{"title":"Efficient Protocol for Expression and Purification of DUSP5.","authors":"Stevan Salinero, Lee Uranga, Marat Talipov","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Dual Specificity Phosphatase 5 (DUSP5) is a human protein that targets specific kinases and dephosphorylates phosphoserine/threonine and phosphotyrosine residues. DUSP5 is found to be involved in cardiovascular diseases and many cancer pathways, including skin and breast cancer. For this reason, availability of an efficient protocol of expression and purification of DUSP proteins can play a crucial role in their studies towards better understanding of the disease process and development of better therapeutic approaches. For example, purification of DUSP5 could be used for the in vitro assays of the inhibitors of DUSP5 identified from the in-silico studies. This report provides the full procedure for protein purification thereby allowing the collection of desired amounts of DUSP5 using Glutathione S-transferase (GST) tag. The described method shows an efficient way to solubilize and purify DUSP5 for further protein studies.</p>","PeriodicalId":74302,"journal":{"name":"New Mexico journal of science","volume":"55 ","pages":"12-19"},"PeriodicalIF":0.0000,"publicationDate":"2021-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9799713/pdf/nihms-1855784.pdf","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"New Mexico journal of science","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
Abstract
Dual Specificity Phosphatase 5 (DUSP5) is a human protein that targets specific kinases and dephosphorylates phosphoserine/threonine and phosphotyrosine residues. DUSP5 is found to be involved in cardiovascular diseases and many cancer pathways, including skin and breast cancer. For this reason, availability of an efficient protocol of expression and purification of DUSP proteins can play a crucial role in their studies towards better understanding of the disease process and development of better therapeutic approaches. For example, purification of DUSP5 could be used for the in vitro assays of the inhibitors of DUSP5 identified from the in-silico studies. This report provides the full procedure for protein purification thereby allowing the collection of desired amounts of DUSP5 using Glutathione S-transferase (GST) tag. The described method shows an efficient way to solubilize and purify DUSP5 for further protein studies.