IP Library Granted Patent US 12,240,898
Granted Patent B2
US 12,240,898 · App. 17/522,600 · Granted Mar 4, 2025

Monoclonal anti-IL-1RAcP antibodies

Inventors: Stephan Fischer (Weilheim, DE); Michael Brandt (Munich, DE)
Assignee: SANOFI BIOTECHNOLOGY
C07K16/245C07K16/2866C12N5/12A61K2039/505C07K2317/20C07K2317/33C07K2317/565C07K2317/732C07K2317/76
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Quick Facts
Patent No.
US 12,240,898
App. No.
17/522,600
Granted
Mar 4, 2025
Kind
B2
Abstract

Monoclonal antibody that specifically binds IL-1RAcP, or an antigen binding fragment thereof, comprising: a) a heavy chain variable region (VH) comprising CDR1H, CDR2H and/or CDR3H, wherein the CDR1H region comprises an amino acid sequence selected from the group of SEQ ID NO: 155-231, wherein the CDR2H region comprises an amino acid sequence selected from the group of SEQ ID NO: 232-308, and wherein the CDR3H region comprises an amino acid sequence selected from the group of SEQ ID NO: 309-385; and b) a light chain variable region (VL) comprising CDR1L, CDR2L and/or CDR3L, wherein the CDR1L region comprises an amino acid sequence selected from the group of SEQ ID NO: 386-462, wherein the CDRL2 region comprises an amino acid sequence selected from the group of SEQ ID NO: 463-539, and wherein the CDR3L region comprises an amino acid sequence selected from the group of SEQ ID NO: 540-616 The monoclonal antibody is characterized in that it inhibits IL-1RAcP induced NFkB activity, useful in treatment of IL-1RAcP related diseases.

Claims (16)

1. A monoclonal antibody, or antigen binding fragment thereof, that specifically binds to human IL-1RAcP, wherein the monoclonal antibody or antigen binding fragment thereof comprises:

a heavy chain variable (VH) region comprising the CDR1H region of SEQ ID NO: 158, the CDR2H region of SEQ ID NO: 235 and the CDR3H region of SEQ ID NO: 312, and

a light chain variable (VL) region comprising the CDR1L region of SEQ ID NO: 389, the CDR2L region of SEQ ID NO: 466 and the CDR3L region of SEQ ID NO: 543.

2. The monoclonal antibody, or antigen binding fragment thereof, of claim 1 , wherein ADCC activity of the antibody is reduced by at least 20% relative to an antibody comprising a wild-type human IgG1 Fc region.

3. The monoclonal antibody, or antigen binding fragment thereof, of claim 1 , wherein the antibody has reduced affinity to the human FcγRIIIA, FcγRIIA, and/or FcγRI relative to an antibody comprising a wild-type human IgG1 Fc region.

4. The monoclonal antibody, or antigen binding fragment thereof, of claim 1 , comprising amino acid substitutions at L234A and L235A of the human IgG1 Fc region, or S228P and L235E of the human IgG4 Fc region.

5. The monoclonal antibody, or antigen binding fragment thereof, of claim 1 , comprising a heavy chain variable (VH) region that is at least 90% identical to the VH region of SEQ ID NO: 4.

6. The monoclonal antibody, or antigen binding fragment thereof, of claim 1 , comprising a light chain variable (VL) region that is at least 90% identical to the VL region of SEQ ID NO: 81.

7. The monoclonal antibody, or antigen binding fragment thereof, of claim 1 , comprising the VH region amino acid sequence of SEQ ID NO:4.

8. The monoclonal antibody, or antigen binding fragment thereof, of claim 1 , comprising the VL region amino acid sequence of SEQ ID NO: 81.

9. The monoclonal antibody, or antigen binding fragment thereof, of claim 1 , comprising the VH region of SEQ ID NO:4, and comprising the VL region of SEQ ID NO: 81.

10. The monoclonal antibody, or antigen binding fragment thereof, of claim 1 , comprising a rabbit/human chimeric antibody, or antigen binding fragment thereof.

11. A pharmaceutical composition comprising a pharmaceutically acceptable carrier and a therapeutically effective amount of the monoclonal antibody, or antigen binding fragment thereof, of claim 1 .

12. The monoclonal antibody, or antigen binding fragment thereof, of claim 1 , comprising a humanized antibody, or antigen binding fragment thereof.

13. The monoclonal antibody, or antigen binding fragment thereof, of claim 1 , comprising a human IgG1 Fc region.

14. The monoclonal antibody, or antigen binding fragment thereof, of claim 1 , comprising a human IgG4 Fc region.

Assignments (2)
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Jan 27, 2025
From: FISCHER, STEPHAN; BRANDT, MICHAEL
To: MAB DISCOVERY GMBH
Reel/Frame 070009/0845 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Jan 27, 2025
From: MAB DISCOVERY GMBH
To: SANOFI BIOTECHNOLOGY
Reel/Frame 070010/0006 →
Priority Claims (2)
EP 15174184 · Jun 26, 2015 · regional
EP 15200772 · Dec 17, 2015 · regional
Continuity (3)
Continuation 16898074 · Jun 10, 2020
Continuation 15739410
Related Publication 20220169718A1 · Jun 2, 2022
References Cited (195)
US 5202238A · Fell, Jr. et al. · 1993 [cited by applicant]
US 5204244A · Fell et al. · 1993 [cited by applicant]
US 5283179A · Wood · 1994 [cited by applicant]
US 5641641A · Wood · 1997 [cited by applicant]
US 5650289A · Wood · 1997 [cited by applicant]
US 6280955B1 · Cao · 2001 [cited by applicant]
US 6586207B2 · Tirrell et al. · 2003 [cited by applicant]
US 6602684B1 · Umana et al. · 2003 [cited by applicant]
US 7390880B2 · Bednarik et al. · 2008 [cited by applicant]
US 10906971B2 · Fischer et al. · 2021 [cited by applicant]
US 11198728B2 · Fischer et al. · 2021 [cited by applicant]
US 11203642B2 · Fischer et al. · 2021 [cited by applicant]
US 11639392B2 · Fischer et al. · 2023 [cited by applicant]
US 12024564B2 · Fischer et al. · 2024 [cited by applicant]
US 12054552B2 · Lange et al. · 2024 [cited by applicant]
US 20030026806A1 · Witte et al. · 2003 [cited by applicant]
US 20040214988A1 · Tirrell et al. · 2004 [cited by applicant]
US 20120251531A1 · Baehner et al. · 2012 [cited by applicant]
US 20140017167A1 · Fioretos et al. · 2014 [cited by applicant]
US 20150315179A1 · Jiang et al. · 2015 [cited by applicant]
US 20150315279A1 · Jiang · 2015 [cited by examiner]
US 20190106487A1 · Fischer et al. · 2019 [cited by applicant]
US 20190194336A1 · Fischer et al. · 2019 [cited by applicant]
US 20200140559A1 · Fischer et al. · 2020 [cited by applicant]
US 20200407438A1 · Fischer et al. · 2020 [cited by applicant]
US 20220089751A1 · Fischer et al. · 2022 [cited by applicant]
US 20230383000A1 · Fischer et al. · 2023 [cited by applicant]
US 20240101691A1 · Coolbaugh et al. · 2024 [cited by applicant]
CN 1934072A · 2007 [cited by applicant]
CN 102939304A · 2013 [cited by applicant]
EP 0120694A2 · 1984 [cited by applicant]
EP 0125023A1 · 1984 [cited by applicant]
EP 0239400A2 · 1987 [cited by applicant]
EP 0488470A1 · 1992 [cited by applicant]
EP 0519596A1 · 1992 [cited by applicant]
EP 0194276B2 · 2002 [cited by applicant]
EP 1255780A1 · 2002 [cited by applicant]
EP 1633787A1 · 2006 [cited by applicant]
WO WO1986001533A1 · 1986 [cited by applicant]
WO WO1988007089A1 · 1988 [cited by applicant]
WO WO1996014339A1 · 1996 [cited by applicant]
WO WO1996023067A1 · 1996 [cited by applicant]
WO WO1997037016A1 · 1997 [cited by applicant]
WO WO1998005787A1 · 1998 [cited by applicant]
WO WO1998023289A1 · 1998 [cited by applicant]
WO WO1998048032A2 · 1998 [cited by applicant]
WO WO1999051642A1 · 1999 [cited by applicant]
WO WO1999058572A1 · 1999 [cited by applicant]
WO WO2000009560A2 · 2000 [cited by applicant]
WO WO2000032767A1 · 2000 [cited by applicant]
WO WO2000042072A2 · 2000 [cited by applicant]
WO WO2001055216A1 · 2001 [cited by applicant]
WO WO2002044215A2 · 2002 [cited by applicant]
WO WO2002060919A2 · 2002 [cited by applicant]
WO WO2002064630A2 · 2002 [cited by applicant]
WO WO2003014309A2 · 2003 [cited by applicant]
WO WO2002064630A3 · 2003 [cited by applicant]
WO WO2003073238A2 · 2003 [cited by applicant]
WO WO2003074569A2 · 2003 [cited by applicant]
WO WO2004009823A1 · 2004 [cited by applicant]
WO WO2004016750A2 · 2004 [cited by applicant]
WO WO2004022718A2 · 2004 [cited by applicant]
WO WO2004029207A2 · 2004 [cited by applicant]
WO WO2004035752A2 · 2004 [cited by applicant]
WO WO2004063351A2 · 2004 [cited by applicant]
WO WO2004065540A2 · 2004 [cited by applicant]
WO WO2004074455A2 · 2004 [cited by applicant]
WO WO2004099249A2 · 2004 [cited by applicant]
WO WO2004100987A2 · 2004 [cited by applicant]
WO WO2004106377A1 · 2004 [cited by applicant]
WO WO2005035727A2 · 2005 [cited by applicant]
WO WO2005040217A2 · 2005 [cited by applicant]
WO WO2005044859A2 · 2005 [cited by applicant]
WO WO2005070963A1 · 2005 [cited by applicant]
WO WO2005073164A1 · 2005 [cited by applicant]
WO WO2005074524A2 · 2005 [cited by applicant]
WO WO2005077981A2 · 2005 [cited by applicant]
WO WO2005092925A2 · 2005 [cited by applicant]
WO WO2005123780A2 · 2005 [cited by applicant]
WO WO2006019447A1 · 2006 [cited by applicant]
WO WO2006047350A2 · 2006 [cited by applicant]
WO WO2006085967A2 · 2006 [cited by applicant]
WO WO2007003041A1 · 2007 [cited by applicant]
WO WO2007031875A2 · 2007 [cited by applicant]
WO WO2008045140A1 · 2008 [cited by applicant]
WO WO2009120903A2 · 2009 [cited by applicant]
WO WO2010108127A1 · 2010 [cited by applicant]
WO WO2011021014A2 · 2011 [cited by applicant]
WO WO2011124718A1 · 2011 [cited by applicant]
WO WO2011147903A1 · 2011 [cited by applicant]
WO WO2012098407A1 · 2012 [cited by applicant]
WO WO2012142391A1 · 2012 [cited by applicant]
WO WO2012177595A1 · 2012 [cited by applicant]
WO WO2013023015A2 · 2013 [cited by applicant]
WO WO2013165894A2 · 2013 [cited by applicant]
WO WO2013165894A3 · 2013 [cited by applicant]
WO WO2014100772A1 · 2014 [cited by applicant]
WO WO2014113433A1 · 2014 [cited by applicant]
WO WO2015132602A1 · 2015 [cited by applicant]
WO WO2016020502A1 · 2016 [cited by applicant]
WO WO2016207304A2 · 2016 [cited by applicant]
Paul, Fundamental Immunology, 3rd Edition, Raven Press, New York, 1993, Chapter 9, pp. 292-295. [cited by applicant]
Zhao et al., Construction of hydridoma calls with ILIRAP as a new marker for leukemia stem cells and detection of its monoclonal antibody, Journal of Exp Hematology, 2013, 21(6): 1390-1393. [cited by applicant]
Zubler, Polyclonal B Cell Responses in the Presence of Defined Filler Cells: Complementary Effects of Lipopolysaccharide and Anti-Immunoglobulin Antibodies, Eur J Immunol., 1984, 14(4):,357-363. [cited by applicant]
Rudikoff et al., Single amino acid substitution altering antigen-binding specificity, PNAS USA, Mar. 1982, 79: 1979-1983. [cited by applicant]
Vajdos et al., Comprehensive Functional Maps of the Antigen-Binding Site of an Anti-ErbB2 Antibody Obtained with Shotgun Scanning Mutagenesis, Journal of Molecular Biology, 2002, 320: 415-428. [cited by applicant]
Alam, J. and Cook, J.L., Reporter Genes: Application to the Study of Mammalian Gene Transcription. Anal Biochem. 1990; 188(2):245-54. [cited by applicant]
Ali, S. et al., IL-1 receptor Accessory Protein is Essential for IL-33-induced Activation of T Lymphocytes and Mast Cells. Proc Natl Acad Sci USA, 2007; 104(47):18660-5. [cited by applicant]
Ausubel, F. et al., ed. Current Protocols in Molecular Biology, Green Publishing and Wiley Interscience, New York (1987). [cited by applicant]
Balagurunathan, Y. et al., Gene Expression Profiling-Based Identification of Cell-Surface Targets for Developing Multimeric Ligands in Pancreatic Cancer. Mol Cancer Ther. 2008: 7(9):3071-80. [cited by applicant]
Barbas, C.F., III et al., In vitro Evolution of a Neutralizing Human Antibody to Human Immunodeficiency Virus Type 1 to Enhance Affinity and Broaden Strain Cross-Reactivity. Proc Natl Acad Sci USA. 1994; 91(9):3809-13. [cited by applicant]
Bardin, “Canakinumab for the Patient With Difficult-to-Treat Gouty Arthritis: Review of the Clinical Evidence”, Joint Bone Spine, 2015, 82: eS9-eS16. [cited by applicant]
Barnes, L.M. et al., Advances in Animal Cell Recombinant Protein Production: GS-NSO Expression System. Cytotechnology. 2000; 32(2):109-23. [cited by applicant]
Barnes, L.M. et al., Characterization of the Stability of Recombinant Protein Production in the GS-NSO Expression System. Biotech Bioeng. 2001; 73(4):261-70. [cited by applicant]
Brueggemann, M. et al., Comparison of the Effector Functions of Human Immunoglobulins Using a Matched Set of Chimeric Antibodies. J Exp Med. 1987; 166(5):1351-61. [cited by applicant]
Capel, P.J.A. et al., Heterogeneity of Human IgG Fc Receptors. Immunomethods. 1994; 4(1):2534. [cited by applicant]
Carter, P. et al., Humanization of an Anti-p185 [cited by applicant]
Chin, J.W. and Schultz, P.G., In Vivo Photocrosslinking with Unnatural Amino Acid Mutagenesis. ChemBioChem. 2002; 3(11):1135-7. [cited by applicant]
Chin, J.W. et al., Addition of a Photocrosslinking Amino Acid to the Genetic Code of [cited by applicant]
Chin, J.W et al., Addition of p-Azido-L-phenylalanine to the Genetic Code of [cited by applicant]
Cullinan et al., The IL-1 Receptor Accessory Protein Is an Essential Component of the IL-1 Receptor, J. Immunology, Nov. 15, 1998, 161(10): 5614-5620. [cited by applicant]
Daeron, M., Fc Receptor Biology. Annu Rev Immunol. 1997; 15:203-34. [cited by applicant]
Davis, R.S. et al., Fc Receptor Homologs: Newest Members of a Remarkably Diverse Fc Receptor Gene Family. Immunol Rev. 2002; 190:123-36. [cited by applicant]
De Haas et al., Fcy Receptors of Phagocytes. J Lab Clin Med. 1995; 126(4):330-41. [cited by applicant]
De Wet, J.R. et al., Firefly Luciferase Gene: Structure and Expression in Mammalian Cells. Mol Cell Biol. 1987; 7:725-37. [cited by applicant]
De Wildt, R.M. and Hoet, R.M., The Recovery of Immunoglobulin Sequences from Single Human B Cells by Clonal Expansion. Methods Mol Biol. 2002; 178:121-31. [cited by applicant]
Dinarello, C.A., Interleukin-1 in the Pathogenesis and Treatment of Inflammatory Diseases. Blood. 2011; 117(14):3720-32. [cited by applicant]
Dinarello, C.A., Immunological and Inflammatory Functions of the Interleukin-1 Family, Annual Review of Immunology, 2009, 27: 519-550. [cited by applicant]
Diu, A. et al., Activation of Resting Human B Cells by Helper T-cell Clone Supernatant: Characterization of a Human B-cell-activating Factor. Proc Natl Acad Sci USA. 1987; 84(24):91404. [cited by applicant]
Durocher, Y. et al., High-level and High-throughput Recombinant Protein Production by Transient Transfection of Suspension-growing Human 293-EBNA1 Cells. Nucleic Acids Res. 2002; 30(2):E9 (9 pages). [cited by applicant]
Edelman, et al., “The Covalent Structure of an Entire γG Immunoglobulin Molecule”, PNAS USA, May 1, 1969, 63(1): 78-85. [cited by applicant]
Extended European Search Report for European Patent Application No. 21191122.7, mailed Nov. 24, 2021. [cited by applicant]
Geisse, S. et al., Eukaryotic Expression Systems: A Comparison. Protein Expr Purif. 1996; 8(3):271-82. [cited by applicant]
Guyer, R.L. et al., Immunoglobulin Binding by Mouse Intestinal Epithelial Cell Receptors. J Immunol. 1976; 117(2):587-93. [cited by applicant]
Hawkins, R.E. et al., Selection of Phage Antibodies by Binding Affinity: Mimicking Affinity Maturation. J Mol Biol. 1992; 226(3):889-96. [cited by applicant]
Hoffmann, P. et al., Murine Bone Marrow-derived Macrophages Constitute Feeder Cells for Human B Cell Hybridomas. J Immunol Methods. 1996; 196(1):85-91. [cited by applicant]
Huang, J. et al., Recruitment of IRAK to the Interleukin 1 Receptor Complex Requires Interleukin 1 Receptor Accessory Protein. Proc Natl Acad Sci USA. 1997; 94(24):12829-32. [cited by applicant]
Huston, J.S., Protein Engineering of Single-Chain Fv Analogs and Fusion Proteins. Methods Enzymol. 1991; 203:46-88. [cited by applicant]
International Preliminary Report on Patentability mailed on Dec. 26, 2017 by the International Searching Authority for Patent Application No. PCT/EP2016/064588, which was filed on Jun. 23, 2016 and published as WO 2016/… [cited by applicant]
International Search Report and Written Opinion for PCT International Patent Application No. PCT/EP2018/061846, mailed Jul. 6, 2018, 12 pages. [cited by applicant]
International Search Report and Written Opinion for PCT International Patent Application No. PCT/EP2017/060925, mailed Jul. 7, 2017, 13 pages. [cited by applicant]
International Search Report and Written Opinion mailed on Jan. 11, 2017 by the International Searching Authority for Patent Application No. PCT/EP2016/064588, which was filed on Jun. 23, 2016 and published as WO 2016/20… [cited by applicant]
Jackson, J.R. et al., In vitro Antibody Maturation. Improvement of a High Affinity, Neutralizing Antibody Against IL-1 R. J Immunol. 1995; 154(7):3310-9. [cited by applicant]
Jaras, M. et al., Isolation and Killing of Candidate Chronic Myeloid Leukemia Stem Cells by Antibody Targeting of IL-1 Receptor Accessory Protein. Proc Natl Acad Sci USA. 2010; 107(37):16280-5. [cited by applicant]
Jefferis, R. et al., Interaction Sites on Human IgG-Fc for FOR: Current Models. Immunol Lett. 2002; 82(1-2):57-65. [cited by applicant]
Johnson, G. and Wu, T.T., Kabat Database and Its Applications: 30 Years After the First Variability Plot. Nucleic Acids Res. 2000; 28(1):214-8. [cited by applicant]
Kabat, E.A. et al., Sequences of Proteins of Immunological Interest, 5th ed., Public Health Service, National Institutes of Health, Bethesda, MD (1991). [cited by applicant]
Kaufman, R.J., Overview of Vector Design for Mammalian Gene Expression. Mol Biotechnol. 2000; 16(2):151-60. [cited by applicant]
Kim, J.-K et al., Localization of the Site of Murine IgG1 Molecule that is Involved in Binding to the Murine Intestinal Fc Receptor. Eur J Immunol. 1994; 24(10):2429-34. [cited by applicant]
Kodituwakko, A.P. et al., Isolation of Antigen-Specific B Cells. Immunol Cell Biol. 2003; 81(3):163-70. [cited by applicant]
Krupke, D.M. et al., The Mouse Tumor Biology Database. Nat Rev Cancer. 2008; 8(6):459-65. [cited by applicant]
Lefranc, M.-P., Nomenclature of the Human Immunoglobulin Genes. Curr Protoc Immunol. 2000; Appendix 1P (37 pages). [cited by applicant]
Li, X. et al., Mutant Cells That Do Not Respond to Interleukin-1 (IL-1) Reveal a Novel Role for IL-1 Receptor-Associated Kinase. Mol Cel Biol. 1999; 19(7):4643-52. [cited by applicant]
Love, T.W. et al., Recombinant Antibodies Possessing Novel Effector Functions. Methods Enzymol. 1989; 178:515-27. [cited by applicant]
Makrides, S.C., Components of Vectors for Gene Transfer and Expression in Mammalian Cells. Protein Expr Purif. 1999; 17(2):183-202. [cited by applicant]
Mansur et al., Engagement of IL-1 receptor accessory protein (IL-1RAcP) with the monoclonal antibody AY19 provides co-activating signals and prolongs the CD2-induced proliferation of peripheral blood lymphocytes, Immuno… [cited by applicant]
Marks, J.D. et al., Bypassing Immunization: Building High Affinity Human Antibodies by Chain Shuffling. BioTechnology. 1992; 10(7):779-83. [cited by applicant]
Morrison, S.L. et al., Chimeric Human Antibody Molecules: Mouse Antigen-Binding Domains with Human Constant Region Domains. Proc Natl Acad Sci USA. 1984; 81(21):6851-5. [cited by applicant]
Neuberger, M.C. et al., A Hapten-Specific Chimaeric IgE with Human Physiological Effector Function. Nature. 1985; 314(6008):268-70. [cited by applicant]
Norderhaug, L. et al., Versatile Vectors for Transient and Stable Expression of Recombinant Antibody Molecules in Mammalian Cells. J Immunol Methods. 1997; 204(1):77-87. [cited by applicant]
Orencole, S.F. and Dinarello, C.A., Characterization of a Subclone (D10S) of the D10.G4.1 Helper T-cell Line which Proliferates to Attomolar Concentrations of Interleukin-1 in the Absence of Mitogens. Cytokine. 1989; 1(… [cited by applicant]
Orlandi, R. et al., Cloning Immunoglobulin Variable Domains for Expression by the Polymerase Chain Reaction. Proc Natl Acad Sci USA. 1989; 86(10):3833-7. [cited by applicant]
Ow, D.W. et al., Transient and Stable Expression of the Firefly Luciferase Gene in Plant Cells and Transgenic Plants. Science. 1986; 234(4778):856-9. [cited by applicant]
Raju, T.S., Glycosylation Variations with Expression Systems and Their Impact on Biological Activity of Therapeutic Immunoglobulins. BioProcess Intl. 2003; 1(4):44-53. [cited by applicant]
Ravetch, J.V. and Kinet, J.P., Fc Receptors. Annu Rev Immunol. 1991; 9:457-92. [cited by applicant]
Riechmann, L. et al., Reshaping Human Antibodies for Therapy. Nature. 1988; 332:323-7. [cited by applicant]
Routier, F.H., The Glycosylation Pattern of a Humanized IgGI Antibody (D1.3) Expressed in CHO Cells. Glycoconj J. 1997; 14(2):201-7. [cited by applicant]
Roy, A. et al., Increased Efficiency of 7-Irradiated versus Mitomycin C-Treated Feeder Cells for the Expansion of Normal Human Cells in Long-Term Cultures. J Hematother Stem Cell Res. 2001; 10(6):873-80. [cited by applicant]
Schier, R. et al., Identification of Functional and Structural Amino-Acid Residues by Parsimonious Mutagenesis. Gene. 1995; 169(2):147-55. [cited by applicant]
Schlaeger, E.-J and Christensen, K., Transient Gene Expression in Mammalian Cells Grown in Serum-Free Suspension Culture. Cytotechnology. 1999; 30(1-3):71-83. [cited by applicant]
Schlaeger, E.-J., The Protein Hydrolysate, Primatone RL, is a Cost-Effective Multiple Growth Promoter of Mammalian Cell Culture in Serum-Containing and Serum-Free Media and Displays Anti-Apoptosis Properties. J Immunol … [cited by applicant]
Sonderman, P. et al., The 3.2-A Crystal Structure of the Human IgG1 Fc Fragment-FcyRIII Complex. Nature. 2000; 406(6793):267-73. [cited by applicant]
Towne, J.E. et al., Interleukin (IL)-1 F6, IL-1F8, and IL-F9 Signal Through IL-1 Rrp2 and IL-1RAcP to Activate the Pathway Leading to NF-KB and MAPKs. J Biol Chem. 2004; 279(14):13677-13688. [cited by applicant]
Umaria, P. et al., Engineered Glycoforms of an Antineuro-Blastoma IgG1 with Optimized Antibody-Dependent Cellular Cytotoxic Activity. Nature Biotechnol. 1999; 17(2):176-80. [cited by applicant]
Wang, L. and Schultz, P.G., Expanding the Genetic Code. Chem Commun. 2002; 0(1):1-11. [cited by applicant]
Wedemayer, G.J. et al., Structural Insights into the Evolution of an Antibody Combining Site. Science. 1997; 276(5319):1665-9. [cited by applicant]
Wen, L. et al., Limiting Dilution Assay for Human B Cells Based on Their Activation by Mutant EL4 Thymoma Cells: Total and Anti-Malaria Responder B Cell Frequencies. Eur J Immunol. 1987; 17(6):887-92. [cited by applicant]
Werner, R.G., Appropriate Mammalian Expression Systems for Biopharmaceuticals. Arzneimittelforschung. 1998; 48(8):870-80. [cited by applicant]
Windheim, M. et al., Interleukin-1 (IL-1) Induces the Lys63-linked Polyubiquitination of IL-1 Receptor-Associated Kinase 1 to Facilitate NEMO Binding and the Activation of 1-K13a Kinase. Mol Cell Biol. 2008; 28(5):1783-… [cited by applicant]
Wood, K.V., Bioluminescence and Chemiluminescence: Current Status, Stanley, P. and Kricka, L. eds., John Wiley and Sons, Chichester, NY, 11 and 543. [cited by applicant]
Wood, K.V., Firefly Luciferase: A New Tool for Molecular Biologists. Promega Notes. 1990; 28:1-3. [cited by applicant]
Yamane-Ohnuki, N. and Satoh, M., Production of Therapeutic Antibodies with Controlled Fucosylation. MAbs. 2009; 1(3):230-6. [cited by applicant]
Yelton, D.E. et al., Affinity Maturation of the BR96 Anti-Carcinoma Antibody by Codon-Based Mutagenesis. J Immunol. 1995; 155(4):1994-2004. [cited by applicant]
Yoon, D.-Y. and Dinarello, C.A., Antibodies to Domains II and III of the IL-1 Receptor Accessory Protein Inhibit IL-1R Activity But Not Binding: Regulation of IL-1 Responses Is via Type I Receptor, Not the Accessory Pro… [cited by applicant]
Yoon, D.-Y. and Dinarello, C.A., Differential Effects of Anti-IL-1 R Accessory Protein Antibodies on IL-1a or IL-1 R-induced Production of PGE(2) and IL-6 from 3T3-L1 Cells. J Biochem Mol Biol. 2007; 40(4): 562-70. [cited by applicant]
Zhao et al., Construction of hybridoma cells with IL1RAP as a new marker for leukemia stem cells and detection of its monoclonal antibody, J Experimental Hematology, Dec. 2013, 12(6): 1390-1393. [cited by applicant]
Zubler, R.H. et al., Polyclonal B Cell Responses in the Presence of Defined Filler Cells: Complementary Effects of Lipopolysaccharide and Anti-Immunoglobulin Antibodies. Eur J Immunol. 1984; 14(4):357-63. [cited by applicant]
U.S. Appl. No. 15/739,410 2019/0106487 U.S. Pat. No. 10,906,971, filed Dec. 22, 2017 Apr. 11, 2019 Feb. 2, 2021, Stephan Fischer, Monoclonal Anti-IL-1RACP Antibodies. [cited by applicant]
U.S. Appl. No. 16/898,074 2020/0407438 U.S. Pat. No. 11,198,728, filed Jun. 10, 2020 Dec. 31, 2020 Dec. 14, 2021, Stephan Fischer, Monoclonal Anti-IL-1RACP Antibodies. [cited by applicant]
U.S. Appl. No. 17/522,600 2022/0169718, filed Nov. 9, 2021 Jun. 2, 2022, Stephan Fischer, Monoclonal Anti-IL-1RACP Antibodies. [cited by applicant]
U.S. Appl. No. 16/099,059 2019/0194336 U.S. Pat. No. 11,203,642, filed Nov. 5, 2018 Jun. 27, 2019 Dec. 21, 2021, Stephan Fischer, Humanized Anti-IL-1R3 Antibodies. [cited by applicant]
U.S. Appl. No. 17/410,153 2022/0089751, filed Aug. 24, 2021 Mar. 24, 2022, Stephan Fischer, Humanized Anti-IL-1R3 Antibodies. [cited by applicant]
U.S. Appl. No. 16/612,052 2020/0140559 U.S. Pat. No. 11,639,392, filed Nov. 8, 2019 May 7, 2020 May 2, 2023, Stephan Fischer, Anti-IL-1R3 Antibodies for Use in Inflammatory Conditions. [cited by applicant]
U.S. Appl. No. 18/184,759, filed Mar. 16, 2023, Stephan Fischer, Anti-IL-1R3 Antibodies for Use in Inflammatory Conditions. [cited by applicant]
U.S. Appl. No. 18/471,388, filed Sep. 21, 1023, Christian Lange, Humanized Anti-IL-1R3 Antibody and Methods of Use. [cited by applicant]
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US 12,698,334