IP Library › Granted Patent US 12,655,205
Granted Patent B2
US 12,655,205 · App. 18/390,942 · Granted Jun 16, 2026

Antibodies and assays for CCL14

Inventors: Ravi A. Vijayendran (San Diego, CA); Hua Wang (San Diego, CA)
Assignee: bioMerieux, Inc.
C07K16/24C07K16/00C07K16/18G01N33/543G01N33/54388G01N33/6863C07K2317/20C07K2317/34C07K2317/54C07K2317/55C07K2317/565C07K2317/567C07K2317/62
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 12,655,205
App. No.
18/390,942
Granted
Jun 16, 2026
Kind
B2
Abstract

The invention provides CCL14 antibodies.

Claims (47)

1 . A monoclonal antibody or antigen binding fragment thereof which specifically binds human CCL14, wherein the antibody or antigen binding fragment thereof comprises

a heavy chain variable region comprising a CDR1, CDR2, and CDR3 sequence from SEQ ID NO: 19, and a light chain variable region comprising a CDR1, CDR2, and CDR3 sequence from SEQ ID NO: 20 (31H1/31K1).

2 . The monoclonal antibody or antigen binding fragment thereof of claim 1 , wherein the antibody comprises

a heavy chain variable region of SEQ ID NO: 19 or a corresponding heavy chain variable region having at least 90% sequence similarity to the framework region thereof, and a light chain variable region of SEQ ID NO: 20 or a corresponding light chain variable region having at least 90% sequence similarity to the framework region thereof (31H1/31K1).

3 . The monoclonal antibody or antigen binding fragment thereof of claim 1 , wherein the monoclonal antibody or antigen binding fragment thereof

(a) is conjugated to a signal development element;

(b) is immobilized on a solid support;

(c) is an F(ab) or F(ab′)2 fragment; or

(d) is a rabbit antibody or an antigen binding fragment thereof.

4 . A kit comprising:

a first monoclonal antibody or antigen binding fragment thereof that is the monoclonal antibody or antigen binding fragment of claim 1 , and

a second monoclonal antibody or antigen binding fragment thereof which specifically binds human CCL14, wherein the first antibody or antigen binding fragment thereof and the second antibody or antigen binding fragment thereof form sandwich complexes with human CCL14.

5 . The kit of claim 4 , wherein the second antibody or antigen binding fragment is a monoclonal antibody or antigen binding fragment that is different from the first monoclonal antibody or antigen binding fragment.

6 . The kit of claim 4 , further comprising a disposable test device configured to generate a detectable signal related to the presence or amount of human CCL14 in a biological sample, wherein the first monoclonal antibody or antigen binding fragment thereof or the second monoclonal antibody or antigen binding fragment thereof is immobilized on a surface within the disposable test device.

7 . The kit of claim 6 , wherein the disposable test device is a lateral flow test device.

8 . The kit of claim 6 , wherein

(a) the first monoclonal antibody or antigen binding fragment thereof is immobilized to a surface within the disposable test device, and the second monoclonal antibody or antigen binding fragment thereof is conjugated to a detectable label;

(b) the first monoclonal antibody or antigen binding fragment thereof is immobilized to a surface within the disposable test device, and the second monoclonal antibody or antigen binding fragment thereof is conjugated to a detectable label and is provided in a separate container from the disposable test device;

(c) the kit is configured to perform an assay method which provides a signal related to the presence or amount of human CCL14 in a biological sample, and wherein the minimum detectable concentration of CCL14 in the assay method is 10 ng/ml or less;

(d) one or both of the first or second monoclonal antibodies or antigen binding fragment thereof is an F(ab) or F(ab′)2 fragment;

(e) one or both of the first or second monoclonal antibodies or antigen binding fragment thereof is a rabbit antibody or an antigen binding fragment thereof; or

(f) the first and second monoclonal antibodies or antigen binding fragments thereof in the kit are a 31H1/31K1-10H3/10K1 pair, or a corresponding antigen binding fragment thereof,

wherein 10H3/10K1 comprises three CDRs of a heavy chain variable region comprising the amino acid sequence of SEQ ID NO: 7, and three CDRs of a light chain variable region comprising the amino acid sequence of SEQ ID NO: 8.

9 . The kit of claim 6 , wherein the kit further comprises a calibration to relate the detectable signal to a concentration of CCL14.

10 . The kit of claim 9 , wherein the calibration is a calibration curve provided on an electronic memory device.

11 . A method for determining the presence or amount of human CCL14 in a biological sample, comprising:

performing an immunoassay on the biological sample with a first monoclonal antibody or antigen binding fragment thereof and a second monoclonal antibody or antigen binding fragment thereof which together form sandwich complexes with human CCL14, wherein the immunoassay provides a detectable signal that is related to the presence or amount of human CCL14 in the biological sample bound in the sandwich complexes; and

relating the detectable signal to the presence or amount of human CCL14 in the biological sample, wherein the first monoclonal antibody or antigen binding fragment thereof is the monoclonal antibody or fragment thereof of claim 1 .

12 . The method of claim 11 , wherein

(a) the minimum detectable concentration of CCL14 in the immunoassay is 10 ng/ml or less;

(b) the immunoassay is performed in a lateral flow format;

(c) the immunoassay is an in vitro diagnostic; or

(d) the immunoassay is performed by applying the biological sample to a disposable test device, and the detectable signal is obtained by inserting the disposable test device into an analytical instrument, wherein the sandwich complexes comprising the first and second monoclonal antibodies or antigen binding fragments thereof are immobilized for detection in a predetermined zone of the disposable test device, and wherein the analytical instrument detects the immobilized sandwich complexes to provide the detectable signal.

13 . The method of claim 11 , wherein

(a) the first monoclonal antibody or antigen binding fragment thereof is conjugated to a signal development element;

(b) the first monoclonal antibody or antigen binding fragment thereof forms a reaction mixture with the biological sample, and the biological sample is applied to the disposable test device by applying the reaction mixture to the disposable test device;

(c) the second monoclonal antibody or antigen binding fragment thereof is immobilized at the predetermined zone of a solid support;

(d) each of the first and second monoclonal antibodies or antigen binding fragments thereof is a rabbit, mouse, chicken, goat, sheep, donkey, human, llama or camelid antibody or antigen binding fragment thereof;

(e) at least one of the first and second monoclonal antibodies or antigen binding fragment thereof is a rabbit antibody or antibody fragment;

(f) one or both of the first or second monoclonal antibodies or antigen binding fragment thereof is an F(ab) or F(ab′)2 fragment;

(g) the second monoclonal antibody or antigen binding fragment thereof forms a sandwich complex with CCL14 and the first monoclonal antibody or antigen binding fragment thereof; or

(h) the first and second monoclonal antibodies or antigen binding fragments thereof are a 31H1/31K1-10H3/10K1 pair, or a corresponding antigen binding fragment thereof,

wherein 10H3/10K1 comprises three CDRs of a heavy chain variable region comprising the amino acid sequence of SEQ ID NO: 7, and three CDRs of a light chain variable region comprising the amino acid sequence of SEQ ID NO: 8.

14 . A method for determining the presence or amount of human CCL14 in a biological sample, comprising:

performing an immunoassay on the biological sample with a monoclonal antibody or antigen binding fragment thereof which binds human CCL14, wherein the immunoassay provides a detectable signal that is related to the presence or amount of human CCL14 in the biological sample; and

relating the detectable signal to the presence or amount of human CCL14 in the biological sample, wherein the assay is a competitive assay and the monoclonal antibody or antigen binding fragment thereof is the monoclonal antibody or an antigen binding fragment thereof of claim 1 .

15 . A monoclonal antibody or antigen binding fragment thereof comprising a heavy chain variable region comprising a CDR1, CDR2, and CDR3 sequence from SEQ ID NO: 19, and a light chain variable region comprising a CDR1, CDR2, and CDR3 sequence from SEQ ID NO: 20 (31H1/31K1), wherein the heavy chain variable region has at least 90% sequence similarity within the framework sequences to the framework sequences of SEQ ID NO: 19, and the light chain variable region has at least 90% sequence similarity within the framework sequences to the framework sequences of SEQ ID NO: 20.

Assignments (2)
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Jan 8, 2025
From: ASTUTE MEDICAL, INC.
To: BIOMERIEUX, INC.
Reel/Frame 069778/0363 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Dec 21, 2023
From: VIJAYENDRAN, RAVI A.; WANG, HUA
To: ASTUTE MEDICAL, INC.
Reel/Frame 065930/0514 →
Continuity (3)
Division 16958072
Provisional Application 62611510 · Dec 28, 2017
Related Publication 20240124569A1 · Apr 18, 2024
References Cited (157)
US 4477575A · Vogel et al. · 1984 [cited by applicant]
US 5166051A · Killeen et al. · 1992 [cited by applicant]
US 5413923A · Kucherlapati et al. · 1995 [cited by applicant]
US 5480792A · Buechler et al. · 1996 [cited by applicant]
US 5525524A · Buechler et al. · 1996 [cited by applicant]
US 5530101A · Queen et al. · 1996 [cited by applicant]
US 5545806A · Lonberg et al. · 1996 [cited by applicant]
US 5569825A · Lonberg et al. · 1996 [cited by applicant]
US 5571698A · Ladner et al. · 1996 [cited by applicant]
US 5585089A · Queen et al. · 1996 [cited by applicant]
US 5625126A · Lonberg et al. · 1997 [cited by applicant]
US 5631171A · Sandstrom et al. · 1997 [cited by applicant]
US 5633425A · Lonberg et al. · 1997 [cited by applicant]
US 5661016A · Lonberg et al. · 1997 [cited by applicant]
US 5679526A · Buechler et al. · 1997 [cited by applicant]
US 5693761A · Queen et al. · 1997 [cited by applicant]
US 5693762A · Queen et al. · 1997 [cited by applicant]
US 5807715A · Morrison et al. · 1998 [cited by applicant]
US 5814318A · Lonberg et al. · 1998 [cited by applicant]
US 5821337A · Carter et al. · 1998 [cited by applicant]
US 5824799A · Buechler et al. · 1998 [cited by applicant]
US 5851776A · Valkirs · 1998 [cited by applicant]
US 5859205A · Adair et al. · 1999 [cited by applicant]
US 5885527A · Buechler · 1999 [cited by applicant]
US 5922615A · Nowakowski et al. · 1999 [cited by applicant]
US 5939272A · Buechler et al. · 1999 [cited by applicant]
US 5939598A · Kucherlapati et al. · 1999 [cited by applicant]
US 5947124A · Buechler et al. · 1999 [cited by applicant]
US 5955377A · Maul et al. · 1999 [cited by applicant]
US 5985579A · Buechler et al. · 1999 [cited by applicant]
US 6019944A · Buechler · 2000 [cited by applicant]
US 6054297A · Carter et al. · 2000 [cited by applicant]
US 6057098A · Buechler et al. · 2000 [cited by applicant]
US 6113855A · Buechler · 2000 [cited by applicant]
US 6143576A · Buechler · 2000 [cited by applicant]
US 6180370B1 · Queen et al. · 2001 [cited by applicant]
US 6391265B1 · Buechler et al. · 2002 [cited by applicant]
US 6407213B1 · Carter et al. · 2002 [cited by applicant]
US 6797492B2 · Daugherty et al. · 2004 [cited by applicant]
US 6946292B2 · Kanda et al. · 2005 [cited by applicant]
US 7125493B2 · Wang et al. · 2006 [cited by applicant]
US 7214775B2 · Hanai et al. · 2007 [cited by applicant]
US 7657380B2 · Lazar et al. · 2010 [cited by applicant]
US 11891439B2 · Vijayendran · 2024 [cited by examiner]
US 20050118586A1 · Bejanin et al. · 2005 [cited by applicant]
US 20080085241A1 · Stassar et al. · 2008 [cited by applicant]
US 20110059107A1 · Allison et al. · 2011 [cited by applicant]
US 20120301488A1 · Zhang et al. · 2012 [cited by applicant]
US 20130108640A1 · Allison et al. · 2013 [cited by applicant]
US 20130203079A1 · Goodman et al. · 2013 [cited by applicant]
US 20150030586A1 · Warren et al. · 2015 [cited by applicant]
US 20170226228A1 · Desir et al. · 2017 [cited by applicant]
US 20180086846A1 · Wiltzius et al. · 2018 [cited by applicant]
US 20180209990A1 · Anderberg et al. · 2018 [cited by applicant]
US 20190339289A1 · Kampf et al. · 2019 [cited by applicant]
US 20210061900A1 · Vijayendran et al. · 2021 [cited by applicant]
CN 102597001A · 2012 [cited by applicant]
CN 102782148A · 2012 [cited by applicant]
CN 112041341A · 2020 [cited by applicant]
WO WO199211018 · 1992 [cited by applicant]
WO WO199633735 · 1996 [cited by applicant]
WO WO199634096 · 1996 [cited by applicant]
WO WO199824893 · 1998 [cited by applicant]
WO WO2012177595 · 2012 [cited by applicant]
WO WO2011025962 · 2013 [cited by applicant]
WO 2014003744A1 · 2014 [cited by applicant]
WO 2015164330A1 · 2015 [cited by applicant]
WO 2016064877A2 · 2016 [cited by applicant]
WO 2017004151A1 · 2017 [cited by applicant]
WO 2018132702A1 · 2018 [cited by applicant]
WO 2019133902A2 · 2019 [cited by applicant]
Shijing et al., “Clinical Immunological Testing,” Chinese Medicine Publishing House, 2015, 11 pp (including English translation). [cited by applicant]
Official action issued Feb. 1, 2024, in Chinese Application No. 201880088190.3. [cited by applicant]
Baldridge et al., “Monophosphoryl Lipid A (MPL) Formulations for the Next Generation of Vaccines,” Methods, 1999, 19:103-107. [cited by applicant]
Bieg et al., “GAD65 and Insulin B Chain Peptide (9-23) are not Primary Autoantigens in the Type 1 Diabetes Syndrome pf the BB Rat,” Autoimmunity, 1999, 31:15-24. [cited by applicant]
Bitter et al., “Expression and Secretion Vectors for Yeast,” Methods Enzymol, 1987, 153:516-544. [cited by applicant]
Brüggemann et al., “Production of human antibody repertoiries in transgenic mice,” Curr Opin Biotechnol, Aug. 1997, 8(4):455-458. [cited by applicant]
Carter et al., “Humanization of an anti-p185HER2 antibody for human cancer therapy,” Proc Natl Acad Sci USA, May 1992, 89:4285-4289. [cited by applicant]
Crouse et al., “Expression and Amplification of Engineered Mouse Dihydrofolate Reductase Minigenes,” Mol Cell Biol, Feb. 1983, 3:257-266. [cited by applicant]
Cwirla et al., “Peptides on phage: A vast library of peptides for identifying ligands,” Proc Natl Acad Sci USA, Aug. 1990, 87:6378-6382. [cited by applicant]
De Pascalis et al., “Grafting of ‘Abbreviated’ Complementarity-Determining Regions Containing Specificity-Determining Residues Essential for Ligand Contact to Engineer a Less Immunogenic Humanized Monoclonal Antibody,” … [cited by applicant]
Devlin et al., “Random Peptide Libraries: A Source of Specific Protein Binding Molecules,” Science, 1990, 249:404-406. [cited by applicant]
Eton et al., “Active Immunotherapy with Ultraviolet B-Irradiated Autologous Whole Melanoma Cells plus Detox in Patients with Metastatic Melanoma,” Clin Cancer Res, Mar. 1998, 4:619-627. [cited by applicant]
Fischer et al., “A readers' guide to the interpretation of diagnostic test properties: clinical example of sepsis,” Intensive Care Med, 2003, 29:1043-1051. [cited by applicant]
Geysen et al., “Use of peptide synthesis to probe viral antigens for epitopes to a resoluton of a single amino acid,” Proc Natl Acad Sci USA, Jul. 1984, 81:3998-4002. [cited by applicant]
Goel et al., “Plasticity within the Antigen-Combining Site May Manifest as Molecular Mimicry in the Humoral Immune Response,” J Immunol, 2004, 173:7358-7367. [cited by applicant]
Gorman et al., “Reshaping a therapeutic CD4 antibody,” Proc Natl Acad Sci USA, May 1991, 88:4181-4185. [cited by applicant]
Griffiths et al., “Strategies for selection of antibodies by phage display,” Curr Opin Biotechnol. 1998, 9:102-108. [cited by applicant]
Gupta et al., “Adjuvants for human vaccines—current status, problems and future prospects,” Vaccine, 1995, 13(14):1263-1276. [cited by applicant]
Inouye et al.,“Up-promoter mutations in the Ipp gene of [cited by applicant]
Johnson et al., “3-0-Desacyl Monophosphoryl Lipid A Derivatives: Synthesis and Immunostimulant Activities,” J Med Chem, 1999, 42:4640-4649. [cited by applicant]
Jones et al., “Replacing the complementarity-determining regions in a human antibody with those from a mouse,” Nature, May 29-Jun. 4, 1986, 321:522-525. [cited by applicant]
Kahn et al., “Adjustable Locks and Flexible Keys: Plasticity of Epitote-Paratope Interactions in Germline Antibodies,” J Immunol, 2014, 192:5398-5405. [cited by applicant]
Kohler, “Immunoglobulin chain loss in hybridoma lines,” Proc Natl Acad Sci USA, Apr. 1980, 77(4):2197-2199. [cited by applicant]
Krauss et al., “Specificity grafting of human antibody frameworks selected from a phage display library: generation of a highly stable humanized anti-CD22 single-chain Fv fragment,” Protein Eng, 2003, 16(10):753-759. [cited by applicant]
Lodmell et al., “DNA vaccination of mice against rabies virus: effects of the route of vaccination and the adjuvant monophosphoryl lipid A (MPL),” Vaccine, 2000, 18:1059-1066. [cited by applicant]
Logan et al., “Adenovirus tripartite leader sequence enhances translation of mRNAs late after infection,” Proc Natl Acad Sci USA, Jun. 1984, 81:3655-3659. [cited by applicant]
Lonberg et al., “Human Antibodies From Transgenic Mice,” Intern Rev Immunol, 1995, 13:65-93. [cited by applicant]
Lowy et al., “Isolation of Transforming DNA: Cloning the Hamster aprt Gene,” Cell, Dec. 1980, 22:817-823. [cited by applicant]
Maccallum et al., “Antibody-antigen Interactions: Contact Analysis and Binding Site Topography,” J.Mol. Biol., 1996, 262:732-745. [cited by applicant]
Mariuzza et al., “The Structural Basis of Antigen-Antibody Recognition,” Ann. Rev. Biophys. Biophys. Chem., 1987, 16:139-159. [cited by applicant]
Morgan et al., “Human Gene Therapy,” Annu Rev Biochem, 1993, 62:191-217. [cited by applicant]
Mulligan, “The Basic Science of Gene Therapy,” Science, May 14, 1993, 260:926-932. [cited by applicant]
Mulligan et al., “Selection for animal cells that express the [cited by applicant]
Nelson et al., “A computer program for calculating antibody affinity constants,” Comput Methods Programs Biomed, 1988, 27:65-68. [cited by applicant]
O'Connor et al., “Humanization of an antibody against human protein C and calcium-dependence involving framework residues,” Protein Eng, 1998, 11(4):321-328. [cited by applicant]
O'Hare et al., “Transformation of mouse fibroblasts to methotrexate resistance by a recombinant plasmid expressing a prokaryotic dihydrofolate reductase,” Proc Natl Acad Sci USA, Mar. 1981, 78(3):1527-1531. [cited by applicant]
Piche-Nicholas et al., “Changes in complementarity-determining regions significantly alter IgG binding to the neonatal Fc receptor (FcRn) and pharmacokinetics,” MABS, 2018, 10(1):81-94. [cited by applicant]
Poosarla et al., “Computational De Novo Design of Anitbodies Binding to a Peptide With High Affinity,” Biotechnology and Bioengineering, 2017, 114(6):1331-1342. [cited by applicant]
Presta et al., “Humanization of an Anti-Vascular Endothelial Growth Factor Monoclonal Antibody for the Therapy of Solid Tumors and Other Disorders,” Cancer Res, Oct. 15, 1997, 57:4593-4599. [cited by applicant]
Proudfoot, “Transcriptional interference and termination between duplicated alpha-globin gene constructs suggests a novel mechanism for gene regulation,” Nature, 1986, 322:562-565. [cited by applicant]
Queen et al., “A humanized antibody that binds to the interleukin 2 receptor,” Proc Natl Acad Sci USA, Dec. 1989, 86:10029-10033. [cited by applicant]
Rader et al., “A phage display approach for rapid antibody humanization: Designed combinatorial V gene libraries,” Proc Natl Acad Sci USA, Jul. 1998, 95:8910-8915. [cited by applicant]
Riechmann et al., “Reshaping human antibodies for therapy,” Nature, Mar. 1988, 332:323-327. [cited by applicant]
Roguska et al., “Humanization of murine monoclonal antibodies through variable domain resurfacing,” Proc Natl Acad Sci USA, Feb. 1994, 91:969-973. [cited by applicant]
Roque et al., “Antibodies and Genetically Engineered Related Molecules: Production and Purification,” Biotechnol Prog, 2004, 20:639-654. [cited by applicant]
Rosok et al., “A Combinatorial Library Strategy for the Rapid Humanization of Anticarcinoma BR96 Fab,” J Biol Chem, Sep. 13, 1996, 271(37)22611-22618. [cited by applicant]
Rossi et al., “A Comparative Study Between a Novel Category of Immunoreagents and the Corresponding Mouse Monoclonal Antibodies,” Am J Clin Pathol, 2005, 124:295-302. [cited by applicant]
Rudikoff et al., “Single amino acid substitution altering antigen-binding specificity,” Proc. Natl. Acad. Sci. USA, 1982, 79:1979-1983. [cited by applicant]
Rump et al., “An initial investigation into endothelial CC chemokine expression in the human rheumatoid synovium,” Cytokine, 2017, 97:133-140. [cited by applicant]
Ruther et al., “Easy identification of cDNA clones,” Embo J, 1983, 2(10):1791-1794. [cited by applicant]
Santerre et al., “Expression of prokaryotic genes for hygromycin B and G418 resistance as dominant-selection markers in mouse L cells,” Gene, 1984, 30:147-156. [cited by applicant]
Scott et al., “Searching for Peptide Ligands with an Epitope Library,” Science, 1990, 249:386-390. [cited by applicant]
Shinkawa et al., “The Absence of Fucose but Not the Presence of Galactose or Bisecting N-Acetylglucosamine of Human IgG1 Complex-type Oligosaccharides Shows the Critical Role of Enhancing Antibody-dependent Cellular Cyt… [cited by applicant]
Szybalska et al., “Genetics of Human Cell Lines, IV. DNA-Mediated Heritable Transformation of a Biochemical Trait,” Proc Natl Acad Sci USA, 1962, 48:2026-2034. [cited by applicant]
Tachibana et al., “Altered reactivity of immunoglobulin produced by human-human hybridoma cells transfected by pSV2-neo gene,” Cytotechnology, 1991, 6:219-226. [cited by applicant]
Tan et al., “Superhumanized Antibodies: Reduction of Immunogenic Potential by Complementarity-Determining Region Grafting with Human Germline Sequences: Application to an Anti-CD28,” J Immunol, 2002, 169:1119-1125. [cited by applicant]
Tolstoshev, “Gene Therapy, Concepts, Current Trials and Future Directions,” Annu Rev Pharmacol Toxicol, 1993, 33:573-596. [cited by applicant]
Tsurushita et al., “Humanization of Monoclonal Antibodies,” Molecular Biology of B Cells, 2004:533-545. [cited by applicant]
UniProtKB Q16627, “(CCL14_Human),” Nov. 1, 1997. [cited by applicant]
Van Erp et al., “Application of a Sol Particle Immunoassay to the Determination of Affinity Constants of Monoclonal Antibodies,” J Immunoassay, 1991, 12(3):425-443. [cited by applicant]
Van Heeke et al., “Expression of Human Asparagine Synthetase in [cited by applicant]
Verhoeyen et al., “Reshaping Human Antibodies: Grafting an Antilysozyme Activity,” Science, 1988, 239:1534-1536. [cited by applicant]
Ward et al., “Binding activities of a repertoire of single immunoglobulin variable domains secreted from [cited by applicant]
Wigler et al., “Transfer of Purified Herpes Virus Thymidine Kinase Gene to Cultured Mouse Cells,” Cell, May 1977, 11:223-232. [cited by applicant]
Wigler et al., “Transformation of mammalian cells with an amplifiable dominant-acting gene,” Proc Natl Acad Sci USA, Jun. 1980, 77(6):3567-3570. [cited by applicant]
Wilson et al., “Simplified conjugation chemistry for coupling peptides to F(ab') fragments: autologous red cell agglutination assay for HIV-1 antibodies,” J Immunol Methods, 1994, 175:267-273. [cited by applicant]
Wu et al., “Humanization of a Murine Monoclonal Antibody by Simultaneous Optimization of Framework and CDR Residues,” J Mol Biol, 1999, 294:151-162. [cited by applicant]
Yarmush et al., “Coupling of antibody-binding fragments to solid-phase supports: site-directed binding of F(ab')2 fragments,” J Biochem Biophys Methods, 1992, 25:285-297. [cited by applicant]
Official action issued Jun. 21, 2023, in Chinese Application No. 201880088190.3. [cited by applicant]
Extended European Search Report issued Dec. 6, 2021, in European Patent Application No. 18893753.6. [cited by applicant]
Official action issued Jul. 11, 2023, in European Application No. 18893753.6. [cited by applicant]
Official action issued Dec. 1, 2022, in European Application No. 18893753.6. [cited by applicant]
Partial Supplementary European Search Report issued Aug. 4, 2021, in European Patent Application No. 18893753.6. [cited by applicant]
International Search Report and Written Opinion issued Aug. 27, 2019, in PCT Application No. PCT/US2018/068000. [cited by applicant]
Official action issued Nov. 22, 2022, in Japanese Application No. 2022-555739. [cited by applicant]
Extended European Search Report issued Oct. 4, 2023 in European Patent Application No. 20834440.8. [cited by applicant]
GenBank: AAA31367.1, “immunoglobulin heavy chain, partial [Oryctolagus cuniculus],” Jun. 2, 1994. [cited by applicant]
International Preliminary Report on Patentability dated Dec. 28, 2021 issued in PCT/US2020/040520. [cited by applicant]
International Preliminary Report on Patentability received for PCT Patent Application No. PCT/US2018/068000, mailed on Jul. 9, 2020, 8 pages. [cited by applicant]
International Search Report and Written Opinion dated Oct. 14, 2020 issued in PCT/US2020/040520. [cited by applicant]
Li, “Chemokines CCL2, 3, 14 regulate macrophage bone marrow homing, proliferation and polarization in multiple myeloma,” Zhejiang University School of Medicine, May 1, 2015, 10:1-106, English abstract. [cited by applicant]
Official action issued Dec. 14, 2023, in Chinese Patent Application No. 202080060781. 7. [cited by applicant]
Official action issued Feb. 5, 2024, in Canadian Patent Application No. 3145667. [cited by applicant]
Official action issued Jul. 11, 2023, in European Patent Application No. 20834440.8. [cited by applicant]
Official action issued Jun. 1, 2023, in Chinese Patent Application No. 202080060781. 7. [cited by applicant]
R&D Systems: “Human CCL 14/HCC-1 /HCC-3Antibody MAB3241”, Jul. 2, 2018, XP93059968, Retrieved from the Internet: URL:https://resources.rndsystems.com/pdfs/datasheets/mab3241.pdf? [cited by applicant]