alcohol dehydrogenase adh (Worthington Biochemical)

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Name:

Alcohol Dehydrogenase Lyophilized

Description:

Two times crystallized A lyophilized powder

Catalog Number:

ls001069

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Size:

100 mg

Source:

Yeast

Cas Number:

9031.72.5

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Structured Review

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.

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.

Two times crystallized A lyophilized powder
https://www.bioz.com/result/alcohol dehydrogenase adh/product/Worthington Biochemical
Average 90 stars, based on 236 article reviews
Price from $9.99 to $1999.99

alcohol dehydrogenase adh - by Bioz Stars, 2020-10

90/100 stars

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Images

1) Product Images from "Deletion of 54FLRAPSWF61 Residues Decreases the Oligomeric Size and Enhances the Chaperone Function of ?B-Crystallin"

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

Journal: Biochemistry

doi: 10.1021/bi900085v

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.

Figure Legend 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.

Techniques Used: 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

Figure Legend 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

Techniques Used: 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,

Figure Legend 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,

Techniques Used:

2) 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

3) Product Images from "Deletion of 54FLRAPSWF61 Residues Decreases the Oligomeric Size and Enhances the Chaperone Function of ?B-Crystallin"

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

Journal: Biochemistry

doi: 10.1021/bi900085v

Techniques Used: Labeling

Techniques Used: Concentration Assay, Incubation

Techniques Used:

Dynamic light scattering analysis of wild-type αB-crystallin (solid line, filled circle) and the αBΔ54–61 mutant (broken line, open circle). Proteins (0.15mg in 0.05mL) were incubated at 37 °C for 1 h prior to analysis.

Figure Legend Snippet: Dynamic light scattering analysis of wild-type αB-crystallin (solid line, filled circle) and the αBΔ54–61 mutant (broken line, open circle). Proteins (0.15mg in 0.05mL) were incubated at 37 °C for 1 h prior to analysis.

Techniques Used: Mutagenesis, Incubation

Transmission electron micrographs of wild-type and mutant αB-crystallins. A drop of 1 mg/mL protein was negatively stained with 2% uranyl acetate and observed under the JEOL 1200EX electron microscope. (A) Wild-type αB-crystallin; (B)

Figure Legend Snippet: Transmission electron micrographs of wild-type and mutant αB-crystallins. A drop of 1 mg/mL protein was negatively stained with 2% uranyl acetate and observed under the JEOL 1200EX electron microscope. (A) Wild-type αB-crystallin; (B)

Techniques Used: Transmission Assay, Mutagenesis, Staining, Microscopy

Spectroscopic characterization of wild-type αB-crystallin (solid line) and mutant αBΔ54–61 (broken line). (A) Tryptophan fluorescence intensity. Protein samples of 0.2 mg/mL in phosphate buffer were used. The excitation

Figure Legend Snippet: Spectroscopic characterization of wild-type αB-crystallin (solid line) and mutant αBΔ54–61 (broken line). (A) Tryptophan fluorescence intensity. Protein samples of 0.2 mg/mL in phosphate buffer were used. The excitation

Techniques Used: Mutagenesis, Fluorescence

Amino acid sequence of human αB-crystallin showing the deleted 54 FLRAPSWF 61 region: N-terminal domain (green shaded), α-crystallin domain (orange shaded), and C-terminal tail (yellow shaded). The putative αA-crystallin interacting

Figure Legend Snippet: Amino acid sequence of human αB-crystallin showing the deleted 54 FLRAPSWF 61 region: N-terminal domain (green shaded), α-crystallin domain (orange shaded), and C-terminal tail (yellow shaded). The putative αA-crystallin interacting

Techniques Used: Sequencing

4) 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

Techniques Used: Mutagenesis

Effect of deletion of 70–88 amino acids on the stability of αA-crystallin by equilibrium urea denaturation study Equilibrium urea unfolding profiles of wild-type αA-crystallin and αAΔ70–76 and αAΔ70–88 deletion mutants were obtained by plotting the ratio of tryptophan fluorescence emission at 337 nm and 350 nm with the excitation wavelength of 295 nm, at different urea concentrations at 25 °C. Protein solutions (0.1 mg/ml) were incubated with increasing concentrations of urea for recording the tryptophan fluorescence spectra. The data points are the average of three experiments.

Figure Legend Snippet: Effect of deletion of 70–88 amino acids on the stability of αA-crystallin by equilibrium urea denaturation study Equilibrium urea unfolding profiles of wild-type αA-crystallin and αAΔ70–76 and αAΔ70–88 deletion mutants were obtained by plotting the ratio of tryptophan fluorescence emission at 337 nm and 350 nm with the excitation wavelength of 295 nm, at different urea concentrations at 25 °C. Protein solutions (0.1 mg/ml) were incubated with increasing concentrations of urea for recording the tryptophan fluorescence spectra. The data points are the average of three experiments.

Techniques Used: Fluorescence, Incubation

Preparation of chaperone-site deletion mutants A, Amino acid sequence of human αA-crystallin showing the α-crystallin domain (blue shaded) flanked by the N-terminal region (red shaded) and a C-terminal tail (yellow shaded). The residues of the chaperone site that were deleted to generate α AΔ70–76 and αAΔ70–88 mutants are highlighted. B, Plasmid DNA sequencing confirming the deletion of nucleotides that code for the amino acids of the chaperone-site region. C, SDS-PAGE analysis of the proteins. Lane 1, molecular mass marker; lane 2, water-soluble extract of cells expressing αAΔ70–88; lane 3, urea-solubilized cell pellet from cells expressing α AΔ70–76; lane 4, purified αAΔ70–88; lane 5, purified αAΔ70–76; lane 6, purified wild-type protein. The bands above the crystallin bands in lanes 4, 5 and 6 are contaminants (

Figure Legend Snippet: Preparation of chaperone-site deletion mutants A, Amino acid sequence of human αA-crystallin showing the α-crystallin domain (blue shaded) flanked by the N-terminal region (red shaded) and a C-terminal tail (yellow shaded). The residues of the chaperone site that were deleted to generate α AΔ70–76 and αAΔ70–88 mutants are highlighted. B, Plasmid DNA sequencing confirming the deletion of nucleotides that code for the amino acids of the chaperone-site region. C, SDS-PAGE analysis of the proteins. Lane 1, molecular mass marker; lane 2, water-soluble extract of cells expressing αAΔ70–88; lane 3, urea-solubilized cell pellet from cells expressing α AΔ70–76; lane 4, purified αAΔ70–88; lane 5, purified αAΔ70–76; lane 6, purified wild-type protein. The bands above the crystallin bands in lanes 4, 5 and 6 are contaminants (

Techniques Used: Sequencing, Plasmid Preparation, DNA Sequencing, SDS Page, Marker, Expressing, Purification

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.

other:

Article Title: The YhhN Protein of Legionella Pneumophila is a Lysoplasmalogenase
Article Snippet: Yeast alcohol dehydrogenase ( ) was from Worthington Biochemical Corporation (Lakewood, N.J.).

Article Title: Building carbon–carbon bonds using a biocatalytic methanol condensation cycle
Article Snippet: Alcohol dehydrogenase ( S. cerevisiae ) and formate dehydrogenase ( C. boindii ) were purchased from Worthington Biochemical Corporation.