The novel Fh8 and H fusion partners for soluble protein expression in Escherichia coli: A comparison with the traditional gene fusion technology

Applied Microbiology and Biotechnology

Volumn 97, Issue 15, 2013, Pages 6779-6791

  Costa, Sofia J ^a,b   Almeida, André ^c,d   Castro, António ^b   Domingues, Lucília ^a   Besir, Hüseyin ^e  

^a Campus de Gualtar   (Portugal)

^b NATIONAL INSTITUTE OF HEALTH   (Portugal)

^c Biocant Biotechnology Innovation Center   (Portugal)

^d UNIVERSITY OF PORTO   (Portugal)

^e EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

Escherichia coli; Fh8 fusion tag; Fusion protein; Protein solubility; Tag removal; Traditionally used fusion tags

Indexed keywords

EFFECTIVE SOLUBILITIES; FUSION PROTEINS; FUSION TAG; GENE FUSION TECHNOLOGY; PROTEIN SOLUBILITY; RECOMBINANT PROTEIN PRODUCTIONS; SODIUM DODECYL SULFATE-POLYACRYLAMIDE GEL ELECTROPHORESIS; TAG REMOVAL;

ELECTROPHORESIS; ESCHERICHIA COLI; SODIUM DODECYL SULFATE; SOLUBILITY;

PROTEINS;

BACTERIAL PROTEIN;

COLIFORM BACTERIUM; ELECTROKINESIS; GENE EXPRESSION; MOLECULAR ANALYSIS; POLLUTANT REMOVAL; PROTEIN; SOLUBILIZATION;

ARTICLE; CELL CULTURE; CYTOLYSIS; ESCHERICHIA COLI; GENE FUSION; NONHUMAN; PROTEIN EXPRESSION; PROTEIN PURIFICATION; SOLUBILITY;

BASE SEQUENCE; CLONING, MOLECULAR; DNA PRIMERS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GENE FUSION; POLYMERASE CHAIN REACTION; SOLUBILITY;

ESCHERICHIA COLI;

EID: 84880514065     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-012-4559-1     Document Type: Article

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