clustalw multiple alignment algorithm of bioedit sequence alignment editor version 7.0.9.0 (Bioedit Company)
90
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Bioedit Company
clustalw multiple alignment algorithm of bioedit sequence alignment editor version 7.0.9.0
Clustalw Multiple Alignment Algorithm Of Bioedit Sequence Alignment Editor Version 7.0.9.0, 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/clustalw+multiple+sequence+alignment+algorithm+bioedit+sequence+alignment+editor+version+7%2E0%2E9%2E0/clustalw+in+bioedit/pmc03898820-66-12-11
Average 90 stars, based on 1 article reviews
Clustalw Multiple Alignment Algorithm Of Bioedit Sequence Alignment Editor Version 7.0.9.0, 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/clustalw+multiple+sequence+alignment+algorithm+bioedit+sequence+alignment+editor+version+7%2E0%2E9%2E0/clustalw+in+bioedit/pmc03898820-66-12-11
Average 90 stars, based on 1 article reviews
clustalw multiple alignment algorithm of bioedit sequence alignment editor version 7.0.9.0 - by Bioz Stars,
2026-10
90/100 stars
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Sequencing:Article Title: Matrix metalloproteinase 2 of grass carp Ctenopharyngodon idella (CiMMP2) is involved in the immune response against bacterial infection. Article Snippet: The gene encoding matrix metalloproteinase 2 (MMP2) was cloned from grass carp (Ctenopharyngodon idella), and its expression levels during Aeromonas hydrophila infection and embryonic development stages were evaluated.. The complete open reading frame of CiMMP2 was 1974 bp in length, encoding a 658-amino acid polypeptide.. The deduced MMP2 protein contained four conserved domain structures, including an N-terminal signal sequence, a propeptide domain, three repeats of fibronectin-type II domain inserted in the catalytic domain and a C-terminal hemopexin-like domain. |