β agarase  (New England Biolabs)


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    Name:
    beta Agarase I
    Description:
    beta Agarase I 500 units
    Catalog Number:
    m0392l
    Price:
    322
    Size:
    500 units
    Category:
    Agarase
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    Structured Review

    New England Biolabs β agarase
    beta Agarase I
    beta Agarase I 500 units
    https://www.bioz.com/result/β agarase/product/New England Biolabs
    Average 99 stars, based on 95 article reviews
    Price from $9.99 to $1999.99
    β agarase - by Bioz Stars, 2020-10
    99/100 stars

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    1) Product Images from "Molecular cloning, characterization and enzymatic properties of a novel ?eta-agarase from a marine isolate Psudoalteromonas SP. AG52"

    Article Title: Molecular cloning, characterization and enzymatic properties of a novel ?eta-agarase from a marine isolate Psudoalteromonas SP. AG52

    Journal: Brazilian Journal of Microbiology

    doi: 10.1590/S1517-83822010000400006

    Multiple alignment of β-agarase amino acid sequences of Pseudoalteromonas sp. AG52 with known agarases. The inverted triangles (▼) highlight the conserved catalytic residues, and black circles (●) represent the conserved residues involved in calcium ion binding. Identical residues in all sequences are shaded in gray and indicated by (*) under the column, conserved substitutions are indicated by (:), and semi-conserved substitutions are indicated by (.). Deletions are indicated by dashes. Sequence sources: Aeromonas sp. β-agarase (AAF03246), Pseudoalteromonas atlantica β-agarase I (AAA91888), Zobellia galactanivorans β-agarase A (AAF21820), Zobellia galactanivorans β-agarase B (AAF21821).
    Figure Legend Snippet: Multiple alignment of β-agarase amino acid sequences of Pseudoalteromonas sp. AG52 with known agarases. The inverted triangles (▼) highlight the conserved catalytic residues, and black circles (●) represent the conserved residues involved in calcium ion binding. Identical residues in all sequences are shaded in gray and indicated by (*) under the column, conserved substitutions are indicated by (:), and semi-conserved substitutions are indicated by (.). Deletions are indicated by dashes. Sequence sources: Aeromonas sp. β-agarase (AAF03246), Pseudoalteromonas atlantica β-agarase I (AAA91888), Zobellia galactanivorans β-agarase A (AAF21820), Zobellia galactanivorans β-agarase B (AAF21821).

    Techniques Used: Binding Assay, Sequencing

    Phylogenetic analysis of AgaA with known agarases based on amino acid sequence. Phylogenetic analysis was done by the Neighbor Joining method using MEGA3.1, based on sequence alignment using ClustalW (1.81). Numbers indicate the bootstrap confidence values of 1000 replicates. The accession numbers of the selected agarase sequences are as follows: AB178483, agarase ( Agarivorans sp. JAMB-A11); EF051475, QM38 agarase ( Agarivorans sp. QM38); EF100136, β-agarase ( Agarivorans sp. JA-1); AAA25696, β-agarase precursor ( Pseudoalteromonas atlantica ); AAP49346, AguB; AAP70390, AguH; AAP70365, AguK; AAP49316, AguD from uncultured bacterium; AAA91888, β-agarase I ( Pseudoalteromonas atlantica ); AAF03246, β-agarase ( Aeromonas sp.); AB124837, agarase ( Microbulbifer thermotolerans ); BAC99022, agarase ( Microbulbifer elongatus ); BAB79291, agarase, ( Pseudomonas sp. ND137; AAF21821, β-agarase B precursor ( Zobellia galactanivorans ); AAF21820, β-agarase A precursor ( Zobellia galactanivorans ); AAN39119, extracellular agarase precursor, ( Pseudoalteromonas sp. CY24); CAB61795, extracellular agarase precursor ( Streptomyces coelicolor A3); AAP70364, AguJ (uncultured bacterium); BAA04744, β-agarase ( Vibrio sp.); BAA03541, β-agarase ( Vibrio sp. JT0107); BAH16616, agarase ( Cellvibrio sp. OA-2007); AAT67062, β-agarase I ( Saccharophagus degradans ); AB160954, β-agarase ( Microbulbifer thermotolerans ).
    Figure Legend Snippet: Phylogenetic analysis of AgaA with known agarases based on amino acid sequence. Phylogenetic analysis was done by the Neighbor Joining method using MEGA3.1, based on sequence alignment using ClustalW (1.81). Numbers indicate the bootstrap confidence values of 1000 replicates. The accession numbers of the selected agarase sequences are as follows: AB178483, agarase ( Agarivorans sp. JAMB-A11); EF051475, QM38 agarase ( Agarivorans sp. QM38); EF100136, β-agarase ( Agarivorans sp. JA-1); AAA25696, β-agarase precursor ( Pseudoalteromonas atlantica ); AAP49346, AguB; AAP70390, AguH; AAP70365, AguK; AAP49316, AguD from uncultured bacterium; AAA91888, β-agarase I ( Pseudoalteromonas atlantica ); AAF03246, β-agarase ( Aeromonas sp.); AB124837, agarase ( Microbulbifer thermotolerans ); BAC99022, agarase ( Microbulbifer elongatus ); BAB79291, agarase, ( Pseudomonas sp. ND137; AAF21821, β-agarase B precursor ( Zobellia galactanivorans ); AAF21820, β-agarase A precursor ( Zobellia galactanivorans ); AAN39119, extracellular agarase precursor, ( Pseudoalteromonas sp. CY24); CAB61795, extracellular agarase precursor ( Streptomyces coelicolor A3); AAP70364, AguJ (uncultured bacterium); BAA04744, β-agarase ( Vibrio sp.); BAA03541, β-agarase ( Vibrio sp. JT0107); BAH16616, agarase ( Cellvibrio sp. OA-2007); AAT67062, β-agarase I ( Saccharophagus degradans ); AB160954, β-agarase ( Microbulbifer thermotolerans ).

    Techniques Used: Sequencing

    The nucleotide and deduced amino acid sequences of the β-agarase of Pseudoalteromonas sp. AG52. The predicted lipoprotein signal peptide is underlined and signal peptide sequence is in bold face. The start (ATG) and stop (TAA) codons are in bold italics and stop codon is marked with an asterisk (*). The GHF-16 β-agarase domain is in italics. Active sites and calcium binding residues are in boxes and dotted boxes, respectively.
    Figure Legend Snippet: The nucleotide and deduced amino acid sequences of the β-agarase of Pseudoalteromonas sp. AG52. The predicted lipoprotein signal peptide is underlined and signal peptide sequence is in bold face. The start (ATG) and stop (TAA) codons are in bold italics and stop codon is marked with an asterisk (*). The GHF-16 β-agarase domain is in italics. Active sites and calcium binding residues are in boxes and dotted boxes, respectively.

    Techniques Used: Sequencing, Binding Assay

    Related Articles

    Filtration:

    Article Title: Divergent Phenotypes in Mutant TDP-43 Transgenic Mice Highlight Potential Confounds in TDP-43 Transgenic Modeling
    Article Snippet: .. The transgenic fragment was obtained by BsrBI digestion, gel purified followed by β–agarase digestion (NEB), filtration and concentration. .. The modified TDP-43 transgene was injected into the pronuclei of donor FVB/NCr embryos (Charles River).

    Transgenic Assay:

    Article Title: Divergent Phenotypes in Mutant TDP-43 Transgenic Mice Highlight Potential Confounds in TDP-43 Transgenic Modeling
    Article Snippet: .. The transgenic fragment was obtained by BsrBI digestion, gel purified followed by β–agarase digestion (NEB), filtration and concentration. .. The modified TDP-43 transgene was injected into the pronuclei of donor FVB/NCr embryos (Charles River).

    Ethanol Precipitation:

    Article Title: A High-Resolution HAPPY Map of Dictyostelium discoideum Chromosome 6
    Article Snippet: .. DNA was recovered from the gel slice by digestion with β-Agarase 1 (New England Biolabs), phenol extraction, and ethanol precipitation following standard procedures and then digested to completion with either Rsa I (library MRC-L0) or Ssp I (library MRC-L1). .. Then, using a PCR-Script Amp SK+ cloning kit (Stratagene), 500 ng of digested DNA was cloned.

    Purification:

    Article Title: Cloning whole bacterial genomes in yeast.
    Article Snippet: .. Preparation of vector pARS-VN The vector pARS-VN (30) was linearized by a double digest with ClaI and XhoI, treated with antarctic phosphatase and gel purified using beta-agarase. .. A sample of 5 ng was used as template in a 100-ml PCR with Phusion DNA polymerase and HF buffer, according to the manufacturer’s protocol.

    Article Title: Rat Parvovirus Type 1: the Prototype for a New Rodent Parvovirus Serogroup
    Article Snippet: .. A 2.5- to 2.6-kb band was excised, and the DNA was purified by digestion with β-agarase (New England Bioloabs, Beverly, Mass.). .. The BluescriptII KS− vector (Stratagene, La Jolla, Calif.) was digested with Hin dIII and Bam HI, treated with shrimp alkaline phosphatase (Amersham Life Sciences, Arlington Heights, Ill.), and ligated with the gel-purified RPV-1 DNA.

    Article Title: Divergent Phenotypes in Mutant TDP-43 Transgenic Mice Highlight Potential Confounds in TDP-43 Transgenic Modeling
    Article Snippet: .. The transgenic fragment was obtained by BsrBI digestion, gel purified followed by β–agarase digestion (NEB), filtration and concentration. .. The modified TDP-43 transgene was injected into the pronuclei of donor FVB/NCr embryos (Charles River).

    Concentration Assay:

    Article Title: Divergent Phenotypes in Mutant TDP-43 Transgenic Mice Highlight Potential Confounds in TDP-43 Transgenic Modeling
    Article Snippet: .. The transgenic fragment was obtained by BsrBI digestion, gel purified followed by β–agarase digestion (NEB), filtration and concentration. .. The modified TDP-43 transgene was injected into the pronuclei of donor FVB/NCr embryos (Charles River).

    Incubation:

    Article Title: Altered editing level of microRNAs is a potential biomarker in lung adenocarcinoma, et al. Altered editing level of microRNAs is a potential biomarker in lung adenocarcinoma
    Article Snippet: .. The ladder between approximately 300‐700 base pairs was cut out, and melted at 65°C. β‐Agarase (New England Biolabs) was added, followed by incubation at 42°C for 60 minutes. ..

    Staining:

    Article Title: Genome-scale analysis of metazoan replication origins reveals their organization in specific but flexible sites defined by conserved features
    Article Snippet: .. After staining of proteinase K-treated DNA plugs with YOYO-1 (Molecular Probes) and digestion with agarase (New England Biolabs), DNA fibers were combed on silanized cover slips ( ). .. Immunodetection was done with mouse anti-BrdU (Becton Dickinson) and rat anti-BrdU (Sera Lab) antibodies and DNA was stained with the anti-ssDNA antibody (Chemicon).

    Plasmid Preparation:

    Article Title: Cloning whole bacterial genomes in yeast.
    Article Snippet: .. Preparation of vector pARS-VN The vector pARS-VN (30) was linearized by a double digest with ClaI and XhoI, treated with antarctic phosphatase and gel purified using beta-agarase. .. A sample of 5 ng was used as template in a 100-ml PCR with Phusion DNA polymerase and HF buffer, according to the manufacturer’s protocol.

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    New England Biolabs β agarase
    Multiple alignment of <t>β-agarase</t> amino acid sequences of Pseudoalteromonas sp. AG52 with known agarases. The inverted triangles (▼) highlight the conserved catalytic residues, and black circles (●) represent the conserved residues involved in calcium ion binding. Identical residues in all sequences are shaded in gray and indicated by (*) under the column, conserved substitutions are indicated by (:), and semi-conserved substitutions are indicated by (.). Deletions are indicated by dashes. Sequence sources: Aeromonas sp. β-agarase (AAF03246), Pseudoalteromonas atlantica β-agarase I (AAA91888), Zobellia galactanivorans β-agarase A (AAF21820), Zobellia galactanivorans β-agarase B (AAF21821).
    β Agarase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 50 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/β agarase/product/New England Biolabs
    Average 99 stars, based on 50 article reviews
    Price from $9.99 to $1999.99
    β agarase - by Bioz Stars, 2020-10
    99/100 stars
      Buy from Supplier

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    Multiple alignment of β-agarase amino acid sequences of Pseudoalteromonas sp. AG52 with known agarases. The inverted triangles (▼) highlight the conserved catalytic residues, and black circles (●) represent the conserved residues involved in calcium ion binding. Identical residues in all sequences are shaded in gray and indicated by (*) under the column, conserved substitutions are indicated by (:), and semi-conserved substitutions are indicated by (.). Deletions are indicated by dashes. Sequence sources: Aeromonas sp. β-agarase (AAF03246), Pseudoalteromonas atlantica β-agarase I (AAA91888), Zobellia galactanivorans β-agarase A (AAF21820), Zobellia galactanivorans β-agarase B (AAF21821).

    Journal: Brazilian Journal of Microbiology

    Article Title: Molecular cloning, characterization and enzymatic properties of a novel ?eta-agarase from a marine isolate Psudoalteromonas SP. AG52

    doi: 10.1590/S1517-83822010000400006

    Figure Lengend Snippet: Multiple alignment of β-agarase amino acid sequences of Pseudoalteromonas sp. AG52 with known agarases. The inverted triangles (▼) highlight the conserved catalytic residues, and black circles (●) represent the conserved residues involved in calcium ion binding. Identical residues in all sequences are shaded in gray and indicated by (*) under the column, conserved substitutions are indicated by (:), and semi-conserved substitutions are indicated by (.). Deletions are indicated by dashes. Sequence sources: Aeromonas sp. β-agarase (AAF03246), Pseudoalteromonas atlantica β-agarase I (AAA91888), Zobellia galactanivorans β-agarase A (AAF21820), Zobellia galactanivorans β-agarase B (AAF21821).

    Article Snippet: Neoagarohexanitol (NA6) was purchased from Sigma (USA) and neoagarotetraose (NA4) and neoagarobiose (NA2) (NA4 + NA2) were prepared by digestion of neoagarohexanitol using commercial β-agarase (New England Biolab, USA).

    Techniques: Binding Assay, Sequencing

    Phylogenetic analysis of AgaA with known agarases based on amino acid sequence. Phylogenetic analysis was done by the Neighbor Joining method using MEGA3.1, based on sequence alignment using ClustalW (1.81). Numbers indicate the bootstrap confidence values of 1000 replicates. The accession numbers of the selected agarase sequences are as follows: AB178483, agarase ( Agarivorans sp. JAMB-A11); EF051475, QM38 agarase ( Agarivorans sp. QM38); EF100136, β-agarase ( Agarivorans sp. JA-1); AAA25696, β-agarase precursor ( Pseudoalteromonas atlantica ); AAP49346, AguB; AAP70390, AguH; AAP70365, AguK; AAP49316, AguD from uncultured bacterium; AAA91888, β-agarase I ( Pseudoalteromonas atlantica ); AAF03246, β-agarase ( Aeromonas sp.); AB124837, agarase ( Microbulbifer thermotolerans ); BAC99022, agarase ( Microbulbifer elongatus ); BAB79291, agarase, ( Pseudomonas sp. ND137; AAF21821, β-agarase B precursor ( Zobellia galactanivorans ); AAF21820, β-agarase A precursor ( Zobellia galactanivorans ); AAN39119, extracellular agarase precursor, ( Pseudoalteromonas sp. CY24); CAB61795, extracellular agarase precursor ( Streptomyces coelicolor A3); AAP70364, AguJ (uncultured bacterium); BAA04744, β-agarase ( Vibrio sp.); BAA03541, β-agarase ( Vibrio sp. JT0107); BAH16616, agarase ( Cellvibrio sp. OA-2007); AAT67062, β-agarase I ( Saccharophagus degradans ); AB160954, β-agarase ( Microbulbifer thermotolerans ).

    Journal: Brazilian Journal of Microbiology

    Article Title: Molecular cloning, characterization and enzymatic properties of a novel ?eta-agarase from a marine isolate Psudoalteromonas SP. AG52

    doi: 10.1590/S1517-83822010000400006

    Figure Lengend Snippet: Phylogenetic analysis of AgaA with known agarases based on amino acid sequence. Phylogenetic analysis was done by the Neighbor Joining method using MEGA3.1, based on sequence alignment using ClustalW (1.81). Numbers indicate the bootstrap confidence values of 1000 replicates. The accession numbers of the selected agarase sequences are as follows: AB178483, agarase ( Agarivorans sp. JAMB-A11); EF051475, QM38 agarase ( Agarivorans sp. QM38); EF100136, β-agarase ( Agarivorans sp. JA-1); AAA25696, β-agarase precursor ( Pseudoalteromonas atlantica ); AAP49346, AguB; AAP70390, AguH; AAP70365, AguK; AAP49316, AguD from uncultured bacterium; AAA91888, β-agarase I ( Pseudoalteromonas atlantica ); AAF03246, β-agarase ( Aeromonas sp.); AB124837, agarase ( Microbulbifer thermotolerans ); BAC99022, agarase ( Microbulbifer elongatus ); BAB79291, agarase, ( Pseudomonas sp. ND137; AAF21821, β-agarase B precursor ( Zobellia galactanivorans ); AAF21820, β-agarase A precursor ( Zobellia galactanivorans ); AAN39119, extracellular agarase precursor, ( Pseudoalteromonas sp. CY24); CAB61795, extracellular agarase precursor ( Streptomyces coelicolor A3); AAP70364, AguJ (uncultured bacterium); BAA04744, β-agarase ( Vibrio sp.); BAA03541, β-agarase ( Vibrio sp. JT0107); BAH16616, agarase ( Cellvibrio sp. OA-2007); AAT67062, β-agarase I ( Saccharophagus degradans ); AB160954, β-agarase ( Microbulbifer thermotolerans ).

    Article Snippet: Neoagarohexanitol (NA6) was purchased from Sigma (USA) and neoagarotetraose (NA4) and neoagarobiose (NA2) (NA4 + NA2) were prepared by digestion of neoagarohexanitol using commercial β-agarase (New England Biolab, USA).

    Techniques: Sequencing

    The nucleotide and deduced amino acid sequences of the β-agarase of Pseudoalteromonas sp. AG52. The predicted lipoprotein signal peptide is underlined and signal peptide sequence is in bold face. The start (ATG) and stop (TAA) codons are in bold italics and stop codon is marked with an asterisk (*). The GHF-16 β-agarase domain is in italics. Active sites and calcium binding residues are in boxes and dotted boxes, respectively.

    Journal: Brazilian Journal of Microbiology

    Article Title: Molecular cloning, characterization and enzymatic properties of a novel ?eta-agarase from a marine isolate Psudoalteromonas SP. AG52

    doi: 10.1590/S1517-83822010000400006

    Figure Lengend Snippet: The nucleotide and deduced amino acid sequences of the β-agarase of Pseudoalteromonas sp. AG52. The predicted lipoprotein signal peptide is underlined and signal peptide sequence is in bold face. The start (ATG) and stop (TAA) codons are in bold italics and stop codon is marked with an asterisk (*). The GHF-16 β-agarase domain is in italics. Active sites and calcium binding residues are in boxes and dotted boxes, respectively.

    Article Snippet: Neoagarohexanitol (NA6) was purchased from Sigma (USA) and neoagarotetraose (NA4) and neoagarobiose (NA2) (NA4 + NA2) were prepared by digestion of neoagarohexanitol using commercial β-agarase (New England Biolab, USA).

    Techniques: Sequencing, Binding Assay