Pectate lyase signal sequence

Chemistry: molecular biology and microbiology – Vector – per se

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435 691, 435 697, 435 698, 4351723, 4352523, 43525233, 435 48, 536 234, 536 237, C12N 1500, C12N 1531, C12N 1562, C12P 2100

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active

058468188

ABSTRACT:
The invention is directed to the pectate lyase B secretion signal and its use to express operably linked sequences in bacterial hosts.

REFERENCES:
patent: 4338397 (1982-07-01), Gilbert et al.
patent: 4642334 (1987-02-01), Moore et al.
patent: 4656134 (1987-04-01), Ringold
patent: 4816397 (1989-03-01), Boss et al.
patent: 4816567 (1989-03-01), Cabilly et al.
patent: 4935496 (1990-06-01), Kudo et al.
patent: 4963495 (1990-10-01), Chang et al.
patent: 5576195 (1996-11-01), Robinson et al.
Nikaido, N. et al., "Cloning of a Pectate Lyase Gene From Erwinia Carotovora and its Expression in Escheria Coli," J. Gen. Appl. Microbiol. 31:293-296 (1985).
Nikaido et al. Journal of General and Applied Microbiology, vol. 31, pp. 573-576, 1985.
Abrahmsen, L. et al., "Secretion of heterologous gene products to the culture medium of Escherichia coli," Nucl. Acids Res. 14(18):7487-7500 (Aug. 1986).
Alexander, A. et al., ".gamma. heavy chain disease in man: cDNA sequence supports partial gene deletion model," Proc. Natl. Acad. Sci. USA 79:3260-3264 (1982).
Anand, N.N. et al., "Synthesis and expression in Escherichia coli of cistronic DNA encoding an antibody fragment specific for a Salmonella serotyp B O-antigen," Gene 100:39-44 (Jun. 1991).
Anand, N.N. et al., "Bacterial Expression and Secretion of Various Single-chain Fv Genes Encoding Proteins Specific for a Salmonella Serotype B O-Antigen," J. Biol. Chem. 266(32):21874-21879 (Nov. 1991).
Banerji, J. et al., "A Lymphocyte-Specific Cellular Enhancer Is Located Downstream of the Joining Region in Immunoglobul in Heavy chain Genes," Cell 33:729-740 (1983).
Babas III, C.F. et al., "Assembly of combinatorial antibody libraries on phage surfaces: The gene III site," Proc. Natl. Acad. Sci. USA 88(18):7978-7982 (Sep. 1991).
Bebbington, C.R. et al., "High-Level Expression Of A Recombinant Antibody From Myeloma Cells Using A Glutamine Synthetase Gene As An Amplifiable Selectable Marker," Bio/Tech. 10:169-175 (Feb. 1992).
Beckwith, J. and S. Ferro-Novick, "Genetic Studies on Protein Export in Bacteria," Curr. Top. Microbiol. Immunol. 125:5-27 (Jul. 1986).
Beggs, J.D., "Multiple-copy Yeast Plasmid Vectors," Mool. Genet. Yeast. Alfred Benzon Symp. 16:383-389 (1981).
Bernstein, K.E. et al., "Nucleotide Sequence of a Rabbit IgG Heavy chain from the Recombinant F-I Haplotype," Immunogenetics 18(4):387-397 (1983).
Better, M. et al., "Escherichia coli Secretion of an Active Chimeric Antibody Fragment," Science 340:1041-1043 (May 1988).
Better, M. and A.H. Horowitz, "Expression of Engineered Antibodies and Antibody Fragments in Microorganisms," Meth. Enzymol. 178:476-496 (Nov. 1989).
Better, M. et al., "Production And Scale Up of Chimeric Fab Fragments From Bacteria," Advances in Gene Technology: The Molecular Biology of Immune Diseases and the Immune Response. Proceedings of the 1990 Miamo Bio/Technology Winter Symposia 10:105 (Jul. 1990).
Better, M. et al., "Potent anti-CD5 ricin A chain immunoconjugates from bacterially produced Fab' and (Fab').sub.2," Proc. Natl. Acad. Sci. USA 90:457-461 (Jan. 1993).
Better, M. and A.H. Horwitz, "In Vivo Expression of Correctly Folded Antibody Fragments from Microorganisms," in: Protein Folding--In Vivo and In Vitro, Cleland, J.L. , ed., Washington, D.C.: American Chemical Society pp. 203-217 (Apr. 1993).
Boss, M.A. et al., "Assembly of functional antibodies from immunoglobulin in heavy and light chains synthesised in E. coli," Nucl. Acids Res. 12(9):3791-3806 (1984).
Boulianne, G.L. et al., "Production of functional chimaeric mouse/human antibody," Nature 312:643-646 (1984).
Brown, N.A. et al., "Immunoglobulin J.sub.h , C.sub..mu., and C.sub..gamma. gene rearrangements in human B Lymphocytes clonally transformed by Epstein-Barr virus," Proc. Natl. Acad. Sci. USA 82:556-560 (1985).
Cabilly, S. et al., "Generation of antibody activity from immunoglobulin polypeptide chains produced in Escherichia coli," Proc. Natl. Acad. Sci. USA 81:3273-3277 (1984).
Calos, M.P. et al., "High mutation frequency in DNA transfected into mammalian cells," Proc. Natl. Acad. Sci. USA 80:3015-3019 (1983).
Carter, P. et al., "High Level Escherichia Coli Expression And Production Of A Bivalent Humanized Antibody Fragment," Bio/Technol. 10:163-167 (Feb. 1992).
Chan, S.J. et al., "Biosynthesis and periplasmic segregation of human proinsulin in Escherichia coli," Proc. Natl. Acad. Sci. USA 78(9):5401-5405 (1981).
Clackson, T. et al., "Making antibody fragments using phage display libraries," Nature 352:624-628 (Aug. 1991).
Clontech Catalog, Bacterial Strains and Numberical Index, pp. 224 and 277 (Jul. 1993).
Denefle, P. et al., "Heterologous protein export in Escherichia coli: influence of bacterial signal peptides on the export of human interleukin 1.beta.," Gene 85:499-510 (Dec. 1989).
Dickson, S., "Scientists Produce Chimeric Monoclonal Abs," Genetic Engineering News 5(3):1 and 33 (1985).
Dolby, T.W. et al., "Cloning and partial nucleotide sequence of human immunoglobulin .XI. chain cDNA from B cells and mouse-human hybridomas," Proc. Natl. Acad. Sci. USA 77(10):6207-6031 (1980).
Early, P. and L. Hood, "Mouse Immunoglobulin in Genes," in: Genetic Engineering--Principles and Methods. vol. 3, Setlow, J.K. and A. Hollander, eds., New York: Plenum Press pp. 157-188 (1981).
Edelman, G.M. et al., "The Covalent Structure Of An Entire .gamma.G Immunoglobulin Molecule," Proc. Natl. Acad. Sci. USA 63(1):78-85 (1969).
Edens, L. et al., "Cloning of cDNA encoding the sweet-tasting plant protein thaumatin and its expression in Escherichia coli," Gene 18:1-12 (1982).
Ellison, J. and L. Hood, "Linkage and sequence homology of two human immunoglobulin .gamma. heavy chain constant region genes," Proc. Natl. Acad. Sci. USA 79:11984-1988 (1982).
Ellison, J.W. et al., "The nucleotide sequence of a human immunoglobulin C.sub..gamma.1 gene," Nuc. Acids Res. 10(13):4071-4079 (1982).
Ferenci, T. and T.J. Silhavy, "Sequence Information Required for Protein Translocation from the Cytoplasm," J. Bacteriol. 169(12):5339-5342 (Dec. 1987).
Fraser, T.H. and B.J. Bruce, "Chicken ovalbumin is synthesized and secreted by Escherichia coli," Proc. Natl. Acad. Sci. USA 75(12):5936-5940 (1978).
Gherna, R. et al., eds., American Type Culture Collection--Catalogue of Bacteria and Phages. Seventeenth edition, p. 97 (Feb. 1989).
Gillam, S. and M. Smith, "Site-Specific Mutagenesis using Synthetic Oligodeoxyribonucleotide Primers: I. Optimum Conditions And Mimimum Oligodeoxyribonucleotide Length," Gene 8:81-97 (1979).
Gillies, S.D. et al., "A Tissue-specific Transcription Enhancer Element Is Located in the Major Intron of a Rearranged Immunoglobulin Heavy Chain Gene," Cell 33:717-728 (1983).
Gray, G.L. et al., "Periplasmic production of correctly processed human growth hormone in Escherichia coli: natural and bacterial signal sequences are interchangeable," Gene 39:247-254 (1985).
Hieter, P.A. et al., "Cloned Human and Mouse Kappa Immunoglobulin Constant and J Region Genes Conserve Homology in Functional Segments," Cell 22:197-207 (1980).
Hieter, P.A. et al., "Evolution of Human Immunoglobulin .kappa. J Region Genes," J. Biol. Chem. 257(3):1516-1522 (1982).
Holland, I.B. et al., "Secretion of Proteins From Bacteria," Bio/Technol. 4:427-431 (May 1986).
Holland, I.B., "Secretion of Escherichia coli haemolysin," Biochem. Soc. Trans. 17(2):323-325 (Apr. 1989).
Horwitz, A.H. et al., "Secretion of functional antibody and Fab fragment from yeast cells," Proc. Natl. Acad. Sci. USA 85:8678-8682 (Nov. 1988).
Hsiung, H.M. et al., "High-Level Expression, Efficient Secretion And Folding Of Human Growth Hormone In Escherichia coli," Bio/Technol. 4:991-995 (Nov. 1986).
Huse, W.D. et al., "Generation of a Large Combinatorial Library of the Immunoglobulin Repetoire in Phage Lambda," Science 246:1275-1281 (Dec. 1989).
Itakura, K. et al., "Synthesis And Use Of Synthetic Oligonucleotides," Ann. Rev. Biochem. 53:323-356 (1984).
Johnston, S. et al., "High-Level expression of M13 gene II protein from an inducible polycistronic messenger RNA," Gene 34:137-145 (1985).
Jones, P.T. et al., "Replacing the complementarity

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