Homogeneity and secretion of a recombinant follicle...

Drug – bio-affecting and body treating compositions – Antigen – epitope – or other immunospecific immunoeffector – Fusion protein or fusion polypeptide

Reexamination Certificate

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C424S193100, C424S198100, C435S069700, C530S350000, C530S351000, C530S398000, C530S399000

Reexamination Certificate

active

10724226

ABSTRACT:
A hybrid protein includes two coexpressed amino acid sequences forming a dimer. Each sequence contains the binding portion of a receptor, such as TBP1 or TBP2, or a ligand, such as IL-6, IFN-β and TPO, linked to α subunit of a natural heterodimeric scaffold. Each coexpressed sequence contains a corresponding subunit so as to form a heterodimer upon expression. Corresponding DNA molecules, expression vectors and host cells are also disclosed as are pharmaceutical compositions and a method of producing such proteins.

REFERENCES:
patent: 5116964 (1992-05-01), Capon et al.
patent: 5155027 (1992-10-01), Sledziewski et al.
patent: 5447851 (1995-09-01), Beutler et al.
patent: 5567611 (1996-10-01), Ralph et al.
patent: 5650150 (1997-07-01), Gillies
patent: 5705478 (1998-01-01), Boime
patent: 6193972 (2001-02-01), Campbell et al.
patent: WO9319777 (1993-10-01), None
patent: WO95/31544 (1993-11-01), None
Ab Narayan, Prema et al., “Functional expression of yoked human chorionic gonadotropin in baculovirus-infected insect cells.”, Molecular Endocrinology, vol. 9, No. 12, pp. 1719-1726 (1995).
Johnson, Gregory A. et al., “Baculovirus-insect cell production of bioactive choriogonadotropin-immunoglobulin G heavy-chain fusion proteins in sheep.”, Biology of Reproduction, vol. 52, pp. 68-73 (1995).
Wu, Chengbin et al., “Protein engineering of a novel constitutively active hormone-receptor complex.”, Journal of Biological Chemistry, vol. 271, No. 49, pp. 31638-31642 (1996).
Smith, Richard et al., “The active form of tumor necrosis factor is a trimer.”, Journal of Biological Chemistry, col. 262, No. 15, pp. 6951-6954 (1987).
Eck, Michael et al., “The structure of tumor necrosis factor-alpha at 2.6 A resolution.”, Journal of Biological Chemistry, vol. 264, No. 29, pp. 17595-17605 (1989).
Jones, E.Y. et al., “Structure of tumor necrosis factor.”, NATURE, vol. 338, pp. 225-228 (1989).
Eck, Michael et al., “The structure of human lymphotoxin (tumor necrosis factor-beta) at 1.9 A resolution,” Journal of Biological Chemistry, vol. 267, No. 4, pp. 2119-2122 (1992).
Pierce, John et al., “Glycoprotein hormones structure and function.”, Department of Biological Chemistry, Univ. of Cal., (1991).
Lapthorn, A.J., et al., “Crystal structure of human chorionic gonadotropin.”, NATURE, vol. 369, pp. 455-461 (1994).
Wu, Hao et al., “Structure of human chorionic gonadotropin at 2.6-A resolution from MAD analysis of the selenomethionyl protein.”, STRUCTURE, vol. 2, No. 6, pp. 545-558 (1994).
Englemann, Hartmut et al., “Antibodies to a soluble form of a tumor necrosis factor (TNF) receptor have TNF- like activity.” Journal of Biological Chemistry, vol. 265, No. 24, pp. 14497-14504 (1990).
Adam, Dieter et al., “Cross-linking of the p55 tumor necrosis factor receptor cytoplasmic domain by a dimeric ligand induces nuclear factor-Kbeta and mediates cell death.”, Journal of Biological Chemistry, vol. 270, No. 29, pp. 17482-17487 (1995).
Loetscher, Hansruedi et al., “Recombinant 55-kda tumor necrosis factor (tnf) receptor.”, Journal of Biological Chemistry, col. 266, No. 27, pp. 18324-18329 (1991).
Banner, David W. et al., “Crystal structure of the soluble human 55kd tnf receptor-human tnfbeta complex:implications for tnf receptor activation.”, CELL, vol. 73, pp. 431-445 (1993).
Pennica, Diane et al., “Biochemical characterization of the extracellular domain of the 75-kilodalton tumor necrosis factor receptor.”, BIOCHEMISTRY, vol. 32, pp. 3131-3138 (1993).
Engelmann, Hartmut et al., “Two tumor necrosis factor-binding proteins purified from human urine.”, Journal of Biological Chemistry, vol. 265, No. 3, pp. 1531-1536 (1990).
Van Zee, Kimberly et al., “Tumor necrosis factor soluble receptors circulate during experimental and clinical inflammation and can protect against excessive tumor necrosis factor aolha in vitro and in vivo.” Proc. Natl. Acad. Sci., col. 89, pp. 4845-4849 (1992).
Aderka, Dan et al., “Stabilization of th bioactivity of tumor necrosis factor by its soluble receptors.”, J. Exp. Med., col. 175, pp. 323-329 (1992).
Mohler, Kendall et al., “Soluble tumor necrosis factor (tnf) receptors are effective therapeutic agents in lethal endotoxemia and function simultaneously as both tnf carriers and tnf antagonists.”, Journal of Immunology, vol. 151, No. 3, pp. 1548-1561 (1993).
Bertini, Riccardo et al., “Urinary tnf-binding protein (tnf soluble receptor) protects mice against the lethal effect of tnf and endotoxic shock.”, Eur. Cytokine Netw., vol. 4, No. 1, pp. 39-42 (1993).
Piguet, P.F. et al., “Evolution of collagen arthritis in mice is arrested by treatment with anti-tumor necrosis factor (tnf) antibody or a recombinant tnf receptor.”, IMMUNOLOGY, vol. 77, pp. 510-514 (1992).
Williams, Richard et al., “Successful therapy of collagen-induced arthritis with tnf receptor-IgG fusion protein and combination with anti-CD4.”, IMMUNOLOGY, vol. 84, pop. 433-439 (1995).
Capon, Daniel et al., “Designing CDS immunoadhesions for AIDS therapy.” NATURE, vol. 337, pp. 525-531 (1989).
Ashkenzazi, Avi et al., “Protection against endotoxic shock by a tumor necrosis factor receptor immunoadhesion.”, Proc. Natl. Acad. Sci. USA, vol. 88, pp. 10535-10539, 1991.
Suitters et al., Amanda et al., “Differential effect of isotype on efficacy of anti-tumor necrosis factor alpha chimeric antibodies in experimental septic shock.”, J. Exp. Med., vol. 179, pp. 849-956 (1994).
Nolan, Orla et al., “Bifunctional antibodies: concept, production and applications.”, Biochimica Et Biophysica Acta, vol. 1040, pp. 1-11 (1990).
Rodriques, Maria L. et al., “Engineering Fab' fragments for efficient F9ab)2formation inEscherichia coliand for improved in vivo stability.”, Journal of Immunology, vol. 151, No. 12, pp. 6954-6961 (1993).
Chang, Hsiu-Ching et al., “A general method for facilitating heterodimeric pairing between two proteins: application to expression of alpha and beta t-cell receptor extracellular segments.”, Proc. Natl. Acad. Sci. USA, vol. 91, pp. 11408-11412 (1994).
Kirk, Zining et al., “Solution assembly of a soluble, heteromeric, high affininty interleukin-2 receptor complex.”, Journal of Biological Chemistry, vol. 270, No. 27, pp. 16039-16044 (1995).
Bazzioni, F. et al., “Chimeric tumor necrosis factor receptors with constitutive signaling activity.”, Proc. Natl. Acad. Sci. USA, vol. 92, pp. 5376-5380 (1995).
Boldin, Mark et al., “Self-association of the “Death domains” of the p55 tumor necrosis factor (tnf) receptor and fas/apo1 prompts signaling for tnf and fas/apo1 effects.”, Journal of Biological Chemistry, vol. 270, No. 1, pp. 387-391 (1995).
Vu, Thien Khai et al., “Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation.”, CELL, vol. 64, pp. 1057-1068 (1991).
Song, Ho Yeong et al., “Aggregation of the intracellular domain of the type 1 tumor necrosis receptor defined by the two-hybrid system.”, J. of Biological Chemistry, vol. 269, No. 36, pp. 22492-22495 (1994).
Russell, Deborah et al., “Combined inhibition of interleukin-1 and tumor necrosis factor in rodent endotoxemia: improved survival and organ function.”, J. Infectious Diseases, vol. 171, pp. 1528-1538 (1995).
Rao, Ch. et al., “Stability of human chorionic gonadotropin and its alpha subunit in human blood.”, Am. J. Obstet. Gynecol., vol. 146, No. 1, pp. 65-68 (1983).
Damewood, Marian et al., “Disappearance if exogenously administered human chorionic gonadotropin.”, Fertility and Sterility, vol. 52, No. 3, pp. 398-400 (1989).
Chen, Fang et al., “The carboxy-terminal region of the glycoprotein hor

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