{"title":"烟草刻蚀病毒蛋白酶快速蛋白失活系统中原位裂解p115的特异性抗体检测","authors":"Mayuko Koreishi, Yasuko Honjo, Ayano Satoh","doi":"10.2147/ANTI.S22825","DOIUrl":null,"url":null,"abstract":": Gene perturbation methods are commonly used in the study of gene and protein function. The authors of this paper recently developed a rapid protein inactivation technique utilizing tobacco etch virus (TEV)-derived protease. TEV protease recognizes the ENLYFQG (Glu-Asn-Leu-Tyr-Phe-Gln-Gly) amino acid sequence and specifically cleaves between Q and G. The authors developed antibodies that recognize the cleaved TEV (ENLYFQ) sequence, both in vitro and in vivo, but do not bind to uncleaved TEV (ENLYFQG). Using these antibodies, in situ protein cleavage was successfully detected. These antibodies used in combination with the TEV protease may be a useful complement to other perturbation methods.","PeriodicalId":50747,"journal":{"name":"Antibiotiques","volume":"1 1","pages":"5-11"},"PeriodicalIF":0.0000,"publicationDate":"2011-08-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.2147/ANTI.S22825","citationCount":"1","resultStr":"{\"title\":\"Detection of in situ cleaved p115 with the cut specific antibodies in rapid protein inactivation system by tobacco etch viral protease cleavage\",\"authors\":\"Mayuko Koreishi, Yasuko Honjo, Ayano Satoh\",\"doi\":\"10.2147/ANTI.S22825\",\"DOIUrl\":null,\"url\":null,\"abstract\":\": Gene perturbation methods are commonly used in the study of gene and protein function. The authors of this paper recently developed a rapid protein inactivation technique utilizing tobacco etch virus (TEV)-derived protease. TEV protease recognizes the ENLYFQG (Glu-Asn-Leu-Tyr-Phe-Gln-Gly) amino acid sequence and specifically cleaves between Q and G. The authors developed antibodies that recognize the cleaved TEV (ENLYFQ) sequence, both in vitro and in vivo, but do not bind to uncleaved TEV (ENLYFQG). Using these antibodies, in situ protein cleavage was successfully detected. These antibodies used in combination with the TEV protease may be a useful complement to other perturbation methods.\",\"PeriodicalId\":50747,\"journal\":{\"name\":\"Antibiotiques\",\"volume\":\"1 1\",\"pages\":\"5-11\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2011-08-10\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.2147/ANTI.S22825\",\"citationCount\":\"1\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Antibiotiques\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.2147/ANTI.S22825\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Antibiotiques","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.2147/ANTI.S22825","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Detection of in situ cleaved p115 with the cut specific antibodies in rapid protein inactivation system by tobacco etch viral protease cleavage
: Gene perturbation methods are commonly used in the study of gene and protein function. The authors of this paper recently developed a rapid protein inactivation technique utilizing tobacco etch virus (TEV)-derived protease. TEV protease recognizes the ENLYFQG (Glu-Asn-Leu-Tyr-Phe-Gln-Gly) amino acid sequence and specifically cleaves between Q and G. The authors developed antibodies that recognize the cleaved TEV (ENLYFQ) sequence, both in vitro and in vivo, but do not bind to uncleaved TEV (ENLYFQG). Using these antibodies, in situ protein cleavage was successfully detected. These antibodies used in combination with the TEV protease may be a useful complement to other perturbation methods.