chitinase a  (Jena Bioscience)


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    Structured Review

    Jena Bioscience chitinase a
    Purification of <t>chitinase</t> A expressed from E. coli M15 cells. ( a ) Elution profile of recombinant chitinase A obtained from an ÄKTA purifier system with a Superdex 200 HR 10/30 (1.0 × 30 cm) gel-filtration column. The running buffer
    Chitinase A, supplied by Jena Bioscience, 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/chitinase a/product/Jena Bioscience
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    chitinase a - by Bioz Stars, 2021-07
    86/100 stars

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    1) Product Images from "Expression, purification, crystallization and preliminary crystallographic analysis of chitinase A from Vibrio carchariae"

    Article Title: Expression, purification, crystallization and preliminary crystallographic analysis of chitinase A from Vibrio carchariae

    Journal: Acta Crystallographica Section F: Structural Biology and Crystallization Communications

    doi: 10.1107/S1744309105027831

    Purification of chitinase A expressed from E. coli M15 cells. ( a ) Elution profile of recombinant chitinase A obtained from an ÄKTA purifier system with a Superdex 200 HR 10/30 (1.0 × 30 cm) gel-filtration column. The running buffer
    Figure Legend Snippet: Purification of chitinase A expressed from E. coli M15 cells. ( a ) Elution profile of recombinant chitinase A obtained from an ÄKTA purifier system with a Superdex 200 HR 10/30 (1.0 × 30 cm) gel-filtration column. The running buffer

    Techniques Used: Purification, Recombinant, Filtration

    A crystal of recombinant chitinase A (dimensions 1100 × 400 × 100 µm) obtained from a hanging-drop vapour-diffusion setup using 0.1 M sodium acetate pH 4.6 containing 10%( v / v ) PEG 400 and 0.125 M CaCl 2 .
    Figure Legend Snippet: A crystal of recombinant chitinase A (dimensions 1100 × 400 × 100 µm) obtained from a hanging-drop vapour-diffusion setup using 0.1 M sodium acetate pH 4.6 containing 10%( v / v ) PEG 400 and 0.125 M CaCl 2 .

    Techniques Used: Recombinant, Diffusion-based Assay

    Related Articles

    Sequencing:

    Article Title: Biochemical Composition and Assembly of Biosilica-associated Insoluble Organic Matrices from the Diatom Thalassiosira pseudonana *
    Article Snippet: The present study aimed at obtaining comprehensive information on the biochemical composition of the organic microrings with a focus on the structural and functional analysis of its protein components. .. Chemical and reagents were purchased from the following companies: oligonucleotides (Eurofins Genomics), isopropylthiogalactoside (Carl Roth), 6 n HCl sequencing grade (Thermo Scientific), phenyl isothiocyanate (Thermo Scientific), acetonitrile (VWR), phenol (Wako Chemicals), mass spectrometry solvents (Fisher), anhydrous hydrogen fluoride (GHC Gerling), ampicillin (Merck), nourseothricin (Jena Bioscience), tetramethoxysilane (Sigma-Aldrich), ammonium molybdate tetrahydrate (Merck), ammonium fluoride (Merck), chitinase from Streptomyces griseus (Sigma-Aldrich), EDTA (Merck), SDS (Merck), trypsin (mass spectrometry grade; Promega), chymotrypsin (sequencing grade; Roche Applied Science), endoproteinase Asp-N (sequencing grade; Roche Applied Science), endoproteinase Glu-C (sequencing grade; Roche Applied Science). ..

    Mass Spectrometry:

    Article Title: Biochemical Composition and Assembly of Biosilica-associated Insoluble Organic Matrices from the Diatom Thalassiosira pseudonana *
    Article Snippet: The present study aimed at obtaining comprehensive information on the biochemical composition of the organic microrings with a focus on the structural and functional analysis of its protein components. .. Chemical and reagents were purchased from the following companies: oligonucleotides (Eurofins Genomics), isopropylthiogalactoside (Carl Roth), 6 n HCl sequencing grade (Thermo Scientific), phenyl isothiocyanate (Thermo Scientific), acetonitrile (VWR), phenol (Wako Chemicals), mass spectrometry solvents (Fisher), anhydrous hydrogen fluoride (GHC Gerling), ampicillin (Merck), nourseothricin (Jena Bioscience), tetramethoxysilane (Sigma-Aldrich), ammonium molybdate tetrahydrate (Merck), ammonium fluoride (Merck), chitinase from Streptomyces griseus (Sigma-Aldrich), EDTA (Merck), SDS (Merck), trypsin (mass spectrometry grade; Promega), chymotrypsin (sequencing grade; Roche Applied Science), endoproteinase Asp-N (sequencing grade; Roche Applied Science), endoproteinase Glu-C (sequencing grade; Roche Applied Science). ..

    Amplification:

    Article Title: A helminth chitinase structurally similar to mammalian chitinase displays immunomodulatory properties
    Article Snippet: Reverse transcription of 1 µg RNA into cDNA was done using the Transcriptor First Strand cDNA Synthesis Kit (Roche Diagnostics GmbH, Mannheim, Germany). .. The genes corresponding to selected T. suis proteins were amplified and cloned into the vector pLEXSYsat2 of the Leishmania Expression System (LEXSYcon2 Expression Kit, Jena Bioscience GmbH, Jena, Germany). .. The cloning vector was sequenced for verification.

    Clone Assay:

    Article Title: A helminth chitinase structurally similar to mammalian chitinase displays immunomodulatory properties
    Article Snippet: Reverse transcription of 1 µg RNA into cDNA was done using the Transcriptor First Strand cDNA Synthesis Kit (Roche Diagnostics GmbH, Mannheim, Germany). .. The genes corresponding to selected T. suis proteins were amplified and cloned into the vector pLEXSYsat2 of the Leishmania Expression System (LEXSYcon2 Expression Kit, Jena Bioscience GmbH, Jena, Germany). .. The cloning vector was sequenced for verification.

    Plasmid Preparation:

    Article Title: A helminth chitinase structurally similar to mammalian chitinase displays immunomodulatory properties
    Article Snippet: Reverse transcription of 1 µg RNA into cDNA was done using the Transcriptor First Strand cDNA Synthesis Kit (Roche Diagnostics GmbH, Mannheim, Germany). .. The genes corresponding to selected T. suis proteins were amplified and cloned into the vector pLEXSYsat2 of the Leishmania Expression System (LEXSYcon2 Expression Kit, Jena Bioscience GmbH, Jena, Germany). .. The cloning vector was sequenced for verification.

    Expressing:

    Article Title: A helminth chitinase structurally similar to mammalian chitinase displays immunomodulatory properties
    Article Snippet: Reverse transcription of 1 µg RNA into cDNA was done using the Transcriptor First Strand cDNA Synthesis Kit (Roche Diagnostics GmbH, Mannheim, Germany). .. The genes corresponding to selected T. suis proteins were amplified and cloned into the vector pLEXSYsat2 of the Leishmania Expression System (LEXSYcon2 Expression Kit, Jena Bioscience GmbH, Jena, Germany). .. The cloning vector was sequenced for verification.

    Crystallization Assay:

    Article Title: Expression, purification, crystallization and preliminary crystallographic analysis of chitinase A from Vibrio carchariae
    Article Snippet: Initial crystallization experiments were carried out by the microbatch method in 96-well Impact plates (Hampton Research, Aliso Viejo, CA, USA) filled with 10 µl Al’s oil (Hampton Research). .. For each crystallization drop, 0.5 µl chitinase A (10 mg ml−1 in 20 m M Tris–HCl buffer pH 8.0 containing 150 m M NaCl) was added to 0.5 µl of each precipitant from Crystal Screen (Hampton Research) and JB Screen HTS I and HTS II (Jena Bioscience GmbH, Jena, Germany) without mixing. .. Small crystals were obtained after 4 d incubation at 277 K in condition A1 from JBScreen HTS I [15%( v / v ) PEG 400, 0.1 M sodium acetate pH 4.6 and 0.1 M CaCl2 ], condition H4 from JBScreen HTS I [30%( w / v ) PEG 8000, 0.2 M ammonium sulfate] and condition A10 from Crystal Screen [30%( w / v ) PEG 4000, 0.1 M sodium acetate pH 4.6 and 0.2 M ammonium acetate].

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    Jena Bioscience chitinase a
    Purification of <t>chitinase</t> A expressed from E. coli M15 cells. ( a ) Elution profile of recombinant chitinase A obtained from an ÄKTA purifier system with a Superdex 200 HR 10/30 (1.0 × 30 cm) gel-filtration column. The running buffer
    Chitinase A, supplied by Jena Bioscience, 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/chitinase a/product/Jena Bioscience
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    chitinase a - by Bioz Stars, 2021-07
    86/100 stars
      Buy from Supplier

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    Purification of chitinase A expressed from E. coli M15 cells. ( a ) Elution profile of recombinant chitinase A obtained from an ÄKTA purifier system with a Superdex 200 HR 10/30 (1.0 × 30 cm) gel-filtration column. The running buffer

    Journal: Acta Crystallographica Section F: Structural Biology and Crystallization Communications

    Article Title: Expression, purification, crystallization and preliminary crystallographic analysis of chitinase A from Vibrio carchariae

    doi: 10.1107/S1744309105027831

    Figure Lengend Snippet: Purification of chitinase A expressed from E. coli M15 cells. ( a ) Elution profile of recombinant chitinase A obtained from an ÄKTA purifier system with a Superdex 200 HR 10/30 (1.0 × 30 cm) gel-filtration column. The running buffer

    Article Snippet: For each crystallization drop, 0.5 µl chitinase A (10 mg ml−1 in 20 m M Tris–HCl buffer pH 8.0 containing 150 m M NaCl) was added to 0.5 µl of each precipitant from Crystal Screen (Hampton Research) and JB Screen HTS I and HTS II (Jena Bioscience GmbH, Jena, Germany) without mixing.

    Techniques: Purification, Recombinant, Filtration

    A crystal of recombinant chitinase A (dimensions 1100 × 400 × 100 µm) obtained from a hanging-drop vapour-diffusion setup using 0.1 M sodium acetate pH 4.6 containing 10%( v / v ) PEG 400 and 0.125 M CaCl 2 .

    Journal: Acta Crystallographica Section F: Structural Biology and Crystallization Communications

    Article Title: Expression, purification, crystallization and preliminary crystallographic analysis of chitinase A from Vibrio carchariae

    doi: 10.1107/S1744309105027831

    Figure Lengend Snippet: A crystal of recombinant chitinase A (dimensions 1100 × 400 × 100 µm) obtained from a hanging-drop vapour-diffusion setup using 0.1 M sodium acetate pH 4.6 containing 10%( v / v ) PEG 400 and 0.125 M CaCl 2 .

    Article Snippet: For each crystallization drop, 0.5 µl chitinase A (10 mg ml−1 in 20 m M Tris–HCl buffer pH 8.0 containing 150 m M NaCl) was added to 0.5 µl of each precipitant from Crystal Screen (Hampton Research) and JB Screen HTS I and HTS II (Jena Bioscience GmbH, Jena, Germany) without mixing.

    Techniques: Recombinant, Diffusion-based Assay