GAS1 universal leader

Chemistry: molecular biology and microbiology – Vector – per se

Reexamination Certificate

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C435S006120, C536S023100

Reexamination Certificate

active

07846721

ABSTRACT:
Disclosed is a polynucleotide molecule comprising a promoter operably linked to a nucleic acid sequence encoding a GAS1 secretion signal peptide, wherein said promoter is not a rhamnose promoter.

REFERENCES:
patent: 6555310 (2003-04-01), Gray et al.
patent: WO 95/22614 (1995-08-01), None
patent: WO 03/068956 (2003-08-01), None
patent: WO03/068956 (2003-08-01), None
Humphreys et al., 2000, High-Level Periplasmic Expression inEscherichia coliUsing a Eukaryotic Signal Peptide: Importance of Codon Usage a the 5′ End of the Coding Sequence, Protein Expression and Purification, 20: 252-264.
Wada et al., 1991, Codon usage tabulated from the GenBank genetic sequence data, Nucleic Acids Research, 19: 1981-1986.
Wada et al., 1992, Codon usage tabulated from the GenBank genetic sequence data, Nucleic Acids Research, 20: 2111-2118.
Nuoffer, et al., “Determinants for Glycophospholipid Anchoring of theSaccharomyces cerevisaeGAS1 Protein to the Plasma Membrane,” Molecular and Cellular Biology (Jan. 1991), p. 27-37.
Pignatelli, et al., “Expression and secretion of β-galactosidase inSaccharomyces cerevisiaeusing the signal sequences of GgpI, the major yeast glycosylphosphatidylinositol-containing protein,” Biotechnol. Appl. Biochem., vol. 27 (1998), p. 81-88.
Vai, et al., “Isolation and Deduced Amino Acid Sequence of the Gene Encoding gp115, a Yeast Glycophospholipid-anchored Protein Containing a Serine-rich Region,” Journal of Biological Chemistry, vol. 266, No. 19 (Jul. 5, 1991), p. 12242-12248.
Watson, Marion E.E., “Compilation of published signal sequences,” Nucl. Acids Res., vol. 12, No. 13 (1984), p. 5154-5164.

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