IP Library Granted Patent US 12,637,504
Granted Patent B2
US 12,637,504 · App. 17/430,704 · Granted May 26, 2026

Humanized antibody and method for using the same

Inventors: Mitsuhiro Matono (Suita, JP); Jun Sakai (Takarazuka, JP); Toru Nagai (Osaka, JP); Naoki Tanuma (Osaka, JP); Richard Buick (Belfast, GB)
Assignee: Nihon Medi-Physics Co., Ltd.
C07K16/18A61P35/00G01N33/532G01N33/577C07K2317/24
View Patent ↗
Loading inventors, assignments & file history…
Monitor This Case
Get email alerts when status or documents change.
Order Certified Copies
Most orders are placed with the USPTO same day — all within 24 business hours.
Order via The Patent Place →
Pre-filled with this patent's details
Quick Facts
Patent No.
US 12,637,504
App. No.
17/430,704
Granted
May 26, 2026
Kind
B2
Abstract

The present invention aims to provide a humanized antibody or an antigen-binding fragment thereof having stable physical property, superior in tumor accumulation, and capable of binding to mucin subtype 5AC. The above-mentioned problem is solved by the present invention that provides a humanized antibody or an antigen-binding fragment thereof having a heavy chain variable region consisting of the amino acid sequence shown in SEQ ID NO: 1-4 or a mutated amino acid sequence thereof, and a light chain variable region consisting of the amino acid sequence shown in SEQ ID NO: 5-8 or a mutated amino acid sequence thereof, and capable of binding to mucin subtype 5AC.

Claims (63)

1 . A non-conjugated humanized antibody capable of binding to mucin subtype 5AC, comprising:

a heavy chain variable region consisting of

(1) an amino acid sequence having not less than 95% sequence identity with the amino acid sequence shown in SEQ ID NO: 1,

(2) an amino acid sequence having not less than 95% sequence identity with the amino acid sequence shown in SEQ ID NO: 2,

(3) an amino acid sequence having not less than 95% sequence identity with the amino acid sequence shown in SEQ ID NO: 3, or

(4) an amino acid sequence having not less than 95% sequence identity with the amino acid sequence shown in SEQ ID NO: 4; and

a light chain variable region consisting of

(5) an amino acid sequence having not less than 95% sequence identity with the amino acid sequence shown in SEQ ID NO: 5,

(6) an amino acid sequence having not less than 95% sequence identity with the amino acid sequence shown in SEQ ID NO: 6,

(7) an amino acid sequence having not less than 95% sequence identity with the amino acid sequence shown in SEQ ID NO: 7, or

(8) an amino acid sequence having not less than 95% sequence identity with the amino acid sequence shown in SEQ ID NO: 8,

or an antigen-binding fragment thereof,

wherein the sequence of the CDR regions of the heavy and light chains are not modified.

2 . The humanized antibody or an antigen-binding fragment thereof according to claim 1 , wherein the heavy chain variable region consists of

(1) an amino acid sequence having not less than 98% sequence identity with the amino acid sequence shown in SEQ ID NO: 1,

(3) an amino acid sequence having not less than 98% sequence identity with the amino acid sequence shown in SEQ ID NO: 3, or

(4) an amino acid sequence having not less than 98% sequence identity with the amino acid sequence shown in SEQ ID NO: 4 and a light chain variable region consisting of

(5) an amino acid sequence having not less than 98% sequence identity with the amino acid sequence shown in SEQ ID NO: 5,

(6) an amino acid sequence having not less than 98% sequence identity with the amino acid sequence shown in SEQ ID NO: 6,

(7) an amino acid sequence having not less than 98% sequence identity with the amino acid sequence shown in SEQ ID NO: 7, or,

(8) an amino acid sequence having not less than 98% sequence identity with the amino acid sequence shown in SEQ ID NO: 8,

or an antigen-binding fragment thereof.

3 . The humanized antibody or an antigen-binding fragment thereof according to claim 1 , comprising:

a heavy chain variable region consisting of

(1) an amino acid sequence having not less than 99% sequence identity with the amino acid sequence shown in SEQ ID NO: 1,

(3) an amino acid sequence having not less than 99% sequence identity with the amino acid sequence shown in SEQ ID NO: 3, or

(4) an amino acid sequence having not less than 99% sequence identity with the amino acid sequence shown in SEQ ID NO: 4, and

a light chain variable region consisting of

(5) an amino acid sequence having not less than 99% sequence identity with the amino acid sequence shown in SEQ ID NO: 5,

(6) an amino acid sequence having not less than 99% sequence identity with the amino acid sequence shown in SEQ ID NO: 6,

(7) an amino acid sequence having not less than 99% sequence identity with the amino acid sequence shown in SEQ ID NO: 7, or

(8) an amino acid sequence having not less than 99% sequence identity with the amino acid sequence shown in SEQ ID NO: 8.

4 . The humanized antibody or an antigen-binding fragment thereof according to claim 1 , comprising:

(1) a heavy chain variable region consisting of an amino acid sequence having not less than 98% sequence identity with the amino acid sequence shown in SEQ ID NO: 1, and

(7) a light chain variable region consisting of an amino acid sequence having not less than 98% sequence identity with the amino acid sequence shown in SEQ ID NO: 7.

5 . The humanized antibody, or an antigen-binding fragment thereof according to claim 1 , comprising:

a heavy chain variable region consisting of the amino acid sequence shown in SEQ ID NO: 1, and a light chain variable region consisting of the amino acid sequence shown in SEQ ID NO: 7.

6 . The humanized antibody according to claim 1 , having an in vitro binding activity to mucin subtype 5AC comparable to or greater than that of a chimeric antibody.

7 . A composition comprising:

the humanized antibody according to claim 1 , or an antigen-binding fragment thereof.

8 . A nucleic acid encoding the humanized antibody according to claim 1 .

9 . An expression vector, comprising:

the nucleic acid according to claim 8 .

10 . A host cell comprising:

the expression vector according to claim 9 .

11 . A method for producing a non-conjugated humanized antibody or an antigen-binding fragment thereof in the host cell according to claim 10 , comprising:

inserting a nucleic acid encoding the humanized antibody or an antigen-binding fragment thereof into an expression vector,

introducing the nucleic acid containing expression vector into a host cell; culturing the host cell containing the expression vector, and

isolating the humanized antibody or an antigen-binding fragment thereof from a culture supernatant of the host cell by chromatographic purification.

12 . An in vitro method for evaluating an expression level of mucin subtype 5AC in a cell or a tissue sample, comprising:

contacting the cell or tissue sample with a humanized antibody or an antigen-binding fragment thereof of claim 1 , wherein the antibody or fragment thereof is labeled;

detecting the labeled humanized antibody or an antigen-binding fragment in the cell or tissue sample, thereby generating a signal; and

evaluating an expression level of mucin subtype 5AC expressed in the cell or tissue sample based on the signal.

13 . An in vitro method for measuring a volume of a cancer overexpressing mucin subtype 5AC in a subject, comprising:

contacting a tissue sample of the subject and a tissue sample of a healthy subject with a humanized antibody or an antigen-binding fragment thereof of claim 1 , wherein the antibody or fragment thereof is labeled;

detecting the labeled humanized antibody or an antigen-binding fragment in the tissue sample of the subject, thereby generating a first signal;

detecting the labeled humanized antibody or an antigen-binding fragment in the tissue sample of the healthy subject, thereby generating a second signal;

comparing the first signal and the second signal, wherein the comparison correlates to a volume of the cancer present in the subject.

14 . An in vitro method for measuring a volume of a cancerous tissue overexpressing mucin subtype 5AC in a subject, comprising:

contacting a tissue sample of the subject with a humanized antibody or an antigen-binding fragment thereof of claim 1 , wherein the antibody or fragment thereof is labeled;

detecting the labeled humanized antibody or an antigen-binding fragment in the tissue sample of the subject, thereby generating a signal; and

calculating the volume of a cancerous tissue volume based on the signal intensity.

15 . A kit for the in vitro diagnosis of a cancer overexpressing mucin subtype 5AC comprising the humanized antibody or an antigen-binding fragment thereof of claim 1 , and a label for detecting the antibody or an antigen-binding antibody fragment thereof.

Assignments (3)
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Mar 26, 2025
From: SUMITOMO PHARMA CO., LTD.
To: NIHON MEDI-PHYSICS CO., LTD.
Reel/Frame 070632/0774 →
CHANGE OF NAME Recorded Apr 26, 2022
From: SUMITOMO DAINIPPON PHARMA CO., LTD.
To: SUMITOMO PHARMA CO., LTD.
Reel/Frame 059795/0361 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Aug 12, 2021
From: MATONO, MITSUHIRO; SAKAI, JUN; NAGAI, TORU; TANUMA, NAOKI; BUICK, RICHARD
To: SUMITOMO DAINIPPON PHARMA CO., LTD.
Reel/Frame 057166/0633 →
Priority Claims (1)
JP 2019-191560 · Oct 18, 2019 · national
Continuity (1)
Related Publication 20220144927A1 · May 12, 2022
References Cited (20)
US 20120141375A1 · Gold · 2012 [cited by examiner]
US 20120226119A1 · Dobosz et al. · 2012 [cited by applicant]
JP 7203974A · 1995 [cited by applicant]
JP 115749A · 1999 [cited by applicant]
JP 2012532846A · 2012 [cited by applicant]
WO WO2013157102A1 · 2013 [cited by applicant]
WO WO2013157105A1 · 2013 [cited by examiner]
WO WO2026003869 · 2016 [cited by applicant]
Chiu, M.L., et al (2019) Antibody structure and function: The basis for engineering therapeutics Antibodies 8(55); 1-80 (Year: 2019). [cited by examiner]
Rabia, L.A. et al (2018) Understanding and overcoming trade-offs between antibody affinity, specificity, stability and solubility Biochem Eng J 137; 365-374 (Year: 2018). [cited by examiner]
Van Scheltinga, A.G.T.T, et al (2011) Intraoperative near-infrared fluorescence tumor imaging with vascular endothelial growth factor and human epidermal growth factor receptor 2 targeting antibodies J. Nucl. Med 52; 11… [cited by examiner]
Christensen, J., et al (2015) Non-invasive in vivo imaging and quantification of tumor growth and metastasis in rats using cells expressing far-red fluorescence protein PLOS One 10(7); e0132725; 1-14 (Year: 2015). [cited by examiner]
Extended European Search Report issued in European Patent Application No. 20877846.4 on Oct. 9, 2023. [cited by applicant]
Tetsuji Sawada et al., “Immunotherapy for Pancreatic Cancer by Antibody Directed Against Mucin”, Japanese Journal of Clinical Medicine, vol. 64, extra issue 1, 2006, pp. 274 278 (with English Translation). [cited by applicant]
Tetsuji Sawada, et al., “Preoperative Clinical Radioimmunodetection of Pancreatic Cancer by [cited by applicant]
Akimasa Inui, et al., “Radioimmunotherapy for Pancreatic Carcinoma Using [cited by applicant]
International Search Report issued on Dec. 22, 2020 in PCT/JP2020/039075 filed on Oct. 16, 2020, 2 pages. [cited by applicant]
Combined Chinese Office Action and Search Report issued May 25, 2025, (client received Jun. 27, 2025) in corresponding Chinese Patent Application No. 202080072096.6 (with English Translation), 28 pages. [cited by applicant]
Singaporean Written Opinion issued Jun. 20, 2025, (client received Jul. 2, 2025) in corresponding Singaporean Patent Application No. 11202203887U, 9 pages. [cited by applicant]
Vietnamese Office Action issued Aug. 14, 2025, (client received on Sep. 29, 2025) in corresponding Vietnamese Patent Application No. 1-2022-03103 (with English Translation), 6 pages. [cited by applicant]