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Article: Increased solubility of integrin βA domain using maltose-binding protein as a fusion tag

TitleIncreased solubility of integrin βA domain using maltose-binding protein as a fusion tag
Authors
Issue Date2006
PublisherBentham Science Publishers Ltd. The Journal's web site is located at http://www.bentham.org/ppl/index.htm
Citation
Protein And Peptide Letters, 2006, v. 13 n. 5, p. 431-435 How to Cite?
AbstractIn proteomics research, generation of recombinant proteins in their native, soluble form with large quantity is often a challenging task. To tackle the expression difficulties, different expression vectors with distinct affinity fusion tags, i.e. pET-43.1a (N-utilization substance A tag), pMAL-cRI (maltose binding protein tag) (MBP tag), pGEX-4T-2 (glutathione S-transferase tag), and pET-15b (hexahistidine tag) were compared for their effects on the productivity and solubility, which were assessed by SDS-PAGE and immunoblotting, of the integrin βA domain. The incubation temperatures were tested for its effects on these parameters. Our data suggested that MBP tag enhanced the yield and solubility of the βA domain protein, which can also be recognized using an anti-CD18 antibody, at room temperature incubation. Thus, the nature of fusion partner chosen for expression in bacteria and its incubation temperature would significantly affect the yield and solubility of the recombinant target protein. © 2006 Bentham Science Publishers Ltd.
Persistent Identifierhttp://hdl.handle.net/10722/172911
ISSN
2015 Impact Factor: 1.069
2015 SCImago Journal Rankings: 0.472
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLee, NPYen_US
dc.contributor.authorTsang, Sen_US
dc.contributor.authorCheng, RHen_US
dc.contributor.authorLuk, JMen_US
dc.date.accessioned2012-10-30T06:25:45Z-
dc.date.available2012-10-30T06:25:45Z-
dc.date.issued2006en_US
dc.identifier.citationProtein And Peptide Letters, 2006, v. 13 n. 5, p. 431-435en_US
dc.identifier.issn0929-8665en_US
dc.identifier.urihttp://hdl.handle.net/10722/172911-
dc.description.abstractIn proteomics research, generation of recombinant proteins in their native, soluble form with large quantity is often a challenging task. To tackle the expression difficulties, different expression vectors with distinct affinity fusion tags, i.e. pET-43.1a (N-utilization substance A tag), pMAL-cRI (maltose binding protein tag) (MBP tag), pGEX-4T-2 (glutathione S-transferase tag), and pET-15b (hexahistidine tag) were compared for their effects on the productivity and solubility, which were assessed by SDS-PAGE and immunoblotting, of the integrin βA domain. The incubation temperatures were tested for its effects on these parameters. Our data suggested that MBP tag enhanced the yield and solubility of the βA domain protein, which can also be recognized using an anti-CD18 antibody, at room temperature incubation. Thus, the nature of fusion partner chosen for expression in bacteria and its incubation temperature would significantly affect the yield and solubility of the recombinant target protein. © 2006 Bentham Science Publishers Ltd.en_US
dc.languageengen_US
dc.publisherBentham Science Publishers Ltd. The Journal's web site is located at http://www.bentham.org/ppl/index.htmen_US
dc.relation.ispartofProtein and Peptide Lettersen_US
dc.subject.meshAnimalsen_US
dc.subject.meshCarrier Proteins - Genetics - Metabolismen_US
dc.subject.meshChromatography, Affinityen_US
dc.subject.meshHumansen_US
dc.subject.meshIntegrin Beta Chains - Chemistry - Genetics - Isolation & Purification - Metabolismen_US
dc.subject.meshLeukocytes - Cytology - Metabolismen_US
dc.subject.meshMaltose-Binding Proteinsen_US
dc.subject.meshProtein Structure, Tertiaryen_US
dc.subject.meshRecombinant Fusion Proteins - Chemistry - Genetics - Isolation & Purification - Metabolismen_US
dc.subject.meshSolubilityen_US
dc.titleIncreased solubility of integrin βA domain using maltose-binding protein as a fusion tagen_US
dc.typeArticleen_US
dc.identifier.emailLee, NPY: nikkilee@hku.hken_US
dc.identifier.emailLuk, JM: jmluk@hkucc.hku.hken_US
dc.identifier.authorityLee, NPY=rp00263en_US
dc.identifier.authorityLuk, JM=rp00349en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.2174/092986606776819493en_US
dc.identifier.pmid16800794-
dc.identifier.scopuseid_2-s2.0-33646431747en_US
dc.identifier.hkuros136468-
dc.identifier.hkuros118789-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33646431747&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume13en_US
dc.identifier.issue5en_US
dc.identifier.spage431en_US
dc.identifier.epage435en_US
dc.identifier.isiWOS:000237935900003-
dc.publisher.placeNetherlandsen_US
dc.identifier.scopusauthoridLee, NPY=7402722690en_US
dc.identifier.scopusauthoridTsang, S=7102255965en_US
dc.identifier.scopusauthoridCheng, RH=21033815200en_US
dc.identifier.scopusauthoridLuk, JM=7006777791en_US
dc.identifier.citeulike603255-

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