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- Publisher Website: 10.2174/092986606776819493
- Scopus: eid_2-s2.0-33646431747
- PMID: 16800794
- WOS: WOS:000237935900003
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Article: Increased solubility of integrin βA domain using maltose-binding protein as a fusion tag
Title | Increased solubility of integrin βA domain using maltose-binding protein as a fusion tag |
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Authors | |
Keywords | βA domain Leukocyte integrin Maltose-binding protein |
Issue Date | 2006 |
Publisher | Bentham 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? |
Abstract | In 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 Identifier | http://hdl.handle.net/10722/172911 |
ISSN | 2023 Impact Factor: 1.0 2023 SCImago Journal Rankings: 0.349 |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Lee, NPY | en_US |
dc.contributor.author | Tsang, S | en_US |
dc.contributor.author | Cheng, RH | en_US |
dc.contributor.author | Luk, JM | en_US |
dc.date.accessioned | 2012-10-30T06:25:45Z | - |
dc.date.available | 2012-10-30T06:25:45Z | - |
dc.date.issued | 2006 | en_US |
dc.identifier.citation | Protein And Peptide Letters, 2006, v. 13 n. 5, p. 431-435 | en_US |
dc.identifier.issn | 0929-8665 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/172911 | - |
dc.description.abstract | In 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.language | eng | en_US |
dc.publisher | Bentham Science Publishers Ltd. The Journal's web site is located at http://www.bentham.org/ppl/index.htm | en_US |
dc.relation.ispartof | Protein and Peptide Letters | en_US |
dc.subject | βA domain | - |
dc.subject | Leukocyte integrin | - |
dc.subject | Maltose-binding protein | - |
dc.subject.mesh | Animals | en_US |
dc.subject.mesh | Carrier Proteins - Genetics - Metabolism | en_US |
dc.subject.mesh | Chromatography, Affinity | en_US |
dc.subject.mesh | Humans | en_US |
dc.subject.mesh | Integrin Beta Chains - Chemistry - Genetics - Isolation & Purification - Metabolism | en_US |
dc.subject.mesh | Leukocytes - Cytology - Metabolism | en_US |
dc.subject.mesh | Maltose-Binding Proteins | en_US |
dc.subject.mesh | Protein Structure, Tertiary | en_US |
dc.subject.mesh | Recombinant Fusion Proteins - Chemistry - Genetics - Isolation & Purification - Metabolism | en_US |
dc.subject.mesh | Solubility | en_US |
dc.title | Increased solubility of integrin βA domain using maltose-binding protein as a fusion tag | en_US |
dc.type | Article | en_US |
dc.identifier.email | Lee, NPY: nikkilee@hku.hk | en_US |
dc.identifier.email | Luk, JM: jmluk@hkucc.hku.hk | en_US |
dc.identifier.authority | Lee, NPY=rp00263 | en_US |
dc.identifier.authority | Luk, JM=rp00349 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.doi | 10.2174/092986606776819493 | en_US |
dc.identifier.pmid | 16800794 | - |
dc.identifier.scopus | eid_2-s2.0-33646431747 | en_US |
dc.identifier.hkuros | 136468 | - |
dc.identifier.hkuros | 118789 | - |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-33646431747&selection=ref&src=s&origin=recordpage | en_US |
dc.identifier.volume | 13 | en_US |
dc.identifier.issue | 5 | en_US |
dc.identifier.spage | 431 | en_US |
dc.identifier.epage | 435 | en_US |
dc.identifier.isi | WOS:000237935900003 | - |
dc.publisher.place | Netherlands | en_US |
dc.identifier.scopusauthorid | Lee, NPY=7402722690 | en_US |
dc.identifier.scopusauthorid | Tsang, S=7102255965 | en_US |
dc.identifier.scopusauthorid | Cheng, RH=21033815200 | en_US |
dc.identifier.scopusauthorid | Luk, JM=7006777791 | en_US |
dc.identifier.citeulike | 603255 | - |
dc.identifier.issnl | 0929-8665 | - |