# US 2014/0193404 A1 · Glycosylated antibodies > Agents: this data is available as JSON from the patentgrep API and MCP server — see https://patentgrep.com/llms.txt - Number: US 2014/0193404 A1 - Document ID: US20140193404A1 - Status: Published application - Kind: A1 - Application number: 14/195,066 - Filed: 2014-03-03 - Published: 2014-07-10 - Earliest claimed: 2006-04-11 - Assignees: Hoffmann-La Roche Inc. - Applicants: Hoffmann-La Roche Inc. - Inventors: Silke Hansen; Klaus-Peter Kuenkele; Dietmar Reusch; Ralf Schumacher - Web page: https://patentgrep.com/patent/US20140193404A1 ## CPC - C07K 16/2863: {against receptors for growth factors, growth regulators} - A61P 31/00: Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics - A61P 35/00: Antineoplastic agents - A61P 37/00: Drugs for immunological or allergic disorders - A61P 37/02: Immunomodulators - A61P 37/06: Immunosuppressants, e.g. drugs for graft rejection - A61P 43/00: Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00 - C07K 16/00: Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies - C07K 2317/41: Glycosylation, sialylation, or fucosylation - C07K 2317/52: Constant or Fc region; Isotype - C07K: PEPTIDES (peptides in foodstuffs A23; obtaining protein compositions for foodstuffs, working-up proteins for foodstuffs A23J; preparations for medicinal purposes A61K; peptides containing beta-lactam rings C07D; cyclic dipeptides not having in their molecule any other peptide link than those which form their ring, e.g. piperazine-2,5-diones, C07D; ergot alkaloids of the cyclic peptide type C07D519/02; macromolecular compounds having statistically distributed amino acid units in their molecules, i.e. when the preparation does not provide for a specific; but for a random sequence of the amino acid units, homopolyamides and block copolyamides derived from amino acids C08G69/00; macromolecular products derived from proteins C08H1/00; preparation of glue or gelatine C09H; single cell proteins, enzymes C12N; genetic engineering processes for obtaining peptides C12N15/00; compositions for measuring or testing processes involving enzymes C12Q; investigation or analysis of biological material G01N33/00) - A61P: SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS ## Abstract The invention provides an antibody comprising human IgG1 or IgG3 heavy chain constant domains that are glycosylated with a sugar chain at Asn297, said antibody being characterized in that the amount of fucose within said sugar chain is at least 99%, and in addition the amount of NGNA is 1% or less and/or the amount of N-terminal alpha 1,3 galactose is 1% or less, and uses thereof. ## Claims ### Claim 1 A monoclonal antibody of IgG1 or IgG3 type glycosylated at Asn297, said antibody comprising an antibody wherein the sugar chain of said antibody comprises at least 99.4% fructose as analyzed by Liquid Chromatography Mass Spectronety (LCM) peptide map analysis and wherein the amount of fructose within said sugar chain related to the sum of G0, G1, G2 without mannose 4 and mannose 5 is 100%; and, the amount of N-glycolylneuraminic acid is 1% or less of the sugar chain as related to the sum of G0, G1, G2 without mannose 4 and mannose 5 as analyzed by LCMS and the N-terminal alpha-1,3-galactose, is 1% or less of the sugar chain. ### Claim 2 (depends on 1) The antibody according to claim 1, wherein the amount of N-glycolylneuraminic acid is 0.5% or less of the sugar chain. ### Claim 3 (depends on 1) The antibody according to claim 1, wherein the amount of N-terminal alpha-1,3-galactose is 0.5% or less of the sugar chain. ### Claim 4 (depends on 1) The antibody according to claim 1, wherein the antibody is a chimeric, humanized or human antibody. ### Claim 5 (depends on 1) The antibody according to claim 1, wherein the antibody shows one or more properties selected from the group consisting of: a) shows a ratio of IC50 values of inhibition of the binding of IGF-I to IGF-IR to the inhibition of binding of insulin-like growth factor II (IGF-II) to IGF-IR of 1:3 to 3:1, b) inhibits, at a concentration of 5 nM, at least 80% of the IGF-IR phosphorylation in a cellular phosphorylation assay using HT29 cells in a medium containing 0.5% heat-inactivated fetal calf serum when compared to such an assay without said antibody, c) shows no IGF-IR stimulating activity measured as PKB phosphorylation at a concentration of 10 μM in a cellular phosphorylation assay using 3T3 cells providing 400,000 to 600,000 molecules IGF-IR per cell in a medium containing 0.5% heat-inactivated fetal calf serum (FCS) when compared to such an assay without said antibody. ### Claim 6 (depends on 1) The antibody according to claim 1, wherein the antibody has an affinity of about 10−13 to 10−9 M (KD) for IGF-IR. ### Claim 7 (depends on 1) The antibody according to claim 1 produced by the CHO cell line hu MAbB1-4E10—9-16 deposited with the Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH, Germany, under Accession No. DSM ACC 2795. ### Claim 8 (depends on 1) A pharmaceutical composition comprising an antibody according to claim 1 and a pharmaceutically acceptable carrier or excipient. ### Claim 9 (depends on 7) A pharmaceutical composition comprising an antibody according to claim 7 and a pharmaceutically acceptable carrier or excipient. ### Claim 10 (depends on 1) A CHO cell that recombinantly expresses an antibody that when purified is an antibody according to claim 1. ### Claim 11 (depends on 7) A CHO cell that recombinantly expresses an antibody that when purified is an antibody according to claim 7. ### Claim 12 A CHO cell hu MAbB1-4E10—9-16 deposited with the Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH, Germany, under Accession No. DSM ACC 2795.