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

Nikki P Y Lee, Stella Tsang, R. Holland Cheng, John M. Luk

Research output: Contribution to journalArticlepeer-review

8 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)431-435
Number of pages5
JournalProtein and Peptide Letters
Issue number5
StatePublished - May 2006
Externally publishedYes


  • βA domain
  • Leukocyte integrin
  • Maltose-binding protein

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


Dive into the research topics of 'Increased solubility of integrin βA domain using maltose-binding protein as a fusion tag'. Together they form a unique fingerprint.

Cite this