adh  (Worthington Biochemical)


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    Structured Review

    Worthington Biochemical adh
    Comparison of anti-aggregation activities of wild-type <t>αA-crystallin,</t> αAΔ70–76 and αAΔ70–88 using <t>ADH,</t> β L -crystallin and CS as substrates Aggregation of ADH (0.25 mg/ml) was induced at 37 °C by phosphate buffer containing 100 mM EDTA (pH 7.3). Aggregation assays with β L -crystallin (0.25 mg/ml PBS) were performed at 55 °C, and aggregation assays of the CS sample (0.075 mg/ml 40 mM HEPES-NaOH buffer, pH 7.3) were performed at 43 °C. The percentage of substrate proteins aggregated in the presence of various concentrations of wild-type and mutant proteins at the 45 min time point of assay was calculated and plotted. The aggregation of substrate protein in the absence of chaperone protein was considered 100% aggregation.
    Adh, supplied by Worthington Biochemical, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/adh/product/Worthington Biochemical
    Average 91 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    adh - by Bioz Stars, 2020-08
    91/100 stars

    Images

    1) Product Images from "Structural and Functional Consequences of Chaperone Site Deletion in αA-Crystallin"

    Article Title: Structural and Functional Consequences of Chaperone Site Deletion in αA-Crystallin

    Journal: Biochimica et biophysica acta

    doi: 10.1016/j.bbapap.2016.08.006

    Comparison of anti-aggregation activities of wild-type αA-crystallin, αAΔ70–76 and αAΔ70–88 using ADH, β L -crystallin and CS as substrates Aggregation of ADH (0.25 mg/ml) was induced at 37 °C by phosphate buffer containing 100 mM EDTA (pH 7.3). Aggregation assays with β L -crystallin (0.25 mg/ml PBS) were performed at 55 °C, and aggregation assays of the CS sample (0.075 mg/ml 40 mM HEPES-NaOH buffer, pH 7.3) were performed at 43 °C. The percentage of substrate proteins aggregated in the presence of various concentrations of wild-type and mutant proteins at the 45 min time point of assay was calculated and plotted. The aggregation of substrate protein in the absence of chaperone protein was considered 100% aggregation.
    Figure Legend Snippet: Comparison of anti-aggregation activities of wild-type αA-crystallin, αAΔ70–76 and αAΔ70–88 using ADH, β L -crystallin and CS as substrates Aggregation of ADH (0.25 mg/ml) was induced at 37 °C by phosphate buffer containing 100 mM EDTA (pH 7.3). Aggregation assays with β L -crystallin (0.25 mg/ml PBS) were performed at 55 °C, and aggregation assays of the CS sample (0.075 mg/ml 40 mM HEPES-NaOH buffer, pH 7.3) were performed at 43 °C. The percentage of substrate proteins aggregated in the presence of various concentrations of wild-type and mutant proteins at the 45 min time point of assay was calculated and plotted. The aggregation of substrate protein in the absence of chaperone protein was considered 100% aggregation.

    Techniques Used: Mutagenesis

    Related Articles

    Mutagenesis:

    Article Title: Deletion of 54FLRAPSWF61 Residues Decreases the Oligomeric Size and Enhances the Chaperone Function of ?B-Crystallin
    Article Snippet: .. Chaperone-like activity of wild-type αB and the deletion mutant was compared using alcohol dehydrogenase (ADH) (Worthington) and CS (Sigma) substrates, as described previously ( , ). .. Aggregation of substrate proteins was monitored by measuring light scattering at 360 nm in the presence of various amounts of wild-type and mutant proteins as a function of time, using a Shimadzu spectrophotometer equipped with a temperature-regulated multicell holder.

    Activity Assay:

    Article Title: Structural and Functional Consequences of Chaperone Site Deletion in αA-Crystallin
    Article Snippet: .. The chaperone activity of wild-type αA-crystallin and deletion mutants was measured using different substrates, such as ADH (Worthington), Citrate Synthase (CS) (Sigma) and βL -crystallin (purified in the lab from bovine lens). .. Protein aggregation was measured by monitoring the light scattering at 360 nm in Shimadzu UV-VIS spectrophotometer equipped with a temperature-controlled multi-cell transporter.

    Article Title: Metabolic Flux Control at the Pyruvate Node in an Anaerobic Escherichia coli Strain with an Active Pyruvate Dehydrogenase ▿
    Article Snippet: .. ADH-E activity was assayed by measuring the increase in absorbance at 340 nm resulting from the reduction of NAD+ in the presence of ethanol (ADH assay; Worthington Biochemical Corporation). ..

    Article Title: Deletion of 54FLRAPSWF61 Residues Decreases the Oligomeric Size and Enhances the Chaperone Function of ?B-Crystallin
    Article Snippet: .. Chaperone-like activity of wild-type αB and the deletion mutant was compared using alcohol dehydrogenase (ADH) (Worthington) and CS (Sigma) substrates, as described previously ( , ). .. Aggregation of substrate proteins was monitored by measuring light scattering at 360 nm in the presence of various amounts of wild-type and mutant proteins as a function of time, using a Shimadzu spectrophotometer equipped with a temperature-regulated multicell holder.

    Purification:

    Article Title: Structural and Functional Consequences of Chaperone Site Deletion in αA-Crystallin
    Article Snippet: .. The chaperone activity of wild-type αA-crystallin and deletion mutants was measured using different substrates, such as ADH (Worthington), Citrate Synthase (CS) (Sigma) and βL -crystallin (purified in the lab from bovine lens). .. Protein aggregation was measured by monitoring the light scattering at 360 nm in Shimadzu UV-VIS spectrophotometer equipped with a temperature-controlled multi-cell transporter.

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    Worthington Biochemical alcohol dehydrogenase adh
    Subunit exchange studies of wild-type <t>αB-crystallin</t> and αB-Δ54–61 in the presence and absence of <t>ADH.</t> The labeled proteins were mixed in equal amounts (25 µg) in a total volume of 250 µL of phosphate buffer.
    Alcohol Dehydrogenase Adh, supplied by Worthington Biochemical, used in various techniques. Bioz Stars score: 90/100, 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 90 stars, based on 1 article reviews
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    alcohol dehydrogenase adh - by Bioz Stars, 2020-08
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    91
    Worthington Biochemical adh
    Comparison of anti-aggregation activities of wild-type <t>αA-crystallin,</t> αAΔ70–76 and αAΔ70–88 using <t>ADH,</t> β L -crystallin and CS as substrates Aggregation of ADH (0.25 mg/ml) was induced at 37 °C by phosphate buffer containing 100 mM EDTA (pH 7.3). Aggregation assays with β L -crystallin (0.25 mg/ml PBS) were performed at 55 °C, and aggregation assays of the CS sample (0.075 mg/ml 40 mM HEPES-NaOH buffer, pH 7.3) were performed at 43 °C. The percentage of substrate proteins aggregated in the presence of various concentrations of wild-type and mutant proteins at the 45 min time point of assay was calculated and plotted. The aggregation of substrate protein in the absence of chaperone protein was considered 100% aggregation.
    Adh, supplied by Worthington Biochemical, used in various techniques. Bioz Stars score: 91/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/adh/product/Worthington Biochemical
    Average 91 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    adh - by Bioz Stars, 2020-08
    91/100 stars
      Buy from Supplier

    Image Search Results


    Subunit exchange studies of wild-type αB-crystallin and αB-Δ54–61 in the presence and absence of ADH. The labeled proteins were mixed in equal amounts (25 µg) in a total volume of 250 µL of phosphate buffer.

    Journal: Biochemistry

    Article Title: Deletion of 54FLRAPSWF61 Residues Decreases the Oligomeric Size and Enhances the Chaperone Function of ?B-Crystallin

    doi: 10.1021/bi900085v

    Figure Lengend Snippet: Subunit exchange studies of wild-type αB-crystallin and αB-Δ54–61 in the presence and absence of ADH. The labeled proteins were mixed in equal amounts (25 µg) in a total volume of 250 µL of phosphate buffer.

    Article Snippet: Chaperone-like activity of wild-type αB and the deletion mutant was compared using alcohol dehydrogenase (ADH) (Worthington) and CS (Sigma) substrates, as described previously ( , ).

    Techniques: Labeling

    Molar mass distribution of wild-type αB-ADH(solid line, filled circle) and αB-Δ54–61-ADH (broken line, open circle). Crystallins and the ADH in equal concentration (50 µg) in phosphate buffer were incubated at 37

    Journal: Biochemistry

    Article Title: Deletion of 54FLRAPSWF61 Residues Decreases the Oligomeric Size and Enhances the Chaperone Function of ?B-Crystallin

    doi: 10.1021/bi900085v

    Figure Lengend Snippet: Molar mass distribution of wild-type αB-ADH(solid line, filled circle) and αB-Δ54–61-ADH (broken line, open circle). Crystallins and the ADH in equal concentration (50 µg) in phosphate buffer were incubated at 37

    Article Snippet: Chaperone-like activity of wild-type αB and the deletion mutant was compared using alcohol dehydrogenase (ADH) (Worthington) and CS (Sigma) substrates, as described previously ( , ).

    Techniques: Concentration Assay, Incubation

    Comparison of antiaggregation activities of αBΔ54–61 and wild-type αB-crystallins using ADH and CS as substrate proteins. Aggregation of ADH (250 µg) was induced at 37 °C by phosphate buffer containing100mMEDTA,

    Journal: Biochemistry

    Article Title: Deletion of 54FLRAPSWF61 Residues Decreases the Oligomeric Size and Enhances the Chaperone Function of ?B-Crystallin

    doi: 10.1021/bi900085v

    Figure Lengend Snippet: Comparison of antiaggregation activities of αBΔ54–61 and wild-type αB-crystallins using ADH and CS as substrate proteins. Aggregation of ADH (250 µg) was induced at 37 °C by phosphate buffer containing100mMEDTA,

    Article Snippet: Chaperone-like activity of wild-type αB and the deletion mutant was compared using alcohol dehydrogenase (ADH) (Worthington) and CS (Sigma) substrates, as described previously ( , ).

    Techniques:

    Comparison of anti-aggregation activities of wild-type αA-crystallin, αAΔ70–76 and αAΔ70–88 using ADH, β L -crystallin and CS as substrates Aggregation of ADH (0.25 mg/ml) was induced at 37 °C by phosphate buffer containing 100 mM EDTA (pH 7.3). Aggregation assays with β L -crystallin (0.25 mg/ml PBS) were performed at 55 °C, and aggregation assays of the CS sample (0.075 mg/ml 40 mM HEPES-NaOH buffer, pH 7.3) were performed at 43 °C. The percentage of substrate proteins aggregated in the presence of various concentrations of wild-type and mutant proteins at the 45 min time point of assay was calculated and plotted. The aggregation of substrate protein in the absence of chaperone protein was considered 100% aggregation.

    Journal: Biochimica et biophysica acta

    Article Title: Structural and Functional Consequences of Chaperone Site Deletion in αA-Crystallin

    doi: 10.1016/j.bbapap.2016.08.006

    Figure Lengend Snippet: Comparison of anti-aggregation activities of wild-type αA-crystallin, αAΔ70–76 and αAΔ70–88 using ADH, β L -crystallin and CS as substrates Aggregation of ADH (0.25 mg/ml) was induced at 37 °C by phosphate buffer containing 100 mM EDTA (pH 7.3). Aggregation assays with β L -crystallin (0.25 mg/ml PBS) were performed at 55 °C, and aggregation assays of the CS sample (0.075 mg/ml 40 mM HEPES-NaOH buffer, pH 7.3) were performed at 43 °C. The percentage of substrate proteins aggregated in the presence of various concentrations of wild-type and mutant proteins at the 45 min time point of assay was calculated and plotted. The aggregation of substrate protein in the absence of chaperone protein was considered 100% aggregation.

    Article Snippet: The chaperone activity of wild-type αA-crystallin and deletion mutants was measured using different substrates, such as ADH (Worthington), Citrate Synthase (CS) (Sigma) and βL -crystallin (purified in the lab from bovine lens).

    Techniques: Mutagenesis