Show simple item record

dc.contributor.author王生育zh_CN
dc.contributor.author颜江华zh_CN
dc.contributor.author潘阳霖zh_CN
dc.contributor.author李学军zh_CN
dc.contributor.author陈忠zh_CN
dc.date.accessioned2011-04-26T08:24:06Z
dc.date.available2011-04-26T08:24:06Z
dc.date.issued2008-04-25zh_CN
dc.identifier.citation生物工程学报 Chinese Journal of Biotechnology,200824(4):553-557zh_CN
dc.identifier.issn1000-3061zh_CN
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/8488
dc.description.abstract从GenBank获得人PTP1B催化活性区(PTP1Bc)氨基酸序列(1~301aa),通过重叠PCR获得PTP1Bc基因。构建pET-22b(+)/PTP1Bc原核表达载体,转化大肠杆菌BL21(DE3),阳性重组子IPTG诱导表达,Ni柱纯化蛋白。目的蛋白以包涵体的形式表达,表达量占菌体总蛋白30%以上。纯化后,蛋白纯度达95%以上。Western blotting结果表明所得的蛋白可与抗PTP1B抗体发生特异性结合;酶活实验证实复性的蛋白具有一定的磷酸酶活性。PTP1Bc基因的构建、表达纯化及活性分析,为进一步的功能研究奠定了基础。 【英文摘要】 The amino acid sequence (1-301aa) coding the human PTP1B catalytic domain (PTP1Bc) was obtained from the GenBank.The PTP1Bc gene was constructed by overlapping PCR,then was inserted into vector pET-22b(+) and expressed efficiently in E.coli BL21(DE3) under optimum condition after IPTG induction.The proteins were expressed mainly as inclusion bodies with the yield of more than 30% of total bacterial proteins.The expressed products were purified through Ni~(2+)-affinity chromatographic column.After purificati...zh_CN
dc.description.sponsorship厦门市重大疾病攻关研究基金(No.3502220051027);; 卫生部(福建省)卫生教育联合攻关项目(No.Wkj2005-2-019)资助~~zh_CN
dc.language.isozhzh_CN
dc.publisher中国科学院微生物所;中国微生物学会zh_CN
dc.subjectPTP1Bczh_CN
dc.subject基因表达zh_CN
dc.subject蛋白纯化zh_CN
dc.subject活性分析zh_CN
dc.subjectexpressionzh_CN
dc.subjectprotein purificationzh_CN
dc.subjectactivity analysiszh_CN
dc.title蛋白酪氨酸磷酸酶PTP1B催化活性区的原核表达及活性分析zh_CN
dc.title.alternativeExpression and Activity Analysis of Catalytic Domain of PTP1Bzh_CN
dc.typeArticlezh_CN


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record