate using protocols described in supplemental method S1. In DK, significant reduction in enzymatic activity was observed. Bars represent means ± S.E. from three independent experiments. *p < 0.05.

    Techniques Used: Functional Assay, Activity Assay

    Prediction of aggregation prone regions. Protein structures of rat GAPDH, HSP 60, SOD, GST, LDH and ADH were modeled by CPH 3.0 model server and analyzed using PyMol. Aggregation prone regions in these proteins were predicted in silico using Aggrescan, Tango, PASTA, and Waltz web servers (blue color). The regions common to aggregation prone sequences and glycation sites were highlighted in the red color, indicating that most of the glycation sites were overlapping with predicted aggregation hotspots.
    Figure Legend Snippet: Prediction of aggregation prone regions. Protein structures of rat GAPDH, HSP 60, SOD, GST, LDH and ADH were modeled by CPH 3.0 model server and analyzed using PyMol. Aggregation prone regions in these proteins were predicted in silico using Aggrescan, Tango, PASTA, and Waltz web servers (blue color). The regions common to aggregation prone sequences and glycation sites were highlighted in the red color, indicating that most of the glycation sites were overlapping with predicted aggregation hotspots.

    Techniques Used: In Silico

    Expression analysis of PRPs. A, Protein expression of GAPDH, HSP 60, SOD, GST, LDH, and ADH in control (CK) and diabetic (DK) rat kidney was measured by the Western blot analysis. B, The same proteins were analyzed at the transcript level by performing semi-quantitative RT-PCR using total RNA isolated from control and diabetic rat kidney tissues. All samples were analyzed on 2% agarose gels containing gel red. Both analyses showed up-regulation of PRPs in diabetic condition. Results shown are representative of three independent experiments.
    Figure Legend Snippet: Expression analysis of PRPs. A, Protein expression of GAPDH, HSP 60, SOD, GST, LDH, and ADH in control (CK) and diabetic (DK) rat kidney was measured by the Western blot analysis. B, The same proteins were analyzed at the transcript level by performing semi-quantitative RT-PCR using total RNA isolated from control and diabetic rat kidney tissues. All samples were analyzed on 2% agarose gels containing gel red. Both analyses showed up-regulation of PRPs in diabetic condition. Results shown are representative of three independent experiments.

    Techniques Used: Expressing, Western Blot, Quantitative RT-PCR, Isolation

    adh assay  (Worthington Biochemical)


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    Structured Review

    Worthington Biochemical adh assay
    Validation of LC-MSE identified PRPs by Western blotting. Protein lysate of Control (CK) and diabetic (DK) rat kidney was digested with trypsin, and separated on SDS-PAGE, followed by immunoblotting with antibodies against GAPDH, HSP <t>60,</t> <t>SOD,</t> GST, LDH, and <t>ADH.</t> Presence of these proteins in DK after trypsin digestion confirmed the identification of PRPs by mass spectrometry. The experiment was repeated independently three times.
    Adh Assay, supplied by Worthington Biochemical, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/adh assay/product/Worthington Biochemical
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    adh assay - by Bioz Stars, 2023-03
    86/100 stars

    Images

    1) Product Images from "Proteomic Analysis of Protease Resistant Proteins in the Diabetic Rat Kidney "

    Article Title: Proteomic Analysis of Protease Resistant Proteins in the Diabetic Rat Kidney

    Journal: Molecular & Cellular Proteomics : MCP

    doi: 10.1074/mcp.M112.020651

    Validation of LC-MSE identified PRPs by Western blotting. Protein lysate of Control (CK) and diabetic (DK) rat kidney was digested with trypsin, and separated on SDS-PAGE, followed by immunoblotting with antibodies against GAPDH, HSP 60, SOD, GST, LDH, and ADH. Presence of these proteins in DK after trypsin digestion confirmed the identification of PRPs by mass spectrometry. The experiment was repeated independently three times.
    Figure Legend Snippet: Validation of LC-MSE identified PRPs by Western blotting. Protein lysate of Control (CK) and diabetic (DK) rat kidney was digested with trypsin, and separated on SDS-PAGE, followed by immunoblotting with antibodies against GAPDH, HSP 60, SOD, GST, LDH, and ADH. Presence of these proteins in DK after trypsin digestion confirmed the identification of PRPs by mass spectrometry. The experiment was repeated independently three times.

    Techniques Used: Western Blot, SDS Page, Mass Spectrometry

    Functional assays of identified PRPs. The enzymatic activities of A, SOD, B, LDH, C, ADH, and D, GST were analyzed for control (CK) and diabetic (DK) rat kidney protein lysate using protocols described in supplemental method S1. In DK, significant reduction in enzymatic activity was observed. Bars represent means ± S.E. from three independent experiments. *p < 0.05.
    Figure Legend Snippet: Functional assays of identified PRPs. The enzymatic activities of A, SOD, B, LDH, C, ADH, and D, GST were analyzed for control (CK) and diabetic (DK) rat kidney protein lysate using protocols described in supplemental method S1. In DK, significant reduction in enzymatic activity was observed. Bars represent means ± S.E. from three independent experiments. *p < 0.05.

    Techniques Used: Functional Assay, Activity Assay

    Prediction of aggregation prone regions. Protein structures of rat GAPDH, HSP 60, SOD, GST, LDH and ADH were modeled by CPH 3.0 model server and analyzed using PyMol. Aggregation prone regions in these proteins were predicted in silico using Aggrescan, Tango, PASTA, and Waltz web servers (blue color). The regions common to aggregation prone sequences and glycation sites were highlighted in the red color, indicating that most of the glycation sites were overlapping with predicted aggregation hotspots.
    Figure Legend Snippet: Prediction of aggregation prone regions. Protein structures of rat GAPDH, HSP 60, SOD, GST, LDH and ADH were modeled by CPH 3.0 model server and analyzed using PyMol. Aggregation prone regions in these proteins were predicted in silico using Aggrescan, Tango, PASTA, and Waltz web servers (blue color). The regions common to aggregation prone sequences and glycation sites were highlighted in the red color, indicating that most of the glycation sites were overlapping with predicted aggregation hotspots.

    Techniques Used: In Silico

    Expression analysis of PRPs. A, Protein expression of GAPDH, HSP 60, SOD, GST, LDH, and ADH in control (CK) and diabetic (DK) rat kidney was measured by the Western blot analysis. B, The same proteins were analyzed at the transcript level by performing semi-quantitative RT-PCR using total RNA isolated from control and diabetic rat kidney tissues. All samples were analyzed on 2% agarose gels containing gel red. Both analyses showed up-regulation of PRPs in diabetic condition. Results shown are representative of three independent experiments.
    Figure Legend Snippet: Expression analysis of PRPs. A, Protein expression of GAPDH, HSP 60, SOD, GST, LDH, and ADH in control (CK) and diabetic (DK) rat kidney was measured by the Western blot analysis. B, The same proteins were analyzed at the transcript level by performing semi-quantitative RT-PCR using total RNA isolated from control and diabetic rat kidney tissues. All samples were analyzed on 2% agarose gels containing gel red. Both analyses showed up-regulation of PRPs in diabetic condition. Results shown are representative of three independent experiments.

    Techniques Used: Expressing, Western Blot, Quantitative RT-PCR, Isolation

    adh assay  (Worthington Biochemical)


    Bioz Verified Symbol Worthington Biochemical is a verified supplier
    Bioz Manufacturer Symbol Worthington Biochemical manufactures this product  
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    Structured Review

    Worthington Biochemical adh assay
    Validation of LC-MSE identified PRPs by Western blotting. Protein lysate of Control (CK) and diabetic (DK) rat kidney was digested with trypsin, and separated on SDS-PAGE, followed by immunoblotting with antibodies against GAPDH, HSP <t>60,</t> <t>SOD,</t> GST, LDH, and <t>ADH.</t> Presence of these proteins in DK after trypsin digestion confirmed the identification of PRPs by mass spectrometry. The experiment was repeated independently three times.
    Adh Assay, supplied by Worthington Biochemical, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/adh assay/product/Worthington Biochemical
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    adh assay - by Bioz Stars, 2023-03
    86/100 stars

    Images

    1) Product Images from "Proteomic Analysis of Protease Resistant Proteins in the Diabetic Rat Kidney "

    Article Title: Proteomic Analysis of Protease Resistant Proteins in the Diabetic Rat Kidney

    Journal: Molecular & Cellular Proteomics : MCP

    doi: 10.1074/mcp.M112.020651

    Validation of LC-MSE identified PRPs by Western blotting. Protein lysate of Control (CK) and diabetic (DK) rat kidney was digested with trypsin, and separated on SDS-PAGE, followed by immunoblotting with antibodies against GAPDH, HSP 60, SOD, GST, LDH, and ADH. Presence of these proteins in DK after trypsin digestion confirmed the identification of PRPs by mass spectrometry. The experiment was repeated independently three times.
    Figure Legend Snippet: Validation of LC-MSE identified PRPs by Western blotting. Protein lysate of Control (CK) and diabetic (DK) rat kidney was digested with trypsin, and separated on SDS-PAGE, followed by immunoblotting with antibodies against GAPDH, HSP 60, SOD, GST, LDH, and ADH. Presence of these proteins in DK after trypsin digestion confirmed the identification of PRPs by mass spectrometry. The experiment was repeated independently three times.

    Techniques Used: Western Blot, SDS Page, Mass Spectrometry

    Functional assays of identified PRPs. The enzymatic activities of A, SOD, B, LDH, C, ADH, and D, GST were analyzed for control (CK) and diabetic (DK) rat kidney protein lysate using protocols described in supplemental method S1. In DK, significant reduction in enzymatic activity was observed. Bars represent means ± S.E. from three independent experiments. *p < 0.05.
    Figure Legend Snippet: Functional assays of identified PRPs. The enzymatic activities of A, SOD, B, LDH, C, ADH, and D, GST were analyzed for control (CK) and diabetic (DK) rat kidney protein lysate using protocols described in supplemental method S1. In DK, significant reduction in enzymatic activity was observed. Bars represent means ± S.E. from three independent experiments. *p < 0.05.

    Techniques Used: Functional Assay, Activity Assay

    Prediction of aggregation prone regions. Protein structures of rat GAPDH, HSP 60, SOD, GST, LDH and ADH were modeled by CPH 3.0 model server and analyzed using PyMol. Aggregation prone regions in these proteins were predicted in silico using Aggrescan, Tango, PASTA, and Waltz web servers (blue color). The regions common to aggregation prone sequences and glycation sites were highlighted in the red color, indicating that most of the glycation sites were overlapping with predicted aggregation hotspots.
    Figure Legend Snippet: Prediction of aggregation prone regions. Protein structures of rat GAPDH, HSP 60, SOD, GST, LDH and ADH were modeled by CPH 3.0 model server and analyzed using PyMol. Aggregation prone regions in these proteins were predicted in silico using Aggrescan, Tango, PASTA, and Waltz web servers (blue color). The regions common to aggregation prone sequences and glycation sites were highlighted in the red color, indicating that most of the glycation sites were overlapping with predicted aggregation hotspots.

    Techniques Used: In Silico

    Expression analysis of PRPs. A, Protein expression of GAPDH, HSP 60, SOD, GST, LDH, and ADH in control (CK) and diabetic (DK) rat kidney was measured by the Western blot analysis. B, The same proteins were analyzed at the transcript level by performing semi-quantitative RT-PCR using total RNA isolated from control and diabetic rat kidney tissues. All samples were analyzed on 2% agarose gels containing gel red. Both analyses showed up-regulation of PRPs in diabetic condition. Results shown are representative of three independent experiments.
    Figure Legend Snippet: Expression analysis of PRPs. A, Protein expression of GAPDH, HSP 60, SOD, GST, LDH, and ADH in control (CK) and diabetic (DK) rat kidney was measured by the Western blot analysis. B, The same proteins were analyzed at the transcript level by performing semi-quantitative RT-PCR using total RNA isolated from control and diabetic rat kidney tissues. All samples were analyzed on 2% agarose gels containing gel red. Both analyses showed up-regulation of PRPs in diabetic condition. Results shown are representative of three independent experiments.

    Techniques Used: Expressing, Western Blot, Quantitative RT-PCR, Isolation

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