人HAX-1的同源表达和纯化用于结构研究。

IF 2.3 4区生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY

FEBS Open Bio Pub Date : 2025-09-25 DOI:10.1002/2211-5463.70131

Mariana Grieben

{"title":"人HAX-1的同源表达和纯化用于结构研究。","authors":"Mariana Grieben","doi":"10.1002/2211-5463.70131","DOIUrl":null,"url":null,"abstract":"The human HAX-1 protein is a ubiquitously expressed multifunctional protein that regulates various cellular processes through interactions with numerous cellular proteins and RNA. The purification protocol presented here is designed explicitly for HAX-1 expressed in mammalian cells and yields high amounts of soluble HAX-1 protein constructs N-terminally fused to a cleavable superfolder GFP. This protocol will enable structural studies of HAX-1, which is predicted to undergo posttranslational modifications and be partially disordered in the absence of a binding partner.","PeriodicalId":12187,"journal":{"name":"FEBS Open Bio","volume":" ","pages":""},"PeriodicalIF":2.3000,"publicationDate":"2025-09-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Homologous expression and purification of human HAX-1 for structural studies.\",\"authors\":\"Mariana Grieben\",\"doi\":\"10.1002/2211-5463.70131\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"The human HAX-1 protein is a ubiquitously expressed multifunctional protein that regulates various cellular processes through interactions with numerous cellular proteins and RNA. The purification protocol presented here is designed explicitly for HAX-1 expressed in mammalian cells and yields high amounts of soluble HAX-1 protein constructs N-terminally fused to a cleavable superfolder GFP. This protocol will enable structural studies of HAX-1, which is predicted to undergo posttranslational modifications and be partially disordered in the absence of a binding partner.\",\"PeriodicalId\":12187,\"journal\":{\"name\":\"FEBS Open Bio\",\"volume\":\" \",\"pages\":\"\"},\"PeriodicalIF\":2.3000,\"publicationDate\":\"2025-09-25\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"FEBS Open Bio\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.1002/2211-5463.70131\",\"RegionNum\":4,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"FEBS Open Bio","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1002/2211-5463.70131","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}

引用次数: 0

摘要

人类HAX-1蛋白是一种普遍表达的多功能蛋白，通过与许多细胞蛋白和RNA的相互作用来调节各种细胞过程。本文提出的纯化方案是为在哺乳动物细胞中表达的HAX-1明确设计的，并产生大量可溶性HAX-1蛋白构建体n端融合到可切割的超级折叠GFP上。该方案将使HAX-1的结构研究成为可能，预计HAX-1在缺乏结合伙伴的情况下会经历翻译后修饰和部分紊乱。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

查看原文本刊更多论文

Homologous expression and purification of human HAX-1 for structural studies.

The human HAX-1 protein is a ubiquitously expressed multifunctional protein that regulates various cellular processes through interactions with numerous cellular proteins and RNA. The purification protocol presented here is designed explicitly for HAX-1 expressed in mammalian cells and yields high amounts of soluble HAX-1 protein constructs N-terminally fused to a cleavable superfolder GFP. This protocol will enable structural studies of HAX-1, which is predicted to undergo posttranslational modifications and be partially disordered in the absence of a binding partner.

求助全文

通过发布文献求助，成功后即可免费获取论文全文。去求助

来源期刊

FEBS Open Bio BIOCHEMISTRY & MOLECULAR BIOLOGY-

CiteScore

5.10

自引率

0.00%

发文量

173

审稿时长

10 weeks

期刊介绍： FEBS Open Bio is an online-only open access journal for the rapid publication of research articles in molecular and cellular life sciences in both health and disease. The journal''s peer review process focuses on the technical soundness of papers, leaving the assessment of their impact and importance to the scientific community. FEBS Open Bio is owned by the Federation of European Biochemical Societies (FEBS), a not-for-profit organization, and is published on behalf of FEBS by FEBS Press and Wiley. Any income from the journal will be used to support scientists through fellowships, courses, travel grants, prizes and other FEBS initiatives.