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clustal w alignment function  (Bioedit Company)

 
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    Bioedit Company clustal w alignment function
    Clustal W Alignment Function, supplied by Bioedit Company, 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/product/clustal+w+alignment+function/clustalw+function/pmc12097280-121-21-26
    Average 90 stars, based on 1 article reviews
    clustal w alignment function - by Bioz Stars, 2026-09
    90/100 stars

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    other:

    Article Title: A comprehensive pathological and molecular investigation of viral co-infections in ducks in Egypt
    Article Snippet: The viruses under investigation’s obtained nucleotide and deduced amino acid sequences, together with additional sequences from GenBank, were aligned using the Clustal W alignment function in Bioedit software ( ).



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    The feature of selected VNARs ( a ) The characterization of selected clone from each pool. n.d. = not detected. ( b ) VNAR amino acid sequence of selected clone. Complementarity determining region 1 (CDR1), Hyper variable region 2 (HV2), HV4 and CDR3 are expressed under the sequences. The sequences were expressed by using BioEdit version 7.2.5. Cysteine residues are highlighted in yellow. Positively charged amino acids, negatively charged amino acids, and hydrophobic amino acids in CDR3 are shown in red, green, and blue, respectively. ( c ) Sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE) of the selected clones under non-reducing condition. M: Protein Marker.
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    The feature of selected VNARs ( a ) The characterization of selected clone from each pool. n.d. = not detected. ( b ) VNAR amino acid sequence of selected clone. Complementarity determining region 1 (CDR1), Hyper variable region 2 (HV2), HV4 and CDR3 are expressed under the sequences. The sequences were expressed by using BioEdit version 7.2.5. Cysteine residues are highlighted in yellow. Positively charged amino acids, negatively charged amino acids, and hydrophobic amino acids in CDR3 are shown in red, green, and blue, respectively. ( c ) Sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE) of the selected clones under non-reducing condition. M: Protein Marker.

    Journal: Marine Drugs

    Article Title: Novel Approach for Obtaining Variable Domain of New Antigen Receptor with Different Physicochemical Properties from Japanese Topeshark ( Hemitriakis japanica )

    doi: 10.3390/md21110550

    Figure Lengend Snippet: The feature of selected VNARs ( a ) The characterization of selected clone from each pool. n.d. = not detected. ( b ) VNAR amino acid sequence of selected clone. Complementarity determining region 1 (CDR1), Hyper variable region 2 (HV2), HV4 and CDR3 are expressed under the sequences. The sequences were expressed by using BioEdit version 7.2.5. Cysteine residues are highlighted in yellow. Positively charged amino acids, negatively charged amino acids, and hydrophobic amino acids in CDR3 are shown in red, green, and blue, respectively. ( c ) Sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE) of the selected clones under non-reducing condition. M: Protein Marker.

    Article Snippet: CDR3 sequence comparison figures were created using the alignment function (Clustal W [ ]) in BioEdit version 7.2.5 (Bioedit, Manchester, UK).

    Techniques: Sequencing, Polyacrylamide Gel Electrophoresis, SDS Page, Clone Assay, Marker