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Article: High level expression, purification and characterization of active fusion human C1q and tumor necrosis factor related protein 2 (hCTRP2) in Escherichia coli

TitleHigh level expression, purification and characterization of active fusion human C1q and tumor necrosis factor related protein 2 (hCTRP2) in Escherichia coli
Authors
KeywordsEscherichia coli
Expression and purification
Fusion protein
Human C1q and tumor necrosis factor related protein 2 (hCTRP2)
Pichia pastoris
Issue Date2011
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yprep
Citation
Protein Expression And Purification, 2011, v. 79 n. 1, p. 1-6 How to Cite?
AbstractC1q and tumor necrosis factor related proteins (CTRPs) are a family of adiponectin paralogues. Among them, CTRP2 is the only CTRP protein that has been shown to possess similar biological activities as adiponectin. To further explore the physiological roles of human CTRP2 and its mechanisms of action, hCTRP2 gene was expressed in Escherichia coli and Pichia pastoris, respectively. In the P. pastoris expression system, recombinant hCTRP2 could be secreted into the culture medium under induction condition, however, the resultant recombinant protein was highly unstable, resulting two main degradation products with molecular masses of approximately 20 and 26 kDa, respectively. In the E. coli expression system, a large amount of soluble thioredoxin (Trx)-hCTRP2 fusion protein could be produced, which accounts about 42% of the total soluble bacterial proteins. The recombinant Trx-hCTRP2 fusion protein was purified to an approximately 95% purity using Ni-NTA affinity chromatography and Superdex G-75 column with a yield of about 15 mg/l protein from 1 l bacterial culture. The purified recombinant Trx-hCTRP2 was shown to be active under in vitro assay conditions. © 2011 Elsevier Inc. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/163385
ISSN
2015 Impact Factor: 1.407
2015 SCImago Journal Rankings: 0.767
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLi, Hen_HK
dc.contributor.authorGao, Xen_HK
dc.contributor.authorZhou, Yen_HK
dc.contributor.authorLi, Nen_HK
dc.contributor.authorGe, Cen_HK
dc.contributor.authorHui, Xen_HK
dc.contributor.authorWang, Yen_HK
dc.contributor.authorXu, Aen_HK
dc.contributor.authorJin, Sen_HK
dc.contributor.authorWu, Den_HK
dc.date.accessioned2012-09-05T05:30:46Z-
dc.date.available2012-09-05T05:30:46Z-
dc.date.issued2011en_HK
dc.identifier.citationProtein Expression And Purification, 2011, v. 79 n. 1, p. 1-6en_HK
dc.identifier.issn1046-5928en_HK
dc.identifier.urihttp://hdl.handle.net/10722/163385-
dc.description.abstractC1q and tumor necrosis factor related proteins (CTRPs) are a family of adiponectin paralogues. Among them, CTRP2 is the only CTRP protein that has been shown to possess similar biological activities as adiponectin. To further explore the physiological roles of human CTRP2 and its mechanisms of action, hCTRP2 gene was expressed in Escherichia coli and Pichia pastoris, respectively. In the P. pastoris expression system, recombinant hCTRP2 could be secreted into the culture medium under induction condition, however, the resultant recombinant protein was highly unstable, resulting two main degradation products with molecular masses of approximately 20 and 26 kDa, respectively. In the E. coli expression system, a large amount of soluble thioredoxin (Trx)-hCTRP2 fusion protein could be produced, which accounts about 42% of the total soluble bacterial proteins. The recombinant Trx-hCTRP2 fusion protein was purified to an approximately 95% purity using Ni-NTA affinity chromatography and Superdex G-75 column with a yield of about 15 mg/l protein from 1 l bacterial culture. The purified recombinant Trx-hCTRP2 was shown to be active under in vitro assay conditions. © 2011 Elsevier Inc. All rights reserved.en_HK
dc.languageengen_US
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yprepen_HK
dc.relation.ispartofProtein Expression and Purificationen_HK
dc.subjectEscherichia colien_HK
dc.subjectExpression and purificationen_HK
dc.subjectFusion proteinen_HK
dc.subjectHuman C1q and tumor necrosis factor related protein 2 (hCTRP2)en_HK
dc.subjectPichia pastorisen_HK
dc.subject.meshCloning, Molecularen_US
dc.subject.meshEscherichia Coli - Geneticsen_US
dc.subject.meshGene Expressionen_US
dc.subject.meshHumansen_US
dc.subject.meshPichia - Geneticsen_US
dc.subject.meshProteins - Genetics - Isolation & Purification - Metabolismen_US
dc.subject.meshRecombinant Fusion Proteins - Genetics - Isolation & Purification - Metabolismen_US
dc.titleHigh level expression, purification and characterization of active fusion human C1q and tumor necrosis factor related protein 2 (hCTRP2) in Escherichia colien_HK
dc.typeArticleen_HK
dc.identifier.emailWang, Y: yuwanghk@hku.hken_HK
dc.identifier.emailXu, A: amxu@hkucc.hku.hken_HK
dc.identifier.authorityWang, Y=rp00239en_HK
dc.identifier.authorityXu, A=rp00485en_HK
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/j.pep.2011.03.013en_HK
dc.identifier.pmid21453774-
dc.identifier.scopuseid_2-s2.0-79960133528en_HK
dc.identifier.hkuros206391-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-79960133528&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume79en_HK
dc.identifier.issue1en_HK
dc.identifier.spage1en_HK
dc.identifier.epage6en_HK
dc.identifier.isiWOS:000292996100001-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridLi, H=40261980700en_HK
dc.identifier.scopusauthoridGao, X=26028577700en_HK
dc.identifier.scopusauthoridZhou, Y=25654258200en_HK
dc.identifier.scopusauthoridLi, N=36065390000en_HK
dc.identifier.scopusauthoridGe, C=54389034600en_HK
dc.identifier.scopusauthoridHui, X=26666795900en_HK
dc.identifier.scopusauthoridWang, Y=34973733700en_HK
dc.identifier.scopusauthoridXu, A=7202655409en_HK
dc.identifier.scopusauthoridJin, S=7401822323en_HK
dc.identifier.scopusauthoridWu, D=7404297751en_HK
dc.identifier.citeulike9126065-

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