Cell-free expression systems for disulfide rich proteins
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Bester Preis: € 60,00 (vom 24.11.2019)1
Cell-free expression systems for disulfide rich proteins
DE PB NW
ISBN: 9783639666847 bzw. 3639666844, in Deutsch, Scholar'S Press, Taschenbuch, neu.
Lieferung aus: Deutschland, Versandkostenfrei.
buecher.de GmbH & Co. KG, [1].
Most extracellular proteins are stabilized by multiple disulfide bonds formed by the oxidation of pairs of cysteine residues. The most popular host for recombinant protein production is Escherichia coli, but disulfide rich proteins are here often misfolded, degraded, or found in inclusion bodies. An alternative expression system is the cell-free in vitro translation system based on wheat germ extract. It is an open system in which an optimized mix of thiol-disulfide oxidoreductases or chaperones can be added, so that disulfide rich proteins have no chance to aggregate the moment their polypeptide chain emerges from the ribosomes. We have challenged this in vitro translation system with three disulfide rich proteins: mouse Found in Inflammatory Zone (mFIZZ1), Androctonus australis hector (AahII) scorpion toxin, and mouse Vascular Endothelial Growth Factor (mVEGF164). By co-translation of the thiol/disulfide oxidoreductase hQSOX1b, soluble and biological active protein were obtained.2014. 200 S. 220 mmVersandfertig in 3-5 Tagen, Softcover.
buecher.de GmbH & Co. KG, [1].
Most extracellular proteins are stabilized by multiple disulfide bonds formed by the oxidation of pairs of cysteine residues. The most popular host for recombinant protein production is Escherichia coli, but disulfide rich proteins are here often misfolded, degraded, or found in inclusion bodies. An alternative expression system is the cell-free in vitro translation system based on wheat germ extract. It is an open system in which an optimized mix of thiol-disulfide oxidoreductases or chaperones can be added, so that disulfide rich proteins have no chance to aggregate the moment their polypeptide chain emerges from the ribosomes. We have challenged this in vitro translation system with three disulfide rich proteins: mouse Found in Inflammatory Zone (mFIZZ1), Androctonus australis hector (AahII) scorpion toxin, and mouse Vascular Endothelial Growth Factor (mVEGF164). By co-translation of the thiol/disulfide oxidoreductase hQSOX1b, soluble and biological active protein were obtained.2014. 200 S. 220 mmVersandfertig in 3-5 Tagen, Softcover.
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Cell-free expression systems for disulfide rich proteins
~EN PB NW
ISBN: 9783639666847 bzw. 3639666844, vermutlich in Englisch, SPS, Taschenbuch, neu.
Lieferung aus: Deutschland, Versandkostenfrei.
Cell-free expression systems for disulfide rich proteins: Most extracellular proteins are stabilized by multiple disulfide bonds formed by the oxidation of pairs of cysteine residues. The most popular host for recombinant protein production is Escherichia coli, but disulfide rich proteins are here often misfolded, degraded, or found in inclusion bodies. An alternative expression system is the cell-free in vitro translation system based on wheat germ extract. It is an open system in which an optimized mix of thiol-disulfide oxidoreductases or chaperones can be added, so that disulfide rich proteins have no chance to aggregate the moment their polypeptide chain emerges from the ribosomes. We have challenged this in vitro translation system with three disulfide rich proteins: mouse Found in Inflammatory Zone (mFIZZ1), Androctonus australis hector (AahII) scorpion toxin, and mouse Vascular Endothelial Growth Factor (mVEGF164). By co-translation of the thiol/disulfide oxidoreductase hQSOX1b, soluble and biological active protein were obtained. Englisch, Taschenbuch.
Cell-free expression systems for disulfide rich proteins: Most extracellular proteins are stabilized by multiple disulfide bonds formed by the oxidation of pairs of cysteine residues. The most popular host for recombinant protein production is Escherichia coli, but disulfide rich proteins are here often misfolded, degraded, or found in inclusion bodies. An alternative expression system is the cell-free in vitro translation system based on wheat germ extract. It is an open system in which an optimized mix of thiol-disulfide oxidoreductases or chaperones can be added, so that disulfide rich proteins have no chance to aggregate the moment their polypeptide chain emerges from the ribosomes. We have challenged this in vitro translation system with three disulfide rich proteins: mouse Found in Inflammatory Zone (mFIZZ1), Androctonus australis hector (AahII) scorpion toxin, and mouse Vascular Endothelial Growth Factor (mVEGF164). By co-translation of the thiol/disulfide oxidoreductase hQSOX1b, soluble and biological active protein were obtained. Englisch, Taschenbuch.
3
Cell-free expression systems for disulfide rich proteins
DE NW
ISBN: 9783639666847 bzw. 3639666844, in Deutsch, VDM Verlag Dr. Müller, Saarbrücken, Deutschland, neu.
Lieferung aus: Deutschland, zzgl. Versandkosten.
Most extracellular proteins are stabilized by multiple disulfide bonds formed by the oxidation of pairs of cysteine residues. The most popular host for recombinant protein production is Escherichia coli, but disulfide rich proteins are here often misfolded, degraded, or found in inclusion bodies. An alternative expression system is the cell-free in vitro translation system based on wheat germ extract. It is an open system in which an optimized mix of thiol-disulfide oxidoreductases or chaperones can be added, so that disulfide rich proteins have no chance to aggregate the moment their polypeptide chain emerges from the ribosomes. We have challenged this in vitro translation system with three disulfide rich proteins: mouse Found in Inflammatory Zone (mFIZZ1), Androctonus australis hector (AahII) scorpion toxin, and mouse Vascular Endothelial Growth Factor (mVEGF164). By co-translation of the thiol/disulfide oxidoreductase hQSOX1b, soluble and biological active protein were obtained.
Most extracellular proteins are stabilized by multiple disulfide bonds formed by the oxidation of pairs of cysteine residues. The most popular host for recombinant protein production is Escherichia coli, but disulfide rich proteins are here often misfolded, degraded, or found in inclusion bodies. An alternative expression system is the cell-free in vitro translation system based on wheat germ extract. It is an open system in which an optimized mix of thiol-disulfide oxidoreductases or chaperones can be added, so that disulfide rich proteins have no chance to aggregate the moment their polypeptide chain emerges from the ribosomes. We have challenged this in vitro translation system with three disulfide rich proteins: mouse Found in Inflammatory Zone (mFIZZ1), Androctonus australis hector (AahII) scorpion toxin, and mouse Vascular Endothelial Growth Factor (mVEGF164). By co-translation of the thiol/disulfide oxidoreductase hQSOX1b, soluble and biological active protein were obtained.
4
Cell-free expression systems for disulfide rich proteins
~EN NW AB
ISBN: 9783639666847 bzw. 3639666844, vermutlich in Englisch, VDM Verlag Dr. Müller, Saarbrücken, Deutschland, neu, Hörbuch.
Lieferung aus: Deutschland, Lieferzeit: 5 Tage.
Most extracellular proteins are stabilized by multiple disulfide bonds formed by the oxidation of pairs of cysteine residues. The most popular host for recombinant protein production is Escherichia coli, but disulfide rich proteins are here often misfolded, degraded, or found in inclusion bodies. An alternative expression system is the cell-free in vitro translation system based on wheat germ extract. It is an open system in which an optimized mix of thiol-disulfide oxidoreductases or chaperones can be added, so that disulfide rich proteins have no chance to aggregate the moment their polypeptide chain emerges from the ribosomes. We have challenged this in vitro translation system with three disulfide rich proteins: mouse Found in Inflammatory Zone (mFIZZ1), Androctonus australis hector (AahII) scorpion toxin, and mouse Vascular Endothelial Growth Factor (mVEGF164). By co-translation of the thiol/disulfide oxidoreductase hQSOX1b, soluble and biological active protein were obtained.
Most extracellular proteins are stabilized by multiple disulfide bonds formed by the oxidation of pairs of cysteine residues. The most popular host for recombinant protein production is Escherichia coli, but disulfide rich proteins are here often misfolded, degraded, or found in inclusion bodies. An alternative expression system is the cell-free in vitro translation system based on wheat germ extract. It is an open system in which an optimized mix of thiol-disulfide oxidoreductases or chaperones can be added, so that disulfide rich proteins have no chance to aggregate the moment their polypeptide chain emerges from the ribosomes. We have challenged this in vitro translation system with three disulfide rich proteins: mouse Found in Inflammatory Zone (mFIZZ1), Androctonus australis hector (AahII) scorpion toxin, and mouse Vascular Endothelial Growth Factor (mVEGF164). By co-translation of the thiol/disulfide oxidoreductase hQSOX1b, soluble and biological active protein were obtained.
6
Cell-free expression systems for disulfide rich proteins
~EN PB NW
ISBN: 3639666844 bzw. 9783639666847, vermutlich in Englisch, SPS, Taschenbuch, neu.
Die Beschreibung dieses Angebotes ist von geringer Qualität oder in einer Fremdsprache. Trotzdem anzeigen
7
Cell-free expression systems for disulfide rich proteins
EN NW
ISBN: 9783639666847 bzw. 3639666844, in Englisch, OmniScriptum GmbH & Co. KG, OmniScriptum GmbH & Co. KG, neu.
Lieferung aus: Vereinigte Staaten von Amerika, zzgl. Versandkosten, Free Shipping on eligible orders over $25.
Gad Wael, Paperback, English-language edition, Pub by OmniScriptum GmbH & Co. KG.
Gad Wael, Paperback, English-language edition, Pub by OmniScriptum GmbH & Co. KG.
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Cell-free expression systems for disulfide rich proteins (2014)
~EN PB NW
ISBN: 9783639666847 bzw. 3639666844, vermutlich in Englisch, VDM Verlag Dr. Müller, Saarbrücken, Deutschland, Taschenbuch, neu.
Lieferung aus: Deutschland, Next Day, Versandkostenfrei.
Die Beschreibung dieses Angebotes ist von geringer Qualität oder in einer Fremdsprache. Trotzdem anzeigen
Die Beschreibung dieses Angebotes ist von geringer Qualität oder in einer Fremdsprache. Trotzdem anzeigen
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