Literature DB >> 16786266

Expression, renaturation and simultaneous purification of recombinant human stem cell factor in Escherichia coli.

Wang Lili1, Wang Chaozhan, Geng Xindu.   

Abstract

Recombinant human stem cell factor (rhSCF) was produced as an inclusion body by Escherichia coli DH5alpha grown in a 5 l fermentor. Inclusion bodies of rhSCF were purified and solubilized in urea solution, then renatured with simultaneous purification using a high performance hydrophobic interaction chromatographic (HPHIC) squat column. The refolded rhSCF had a purity of 94% and a bioactivity of 1.2 x 10(6 )IU mg(-1)of rhSCF protein. The method described is fast and simple to implement.

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Year:  2006        PMID： 16786266     DOI： 10.1007/s10529-006-9032-8

Source DB:  PubMed          Journal:  Biotechnol Lett        ISSN： 0141-5492            Impact factor:   2.461


  2 in total

1.  Low-scale expression and purification of an active putative iduronate 2-sulfate sulfatase-Like enzyme from Escherichia coli K12.

Authors:  Edwin David Morales-Álvarez; Claudia Marcela Rivera-Hoyos; Angélica María Baena-Moncada; Patricia Landázuri; Raúl A Poutou-Piñales; Homero Sáenz-Suárez; Luis A Barrera; Olga Y Echeverri-Peña
Journal:  J Microbiol       Date:  2013-04-27       Impact factor: 3.422

2.  Novel Bacterial Production of Two Different Bioactive Forms of Human Stem-Cell Factor.

Authors:  Eunyoung Lee; Michelle Novais de Paula; Sangki Baek; Huynh Kim Khanh Ta; Minh Tan Nguyen; Taeck-Hyun Jeong; Chong Jai Kim; Yeon Jin Jang; Han Choe
Journal:  Int J Mol Sci       Date:  2021-06-14       Impact factor: 5.923
  2 in total

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