{"title":"pIN-III-ompA分泌载体新衍生物的构建与测序","authors":"Alan Fauconnier, Ary Van Elsen, Alex Bollen","doi":"10.1016/S1050-3862(98)00005-9","DOIUrl":null,"url":null,"abstract":"<div><p>The growing interest in proteins exported by bacteria led to the development of cloning vectors designed for targeting recombinant proteins to extracytoplasmic compartments. The pIN-III-<em>ompA</em> vector family fulfils such a function. Here we report the construction and sequencing of new pIN-III-<em>ompA</em> derivatives with alternate polylinker sites, increasing the cloning flexibility of these vectors.</p></div>","PeriodicalId":77142,"journal":{"name":"Genetic analysis, techniques and applications","volume":"14 4","pages":"Pages 129-131"},"PeriodicalIF":0.0000,"publicationDate":"1998-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S1050-3862(98)00005-9","citationCount":"5","resultStr":"{\"title\":\"Construction and sequencing of new derivatives of the pIN-III-ompA secretion vector\",\"authors\":\"Alan Fauconnier, Ary Van Elsen, Alex Bollen\",\"doi\":\"10.1016/S1050-3862(98)00005-9\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>The growing interest in proteins exported by bacteria led to the development of cloning vectors designed for targeting recombinant proteins to extracytoplasmic compartments. The pIN-III-<em>ompA</em> vector family fulfils such a function. Here we report the construction and sequencing of new pIN-III-<em>ompA</em> derivatives with alternate polylinker sites, increasing the cloning flexibility of these vectors.</p></div>\",\"PeriodicalId\":77142,\"journal\":{\"name\":\"Genetic analysis, techniques and applications\",\"volume\":\"14 4\",\"pages\":\"Pages 129-131\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1998-10-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/S1050-3862(98)00005-9\",\"citationCount\":\"5\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Genetic analysis, techniques and applications\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S1050386298000059\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Genetic analysis, techniques and applications","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S1050386298000059","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Construction and sequencing of new derivatives of the pIN-III-ompA secretion vector
The growing interest in proteins exported by bacteria led to the development of cloning vectors designed for targeting recombinant proteins to extracytoplasmic compartments. The pIN-III-ompA vector family fulfils such a function. Here we report the construction and sequencing of new pIN-III-ompA derivatives with alternate polylinker sites, increasing the cloning flexibility of these vectors.
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