Recombinant proteins, produced in cells or microorganisms, play an important role in basic research, medical science and the biotechnology industry. Many foreign gene expression systems using mammalian cells, E. coli, insect cells, yeast and other organisms as hosts have been developed. However, only recently has the expression system of Schizosaccharomyces pombe as a host become a subject of focus, as it is expected to be profitable for expressing foreign genes. The reason for this is that S. pombe is evolutionarily more advanced than other types of yeast. This book describes the use of S. pombe in basic research and industrial applications.…mehr
Recombinant proteins, produced in cells or microorganisms, play an important role in basic research, medical science and the biotechnology industry. Many foreign gene expression systems using mammalian cells, E. coli, insect cells, yeast and other organisms as hosts have been developed. However, only recently has the expression system of Schizosaccharomyces pombe as a host become a subject of focus, as it is expected to be profitable for expressing foreign genes. The reason for this is that S. pombe is evolutionarily more advanced than other types of yeast. This book describes the use of S. pombe in basic research and industrial applications.
1. Fission Yeast Schizosaccharomycespombe: An Attractive Host for Heterologous Protein Production.- 2. Constitution of Expression Vectors.- 3. Exploiting the Thiamine Biosynthetic Gene nmtl for Regulated Expression of Heterologous DNAs in Fission Yeast.- 4. Development of Constitutive Expression Vector for the Highest Production Level of Heterologous Proteins in Fission Yeast Schizosaccharomycespombe.- 5. Overexpression of Proteins with Seven Transmembrane Spanning Segments.- 6. Targeting and Isolation of Tagged Membrane Proteins.- 7. Expression of a Human Cytochrome P450 Form in Schizosaccharomyces pombe: Comparison with Expression in Saccharomyces cerevisiae.- 8. Human Papillomavirus Capsid Protein-pREP in Schizosaccharomyces pombe: Efficient Assembly of the Viral Capsid Protein in S. pombe and S. cerevisiae.- 9. Expression, Purification, and Analyses of Cell-Cycle Regulatory Proteins in S. pombe.- 10. Expression and Secretion of Mammalian Proteins in Schizosaccharomyces pombe.- 11. Secretion of Human Interleukin-6 Using the P-Factor Secretion Signal in Schizosaccharomyces pombe.- Color Figures.
1. Fission Yeast Schizosaccharomycespombe: An Attractive Host for Heterologous Protein Production.- 2. Constitution of Expression Vectors.- 3. Exploiting the Thiamine Biosynthetic Gene nmtl for Regulated Expression of Heterologous DNAs in Fission Yeast.- 4. Development of Constitutive Expression Vector for the Highest Production Level of Heterologous Proteins in Fission Yeast Schizosaccharomycespombe.- 5. Overexpression of Proteins with Seven Transmembrane Spanning Segments.- 6. Targeting and Isolation of Tagged Membrane Proteins.- 7. Expression of a Human Cytochrome P450 Form in Schizosaccharomyces pombe: Comparison with Expression in Saccharomyces cerevisiae.- 8. Human Papillomavirus Capsid Protein-pREP in Schizosaccharomyces pombe: Efficient Assembly of the Viral Capsid Protein in S. pombe and S. cerevisiae.- 9. Expression, Purification, and Analyses of Cell-Cycle Regulatory Proteins in S. pombe.- 10. Expression and Secretion of Mammalian Proteins in Schizosaccharomyces pombe.- 11. Secretion of Human Interleukin-6 Using the P-Factor Secretion Signal in Schizosaccharomyces pombe.- Color Figures.
Es gelten unsere Allgemeinen Geschäftsbedingungen: www.buecher.de/agb
Impressum
www.buecher.de ist ein Internetauftritt der buecher.de internetstores GmbH
Geschäftsführung: Monica Sawhney | Roland Kölbl | Günter Hilger
Sitz der Gesellschaft: Batheyer Straße 115 - 117, 58099 Hagen
Postanschrift: Bürgermeister-Wegele-Str. 12, 86167 Augsburg
Amtsgericht Hagen HRB 13257
Steuernummer: 321/5800/1497