WO2008035527A1 - ANTICORPS MONOCLONAL ANTI-C1q - Google Patents

ANTICORPS MONOCLONAL ANTI-C1q Download PDF

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Publication number
WO2008035527A1
WO2008035527A1 PCT/JP2007/066200 JP2007066200W WO2008035527A1 WO 2008035527 A1 WO2008035527 A1 WO 2008035527A1 JP 2007066200 W JP2007066200 W JP 2007066200W WO 2008035527 A1 WO2008035527 A1 WO 2008035527A1
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Prior art keywords
antibody
clq
antibody according
ferm
protein
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PCT/JP2007/066200
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English (en)
Japanese (ja)
Inventor
Takahiro Ochi
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Mmt Co., Ltd.
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Priority to JP2007545477A priority Critical patent/JPWO2008035527A1/ja
Publication of WO2008035527A1 publication Critical patent/WO2008035527A1/fr

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    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
    • C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans

Definitions

  • the present invention relates to an anti-Clq monoclonal antibody, a force, a method for determining the presence or amount of Clq using such an antibody, and a kit for the same.
  • RA Rheumatoid arthritis
  • Non-patent Document 1 It has been reported that the prognosis of whether or not the joint is destroyed can be made by the amount of Clq protein in the blood of RA patients (Non-patent Document 1). However, in the clinic, an anti-Clq antibody that can be used for the quantification of Clq protein in patient samples has not been established, and its development has been desired.
  • Non-Patent Document 1 Ochi T et al., Arthritis Rheum. 1988 Jan; 31 (1): 37-43
  • the problem to be solved by the present invention is to obtain an anti-Clq antibody that can be used for the quantification of Clq protein, a method for producing such an antibody, a specific and reproducible method for quantifying Clq protein, and a method therefor Is to develop a kit.
  • the present invention provides:
  • the antibody according to (1) which can specifically recognize a peptide having the amino acid sequence of SEQ ID NOs: 1 to 7, (3)
  • the antibody according to (1) or (2) which is produced by a hyperidoma having the patent biological deposit center accession number FERM BP-10649, AIST,
  • a kit for determining the presence or amount of Clq protein in a sample comprising the antibody according to any one of (1) to (8) as an essential component;
  • an anti-Clq monoclonal antibody that specifically recognizes Clq protein a method for producing the same, a hybridoma that produces an anti-Clq monoclonal antibody, and an anti-Clq monoclonal antibody that can be used for quantification of Clq protein are provided.
  • Methods for determining the presence or amount of Clq protein in the sample used, as well as kits and the like are provided.
  • Fig. 1 shows the results of ELISA using the culture supernatant of Hypridoma.
  • FIG. 2 is a graph showing the results of sandwich ELISA using anti-Clq antibody # 8 as a solid phase antibody and anti-Clq antibody # 35 (square) as a sensitizing antibody.
  • Figure 3 shows anti-Clq antibody # 33 as the solid phase antibody, anti-Clq antibody # 3 5 (square), anti-Clq antibody # 54 (circle), and anti-Clq antibody # 76 (diamond) as the sensitizing antibody. It is a graph which shows the result of the sandwich ELISA method using this.
  • Figure 4 shows anti-Clq antibody # 35 as the solid phase antibody, anti-Clq antibody # 3 5 (square), anti-Clq antibody # 54 (circle), and anti-Clq antibody # 76 (diamond) as the sensitizing antibody. It is a graph which shows the result of the sandwich ELISA method using this.
  • Figure 5 shows anti-Clq antibody # 40 as solid phase antibody and anti-Clq antibody # 5 as sensitizing antibody. 4 (circle) is a drape showing the results of sandwich ELISA using anti-Clq antibody # 76 (diamond).
  • Figure 6 shows the results of sandwich ELISA using anti-Clq antibody # 54 as solid phase antibody, anti-Clq antibody # 3 5 (square) and anti-Clq antibody # 54 (circle) as sensitizing antibodies. It is a dull that shows.
  • FIG. 7 is a graph showing the results of sandwich ELISA using anti-Clq antibody # 76 as a solid-phase antibody and anti-Clq antibody # 35 (square) as a sensitizing antibody.
  • FIG. 8 shows the results of sandwich ELISA using anti-Clq antibody # 107 as a solid phase antibody, anti-Clq antibody # 33 (triangle) and anti-Clq antibody # 35 (square) as sensitizing antibodies. It is a graph.
  • Figure 9 shows anti-Clq antibody # 112 as solid phase antibody, anti-Clq antibody # 35 (square), anti-Clq antibody # 54 (circle), and anti-Clq antibody # 76 (diamond) as sensitizing antibodies. It is a graph which shows the result of the used San-Germany ELISA method.
  • FIG. 10 is a graph showing the results of sandwich ELISA using anti-Clq antibody # 119 as a solid phase antibody and anti-Clq antibody # 33 (triangle) as a sensitizing antibody.
  • the present invention relates to an anti-Clq monoclonal antibody (hereinafter also referred to as “anti-Clq antibody”) capable of specifically recognizing Clq protein.
  • the anti-Clq monoclonal antibody of the present invention increases the amount of antigen-antibody conjugate formed depending on the amount of protein that can bind specifically to Clq protein and the amount of protein, that is, Clq protein. It is excellent in that it can be used for quantitative determination.
  • the antibody of the present invention can be obtained, for example, by immunizing a mammal such as a mouse with Clq protein, fusing a lymphocyte of the immunized animal with a myeloma cell line to produce a hyperidoma, and culturing this. That power S. Other known methods such as gene recombination and chemical synthesis may be used to produce such antibodies!
  • the anti-Clq monoclonal antibody of the present invention is preferably (a) a peptide having the amino acid sequence of SEQ ID NOs: 1 to 7, (b) SEQ ID NO: In the amino acid sequence of!
  • a peptide having an amino acid sequence deleted, substituted or appended and (c) at least 50% or more of the amino acid sequence of SEQ ID NOs: 1 to 7, for example, 60, 70, 75, 80, It is possible to specifically recognize a peptide selected from the group consisting of peptides having an amino acid sequence having 85, 90, and 93% of the same age.
  • the homology of amino acid sequences can be measured using, for example, FASTA, BLAST, DNASIS (manufactured by Hitachi Software Engineering Co., Ltd.), GENETYX (manufactured by Genenetics Co., Ltd.).
  • An anti-Clq monoclonal antibody may be obtained by immunizing an animal such as a mouse with the above peptide or a protein containing the peptide, and fusing a lymphocyte of the immunized mouse with a myeloma cell line to produce a hyperprideoma.
  • the antibody of the present invention is a hybridoma of a mouse myeloma cell line and a mouse lymphocyte, such as Neubridoma KS— 0131 # 8, KS — 0131 # 33, KS — 0131 # 35, KS — 0131 # 40, KS— 0131 # 54, or KS— 0131 # 76.
  • the Hypridoma was deposited at the Patent Organism Depositary Center (National Institute of Advanced Industrial Science and Technology) (Tsukuba Ito, 1-chome, 1-chome, 1-Chuo 6) and received on August 2, 2006.
  • Such hypridoma can be prepared by using known culture conditions, for example, composition: RPMI 1640 (ohjin 16005005) 425 mL, L-Glut amine (SIGMA G7513) 5 mL, sodium pyruvate (SIGMA S8636) 5 mL, HAT supplement (GIBCO 21060-017) lOmL, penicillin-streptomycin (SIGMA P4 333) 2. 37 ⁇ 0.1 in medium of 5 mL, FBS 75 mL. C, cultured at 5 ⁇ 0.15% CO
  • the anti-Clq monoclonal antibody can be produced by recovering and purifying the produced anti-Clq monoclonal antibody by a known means / method.
  • the anti-Clq monoclonal antibodies produced by # 40, KS— 0131 # 54, and KS— 0131 # 76 are anti-Clq antibody # 8, anti-Clq antibody # 33, anti-tagged; ⁇ antibody # 35, anti-Clq antibody, respectively. Denote # 40, anti-Clq antibody # 54, and anti-Clq antibody # 76.
  • the anti-Clq monoclonal antibodies of the present invention include fragments thereof, modified antibodies such as chimeric antibodies and humanized antibodies, and mutant antibodies. These fragments, modified antibodies or mutant antibodies also have the same specificity for Clq protein as the original antibody. These can be produced by means and methods known to those skilled in the art.
  • the present invention provides a patent biological deposit center accession number FERM BP-10649, FERM BP-10650, FERM BP-10651, FERM BP 10652, FERM BP—
  • the present invention relates to a hybridoma producing an anti-Clq monoclonal antibody having 10653 or FERM BP-10654.
  • the hyperidoma of the present invention is a cell obtained by fusing a mouse lymphocyte immunized with Clq protein and a mouse myeloma cell line.
  • the present invention relates to a method for producing an anti-Clq monoclonal antibody, wherein a peptide having the amino acid sequence of SEQ ID NOs: 1 to 7 is used.
  • a peptide having the amino acid sequence of SEQ ID NOs: 1 to 7 and (b) one or more, preferably 1, in the amino acid sequence of SEQ ID NOs: 1 to 7 (Masame, Arrangement (, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, or 14 (A solid amino acid has been deleted, substituted or added)
  • a peptide having an amino acid sequence or (c) having at least 50% or more homology with the amino acid IJ of SEQ ID NO:!-7, such as 60, 70, 75, 80, 85, 90, 93%
  • a peptide having an amino acid sequence may be used.
  • the production method of this aspect of the present invention may include a step of purifying an anti-Clq monoclonal antibody, etc., so as to immunize an animal such as a mouse with the peptide.
  • Immunization with peptides and purification of anti-Clq monoclonal antibodies can be performed by methods known to those skilled in the art.
  • the present invention relates to a method for producing an anti-Clq monoclonal antibody, characterized by culturing the hyperpridoma of the present invention.
  • Hypridoma culture includes both in vitro and in vivo culture. In vitro culture is performed under known culture conditions, for example, composition: RPMI 1640 (ohjin 16005005) 425 mL, L-G1 utamine (SIGMA G7513) 5 mL, sodium pyruvate (SIGMA S8636) 5 mL, HA T supplement (GIBCO 21060-017 ) 10mL, penicillin 'streptomycin (SIGMA P4333) 2. 37 ⁇ 0.1 in medium of 5mL, FBS 75mL. C, 5 ⁇ 0. 15% CO
  • Swelling power S In vivo culture is achieved, for example, by transplanting the hyperidoma of the present invention into the abdominal cavity of an animal such as a mouse.
  • the production method of the present invention may further include a step of purifying the obtained antibody. Those skilled in the art can appropriately select and use the purification method.
  • the present invention relates to a method for determining the presence or amount of Clq protein in a sample, characterized by using an anti-Clq monoclonal antibody of the present invention. Since the anti-Clq monoclonal antibody of the present invention has the property that the amount of the antigen-antibody conjugate increases depending on the amount of Clq protein, the presence of the Clq protein in the sample will reduce the force. Can be determined. Two or more anti-Clq monoclonal antibodies may be used in the determination method of the present invention. Using two or more anti-Clq monoclonal antibodies increases the sensitivity and specificity of determination and improves accuracy.
  • the body 76 is used in the determination method of the present invention.
  • the antibody used in the determination method of the present invention may be labeled. Various labels are known and can be appropriately selected and used by those skilled in the art.
  • HRP horseradish peroxidase
  • ALP enzymes such as Glueose oxidase ⁇ ⁇ -galactosidase, FITC, Rhodamine, Cy3, y5, Texas Red, Alexa Fluors, BODIPYs, IRDyes, MFPs, Quantum Dot, Light labels such as AMCA, Allophycocyanin, BMP, Cy2, Cy3.5, Cy5.5, DTAF, DyLight 547, DyLight 647, FluoroNano gold, Phycoerythrin, Phycocyanin, R_PE, Saporin, TRITC, Biotin, Digoxigenin (DIG), Acridium Ester, chemicals such Flashlight, 60 mm MicroBead of which beads, magnetic beads, such as MagCellect Ferrofluid [R], the radiation-labeled, such as 1 1, gold particles, labels such as Agarose used.
  • the determination method of the present invention can be performed efficiently by attaching a force and a
  • the sample may be any sample that may contain Clq protein. Examples include serum, joint fluid, cartilage, bone, and each tissue.
  • the sample is incubated with the anti-Clq monoclonal antibody of the present invention to form a conjugate of the anti-Clq antibody and the Clq protein in the sample, and then the conjugate. May be carried out by measuring.
  • ELISA methods such as sandwich ELISA, immunoblot method, radioimmunoassay (RIA) method, immunoprecipitation method, method using protein array, method using flow cytometer, chemiluminescent enzyme immunoassay (CLEIA), bioluminescent enzyme
  • the determination method of the present invention is performed using immunoassay (BLEIA), measurement using a developing device (immunoassay test piece) that can be infused by capillary action, immunochromatography, immunostaining, aggregation, etc. can do.
  • the ELISA method is preferably used because it does not require special equipment or the like, and the presence or amount of Clq protein can be determined quickly and easily in an actual medical field.
  • the determination method of the present invention is used for the prognosis diagnosis of RA. .
  • the present invention provides a method for diagnosing the prognosis of RA in a patient, comprising determining the presence or amount of Clq protein in a sample using the anti-Clq monoclonal antibody of the present invention. It is about.
  • the presence or amount of Clq protein may be determined as described above! /.
  • the present invention relates to a method for treating RA in a patient, which comprises administering the anti-Clq monoclonal antibody of the present invention.
  • the present invention relates to a kit for determining the presence or amount of Clq protein in a sample, comprising the anti-Clq monoclonal antibody of the present invention as an essential component.
  • Two or more anti-Clq monoclonal antibodies may be included in the kit of the present invention.
  • the kit of the present invention may contain, for example, a sample collection means, a label, a reaction container, a determination reagent and the like.
  • an instruction manual is attached to the kit.
  • anti-Clq monochrome The final antibody may be labeled.
  • kits of the present invention for example, ELISA methods such as sandwich ELISA method, Imnobutt method, Radioimmunoassay (RIA) method, immunoprecipitation method, method using protein array, flow cytometer , Chemiluminescent enzyme immunoassay (CLEIA), bioluminescent enzyme immunoassay (BLEIA), measuring method using expandable device (immunoassay specimen) that can be infused by capillary action, immunochromatography Alternatively, an immunostaining method, an aggregation method, or the like may be used. Since the kit of the present invention can be used to quickly and easily determine the presence or amount of Clq protein, it is possible to prognose RA patients in clinical settings. In addition, pathological studies of RA can be performed using the kit of the present invention.
  • ELISA methods such as sandwich ELISA method, Imnobutt method, Radioimmunoassay (RIA) method, immunoprecipitation method, method using protein array, flow cytometer , Che
  • mice Four female BALB / C mice were given Clq purified protein (purity 99% or higher, Calbiochem 20 4876) 0.1 mg with adjuvant (Titermax, SIGMA) 2-3 times every 2 weeks subcutaneously on the footpad and back And immunized. Lymphocytes were collected from the mouse spleen and cultured in a medium containing the antigen 30, ig for 3 days. After culture, lymphocytes and mouse myeloma cell line P3U1 cells were fused using PEG1500 according to a conventional method.
  • the cells were composed of: R PMI 1640 (ohjin 16005005) 425 mL, L-Glutamine (SIGMA G7513) 5 mL, sodium pyruvate (SIGMA S8636) 5 mL, HAT supplement (GIBCO 21060-017) lOmL, penicillin streptomycin (SIGMA P4333 2. Suspended in 5 mL, 75 mL FBS medium and dispensed into 96 well plates previously seeded with mouse thymocytes. After 8 days, the presence of antibody in the supernatant was screened by ELISA. The procedure for ELISA is as follows.
  • a solution of 1 ag / ml Clq in PBS was prepared, added to an ELISA microplate (3912 Falcon), and allowed to bind by incubation at room temperature for 2 hours. Next, blocking was performed using 1% skim milk / PBS to prepare an antigen plate. The culture supernatant was added to the antigen plate for reaction, and after washing, ALP-labeled goat anti-IgG (Zymet) was bound. Add ALP substrate, allow enzyme reaction, and absorb at 492 nm The light intensity was measured and antibody positive wells were selected. As a control, a polyclonal antibody isolated from the serum of a similarly immunized rabbit was used. The results are shown in Figure 1.
  • the amino acid sequences of human Clq subunits A chain, B chain, and C chain are shown in SEQ ID NOs: 17 to 19, and the nucleotide sequences are shown in SEQ ID NOs: 20 to 22, respectively.
  • a sequence obtained by shifting the amino acid sequence of each subunit by 15 amino acids (residues) at intervals of 3 amino acids is a synthetic peptide (in order, peptide numbers;! -78, 97-; 117, 193-270) on a glass array.
  • Each peptide was synthesized at a specific position on the array, and a peptide array containing a synthetic peptide covering the entire amino acid sequence of the C1 q subunit was prepared.
  • the array was manufactured by JPT.
  • # 8, # 33, # 40, # 54, and # 76 were purified using a Protein G column.
  • the purified antibody was diluted 1,000 times in PBS (10 mM phosphate buffer pH 7.0, 0.1 M NaCl) 330,11 on the peptide array, sealed, and sealed at 4 ° C. Incubated for 12 hours. Thereafter, it was washed once with methanol and then with 0 water for 5 minutes 5 times. Centrifuge to dry the array slide, scan with a fluorescence scanner (Agilent DNA microarray scanner; Agilent), and use software (Feature Extraction software; Agilent) to determine the fluorescence intensity of each peptide spot on the array. Turned into. Several spots showing strong fluorescence intensity were detected.
  • peptide spots that are 1,300 or more higher than the background level! / And show fluorescence intensity are shown in Table 1 (amino acid sequences of peptide numbers 149, 150, and 244 to 246 are shown in SEQ ID NOs: 3 to 7, respectively) ).
  • the peptides 149 and 150 are sequences derived from the ClqB subunit (B chain), and the peptides 24 to 246 are sequences derived from the ClqC subunit (C chain). From these sequences, the amino acid sequence of Clq epitope was predicted to contain 9 residues or a part of CKVPGLYYF (SEQ ID NO: 2).
  • CKVPGLYY (SEQ ID NO: 23), KVPGLYYF (SEQ ID NO: 24)), 7 amino acids (CKVPG LY (SEQ ID NO: 25), KVPGLYY (SEQ ID NO: 26), VPGLYYF (SEQ ID NO: 27)), 6 amino acids ( CKVPGL (SEQ ID NO: 28), KVPGLY (SEQ ID NO: 29), VPGLYY (SEQ ID NO: 30), PGLYYF (SEQ ID NO: 1)), 5 amino acids (CKVPG (SEQ ID NO: 31), KVPGL (SEQ ID NO: 32), VPGLY (SEQ ID NO: 32) 33), PGLYY (SEQ ID NO: 34), GLYYF ( (Column number 3 5)), 4 amino acids (CKVP (SEQ ID NO: 36), KVPG (SEQ ID NO: 37), VPGL (SEQ ID NO: 3 8), PGLY (SEQ ID NO: 39), GLYY (SEQ ID NO: 40),
  • Glycellonore ( ⁇ ⁇ 2 ⁇ 2) was dissolved to prepare ZOO ⁇ g / ml and 50 g / ml human Clq protein solutions.
  • the human Clq protein solution was spotted on a nitrocellulose membrane (Hybond C; manufactured by Amersham) having a size of 5 mm ⁇ 15 mm as shown in Table 3 and air-dried at room temperature for about 1 hour. Soak the nitrocellulose membrane in TBS, let it fit for about 5 minutes, and then use TBS (20 mM Tris-HC1 pH 7.5, 150 mM NaCl) containing 5% blocking agent (Amersham ECL blocking reagent; manufactured by GE Healthcare) at room temperature. Blocking was performed for 1 hour.
  • the blocked nitrocellulose membrane was gently washed with TBS, immersed in a solution (201) containing each anti-Clq antibody and synthetic peptide, and allowed to react at room temperature for 1 hour.
  • the nitrocellulose membrane was lightly washed once with TTBS (TBS added with Tween 20 at a final concentration of 0.05%), and then washed with a sufficient amount of TTBS for 10 minutes x 3 times with shaking. Binding detection was performed as follows.
  • Nitrocellulose membrane with ALP coloring buffer (lOOmM NaCl, 5mM MgCl in Tri
  • the plate was immersed in ALP color buffer 30 containing BCIP / NBT solution (Promega) and developed for 10 minutes at room temperature. When the stained image was obtained, The trocellulose membrane was immersed in a sufficient amount of distilled water to wash away the color developing buffer. After washing, the nitrocellulose membrane was air-dried and stained images were captured using an Epson digital scanner GT-8300UF.
  • the nitrosenololose membrane was immersed in a mixed solution of equal amounts of A and B in Amersham ECL Advance Western Blotting Detection Kit (manufactured by GE healthcare) and allowed to react at room temperature for 1 minute. After that, the reaction solution was lightly shaken, the nitrocellulose membrane was sandwiched between plastic films, and the chemiluminescence on the membrane was detected by exposing the membrane to a bolloid film.
  • a secondary antibody (avidinated ALP antibody) was added at 100 1 / well, and reacted at 4 ° C to room temperature;! ⁇ 2 hours. After washing 4 times with pure water, ALP substrate coloring solution was added to cause color development. Absorbance (OD) at 492 nm was measured with a microplate reader (reference wavelength: 660 nm). The results are shown in FIGS. A positive correlation was observed between Clq protein concentration and absorbance, and it was found that Clq protein in the sample could be quantified by sandwich ELISA using anti-Clq monoclonal antibody. Although not shown, it was quantifiable for Clq protein at concentrations of ⁇ 400 g / mL.
  • an anti-Clq monoclonal antibody that can be used for quantification of Clq protein, a method for detecting and / or quantifying Clq protein using such antibody, and a kit therefor can be obtained. It is extremely useful in fields such as diagnostics and (RA pathological) research.

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Abstract

L'invention concerne un anticorps monoclonal anti-C1q capable de reconnaître de façon spécifique la protéine C1q ; un procédé pour produire l'anticorps monoclonal anti-C1q ; un hybridome capable de produire un anticorps monoclonal anti-C1q ; un procédé pour la détermination de la présence de la quantité de protéine C1q dans un échantillon à l'aide d'un anticorps monoclonal anti-C1q ; et un coffret pour le procédé.
PCT/JP2007/066200 2006-09-21 2007-08-21 ANTICORPS MONOCLONAL ANTI-C1q WO2008035527A1 (fr)

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WO2009025300A1 (fr) * 2007-08-21 2009-02-26 Regenetiss Inc. Peptide capable de se lier à une immunoglobuline
WO2010084851A1 (fr) * 2009-01-23 2010-07-29 株式会社エム・エム・ティー Peptide capable de se lier à une immunoglobuline
WO2012043397A1 (fr) * 2010-10-01 2012-04-05 株式会社エム・エム・ティー Peptide pouvant se lier à l'immunoglobuline
WO2012067267A1 (fr) * 2010-11-18 2012-05-24 Takahiro Ochi Méthode d'essai faisant appel à un anticorps monoclonal anti-c1q
KR20180100944A (ko) * 2017-03-03 2018-09-12 서울대학교병원 아디포넥틴 유래 펩티드 및 이를 포함하는 피부노화 방지 또는 피부주름 개선용 조성물
CN112638358A (zh) * 2018-09-03 2021-04-09 (株)郑振镐效果 包含脂联素衍生肽的促进毛发生长用组合物
WO2023047125A1 (fr) 2021-09-24 2023-03-30 Reflection Therapeutics Limited Thérapies cellulaires ciblées
WO2023047124A2 (fr) 2021-09-24 2023-03-30 Reflection Therapeutics Limited Thérapies cellulaires ciblées

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Cited By (17)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2009025300A1 (fr) * 2007-08-21 2009-02-26 Regenetiss Inc. Peptide capable de se lier à une immunoglobuline
US8461299B2 (en) 2007-08-21 2013-06-11 Mmt Co., Ltd. Peptide capable of binding to immunoglobulin
CN102942616A (zh) * 2009-01-23 2013-02-27 株式会社Mmt 具有免疫球蛋白结合能力的肽
WO2010084851A1 (fr) * 2009-01-23 2010-07-29 株式会社エム・エム・ティー Peptide capable de se lier à une immunoglobuline
EP2383336A1 (fr) * 2009-01-23 2011-11-02 Mmt Co., Ltd Peptide capable de se lier à une immunoglobuline
CN102361979A (zh) * 2009-01-23 2012-02-22 株式会社Mmt 具有免疫球蛋白结合能力的肽
EP2383336A4 (fr) * 2009-01-23 2013-01-23 Mmt Co Ltd Peptide capable de se lier à une immunoglobuline
WO2012043397A1 (fr) * 2010-10-01 2012-04-05 株式会社エム・エム・ティー Peptide pouvant se lier à l'immunoglobuline
WO2012067267A1 (fr) * 2010-11-18 2012-05-24 Takahiro Ochi Méthode d'essai faisant appel à un anticorps monoclonal anti-c1q
KR20180100944A (ko) * 2017-03-03 2018-09-12 서울대학교병원 아디포넥틴 유래 펩티드 및 이를 포함하는 피부노화 방지 또는 피부주름 개선용 조성물
KR101967630B1 (ko) * 2017-03-03 2019-04-11 서울대학교병원 아디포넥틴 유래 펩티드 및 이를 포함하는 피부노화 방지 또는 피부주름 개선용 조성물
CN112638358A (zh) * 2018-09-03 2021-04-09 (株)郑振镐效果 包含脂联素衍生肽的促进毛发生长用组合物
EP3848020A4 (fr) * 2018-09-03 2021-09-08 Jungjinho Effect Inc. Composition favorisant la pousse des cheveux comprenant un peptide dérivé de l'adiponectine
US11771636B2 (en) 2018-09-03 2023-10-03 Jungjinho Effect Inc. Composition for promoting hair growth comprising adiponectin-derived peptide
CN112638358B (zh) * 2018-09-03 2024-01-05 (株)郑振镐效果 包含脂联素衍生肽的促进毛发生长用组合物
WO2023047125A1 (fr) 2021-09-24 2023-03-30 Reflection Therapeutics Limited Thérapies cellulaires ciblées
WO2023047124A2 (fr) 2021-09-24 2023-03-30 Reflection Therapeutics Limited Thérapies cellulaires ciblées

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