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Cash, H.L., Whitham, C.V. and Hooper, L.V. (2006) Refolding, Purification, and Characterization of Human and Murine Reg III Proteins Expressed in Escherichia coli. Protein Expression and Purification, 48, 151-159. https://doi.org/10.1016/j.pep.2006.01.014

has been cited by the following article:

• TITLE: Recombinant Human REG Iα Aggregates Staphylococcus aureus—Exhibits a Lectin-Like Function

  AUTHORS: Nausheen Jamal, Yuichiro Kezuka, Takamasa Nonaka, Kazuaki Ohashi, Koji Nata

  KEYWORDS: Reg Proteins, Lectin-Like Activity, Bacterial Aggregation

  JOURNAL NAME: Advances in Bioscience and Biotechnology, Vol.8 No.3, March 16, 2017

  ABSTRACT: Staphylococcus aureus is pathogenic to humans with worldwide health care concern due to its ability to evade the immune system and develop resistance to multiple drugs. Reg family proteins are C-type lectins with antimicrobial properties. Bacterial aggregation through binding to microbial cell surface sugar and/or lipid moieties is key mechanism employed in the process. In the present study we have analysed the antimicrobial effect of human REG Iα on S. aureus. Aggregation of mid-log phase culture of S. aureus was observed in presence of purified recombinant REG Iα. Therefore REG Iα can be applied in eliminating S. aureus infections in humans.