Glycosylated human G-CSF

Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues

Reexamination Certificate

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

C514S008100

Reexamination Certificate

active

07812127

ABSTRACT:
The invention relates to G-CSF molecules having certain O-linked oligosaccharide structures.

REFERENCES:
patent: 4496537 (1985-01-01), Kwan
patent: 4959317 (1990-09-01), Sauer
patent: 4997763 (1991-03-01), Hughes et al.
patent: 5162215 (1992-11-01), Bosselman et al.
patent: 5304489 (1994-04-01), Rosen
patent: 5364783 (1994-11-01), Ruley et al.
patent: 5367054 (1994-11-01), Lee
patent: 5378618 (1995-01-01), Sternberg et al.
patent: 5464764 (1995-11-01), Capecchi et al.
patent: 5487992 (1996-01-01), Capecchi et al.
patent: 5677177 (1997-10-01), Wahl et al.
patent: 5714353 (1998-02-01), Pathak et al.
patent: 5741957 (1998-04-01), Deboer et al.
patent: 5784992 (1998-07-01), Petitte et al.
patent: 6069133 (2000-05-01), Chiou et al.
patent: 6730822 (2004-05-01), Ivarie et al.
patent: 6825396 (2004-11-01), MacArthur
patent: 7129390 (2006-10-01), Ivarie et al.
patent: 2002/0155998 (2002-10-01), Young et al.
patent: 2003/0126629 (2003-07-01), Rapp et al.
patent: 2004/0019922 (2004-01-01), Ivarie et al.
patent: 2004/0019923 (2004-01-01), Ivarie et al.
patent: 2005/0198700 (2005-09-01), Christmann et al.
patent: 2006/0171921 (2006-08-01), Ivarie et al.
patent: 0 424 027 (1991-04-01), None
patent: 0 424 044 (1991-04-01), None
patent: WO 90/11355 (1990-10-01), None
patent: WO 94/20608 (1994-09-01), None
patent: WO 95/11302 (1995-04-01), None
patent: WO 97/33998 (1997-09-01), None
patent: WO 97/47739 (1997-12-01), None
patent: WO 98/01027 (1998-01-01), None
patent: WO 99/19472 (1999-04-01), None
patent: WO 03/022040 (2003-03-01), None
patent: WO 03/022228 (2003-03-01), None
patent: WO 03/081993 (2003-10-01), None
patent: WO 2004/047531 (2004-06-01), None
patent: WO 2004/067713 (2004-08-01), None
Adolf et al., “Natural human interferon-α2 isO-glycosylated,”Biochem J., 276:511-518, (1991).
Allioli et al., “Use of retroviral vectors to introduce and express the β-galactosidase marker gene in cultured chicken primordial germ cells,”Developmental Biology, 165:30-37 (1994).
Archer et al., “Human growth hormone (hgh) secretion in milk of goats after direct transfer of the hgh gene into the mammary gland by using replication-defective retrovirus vectors,”Proc. Natl. Acad. Sci. USA, 91:6840-6844 (1994).
Bayley et al., “Exchange of Gene Activity in Transgenic plants catalyzed by the Cre-lox site-specific recombination system,”Plant Molecular Biology, 18:353-361 (1992).
Beato, M. “Gene regulation by steroid hormones,”Cell, 56:335-344 (1989).
Bonifer et al., “Tissue specific and position independent expression of the complete gene domain for chicken lysozyme in transgenic mice,”The EMBO Journal, 9:2843-2848 (1990).
Bosselman et al., “Germaine transmission of exogenous genes in the chicken,”Science, 243:533-535 (1989).
Brazolot et al., “Efficient transfection of chicken cells by lipofection, and introduction of transfected blastodermal cells into the embryo,”Molecular Reproduction and Development, 30:304-312 (1991).
Briskin et al., “Heritable retroviral transgenes are highly expressed in chickens,”Proc. Natl. Acad. Sci. USA, 88:1736-1740 (1991).
Brown et al., “Conformational alterations in the proximal portion of the yeast invertase signal peptide do not block secretion,”Mol. Gen. Genet., 197:351-357 (1984).
Burns et al., “Vesicular stomatitis virus G glycoprotein pseudotyped retroviral vectors: concentration to very high titer and efficient gene transfer into mammalian and nonmammalian cells,”Proc. Natl. Acad. Sci. USA, 90:8033-8037 (1993).
Chung et al., “A 5′ element of the chicken β-globin domain serves as an insulator in human erythroid cells and protects against position effect inDrosophila,” Cell, 74:505-514 (1993).
Cosset et al., “Improvement of avian leucosis virus (ALV)-based retrovirus vectors by using different cisacting sequences from ALVs,”Journal of Virology, 65:3388-3394 (1991).
Cosset et al., “Use of helper cells with two host ranges to generate high-titer retroviral vectors,”Virology193:385-395 (1993).
Dean et al., “Regulation of the chicken ovalbumin gene by estrogen and corticosterone requires a novel DNA element that binds a labile protein, chirp-1,”Molecular and Cellular Biology, 16:2015-2024 (1996).
Deeley et al., “Synthesis and Deposition of Egg Proteins,” eds Robert J. Etches, Ph.D, D.Sc.and Ann M. Verrinder Gibbins, Ph.D., Manipulation of the Avian Genome, Boca Raton, CRC Press (1993), p. 205.
Dierich et al., “Cell-specificity of the chicken ovalbumin and conalbumin promoters,”The EMBO Journal, 6:2305-2312 (1987).
Dugaiczyk et al., “The ovalbumin gene: cloning and molecular organization of the entire natural gene,”Proc. Natl. Acad. Sci. USA, 76:2253-2257 (1979).
Etches et al., “Contributions to somatic and germline lineages of chicken blastodermal cells maintained in culture,”Molecular Reproduction and Development, 45:291-298 (1996).
Fiering S. et al., “An ”in-out“ strategy using gene targeting and FLP recombinase for the functional dissection of complex DNA regulatory elements: Analysis of the β-globin locus control region,”Proc. Natl. Acad. Sci USA, vol. 90, 18, Sep. 15, 1993, pp. 8469-8473.
Fisher et al., “Expression of exogenous protein and analysis of morphogenesis in the developing chicken heart using an adenoviral vector,”Cardiovascular Research, 31:E86-E95 (1996).
Galton et al., “Antibodies to Lymphoblastoid Interferon,”Lancet, 2:572-573, (1989).
Gannon et al., “Organization and sequences at the 5′ end of a cloned complete ovalbumin gene,”Nature, 276:428-434 (1979).
Gilbert, Egg albumin and its formation in Physiology and Biochemistry of the Domestic Fowl, Bell and Freeman, eds., Academic Press, London, NY, pp. 1291-1329.
Gu et al., “Deletion of a DNA polymerase β gene segment in T cells using cell type-specific gene targeting,”Science, 265:103-106 (1994).
Haecker et al., “Repression of the ovalbumin gene involves multiple negative elements including an ubiquitous transcriptional silencer,”Molecular Endocrinology, 9:1113-1126 (1995).
Hale, K.L., “Oncolog, Interferon: The Evolution of a Biological Therapy, Taking a New Look at Cytokine Biology,”M.D. Anderson Oncolog, 39(4):1-4 (1994).
Hogan et al., “Manipulating the Mouse Embryo,” Cold Spring Harbor Laboratory, NY, (1988).
Johnson et al., “pXeX, a vector for efficient expression of cloned sequences inZenopusembryos,”Gene, 147:223-226 (1994).
Kato et al., “A far upstream estrogen response element of the ovalbumin gene contains several half-palindromic 5′-TGACC-3′ motifs acting synergistically,”Cell, 68:731-742 (1992).
Kaye et al., “A close association between sites of Dnase I hypersensitivity and sites of enhanced cleavage by micrococcal nuclease in the 5'-flanking region of the actively transcribed ovalbumin gene,”The EMBO Journal, 3:1127-1144 (1984).
Kotani et al., “Improved methods of retroviral vector transduction and production for gene therapy,”Hum. Gene Ther. 5:19-28 (1994).
Lai et al., “The ovalbumin gene: structural sequences in native chicken DNA are not contiguous,”Proc. Natl. Acad. Sci. USA, 75:2205-2209 (1978).
Lin et al., “Integration and germ-line transmission of a pseudotyped retroviral vector in zebrafish,”Science, 265:666-669 (1994).
Lobe et al., “Conditional genome alteration in mice,”BioEssays, 20:200-208 (1998).
Logie et al., “Ligand-regulated site-specific recombination,”Proc. Natl. Acad. Sci. USA, 92:5940-5944 (1995).
Lou et al., “Adenovirus-mediated gene transfer into tendon and tendon sheath,”Journal of Orthopaedic Research, 14:513-517 (1996).
Love et al., “Transgenic birds by DNA microinjection,”Bio/Technology, 12:60-

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Glycosylated human G-CSF does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Glycosylated human G-CSF, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Glycosylated human G-CSF will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-4217584

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.