Article(id=1315696639101223421, tenantId=1146029695717560320, journalId=1315121759093096577, issueId=1315696624781869390, articleNumber=null, orderNo=null, doi=10.3969/j.issn.1005-7021.2026.02.008, pmid=null, cstr=null, oa=null, hot=null, price=null, onlineType=0, articleFormat=0, articleType=null, articleTypeStr=null, receivedDate=1764604800000, receivedDateStr=2025-12-02, revisedDate=null, revisedDateStr=null, acceptedDate=null, acceptedDateStr=null, onlineDate=1791616123223, onlineDateStr=2026-10-10, pubDate=1776614400000, pubDateStr=2026-04-20, doiRegisterDate=null, doiRegisterDateStr=null, onlineIssueDate=1791616123223, onlineIssueDateStr=2026-10-10, onlineJustAcceptDate=null, onlineJustAcceptDateStr=null, onlineFirstDate=null, onlineFirstDateStr=null, sourceXml=null, magXml=null, createTime=1791616123223, creator=13701087609, updateTime=1791616123223, updator=13701087609, issue=Issue{id=1315696624781869390, tenantId=1146029695717560320, journalId=1315121759093096577, year='2026', volume='46', issue='2', pageStart='1', pageEnd='136', issueExtLink='null', onlineDate='null', pubDate='1776614400000', pubDateStr='2026-04-20', beforeIssueId=null, nextIssueId=null, price=null, status=1, issueComplete=1, articleOrder=1, issueType=-1, specialIssue=null, createTime=1791616119809, creator='13701087609', updateTime=1791616211073, updator='13701087609', preIssue=null, nextIssue=null, articleTotal=null, ext={EN=IssueExt(id=1315697007629550369, tenantId=1146029695717560320, journalId=1315121759093096577, issueId=1315696624781869390, language=EN, specialIssueTitle=, coverIllustrator=null, specialIssueEditor=, specialIssueAbout=), CN=IssueExt(id=1315697007629550370, tenantId=1146029695717560320, journalId=1315121759093096577, issueId=1315696624781869390, language=CN, specialIssueTitle=, coverIllustrator=null, specialIssueEditor=, specialIssueAbout=)}, issueFiles=null, downloadFileDto=null}, startPage=83, endPage=91, ext={EN=ArticleExt(id=1315696639298355710, articleId=1315696639101223421, tenantId=1146029695717560320, journalId=1315121759093096577, language=EN, title=Preparation of Monoclonal Antibodies and Development of Immunoassay for against Human β2-Microglobulin, columnId=null, journalTitle=Journal of Microbiology, columnName=null, runingTitle=null, highlight=null, articleAbstract=

This study aimed to prepare monoclonal antibodies against human β2-MG and to establish rapid and accurate quantitative and qualitative immunoassay methods for β2-MG detection. Recombinant β2-MG was produced through prokaryotic expression and purification, and subsequently used for immunizing BALB/c mice. Monoclonal antibodies against human β2-MG were generated using hybridoma technology and screened via double antibody sandwich enzyme-linked immunosorbent assay (DAS-ELISA), which facilitated the development of a chemiluminescence enzyme immunoassay (CLEIA). Clinical serum β2-MG levels were measured to evaluate and analyze the detection performance of the proposed CLEIA. Additionally, a convenient and rapid colloidal gold immunochromatographic assay for β2-MG detection was preliminarily established. The monoclonal antibody pair 5H7/6H9-AP was developed into the CLEIA, demonstrating a linear range of 0.14-120.00 μg/L (extended to 60.00 mg/L). The serum β2-MG CLEIA results showed excellent correlation with the latex enhanced immunoturbidimetry assay conducted in hospitals (R²: 0.96, P<0.000 1). The established colloidal gold immunochromatographic assay exhibited good sensitivity for detecting recombinant β2-MG, with test strips capable of detecting a minimum concentration of 0.20 mg/L. The prepared monoclonal antibodies for β2-MG, along with the established quantitative and qualitative immunoassay methods, hold significant potential for clinical diagnostic applications.

, authors=Qian PENG^{1, 2}, Yao TONG³, Yi WU², Chuan XIA⁴, Ye XU², Song-hui ZHOU², Qiu-nuo LI¹, Ru-shi LIU^{1, 2, *}, Jiao ZHENG^{1, 2, *}, authorsList=Qian PENG, Yao TONG, Yi WU, Chuan XIA, Ye XU, Song-hui ZHOU, Qiu-nuo LI, Ru-shi LIU, Jiao ZHENG, authorCompany=null, correspAuthors=Ru-shi LIU, Jiao ZHENG, authorNote=null, correspAuthorsNote=null, copyrightStatement=null, copyrightOwner=null, extLink=null, articleAbsUrl=null, sourceXml=null, magXml=null, pdfUrl=null, pdf=null, pdfFileSize=null, pdfExtLink=null, richHtmlUrl=null, mobilePdfUrl=null, reviewReport=null, pdfFirstPage=null, abstractGraph=null, abstractGraphContent=null, abstractVideo=null, citation=null, cebUrl=null, magXmlContent=null, mapNumber=null, fund=null), CN=ArticleExt(id=1315696639575179775, articleId=1315696639101223421, tenantId=1146029695717560320, journalId=1315121759093096577, language=CN, title=抗人β2-微球蛋白单克隆抗体的制备及免疫检测方法的建立, columnId=1315696197449405326, journalTitle=微生物学杂志, columnName=研究报告, runingTitle=null, highlight=null, articleAbstract=

制备抗人β2-微球蛋白（Beta-2-microglobulin，β2-MG）单克隆抗体，建立快速、准确的β2-MG定性、定量检测方法。原核表达重组β2-MG并进行纯化后用于BALB/c小鼠免疫，通过杂交瘤技术制备抗人β2-MG单克隆抗体，通过双抗体夹心酶联免疫吸附测定法（double antibody sandwich enzyme-linked immunosorbent assay, DAS-ELISA）进行筛选，建立基于化学发光酶免疫测定法（chemiluminescence enzyme immunoasssay, CLEIA）的检测平台，将其应用于临床血清β2-MG的测定，并初步建立可快速检测β2-MG的胶体金免疫层析法。结果表明，基于5H7/6H9-AP抗体对构建的CLEIA检测体系线性范围为0.14~120.00 μg/L（可扩展至60.00 mg/L），所开发的CLEIA与医院使用的胶乳增强免疫比浊法相比，两种方法具有良好的一致性和较高的相关性，相关系数R²为0.96且P<0.000 1。本研究建立的胶体金免疫层析法检测重组β2-MG的最低限度可达到0.20 mg/L，表现出较好的敏感性，表明筛选的抗人β2-MG单克隆抗体及建立的定量和定性免疫检测方法具有临床诊断应用的潜力。

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彭倩　女，硕士研究生。研究方向为免疫诊断试剂研究。E-mail: 749950764@qq.com

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