PHARMACEUTICAL COMPOSITION CONTAINING ANTIBODIES AGAINST IL-5 AND ITS USE

Abstract

This application describes a pharmaceutical composition containing an antibody against IL-5 and its use. Specifically, this application describes a pharmaceutical composition containing an IL-5 antibody or an antigen-binding fragment thereof in a buffer solution. The pharmaceutical composition also contains a saccharide and a non-ionic surfactant.

Description

PHARMACEUTICAL COMPOSITION CONTAINING ANTIBODIES AGAINST IL-5 AND ITS USE Field of Invention The present invention pertains to the field of pharmaceutical preparations and, in particular, to a pharmaceutical composition comprising an anti-IL-5 antibody or an antigen-binding fragment thereof, and its use as a diagnostic agent for IL-5-related diseases and a therapeutic drug. Background of the Invention The statements in this document are merely background information relating to the present invention and do not necessarily constitute a prior art. Interleukin-5 (IL-5) is one of the important members of the interleukin family, also known as T-cell replacement factor (TRF), B-cell growth factor II (BCGF-II), IgA enhancement factor (IgA-EF), and eosinophil differentiation factor (EDF). Human IL-5 consists of 134 amino acid residues, including signal peptides of 22 amino acids and two glycosylation sites. Active IL-5 exists as an oligomer; the two peptide chains are linked by a disulfide bond in an inverse parallel configuration, and the IL-5 monomer is biologically inactive (Adv-lm-Muonol. 1994; 57: 145-90). Eosinophils (EOS) are associated with a variety of inflammatory diseases in the lungs, including allergic conditions associated with allergic reactions. Asthma is a chronic inflammatory disease of the respiratory tract, affecting approximately 3 billion people worldwide, with an incidence of 10%. Its pathogenesis is associated with a variety of cytokines. IL-5 and its receptor IL-5R play a significant role in the development of asthma. Currently, the most effective methods for treating asthma involve inhibiting the expression of certain critical mediators, including IL-5, by administering a solid alcoholic drug into the nasal or oral cavity to alleviate lung inflammation. However, prolonged use of sterols has numerous side effects. Therefore, it is necessary to identify new pharmacological targets for asthma treatment.The use of anti-IL-5 antibodies to inhibit the binding of IL-5 to its receptor has been shown to significantly reduce eosinophil aggregation in the lungs, as they lower eosinophil levels in blood, tissue, and sputum, reduce the eosinophil-mediated inflammatory response, improve lung function, and have a good curative effect in severe eosinophilic asthma and recurrent asthma. (Drugs. 2017 May; 77(7): 777784). Antibody drugs have a high molecular weight and complex structure, and denaturation, aggregation, contamination, and particle formation are common problems during production, transport, and storage. To maintain the efficacy of the antibody, it must retain its biological activity throughout production, purification, transport, and storage. New production and purification techniques have been developed to produce large quantities of highly purified monoclonal antibodies. However, stabilizing these antibodies for transport and storage, and ensuring they are suitable for various dosage forms, has been a challenge. The only existing anti-IL-5 antibodies currently approved for sale are GSK's Mepolizumab and Teva Pharma's Reslizumab. Related patents include WO 201811916, WO 2017033121, WO 2014141149, WO 2016040007, WO 2015095539, WO 2012138958, WO 9535375, etc. Summary of the invention The present invention provides a pharmaceutical composition comprising an IL-5 antibody or an antigen-binding fragment thereof, a buffer, and a surfactant selected from the group consisting of acetic acid-sodium acetate, succinate-sodium succinate, histidine hydrochloride, and sodium citrate buffer, preferably acetic acid-sodium acetate or succinic acid-sodium succinate buffer. The anti-IL-5 antibody or its antigen-binding fragment comprises a heavy-chain variable region and a light-chain variable region, wherein: (i) the variable region of the heavy chain comprises HCDR1, HCDR2 and HCDR3 as shown in the amino acid sequence of SEQ ID NO's: 16,17,18, respectively, the variable region of the light chain comprising LCDR1, LCDR2 and LCDR3, respectively, as shown in SEQ ID NO's: 19, 20, 21 amino acid sequences; (i) the variable region of the heavy chain comprises HCDR1, HCDR2 and HCDR3 as shown in the amino acid sequence of SEQ ID NO's: 22,23,24, respectively, the variable region of the light chain comprising LCDR1, LCDR2 and LCDR3, respectively, as shown in SEQ ID NO's: 25, 26, 27 amino acid sequences; (iii) the variable region of the heavy chain comprises HCDR1, HCDR2 and HCDR3 as shown in the amino acid sequence of SEQ ID NO's: 28,29,30, respectively, the variable region of the light chain comprising LGDR1, LCDR2 and LCDR3, respectively, as shown in SEQ ID NO's: 31,32, 33 amino acid sequences; (iv) the variable region of the heavy chain comprises HCDR1, HCDR2 and HCDR3 as shown in the amino acid sequence of SEQ ID NO's: 34,35,36, respectively, the variable region of the light chain comprising LCDR1, LCDR2 and LCDR3, respectively, as shown in SEQ ID NO's: 37, 38, 39 amino acid sequences; (v) the variable region of the heavy chain comprises HCDR1, HCDR2 and HCDR3 as shown in the amino acid sequences of SEQ ID NO's: 40, 41, 42, respectively, the variable region of the light chain comprising LCDR1, LCDR2 and LCDR3, respectively, as shown in amino acid sequences of SEQ ID NO's: 43, 44, 45; or (vi) the variable region of the heavy chain comprises HCDR1, HCDR2 and HCDR3, respectively, as shown in amino acid sequences of SEQ ID NO's: 34, 82, 36, the variable region of the light chain comprises LCDR1, LCDR2 and LCDR3, respectively, as shown in amino acid sequences of SEQ ID NO's: 37, 38, 39. In alternative embodiments, the pH of the buffer in the pharmaceutical composition is approximately 5.0 to approximately 6.5, preferably approximately 5.5 to approximately 6.5, preferably approximately 6.0 to approximately 6.5, preferably approximately 5.0 to approximately 6.0, preferably approximately 5.5 to approximately 6.0, preferably approximately 5.0 to approximately 5.5, preferably approximately 5.0 to approximately 5.8, preferably approximately 5.2 to approximately 5.8; non-limiting examples of buffer pH include approximately 5.0, approximately 5.1, approximately 5.2, approximately 5.3, approximately 5.4, approximately 5.5, approximately 5.6, approximately 5.7, approximately 5.8, approximately 5.9, approximately 6.0, approximately 6.5 and most preferably about 5.5. In alternative embodiments, the buffer concentration in the pharmaceutical composition is approximately 10 mM to approximately 40 mM, preferably approximately 15 mM to approximately 30 mM, preferably approximately 20 mM to approximately 30 mM, preferably approximately 25 mM to approximately 30 mM, approximately 30 mM, preferably approximately 10 mM to approximately 25 mM, preferably approximately 15 mM to approximately 25 mM, preferably approximately 20 mM to approximately 25 mM. mM, preferably from approximately 10 mM to approximately 15 mM. Non-limiting buffer concentrations include approximately 10 mM, approximately 12 mM, approximately 14 mM, approximately 16 mM, approximately 18 mM, approximately 20 mM, approximately 22 mM, approximately 24 mM, approximately 26 mM, approximately 28 mM, approximately 30 mM, approximately 32 mM, approximately 34 mM, and more preferably approximately 30 mM. In alternative formulations, the concentration of the anti-IL-5 antibody or its antigen-binding fragment in the pharmaceutical composition is approximately 1 mg / ml. approximately 120 mg / ml, preferably from approximately 1 mg / ml to approximately 100 mg / ml, preferably from approximately 10 mg / ml to approximately 120 mg / ml, preferably from approximately 20 mg / ml to approximately 120 mg / ml, preferably from approximately 30 mg / ml to approximately 120 mg / ml, preferably from approximately 40 mg / ml to approximately 120 mg / ml, preferably from approximately 50 mg / ml to approximately 120 mg / ml, preferably from approximately 60 mg / ml to approximately 120 mg / ml, preferably from approximately 70 mg / ml to approximately 120 mg / ml, preferably from approximately 80 mg / ml to approximately 120 mg / ml, preferably from approximately 90 mg / ml to approximately 120 mg / ml, preferably from approximately 100 mg / ml to approximately 120 mg / ml, preferably from approximately 110 mg / ml to approximately 120 mg / ml, preferably from approximately 20 mg / ml to approximately 100 mg / ml, preferably from approximately 30 mg / ml to approximately 100 mg / ml, preferably from approximately 40 mg / ml to approximately 100 mg / ml, preferably from approximately 50 mg / ml to approximately 100 mg / ml, preferably from approximately 60 mg / ml to approximately 100 mg / ml, preferably from approximately 70 mg / ml to approximately 100 mg / ml,preferably from approximately 80 mg / ml to approximately 100 mg / ml, preferably from approximately 90 mg / ml to approximately 100 mg / ml. As non-limiting examples, the anti-IL-5 antibody or its, The antigen-binding fragment nccLLn / Lznz / e / YiAi is approximately 80 mg / ml, approximately 90 mg / ml, approximately 91 mg / ml, approximately 92 mg / ml, approximately 93 mg / ml, approximately 94 mg / ml, approximately 95 mg / ml, approximately 96 mg / ml, approximately 97 mg / ml, approximately 98 mg / ml, approximately 99 mg / ml, approximately 100 mg / ml, approximately 101 mg / ml, approximately 102 mg / ml, approximately 103 mg / ml, approximately 104 mg / ml, approximately 105 mg / ml, approximately 106 mg / ml, approximately 107 mg / ml, approximately 108 mg / ml, approximately 109 mg / ml, approximately 110 mg / ml, approximately 115 mg / ml, approximately 120 mg / ml, most preferably approximately 100 mg / ml. In alternative embodiments, the surfactant comprising the pharmaceutical composition may be selected from the group consisting of polysorbate 20, polysorbate 80, polyhydroxyalkylene, Triton, sodium dodecylsulfonate, sodium laurylsulfonate, sodium octylglycoside, laurylsulfobetaine, myristylsulfobetaine, linoleylsulfobetaine, stearylsulfobetaine, lauryl sarcosine, myristylsarcosine, linoleylsarcosine, stearylsarcosine, linoleylbetaine, myristylbetaine, cetylbetaine, lauramidopropylbetaine, cocamidopropylbetaine, beta-myristamidoamide, palmitamidopropylbetaine, isosteamidopropylbetaine, myristamidopropyldimethylamine, palmamidopropyldimethylamine, isostearamidopropyl-dimethylamine, sodium methyl cocoyl, sodium methyl oleoyl taurate, polyethylene glycol, polypropylene glycol, ethylene glycol, etc. 80 or polysorbate 20, and more preferably polysorbate 80.In alternative embodiments, the concentration of polysorbate 80 in the pharmaceutical composition is approximately 0.05 mg / ml to approximately 0.6 mg / ml, preferably approximately 0.1 mg / ml to approximately 0.6 mg / ml, preferably approximately 0.2 mg / ml a. about 0.6 mg / ml, preferably from about 0.3 mg / ml to about 0.6 mg / ml, preferably from about 0.4 mg / ml to about 0.6 mg / ml, preferably from about 0.5 mg / ml to about 0.6 mg / ml, preferably । from about 0.2 mg / ml to about 0.5 mg / ml, preferably from about 0.3 mg / ml to about 0.5 mg / ml, preferably from about 0.4 mg / ml to about 0.5 mg / ml, preferably from about 0.3 mg / ml to nccLLn / Lznz / e / YiAi approximately 0.4 mg / ml, as a non-limiting example, the surfactant concentration in the pharmaceutical composition is approximately 0.2 mg / ml, approximately 0.3 mg / ml, approximately 0.4 mg / ml, approximately 0.45 mg / ml, approximately 0.5 mg / ml, approximately 0.55 mg / ml, approximately 0.6 mg / ml and most preferably approximately 0.4 mg / ml. Furthermore, in an alternative embodiment, the pharmaceutical composition further comprises an auxiliary material, wherein the auxiliary material is selected from the group consisting of a stabilizer. In an alternative embodiment, the stabilizer is selected from the group consisting of sugars or amino acids; wherein the sugar can be selected from the group consisting of sucrose, trehalose, mannitol, or sorbitol, preferably sucrose. The amino acid is selected from the group consisting of glycine, methionine, and proline. In alternative embodiments, the sugar concentration is approximately 50 mg / ml to approximately 80 mg / ml, preferably approximately 60 mg / ml, approximately approximately approximately mg / ml, mg / ml, mg / ml, preferably preferably of of of approximately approximately approximately mg / ml mg / ml mg / ml mg / ml approximately 75 mg / ml; as a non-limiting example, the stabilizer concentration in the pharmaceutical composition is approximately 70 mg / ml, approximately 71 mg / ml, approximately 72 mg / ml, approximately 73 mg / ml, approximately 74 mg / ml, approximately 75 mg / ml, approximately 76 mg / ml, approximately 77 mg / ml, approximately 78 mg / ml, approximately 79 mg / ml, approximately 80 mg / ml, more preferably approximately 72 mg / ml. In alternative formulations, the amino acid has a concentration of approximately 8 mg / ml. In alternative modalities, the pharmaceutical composition comprises: (a) from approximately 1 mg / ml to approximately 120 mg / ml of the anti-IL5 antibody or the antigen-binding fragment thereof; (b) acetic acid-sodium acetate buffer from approximately 10 mM to approximately 30 mM, pH from approximately 5.0 to 6.5; and (c) from approximately 0.1 mg / ml to approximately 0.6 mg / ml of polysorbate 80. In alternative modalities, the pharmaceutical composition comprises: (a) from approximately 80 mg / ml to approximately 100 mg / ml of the anti-IL-5 antibody or the antigen-binding fragment thereof; (b) acetic acid-sodium acetate buffer from approximately 10 mM to approximately 30 mM, pH from approximately 5.0 to approximately 6.0; and (c) from approximately 0.1 mg / ml to approximately 0.4 mg / ml of polysorbate 80. In alternative modalities, the pharmaceutical composition comprises: (d) from approximately 80 mg / ml to approximately 120 mg / ml of IL-5 antibody or the antigen-binding fragment thereof; (e) acetic acid-sodium acetate buffer from approximately 10 mM to approximately 30 mM, pH from approximately 5.0 to approximately 5.8; (f) from approximately 0.2 mg / ml to approximately 0.6 mg / ml of polysorbate 80; and (g) from approximately 70 mg / ml to approximately 75 mg / ml of sucrose; preferably, the pharmaceutical composition comprises: (h) approximately 100 mg / ml of IL-5 antibody or the antigen-binding fragment thereof, (i) approximately 30 mM of acetic acid-sodium acetate buffer, pH approximately 5.5, (j) approximately 0.4 mg / ml of polysorbate 80 and (k) approximately 72 mg / ml of sucrose. In some preferred embodiments, the anti-IL-5 antibody or its antigen-binding fragment in the pharmaceutical composition of the present invention is a murine antibody, a chimeric antibody, or a humanized antibody. In alternative embodiments, the humanized anti-IL-5 antibody in the pharmaceutical composition comprises a heavy chain variable region or a variant thereof as shown in SEQ ID NO: 49, 57, 63, 69 or 75; the variant is a heavy chain variable region sequence shown in SEQ ID NO: 49, 57, 63, 69 or 75, having 1 to 10 amino acid salvage mutations. In alternative modalities, the variant is a variant as shown in any selected from the group consisting of: (i) a variant, comprising one or more amino acid reverse mutations selected from the group consisting of S49T, V93T and K98S in the variable region of the heavy chain as shown in SEQ ID NO: 49; (ii) a variant, comprising one or more reverse mutations of amino acids selected from the group consisting of S49T, V93T and K98T in the variable region of the heavy chain as shown in SEQ ID NO: 57; (iii) a variant, comprising one or more reverse amino acid mutations selected from the group consisting of R38K, M48I, R67K, V68A, M70L, R72V, T74K and L83F in the variable region of the heavy chain as shown in SEQ ID NO: 63; (iv) a variant, comprising one or more amino acid reverse mutations selected from the group consisting of F29I, R38K, V48I, R72A and T97F in the heavy chain variable region as shown in SEQ ID NO: 69, and / or N55V mutation in CDR; or nccLLn / Lznz / e / YiAi (v) a variant, comprising one or more amino acid reverse mutations selected from the group consisting of R38K, M48I, R67K, V68A, R72A, T74K, M81L, L83F and D89E in the heavy chain variable region as shown in SEQ ID NO: 75. In alternative embodiments, the humanized anti-IL-5 antibody in the pharmaceutical composition comprises: a variable heavy chain region as shown in SEQ ID NO: 50 or 51; or a variable heavy chain region as shown in SEQ ID NO: 58 or 59; or a variable heavy chain region selected from any of SEQ ID NO: 64, 65 and 66; or a variable heavy chain region as shown in SEQ ID NO: 70 or 71; or a variable heavy chain region as shown in any selected from the group consisting of: SEQ ID NO: 76, 77, 78 and 79. In alternative embodiments, the humanized anti-IL-5 antibody in the pharmaceutical composition comprises a light chain variable region as shown in SEQ ID NO: 46, 54, 60, 67 or 72, or variants thereof; the variant comprises reverse mutations of 1 to 10 amino acids in the light chain variable region as shown in SEQ ID NO: 46, 54, 60, 67 or 72. In alternative modalities, where the variant is a variant as shown in any selected one from the group consisting of: (i) a variant, comprising one or more reverse mutations of amino acids selected from the group consisting of A43S, L47V, G66R, T69S, F71Y and Y87F in the light chain variable region as shown in SEQ ID NO: 46; (ii) a variant, comprising one or more reverse mutations of amino acids selected from the group consisting of A43S, L47M, F71Y and Y87F in the light chain variable region as shown in SEQ ID NO: 54; (iii) a variant, comprising a mutation or reverse mutations of amino acids selected from the group consisting of E1 D, I2T, I57V, V84T and Y86F in the variable region of the light chain as shown in SEQ ID NO: 60, or a combination thereof; (iv) a variant, comprising one or more amino acid reverse mutations selected from the group consisting of M4L, A42S, L45P and L46W in the light chain variable region as shown in SEQ ID NO: 67; and (v) a variant, comprising one or more amino acid reverse mutations selected from the group consisting of A43S, I48V and F71Y in the light chain variable region as shown in SEQ ID NO: 72. In alternative embodiments, the humanized anti-IL-5 antibody in the pharmaceutical composition comprises: a variable light chain region as shown in SEQ ID NO: 47 or 48; or nccLLn / Lznz / e / YiAi a variable light chain region as shown in SEQ ID NO: 55 or 56; or a variable light chain region as shown in SEQ ID NO: 61 or 62; or a variable light chain region as shown in SEQ ID NO: 68; or a variable light chain region as shown in SEQ ID NO: 73 or 74. In alternative embodiments, the humanized anti-IL-5 antibody in the pharmaceutical composition comprises: (i) a heavy chain variable region as shown in any of SEQ ID NO: 49, 50 and 51 or having 95% sequence identity with any of SEQ ID NO: 49, 50 and 51; and a light chain variable region as shown in any of SEQ ID NO: 46, 47 and 48 or having 95% sequence identity with any of SEQ ID NO: 46, 47 and 48; (ii) a heavy-chain variable region as shown in any of SEQ ID NO: 57, 58 and 59 or having a 95% sequence identity with any of SEQ ID NO: 57, 58 and 59; and a light-chain variable region as shown in any of SEQ ID NO: 54, 55 and 56 or having a 95% sequence identity with any of SEQ ID NO: 54, 55 and 56; (iii) a heavy chain variable region as shown in any of SEQ ID NO: 63, 64, 65 and 66 or having 95% sequence identity with any of SEQ ID NO: 63, 64, 65 and 66; and a light chain variable region as shown in any of SEQ ID NO: 60, 61 and 62 or having 95% sequence identity with any of SEQ ID NO: 60, 61 and 62; (iv) a heavy-chain variable region as shown in any of SEQ IDs NO: 69, 70 and 71 or having 95% sequence identity with any of SEQ IDs NO: 69, 70 and 71; and a light-chain variable region as shown in any of SEQ IDs NO: 67 and 68 or having 95% sequence identity with any of SEQ IDs NO: 67 and 68; or (v) a heavy-chain variable region as shown in any of SEQ IDs NO: 75, 76, 77, 78 and 79 or having 95% sequence identity with any of SEQ IDs NO: 75, 76, 77, 78, and 79; and a variable light chain region as shown in any of SEQ IDs NO: 72, 73 and 74 or having 95% sequence identity with any of SEQ IDs NO: 72, 73 and 74; preferably, the humanized anti-IL-5 antibody comprises: (a) the heavy chain variable region as shown in SEQ ID NO: 51 and the light chain variable region as shown in SEQ ID NO: 47; nccLLn / Lznz / e / YiAi (b) the heavy chain variable region as shown in SEQ ID NO: 65 and the light chain variable region as shown in SEQ ID NO: 62; (c) the heavy chain variable region as shown in SEQ ID NO: 58 and the light chain variable region as shown in SEQ ID NO: 56; (d) the heavy chain variable region as shown in SEQ ID NO: 71 and the light chain variable region as shown in SEQ ID NO: 68; or (e) the heavy chain variable region as shown in SEQ ID NO: 79 and the light chain variable region as shown in SEQ ID NO: 73. The amino acid sequence having at least 95% sequence identity as described above, preferably having at least 95%, 96%, 97%, 98% or 99% sequence identity, and more preferably having 97%, 98% or 99% or above, and most preferably having at least 99% sequence identity or more, the amino acid sequence having at least 95% sequence identity as described above comprises one or more deletions, insertions or substitutions of amino acids obtained by mutation. In alternative embodiments, the anti-IL-5 antibody in the pharmaceutical composition comprises a human antibody constant region, preferably a human antibody heavy chain constant region as shown in SEQ ID NO: 52, and a human antibody light chain constant region as shown in SEQ ID NO: 53. In alternative embodiments, the anti-IL-5 antibody in the pharmaceutical composition comprises: (i) a heavy string as shown in SEQ ID NO: 83 and a light string as shown in SEQ ID NO: 84; (ii) a heavy string as shown in SEQ ID NO: 85 and a light string as shown in SEQ ID NO: 86; (iii) a heavy string as shown in SEQ ID NO: 87 and a light string as shown in SEQ ID NO: 88; (iv) a heavy chain as shown in SEQ ID NO: 89 and a light chain as shown in SEQ ID NO: 90; or (v) a heavy chain as shown in SEQ ID NO: 91 and a light chain as shown in SEQ ID NO: 92. In alternative embodiments, the anti-IL-5 antibody in the pharmaceutical composition is a monoclonal antibody or an antigen-binding fragment thereof that competes for IL-5 binding with the anti-IL-5 antibody or its antigen-binding fragment as described above. In a preferred embodiment, the antigen-binding fragment in the pharmaceutical composition of the present invention is selected from the group consisting of Fab, Fab', F(ab')2, nccLLn / Lznz / e / YiAi single-stranded antibody (scFv), dimerized V region (diabody), and disulfide-stabilized V region (dsFv). The present invention further provides a method for preparing the pharmaceutical composition as described above, comprising a step of replacing a stock solution of the anti-IL-5 antibody with a buffer. In alternative embodiments, the buffer is preferably an acetic acid-sodium acetate buffer. The pH of the buffer is from approximately 5.0 to approximately 6.5, preferably from approximately 5.2 to approximately 5.8. Non-limiting examples of the pH value of the buffer include approximately 5.0, approximately 5.1, approximately 5.2, approximately 5.3, approximately 5.4, approximately 5.5, approximately 5.6, and approximately 5.7.approximately 5.8, approximately 5.9, approximately 6.0, approximately 6.5, and most preferably about 5.5. In alternative embodiments, the buffer concentration in the pharmaceutical composition is approximately 10 mM to approximately 30 mM, preferably approximately 15 mM to approximately 30 mM, preferably approximately 20 mM to approximately 30 mM, preferably approximately 25 mM to approximately 30 mM, preferably approximately 5 mM to approximately 25 mM, preferably approximately 10 mM to approximately 25 mM, preferably approximately 15 mM to approximately 25 mM, preferably approximately 20 mM to approximately 25 mM, preferably approximately 5 mM to approximately 20 mM, preferably approximately 10 mM to approximately 15 mM; non-limiting examples of buffer concentration involve approximately 10 mM, approximately 12 mM, approximately 14 mM,approximately 16 mM, approximately 18 mM, approximately 20 mM, approximately 22 mM, approximately 24 mM, approximately 26 mM, approximately 28 mM, approximately 30 mM and most preferably approximately 30 mM. In some formulations, the pharmaceutical composition comprises: 100 mg / ml of anti-IL-5 antibody h1705-008, acetic acid-sodium acetate 10 mM, pH 5.5 and 0.2 mg / ml of polysorbate 80. In some formulations, the pharmaceutical composition comprises: 100 mg / ml of anti-IL-5 antibody h1705-008, acetic acid-sodium acetate 10 mM, pH 5.5 and 0.05 mg / ml of polysorbate 80. In some formulations, the pharmaceutical composition comprises: 100 mg / ml of anti IL 5 h 1705 008 antibody, succinic acid sodium succinate 10 mM, pH 5.0 and 0.2 mg / ml of polysorbate 80. nccLLn / Lznz / e / YiAi In some formulations, the pharmaceutical composition comprises: 100 mg / ml of anti-IL-5 antibody h1705-008, succinic acid-sodium succinate 10 mM, pH 5.5 and 0....2 mg / ml of polysorbate 80. In some formulations, the pharmaceutical composition comprises: 100 mg / ml of anti-IL-5 h antibody 1705-008, succinic acid-sodium succinate 10 mM, pH 6.0 and 0.2 mg / ml of polysorbate 80. In some formulations, the pharmaceutical composition comprises: 100 mg / ml of anti-IL-5 antibody h1705-008, succinic acid-sodium succinate 10 mM, pH 5.0 and 0.05 mg / ml of polysorbate 80. In some formulations, the pharmaceutical composition comprises: 100 mg / ml of anti-IL-5 antibody h1705-008, succinic acid-sodium succinate 10 mM, pH 5.5 and 0.05 mg / ml of polysorbate 80. In some formulations, the pharmaceutical composition comprises: 100 mg / ml of anti-IL-5 antibody h1705-008, succinic acid-sodium succinate 10 mM, pH 6.0 and 0.05 mg / ml of polysorbate 80. nccLLn / Lznz / e / YiAi In some forms, the composition is anti-IL-5 antibody h 1705-008, citric acid-citrate polysorbate 80. In some forms, the composition is anti-IL-5 antibody h 1705-008, citric acid-citrate polysorbate 80. In some forms, the composition is anti-IL-5 antibody h 1705-008, citric acid-citrate polysorbate 80. In some forms, the composition is anti-IL-5 antibody h 1705-008, citric acid-citrate polysorbate 80. In some forms, the composition is anti-IL-5 antibody h 1705-008, citric acid-citrate polysorbate 80. In some forms, the composition is anti-IL-5 antibody h 1705-008, citric acid-citrate polysorbate 80. In some forms, the composition is anti-IL-5 antibody h 1705-008, citric acid-citrate polysorbate 80. The pharmaceutical comprises: 100 mg / ml of sodium 10 mM, pH 6.5 and 0.2 mg / ml of the pharmaceutical comprises: 100 mg / ml of sodium 10 mM, pH 5.5 and 0.2 mg / ml of the pharmaceutical comprises: 100 mg / ml of sodium 10 mM, pH 6.0 and 0.2 mg / ml of the pharmaceutical comprises: 100 mg / ml of sodium 10 mM, pH 6.5 and 0.05 mg / ml of the pharmaceutical comprises: 100 mg / ml of sodium 10 mM, pH 5.5 and 0.05 mg / ml of the pharmaceutical comprises: 100 mg / ml of sodium 10 mM, pH 6.0 and 0.05 mg / ml of the pharmaceutical comprises: 100 mg / ml of sodium 10 mM, pH 6.5 and 0.2 mg / ml of In some formulations, the pharmaceutical composition comprises: 100 mg / ml of anti-IL-5 antibody h1705-008, citric acid-sodium citrate 10 mM, pH 5.5 and 0.2 mg / ml of polysorbate 80. In some formulations, the pharmaceutical composition comprises: 100 mg / ml of anti-IL-5 antibody h1705-008, histidine-hydrochloric acid 10 mM, pH 6.0 and 0.2 mg / ml of polysorbate 80. In some formulations, the pharmaceutical composition comprises: 100 mg / ml of anti-IL-5 antibody h1705-008, histidine-hydrochloric acid 10 mM, pH 6.5 and 0.05 mg / ml of polysorbate 80. In some formulations, the pharmaceutical composition comprises: 100 mg / ml of anti-IL-5 antibody h1705-008, histidine-hydrochloric acid 10 mM, pH 5.5 and 0.05 mg / ml of polysorbate 80. In some formulations, the pharmaceutical composition comprises: 100 mg / ml of anti-IL-5 antibody h1705-008, histidine-hydrochloric acid 10 mM, pH 6.0 and 0.05 mg / ml of polysorbate 80. In some formulations, the pharmaceutical composition comprises: 100 mg / ml of anti-IL-5 h antibody 1705-008, succinic acid-sodium succinate 10 mM, pH 5.0 and 0.1 mg / ml of polysorbate 20. In some formulations, the pharmaceutical composition comprises: 100 mg / ml of anti-IL-5 h antibody 1705-008, succinic acid-sodium succinate 10 mM, pH 5.0 and 0.1 mg / ml of polysorbate 80. In some formulations, the pharmaceutical composition comprises: 100 mg / ml of anti-IL-5 antibody h1705-008, succinic acid-sodium succinate 10 mM pH 5.0, 50 mg / ml of sucrose and 0.1 mg / ml of polysorbate 80. In some formulations, the pharmaceutical composition comprises: 100 mg / ml of anti-IL-5 antibody h1705-008, succinic acid-sodium succinate 10 mM pH 5.0, 50 mg / ml of trehalose and 0.1 mg / ml of polysorbate 80. In some formulations, the pharmaceutical composition comprises: 100 mg / ml of anti-IL-5 antibody h1705-008, succinic acid-sodium succinate 10 mM pH 5.0, 50 mg / ml of mannitol and 0.1 mg / ml of polysorbate 80. In some formulations, the pharmaceutical composition comprises: 100 mg / ml of anti-IL-5 antibody h1705-008, succinic acid-sodium succinate 10 mM pH 5.0, 50 mg / ml of sorbitol and 0.1 mg / ml of polysorbate 80. In some formulations, the pharmaceutical composition comprises: 100 mg / ml of anti-IL-5 antibody h1705-008, succinic acid-sodium succinate 10 mM pH 5.0, 8 mg / ml of glycine and 0.1 mg / ml of polysorbate 80. nccLLn / Lznz / e / YiAi In some formulations, the pharmaceutical composition comprises: 100 mg / ml of anti-IL-5 antibody h1705-008, succinic acid-sodium succinate 10 mM pH 5.0, 8 mg / ml of methionine and 0.1 mg / ml of polysorbate 80. In some formulations, the pharmaceutical composition comprises: 100 mg / ml of anti-IL-5 antibody h1705-008, succinic acid-sodium succinate 10 mM pH 5.0, 8 mg / ml of proline and 0.1 mg / ml of polysorbate 80. In some formulations, the pharmaceutical composition comprises: 100 mg / ml of anti-IL-5 antibody h1705-008, succinic acid-sodium succinate 10 mM pH 5.5, 70 mg / ml of sucrose and 0.4 mg / ml of polysorbate 80. In some formulations, the pharmaceutical composition comprises: 80 mg / ml of anti-IL-5 antibody h1705-008, acetic acid-sodium acetate 10 mM pH 5.8 and 0.2 mg / ml of polysorbate 80. In some formulations, the pharmaceutical composition comprises: 100 mg / ml of anti-IL-5 antibody h1705-008, acetic acid-sodium acetate 10 mM pH 5.4 and 0.6 mg / ml of polysorbate 80. In some formulations, the pharmaceutical composition comprises: 80 mg / ml of anti-IL-5 antibody h1705-008, acetic acid-sodium acetate 10 mM pH 5.4 and 0.4 mg / ml of polysorbate 80. In some formulations, the pharmaceutical composition comprises: 80 mg / ml of anti-IL-5 antibody h1705-008, acetic acid-sodium acetate 10 mM pH 5.0 and 0.2 mg / ml of polysorbate 80. In some formulations, the pharmaceutical composition comprises: 100 mg / ml of anti-IL-5 antibody h1705-008, acetic acid-sodium acetate 10 mM pH 5.4 and 0.2 mg / ml of polysorbate 80. In some formulations, the pharmaceutical composition comprises: 80 mg / ml of anti-IL-5 antibody h1705-008, acetic acid-sodium acetate 10 mM pH 5.8 and 0.6 mg / ml of polysorbate 80. In some formulations, the pharmaceutical composition comprises: 120 mg / ml of anti-IL-5 antibody h1705-008, acetic acid-sodium acetate 10 mM pH 5.0 and 0.2 mg / ml of polysorbate 80. In some formulations, the pharmaceutical composition comprises: 80 mg / ml of anti-IL-5 antibody h1705-008, acetic acid-sodium acetate 10 mM pH 5.0 and 0.6 mg / ml of polysorbate 80. In some formulations, the pharmaceutical composition comprises: 120 mg / ml of anti-IL-5 antibody h1705-008, acetic acid-sodium acetate 10 mM pH 5.8 and 0.6 mg / ml of polysorbate 80. nccLLn / Lznz / e / YiAi In some formulations, the pharmaceutical composition comprises: 120 mg / ml of anti-IL-5 antibody h1705-008, acetic acid-sodium acetate 10 mM pH 5.4 and 0.4 mg / ml of polysorbate 80. In some formulations, the pharmaceutical composition comprises: 100 mg / ml of anti-IL-5 antibody h1705-008, acetic acid-sodium acetate 10 mM pH 5.4 and 0.4 mg / ml of polysorbate 80. In some formulations, the pharmaceutical composition comprises: 120 mg / ml of anti-IL-5 antibody h1705-008, acetic acid-sodium acetate 10 mM pH 5.0 and 0.6 mg / ml of polysorbate 80. In some formulations, the pharmaceutical composition comprises: 120 mg / ml of anti-IL-5 antibody h1705-008, acetic acid-sodium acetate 10 mM pH 5.8 and 0.2 mg / ml of polysorbate 80. In some formulations, the pharmaceutical composition comprises: 100 mg / ml of anti-IL-5 antibody h1705-008, acetic acid-sodium acetate 10 mM pH 5.0 and 0.4 mg / ml of polysorbate 80. In some formulations, the pharmaceutical composition comprises: 100 mg / ml of anti-IL-5 antibody h1705-008, acetic acid-sodium acetate 10 mM pH 5.8 and 0.4 mg / ml of polysorbate 80. In some formulations, the pharmaceutical composition comprises: 100 mg / ml of anti-IL-5 antibody h1705-008, acetic acid-sodium acetate 10 mM pH 5.5, 70 mg / ml of sucrose and 0.4 mg / ml of polysorbate 80. In some formulations, the pharmaceutical composition comprises: 100 mg / ml of anti-IL-5 antibody h1705-008, acetic acid-sodium acetate 20 mM pH 5.5, 70 mg / ml of sucrose and 0.4 mg / ml of polysorbate 80. In some formulations, the pharmaceutical composition comprises: 100 mg / ml of anti-IL-5 antibody h1705-008, acetic acid-sodium acetate 30 mM pH 5.5, 70 mg / ml of sucrose and 0.4 mg / ml of polysorbate 80. In some formulations, the pharmaceutical composition comprises: 100 mg / ml of anti-IL-5 antibody h1705-008, acetic acid-sodium acetate 30 mM pH 5.5, 73 mg / ml of sucrose and 0.4 mg / ml of polysorbate 80. In some formulations, the pharmaceutical composition comprises: 100 mg / ml of anti-IL-5 antibody h1705-008, acetic acid-sodium acetate 30 mM pH 5.5, 75 mg / ml of sucrose and 0.4 mg / ml of polysorbate 80. In some embodiments, the pharmaceutical composition of the present invention is stable at 2-8°C for at least 3 months, at least 6 months, at least 12 months, at least 18 months, or at least 24 months. The pharmaceutical composition may be stable at 25°C for at least 3 months or at least 6 months. nccLLn / Lznz / e / YiAi The present invention further provides a method for preparing a lyophilized formulation comprising an anti-IL-5 antibody, comprising a lyophilization step of the pharmaceutical composition as described above. In an alternative embodiment, lyophilization in the method for preparing the lyophilized formulation comprising an anti-IL-5 antibody comprises the successive steps of pre-freezing, primary drying, and secondary drying. Lyophilization is carried out by freezing the formulation and subsequently sublimating the water at a temperature suitable for primary drying. Under such conditions, the product temperature is lower than the eutectic point or decomposition temperature of the formulation. Under suitable pressure, typically in the range of approximately 50 to 250 mTorr, the storage temperature for primary drying is usually approximately -30 to 25 °C (assuming the product remains frozen during primary drying).The formulation, the size and type of sample container (e.g., a glass vial), and the volume of liquid determine the required drying time, which can range from several hours to several days (e.g., 40 to 60 hours). Secondary drying can be performed between 0 and 40°C, depending primarily on the type and size of the container and the type of protein used. The duration of secondary drying is determined by the desired residual moisture level of the product and typically requires at least approximately 5 hours. Generally, the water content in the freeze-dried formulation prepared under low pressure is less than approximately 5%, preferably less than approximately 3%. The pressure can be the same as that applied in the primary drying stage; preferably, the pressure used in secondary drying is lower than that used in primary drying.The conditions for lyophilization may vary depending on the formulation and vial size. The present invention further provides a lyophilized formulation comprising an IL-5 antibody prepared by the method for preparing a lyophilized formulation comprising an anti-IL-5 antibody as described above. In some formulations, the lyophilized formulation is stable at 2-8°C for at least 3 months, at least 6 months, at least 12 months, at least 18 months, or at least 24 months. In some formulations, the lyophilized formulation is stable at 40°C for at least 7 days, at least 14 days, or at least 28 days. The present invention further provides a method for preparing a reconstituted solution of the lyophilized formulation comprising an anti-IL-5 antibody, wherein it comprises a reconstitution step of the lyophilized formulation as described above, and the solution used for reconstitution comprises, but is not limited to, water for injection, normal saline solution, or glucose solution. The present invention further provides a reconstituted solution of the lyophilized formulation comprising an IL-5 antibody prepared by the method for preparing a reconstituted lyophilized formulation comprising an anti-IL-5 antibody as described above. The present invention further provides an article or kit comprising a container or containers comprising any of the stable pharmaceutical compositions herein. In some embodiments, the container is an injection vial made of neutral borosilicate glass. The present invention further provides an article comprising a container or containers comprising the pharmaceutical composition or the lyophilized formulation or the reconstituted solution of the lyophilized formulation as described above. The present invention further provides a method for treating IL-5-mediated diseases, comprising administering a therapeutically effective amount of the pharmaceutical composition or lyophilized formulation or reconstituted solution or article of manufacture as described above, to a subject in need thereof;where IL-5-mediated disease is preferentially selected from the group consisting of asthma, chronic pneumonia, allergic rhinitis, allergic bronchopulmonary aspergillosis, eosinophilia, Churg-Strauss syndrome, atopic dermatitis, onchocerciasis dermatitis, intermittent angioedema, eosinophilic myalgia syndrome, eosinophilic gastroenteritis, worm infection, Hodgkin's disease, nasal polyps, Loeffler's syndrome, urticaria, hypereosinophilic bronchitis, nodular arteritis, sinusitis, eosinophilic esophagitis, allergic eosinophilic esophagitis, allergic conjunctivitis, onchocerciasis dermatitis, endometriosis, and steroid-dependent bronchitis. The present invention further provides for the use of the pharmaceutical composition or the lyophilized formulation or the reconstituted solution of the lyophilized formulation or the article of manufacture as described above in the preparation of a medicament for treating IL-5-mediated diseases; where IL-5-mediated disease is preferentially selected from the group consisting of asthma, chronic pneumonia, allergic rhinitis, allergic bronchopulmonary aspergillosis disease, eosinophilia, Churg-Strauss syndrome, atopic dermatitis, onchocerciasis dermatitis, intermittent angioedema, eosinophilic myalgia syndrome, eosinophilic gastroenteritis, worm infection, Hodgkin's disease, nasal polyps, Loeffler's syndrome, urticaria, hypereosinophilic bronchitis, nodular arteritis, sinusitis, eosinophilic esophagitis, allergic eosinophilic esophagitis, allergic conjunctivitis, onchocerciasis dermatitis, endometriosis, and steroid-dependent bronchitis.The present invention further provides the pharmaceutical composition or the lyophilized formulation or the reconstituted solution of the lyophilized formulation or the article of manufacture as described above, for use as a therapeutic drug, wherein the drug is for treating IL-5-mediated diseases.; where IL 5-mediated disease is preferentially selected from the group consisting of asthma, chronic pneumonia, allergic rhinitis, allergic bronchopulmonary aspergillosis disease, eosinophilia, Churg-Strauss syndrome, atopic dermatitis, onchocerciasis dermatitis, intermittent angioedema, eosinophilic myalgia syndrome, eosinophilic gastroenteritis, worm infection, Hodgkin's disease, nasal polyps, Loeffler's syndrome, urticaria, hypereosinophilic bronchitis, nodular arteritis, sinusitis, eosinophilic esophagitis, allergic eosinophilic esophagitis, allergic conjunctivitis, onchocerciasis dermatitis, endometriosis, and steroid-dependent bronchitis. As is well known to those skilled in the art, one, some, or all of the features of each embodiment of the present invention may be further combined to form other embodiments of the present invention. The embodiments of the present invention described above and the additional embodiments obtained by combination are further illustrated by the detailed description below. Brief Description of the Figures Figure 1 represents the results of FACS experiments in which anti-IL-5 antibodies block the binding of IL-5 to the IL-5 receptor; Figure 2 represents the result of detecting the binding specificity of the anti-IL-5 antibody for the Th2 cytokine; Figure 3 shows that the anti-IL-5 antibody increases the level of intermittent breathing (Penh). G1: normal control group (PBS); G2: model group (IgG); G3: h1705-008 antibody 10mpk group; G4: h1705-008 antibody 2mpk group; G5: h1706-009 antibody 10mpk group; G6: h1706-009 antibody 2mpk group; G7: Hu39D10 10mpk group; where, *p <0.05, **<0.01 (compared to group G2, by ANOVA / Bonferroni); Figure 4A represents the BALF eosinophil level in the lungs of asthmatic mice; Figure 4B represents the tracheal mucosal thickness score of asthmatic mice. G1: normal control group; G2: model group; G3: h1705-008 antibody 10mpk group; G4: h1705-008 antibody 2mpk group; G5: h1706009 antibody 10mpk group; G6: h1706-009 antibody 2mpk group; G7: Hu39D10 10mpk group; Figure 4C represents the percentage of BALF eosinophils in the lungs of asthmatic mice; Figure 5A and Figure 5B represent the ability of the monoclonal antibody IL5 to reduce the level of eosinophils in BALF. Detailed Description of the Invention Terms To facilitate understanding of the present invention, certain technical and scientific terms are specifically defined below. All other technical and scientific terms used herein have the meaning commonly understood by a person skilled in the art to which the present invention pertains, unless explicitly defined otherwise herein. nccLLn / Lznz / e / YiAi A buffer is a substance that resists changes in pH due to the action of its conjugate acid-base components. Examples of buffers that control pH within an appropriate range include acetate, succinate, gluconate, histidine salt, oxalate, lactate, phosphate, citrate, tartrate, fumarate, glycylglycine, and other organic acid buffers. Histidine salt buffer is a buffer comprising histidine ions. Examples of histidine salt buffer include histidine hydrochloride, histidine acetate, histidine phosphate, histidine sulfate buffer, and the like; preferably, histidine acetate buffer or histidine hydrochloride buffer. Histidine acetate buffer is prepared with histidine and acetic acid, and histidine salt buffer is prepared with histidine and HCl. Citrate buffer is a buffer comprising citrate ions. Examples of citrate buffers include citric acid-sodium citrate, citric acid-potassium citrate, citric acid-calcium citrate, citric acid-magnesium citrate, and similar compounds. A preferred citrate buffer is citric acid-sodium citrate. A succinate buffer is a buffer comprising succinate ions. Examples of succinate buffers include succinic acid-sodium succinate, succinic acid-potassium succinate, succinic acid-calcium succinate, and similar compounds. A preferred succinate buffer is succinic acid-sodium succinate. A phosphate buffer is a buffer comprising phosphate ions. Examples of phosphate buffers include disodium hydrogen phosphate-sodium dihydrogen phosphate, disodium hydrogen phosphate-potassium dihydrogen phosphate, disodium hydrogen phosphate-citric acid, and similar buffers. A preferred phosphate buffer is disodium hydrogen phosphate-sodium dihydrogen phosphate. An acetate buffer is a buffer comprising acetate ions. Examples of acetate buffers include acetic acid-sodium acetate, histidine acetate, acetic acid-potassium acetate, acetic acid-calcium acetate, acetic acid-magnesium acetate, and similar compounds. A preferred acetate buffer is acetic acid-sodium acetate. Pharmaceutical composition means a mixture comprising one or more of the compounds (or their physiologically / pharmaceutically acceptable salt or prodrug) described herein and other chemical components (such as physiologically / pharmaceutically acceptable vehicles and excipients). The purpose of a pharmaceutical composition is to maintain the stability of the active ingredients of the antibodies and to facilitate their administration to the target organism, thereby facilitating the absorption and biological activity of the active ingredient. As used in this document, pharmaceutical composition and formulation are used interchangeably. The saccharide in the present invention includes (CH2O)n and its derivatives, including monosaccharides, disaccharides, trisaccharides, polysaccharides, sugar alcohols, reducing saccharides, non-reducing saccharides, etc. The saccharide may be selected from the group consisting of glucose, sucrose, trehalose, lactose, fructose, maltose, dextran, glycerol, erythritol, arabitol, xylitol, sorbitol, mannitol, melibiose, melezitose, melitriose, mannotriose, stachyose, maltose, lactulose, sorbitol, isomaltulose, etc. The preferred saccharide is a non-reducing disaccharide, most preferably sucrose. According to the present invention, the solvent comprising the solution form of the pharmaceutical composition is water, unless otherwise specified. Lyophilized formulation means a pharmaceutical formulation or composition obtained by vacuum lyophilization of the liquid or solution form of the pharmaceutical composition or formulation. The freeze-drying process in the present invention comprises pre-freezing, primary drying, and secondary drying. The objective of pre-freezing is to freeze the products to obtain crystalline solids. The pre-freezing temperature and pre-freezing rate are two important process parameters. In the present invention, the pre-freezing temperature is set at -45°C, with the pre-freezing rate at 1°C / min. Primary drying, also called main drying, is the main stage for freeze-drying samples. Its purpose is to remove ice from the product while maintaining its shape, thus minimizing damage. If the main drying temperature and vacuum level are not selected correctly, the product will collapse. A higher temperature and a higher vacuum level accelerate the freeze-drying process but also increase the risk of product collapse.The primary drying temperature in the present invention can be a conventional field temperature, such as -30°C to 0°C. Secondary drying, also called vacuum drying, is the main step that removes bound water from a product by pumping in a final vacuum (0.01 mbar) and raising the temperature (20 to 40°C). Since most biological products are temperature-sensitive, the selected secondary drying temperature should be at the lower end of the temperature range, which is 25°C. The freeze-drying time depends on the freezer, the dosage of the formulation to be freeze-dried, and the container holding the formulation. Those skilled in the art are well aware of how to adjust this time. As used in this document, the terms "approximately" and "roughly" mean that a value is within an acceptable range of error of the specified value as measured by a person skilled in the art. The value depends in part on how the value is measured or determined (i.e., the limits of the measuring system). For example, in all practices of the art, "approximately" means a standard deviation within 1 or more. Alternatively, "approximately" or "substantially" means a range of at most ±20%, e.g., a pH of approximately 5.5 means a pH of 5.5 ± 1.1. Furthermore, particularly for biological systems or processes, the term means at most an order of magnitude or at most 5 times a value.Unless otherwise specified, where the specific value is stated in this application and in the claims, the meaning of nccLLn / Lznz / e / YiAi approximately or substantially comprising must be within an acceptable range of error of the specific value. The pharmaceutical composition of the present invention is capable of achieving a stable effect; that is, the antibody comprising the pharmaceutical composition substantially retains its physical and / or chemical stability and / or biological activity after storage. Preferably, the pharmaceutical composition substantially retains its physical and chemical stability as well as its biological activity after storage. The storage period is generally determined based on the predetermined shelf life of the pharmaceutical composition. Currently, several analytical techniques exist for measuring the stability of a protein, which can be used to measure stability after storage for a selected period of time at a selected temperature. A stable pharmaceutical antibody formulation is one for which no significant physical, chemical, and / or biological changes are observed under the following conditions: storage at a cool temperature (2–8°C) for at least 3 months, preferably 6 months, more preferably 1 year, and even more preferably up to 2 years. Additionally, stable liquid formulations include those that exhibit desirable characteristics after being stored at 25°C for 1 month, 3 months, or 6 months.Typically, the criteria for a stable formulation are as follows: normally no more than approximately 10%, preferably no more than approximately 5% of the antibody monomers degrade, as measured by SEC-HPLC; by visual inspection, the pharmaceutical formulation of the antibody is a clear, light yellow, almost colorless, or colorless liquid, or from clear to slightly pale; no more than ±10% variation occurs in the concentration, pH, and osmolality of the formulation; generally no more than approximately 10%, preferably no more than approximately 5% reduction is observed; generally no more than approximately 10%, preferably no more than approximately 5% aggregation forms. An antibody is considered to retain its physical stability in the pharmaceutical formulation when it does not exhibit a significant increase in aggregation, precipitation, and / or denaturation, as determined by visual inspection of color and / or clarity, or by measurement using ultraviolet light spectroscopy, light scattering, size exclusion chromatography (SEC), and dynamic light scattering (DLS). Changes in protein conformation can be assessed using fluorescence spectroscopy, which determines a protein's tertiary structure, and FTIR spectroscopy, which determines a protein's secondary structure. An antibody is considered to retain its chemical stability in a pharmaceutical formulation when it does not exhibit significant chemical modification. Chemical stability can be assessed by detecting and quantifying chemically altered forms of a protein. Degradation processes that frequently alter a protein's chemical structure include hydrolysis or truncation (assessed by methods such as size exclusion chromatography and SDS-PAGE), oxidation (assessed by methods such as peptide spectroscopy in combination with mass spectrometry or MALDI / TOF / MS), deamidation (assessed by methods such as ion-exchange chromatography, capillary isoelectric focusing, peptide spectroscopy, and isoaspartic acid measurement), and isomerization (assessed by methods such as isoaspartic acid content measurement and peptide spectroscopy). An antibody is considered to retain its biological activity in the pharmaceutical formulation when its biological activity at a given time is still within the predetermined range of biological activity exhibited when the pharmaceutical formulation was initially prepared. The antibody's biological activity can be determined, for example, by an antigen-binding assay. The three-letter code and the one-letter code for the amino acids used in the present invention are described in J. bioL chem. 243, p. 3558 (1968). The antibody used in the present invention refers to immunoglobulin; a complete antibody is a tetrapeptide chain structure composed of two identical heavy chains and two identical light chains connected by a disulfide bond between chains. In the present invention, the light chain of the antibody of the present invention further comprises a light chain constant region, and the light chain constant region includes the human or murine κ, λ chain or variant(s) thereof. In the present invention, the antibody heavy chain of the present invention further comprises a heavy chain constant region, and the heavy chain constant region includes human or murine IgG1, lgG2, lgG3, lgG4 or variants thereof. The approximately 110 amino acids adjacent to the N-terminus of the antibody's heavy and light chains are highly variable, known as variable regions (Fv regions); the remaining amino acid sequences near the C-terminus are relatively stable, known as constant regions. The variable region includes three hypervariable regions (HVRs) and four relatively conservative frame regions (FRs). The three hypervariable regions that determine antibody specificity are also known as complementarity-determining regions (CDRs). Each of the light-chain variable regions (LCVR, VL) and the heavy-chain variable region (HCVR, VH) consists of three CDRs and four FRs, with the sequential order from amino terminus to carboxyl terminus being FR1, CDR1, FR2, CDR2, FR3, CDR3, and FR4.The three CDR regions of the light chain are referred to as LCDR1, LCDR2, and LCDR3, and the three CDR regions of the heavy chain are referred to as HCDR1, HCDR2, and HCDR3. The number and position of the amino acid residues nccLLn / Lznz / e / YiAi. The CDRs of the LCVR region and the HCVR region in the antibody or the antigen-binding fragment thereof described in the present invention comply with the known Kabat numbering criteria (LCDR 1 to 3, HCDR 1 to 3). The antibodies of the present invention include murine antibodies, chimeric antibodies, humanized antibodies, and preferably humanized antibodies. In the present invention, the antigen-binding fragment of an antibody, or functional fragment, refers to Fab fragments, Fab' fragments, and F(ab')2 fragments, which have antigen-binding activity, and Fv fragments and scFv fragments, which bind to the antibody. The Fv fragment comprises a heavy-chain variable region and a light-chain variable region of the antibody but lacks a constant region, and the Fv fragment is the smallest antibody fragment that contains all the antigen-binding sites. Generally, the Fv antibody also comprises a polypeptide linker between the VH and VL domains and is capable of forming a structure required for antigen binding. Different linkers can also be used to connect two antibody variable regions to form a polypeptide chain, referred to as a single-stranded antibody or single-stranded Fv (sFv). The term antigen-binding site of the present invention refers to a continuous or discontinuous three-dimensional spatial site on an antigen recognized by the antibody or antigen-binding fragment thereof of the present invention. The term murine antibody in the present invention refers to a monoclonal antibody against human IL-5 prepared according to current knowledge and skill. During preparation, the IL-5 antigen is injected into the test subject, and the antibody expressing the hybridoma with the desired sequence or functional characteristic is then isolated. A chimeric antibody is an antibody formed by fusing the variable region of a murine antibody with the constant region of a human antibody, thereby reducing the immune response induced by the murine antibody. To establish a chimeric antibody, a hybridoma secreting specific murine monoclonal antibodies must first be established. Then, the variable region genes are cloned from mouse hybridoma cells, and the constant region genes from human antibodies are cloned as needed. The murine variable region genes are combined with the human constant region genes to form a chimeric gene, which is then inserted into a human vector. Finally, the chimeric antibody molecule is expressed in either a eukaryotic or prokaryotic industrial system.In a preferred embodiment of the present invention, the light chain of the chimeric IL-5 antibody further comprises the constant region of the human κ, λ light chain or variant(s) thereof. The heavy chain of the chimeric IL-5 antibody further comprises the constant region of the heavy chain of human IgG1, IgG2, IgG3, IgG4 or variants thereof. The constant region of the human antibody may be selected from the group consisting of: the nccLLn / Lznz / e / YiAi heavy chain constant region of human IgG1, IgG2, IgG3 or IgG4 or variant(s), preferably comprising the heavy chain constant region of human IgG2 or IgG4, or IgG4 without ADCC (antibody-dependent cell-mediated cytotoxicity) toxicity following amino acid mutation. The term humanized antibody, also known as a CDR-grafted antibody, refers to an antibody generated by grafting murine CDR sequences onto the human antibody variable region framework—that is, an antibody produced using different types of human germline antibody framework sequences. The humanized antibody avoids the strong, heterogeneous responses induced by a chimeric antibody carrying a large number of murine protein components. Such framework sequences can be obtained from a public DNA database covering germline antibody gene sequences or from published references. For example, germline DNA sequences of the human light and heavy chain variable region genes can be found in the VBase human germline sequence database (available at www.mrccpe.com.ac.uk / vbase), as well as in Kabat, EA, et al.1991 Protein Sequences of Immunological Interest, 5th ed. To avoid a decrease in activity caused by a decrease in immunogenicity, the framework sequences in the variable region of the human antibody can undergo a minimal reverse mutation or retro-mutation to maintain activity. The humanized antibody of the present invention also refers to a humanized antibody in which the affinity maturation of the CDRs is carried out by phage presentation. In the present invention, ADCC (i.e., antibody-dependent cell-mediated cytotoxicity) means that antibody-coated target cells are killed directly by cells expressing Fe receptors through recognition of the Fe segment of the antibody. The ADCC effector function of the antibody can be reduced or eliminated by modifying the Fe segment of IgG. The modification refers to mutations made in the constant region of the heavy chain of an antibody, as selected from the group consisting of N297A, L234A, and L235A in IgG1; the chimeric IgG2 / 4 mutation; and the F234A / L235A mutation in IgG4. The mutation in a mutating sequence in the present invention includes, but is not limited to, reverse mutation, conservative modification, or conservative replacement or substitution. The conservative modification or conservative substitution used in the present invention refers to other amino acids with similar characteristics (such as charge, side chain size, hydrophobicity / hydrophilicity, backbone conformation, and stiffness, etc.) to replace amino acids in a protein, so that the replacement can be carried out frequently without changing the biological activity of a protein. Those skilled in the art know that, generally, the substitution of a single amino acid in a non-essential region of a polypeptide does not substantially change the biological activity (see, for example, Watson et al., (1987) Molecular Biology of the Gene, The Benjamin / Cummings Pub. Co., page 224, (the fourth edition)).Furthermore, substituting amino acids with similar structures or functions is unlikely to alter biological activity. The mutated sequence in the present invention refers to the fact that the nucleotide sequence and / or amino acid sequence of the present invention is appropriately modified by mutation(s) (such as substitution, insertion, or deletion) to obtain a nucleotide sequence and / or amino acid sequence that has a different percentage of sequence identity with the nucleotide sequence and / or amino acid sequence of the present invention. In the present invention, the sequence identity may be at least 85%, 90%, or 95%, preferably at least 95%. Non-limiting examples include 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100%. Sequence alignment and determination of the percentage of identity between two sequences can be performed using the default configuration of the BLASTN / BLASTP algorithm available on the National Center for Biotechnology Institute website. The term IL-5 binding refers to interaction with IL-5, preferably with human IL-5. The terms anti-IL-5 antibody and IL-5 antibody are used interchangeably, and both refer to an antibody that binds to IL-5. In the present invention, the fusion protein is a protein product obtained by co-expressing two genes through DNA recombination. The recombinant IL-5-Fc extracellular region fusion protein is a fusion protein obtained by co-expressing the IL-5 extracellular region and the Fe fragment of a human antibody through DNA recombination. The IL-5 extracellular region refers to the portion of the IL-5 protein expressed outside the cell membrane, and its sequence is as shown in SEQ ID NO: 1. Methods for producing and purifying antibodies and antigen-binding fragments are well known and available in the prior art, such as in Antibodies: A Laboratory Manual, Coid, Spring Harbor Press, Chapters 5-8 and 15. For example, mice can be immunized with human IL-5 or a fragment thereof, and the resulting antibody can be renaturated and purified, and amino acid sequencing can be performed using conventional methods. Antigen-binding fragments can also be prepared using conventional methods. The antibody or antigen-binding fragment according to the present invention is genetically modified to graft one or more human FR regions onto non-human CDR regions. Human FR germline sequences can be obtained from the ImMunoGeneTics (IMGT) website http: / / imgt.cines.fr, or from The Immunoglobulin Journal, 2001 ISBN 012441351. The modified antibody or its antigen-binding fragment can be prepared and purified using conventional methods. For example, cDNA sequences encoding the heavy and light chains can be cloned and recombined into an nccLLn / Lznz / e / YiAi GS expression vector. Recombinant immunoglobulin expression vectors can be stably transfected into CHO cells. As a previously recommended technique, mammalian expression systems can lead to antibody glycosylation, particularly at highly conservative N-terminal positions of the Fe region. Stable clones are obtained by expressing antibodies that bind specifically to human IL-5. Positive clones are expanded in a serum-free bioreactor culture medium to produce antibodies. The culture medium into which the antibodies are secreted can be purified using conventional techniques.For example, the Sepharose FF Protein A or Protein G column, which includes adjusted buffer, can be used for purification. Non-specifically bound components are removed by washing. The bound antibodies are then eluted using a pH gradient, and the antibody fragments are detected and collected by SDS-PAGE. The antibodies can be filtered and concentrated using conventional methods. Soluble mixtures and multimers can also be removed using conventional methods, such as molecular sieves and ion exchange. The resulting product is then immediately frozen, for example, at -70°C, or lyophilized. Optionally means that the event or environment following the term may occur, but does not have to, and the description implies instances where the event or environment would or would not occur. For example, optionally comprising 1 to 3 heavy chain CDR regions of an antibody means that the heavy chain CDR region or regions of an antibody with specific sequences may be present, but are not necessarily. Administering and treating, when applied to animals, humans, experimental subjects, cells, tissues, organs, or biological fluids, refers to the contact of an exogenous drug, therapeutic agent, diagnostic agent, or composition with animals, humans, subjects, cells, tissues, organs, or biological fluids. Administering and treating may refer, for example, to treatments, pharmacokinetics, diagnostics, research, and experimental methods. Cell treatment includes contact of the reagent with cells and contact of the reagent with fluids, where the fluids are in contact with the cells. Administering and treating, for example, also means the treatment of cells by means of reagents, diagnostic agents, binding compositions, or by means of another cell in vitro and ex vivo.When applied to humans, veterinarians, or research subjects, "to treat" refers to therapeutic treatments, prevention or prophylactic measures, research, and diagnostic applications. Treatment means applying an internal or external therapeutic agent, for example, a composition comprising any of the bonding compounds of the present invention, to a patient who has one or more disease symptoms in which the therapeutic agent is known to have a therapeutic effect. Generally, the therapeutic agent is administered in an effective amount to alleviate one or more disease symptoms in the treated patient or population, to induce the regression of such symptoms, or to inhibit the development of such symptoms to any clinically detectable degree. The amount of therapeutic agent that is effective in alleviating any specific disease symptom (also called the therapeutically effective amount) may vary depending on a variety of factors, for example, the patient's disease status, age, and body weight, and the agent's ability to produce the desired therapeutic effect in the patient.It can be assessed whether the symptoms of the disease have been relieved by any clinical testing method used by physicians or other healthcare professionals to evaluate the severity or progression of symptoms. Although an embodiment of the present invention (e.g., a treatment method or manufactured article) may not be effective in relieving every symptom of the target disease, it should relieve the symptom of the target disease in a statistically significant number of patients, as determined by any statistical test, methods known in the art, such as Student's t-test, chi-square test, Mann-Whitney U test, Kruskal-Wallis test (H-test), Jonckheere-Terpstra test, and Wilcoxon test. There is no restriction for IL-5 related diseases, provided it is an IL-5 related disease. For example, the therapeutic response induced by the molecule of the present invention may occur by binding to human IL-5 and subsequently blocking or inhibiting the eosinophil-stimulatory effects.Therefore, when applied to preparations and formulations suitable for therapeutic application, the pharmaceutical composition of the present invention is very useful for those subjects suffering from allergies and / or atopic reactions, or who suffer from eosinophil-related reactions, such as, but not limited to, asthma, asthma exacerbation, malignant onset of asthma, chronic pneumonia, allergic rhinitis, perennial allergic rhinitis, allergic bronchopulmonary aspergillosis, eosinophilia, Churg-Strauss syndrome, atopic dermatitis, onchocerciasis, dermatitis, intermittent angioedema, eosinophilia syndrome, gastroenteritis, worm infection, Hodgkin's disease, nasal polyps, Loeffler's syndrome, urticaria, hypereosinophilic bronchitis, nodular arteritis, sinusitis, eosinophilic esophagitis, allergic eosinophilic esophagitis, allergic conjunctivitis, onchocerciasis dermatitis, endometriosis, or embosinophilic bronchitis preferred by steroids, etc.This treatment can inhibit or alleviate eosinophil infiltration into lung tissue. The frequency of administration of the pharmaceutical composition can range from three times a day to once every six months. The route of administration can be intravenous, subcutaneous, intramuscular, parenteral, or topical. The formulations of the present invention can be used to treat IL-5-mediated diseases. For example, the formulations can be used to, but are not limited to, inhibit or alleviate the IL-5-mediated inflammatory response and the maturation, activation, degranulation, or tissue infiltration of eosinophils in vivo and in vitro; inhibit excessive smooth muscle stress caused by IL-5; and reduce the level of IL-5 in the lungs, airways, or blood.Preferably, the formulation of the present invention can be used to treat IL-5 mediated diseases, preferably the IL-5 mediated disease being selected from the group consisting of asthma, chronic pneumonia, allergic rhinitis, allergic bronchopulmonary aspergillosis disease, eosinophilia, Churg-Strauss syndrome, atopic dermatitis, onchocerciasis dermatitis, intermittent angioedema, eosinophilic myalgia syndrome, eosinophilic gastroenteritis, worm infection, Hodgkin's disease, nasal polyps, Loeffler's syndrome, urticaria, hypereosinophilic bronchitis, nodular arteritis, sinusophagia, esophaginophilitis, eosinophilitis, conjunctivitis, onchocerciasis dermatitis, endometriosis, and steroid-dependent eosinophilic bronchitis. "Effective amount" includes a quantity sufficient to improve or prevent the symptoms or conditions of a medical disease. An effective amount also refers to a quantity sufficient to permit or facilitate diagnosis. The effective amount for a particular veterinary patient or subject may vary depending on the following factors: for example, the condition being treated, the patient's overall condition, the route of administration and dosage, and the severity of side effects. The effective amount may be a maximum dose or a dosing schedule that avoids significant side effects or toxic effects. Exchange refers to the replacement of the solvent system used to dissolve the antibody protein. For example, the hypertonic or high-salt solvent system comprising an antibody protein is replaced with a buffer system of a stable formulation through physical manipulation, so that the antibody protein is present in a stable formulation. Physical manipulation includes, but is not limited to, ultrafiltration, dialysis, or reconstitution after centrifugation. Examples and Test Examples The present invention is further described in conjunction with the following examples, but these examples do not limit the scope of the present invention. Experimental methods not provided under specific conditions in the examples of the present invention are usually in accordance with conventional conditions, such as those referenced in Antibodies: A Laboratory Manual, Molecular Cloning by Coid Spring Harbor Laboratory; or in accordance with the conditions recommended by the manufacturers of materials or products. Reagents not supplied from specific sources are conventional reagents purchased commercially. Example 1. Preparation of the IL-5 antigen and protein used in detection. 1.1 IL-5 antigen design and expression The sequences encoding human IL-5 tagged His, rhesus IL-5 tagged His, mouse IL-5 tagged His, rat IL-5 tagged His, and the human IL-5Ra receptor extracellular region fusion protein comprising the human lgG1-Fc fragment nccLLn / Lznz / e / YiAi were cloned into phr vectors, and expression plasmids were constructed and then transfected onto HEK293. On day 6 post-transfection, samples were collected, and the cell supernatant was collected by centrifugation at 4500 rpm for 10 min. The supernatants comprising the recombinant IL-5 and IL-5a receptor proteins were purified using a nickel column, and the recombinant human IL-5-Fc fusion protein was purified using a Protein A affinity chromatography column. The purified protein can be used in subsequent experiments. The sequences of the specific protein antigens are as follows: The amino acid sequence for human IL-5 with his(rhIL-5-his) tag MRMLLHLSLLALGAAYVYAIPTEIPTSALVKETLALLSTHRTLLIANETLRIPVPVHKNHQLCTEEIF QGIGTLESQTVQGGTVERLFKNLSLIKKYIDGQKKKCGEERRRVNQFLDYLQEFLGVMNTEWII ESHHHHHH SEQ ID NO: 1 Note: The italicized section represents the Hise tag The amino acid sequence for IL-5 cyno with the his tag. MRMLLHLSLLALGAAYVYAIPTEIPASALVKETLALLSTHRTLLIANETLRIPVPVHKNHQLCTEEI FQGIGTLESQTVQGGTVERLFKNLSLIKKYIGGQKKKCGEERRRVNQFLDYLQEFLGVMNTEWI \ESHHHHHH SEQ ID NO: 2 Note: The italicized section represents the Hise tag. The mouse IL-5 amino acid sequence tagged with His. MEIPMSTVVKETLTQLSAHRALLTSNETMRLPVPTHKNHQLCIGEIFQGLDILKNQTVRGGTVE MLFQNLSLIKKYIDRQKEKCGEERRRTRQFLDYLQEFLGVMSTEWAMEGHHHHH / - / SEQ ID NO: 3 Note: The italicized section represents the Hise tag. The amino acid sequence of rat IL-5 with Hise tag MEIPMSTVVKETLIQLSTHRALLTSNETMRLPVPTHKNHQLCIGEIFQGLDILKNQTVRGGTVEIL FQNLSLIKKYIDGQKEKCGEERRKTRHFLDYLQEFLGVMSTEWAMEV / - / / - / / - / / - / / - / H SEQ ID NO: 4 Note: The section and cursive representation of this style. The aminoacid secretion of the human IL-5a receptor fusionado del human Fe fragment. DLLPDEKISLLPPVNFTIKVTGLAQVLLQWKPNPDQEQRNVNLEYQVKINAPKEDDYETRITESK CVTILHKGFSASVRTILQNDHSLLASSWASAELHAPPGSPGTSIVNLTCTTNTTEDNYSRLRSYQ VSLHCTWLVGTDAPEDTQYFLYYRYGSWTEECQEYSKDTLGRNIACWFPRTFILSKGRDWLA VLVNGSSKHSAIRPFDQLFALHAIDQINPPLNVTAEIEGTRLSIQWEKPVSAFPIHCFDYEVKIHN TRNGYLQIEKLMTNAFISIIDDLSKYDVQVRAAVSSMCREAGLWSEWSQPIYVGNDEHKPLRE WIEG RMD EPKSCDKTH TCPPCPAPELLGGPS VFLFPPKPKDTLMISRTPEVTC VVVD VSHEDP nccLLn / Lznz / e / YiAi EVKFNWYVDG VE VHNAKTKPREEQYNSTYRVVS VL TVLHQDWLNGKEYKCKVSNKALPAPIE KTISKAKGQPREPQ VYTLPPSRDEL TKNQ VSL TCL VKGFYPSDIA VEWESNGQPENNYKTTPP VLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK SEQ ID NO. 5 Note: The italicized section represents the human lgG1-Fc label. Example 2. Construction and identification of recombinant IL-5a receptor and IL-5a / β receptor cell lines To select functional antibodies, the present invention constructed CHO-S / IL-5a cell lines that express IL-5a and CHO-S / IL-5a / IL-δβ cell lines that express both IL-5a and IL-δβ. Specifically, the full-length human IL-5α gene (Q01344) was cloned into a pTargeT mammalian cell expression vector. The linearized plasmid was electrotransfected into CHO-S cells and screened in the presence of G418 for 2 weeks, followed by two limited dilutions. The IL-5α gene was detected on the cell surface using FACS, and the CHO-S / IL-5α cell line with high IL-5α expression was selected. Based on this, the linearized ροϋΝΑ3.1-Iί-5β was electrotransfected and screened in the presence of G418 and zeocin for 2 weeks, followed by two limited dilutions. The IL-5a and IL-δβ genes were detected on the cell surface by FACS, and the CHO-S / IL-5a / IL-δβ cell line with the high level of IL-5a and IL-δβ expression was selected. Example 3. Preparation of murine anti-human IL-5 monoclonal antibody Two doses of recombinant rhlL-5-his protein, Freund's adjuvant CFA (Sigma, lot # SLBQ1109V), and IFA (Sigma, lot # SLBJ2845V) (100 µg / 50 µg / 50 µg (high) and 25 µg / 12.5 µg / 12.5 µg (low)) were used to immunize two groups of Balb / c mice (5 mice / group) and four groups of SJL mice (5 mice / group), respectively. The specific immune response to IL-5 was determined by detecting serum titers by ELISA, by ligand-receptor blockade assay, and by TF-1 proliferation inhibition assay. Mice with good specific immune responses were selected and sacrificed; spleen cells were collected and fused with myeloma cells. Primary screening was performed using an ELISA binding assay against human IL-5. Once hybridoma cells were transferred to a 24-well plate, the supernatants were again screened using the human, cynomolgus monkey, and mouse IL-5 binding ELISA assays, an IL-5 receptor-blockade ELISA, and a TF-1 proliferation inhibition assay. After positive clones underwent two rounds of subcloning, hybridoma clones were obtained and used for antibody production; the resulting antibodies were then purified by affinity chromatography. nccLLn / Lznz / e / YiAi The purified antibodies were subjected to SEC-HPLC, endotoxin content detection, Biacore affinity assay for various IL-5 species, FACS-based receptor blockade assay against IL-5, TF-1 proliferation inhibition assay, eosinophil adhesion assay, and efficacy assessment in a mouse model of asthma and an in vivo guinea pig neutralization model; the monoclonal hybridoma cell lines mAb1705, mAb1706, mAb1780, mAb1773, and mAb1779, which show favorable activity in vivo and in vitro, were selected. The procedure for cloning positive hybridoma sequences was as follows: hybridoma cells in logarithmic growth phase were collected, RNA was extracted with Trizol (Invitrogen, Cat. No. 15596-018) according to the kit instructions, and the PrimeScript™ Reverse Transcriptase kit (Takara, Cat. No. 2680A) was used for reverse transcription. The cDNA obtained by reverse transcription was amplified by PCR using a mouse Ig-Primer Set (Novagen, TB326 Rev. B0503) and then sequenced. The corresponding heavy chain amino acid sequences and light chain variable region DNA sequences were obtained for mAb1705, mAb1706, mAb1780, mAb1773, and mAb1779 (the amino acid residues of the VH / VL CDRs were determined and annotated according to Kabat's numbering criteria). The sequence of the variable region of the murine heavy chain of mAb1705 EVQLVESGGGLVQPGRSLKLSCTASGFTFSHYYMAWVRQAPKKGLEWVTSISYEGDITYYGD SVKGRFTISRDNAKSTLYLQMNSLRSEDTATYYCASQTLRESFDYWGQGVMVTVSS SEQ ID NO: 6 The sequence for the murine mAb1705 light chain variable region. DIQMTQSPSSMSVSLGDRVTITCRASQDIANYLSWYQQKIARSPKLVIYGTSNLEVGVPSRFSG SRSGSDYSLTINTLESEDTGIYFCLQDKEFPRTFGGGTRLELK SEQ ID NO:7 The sequence for the murine mAb1706 heavy chain variable region: EVQLVESGGGLVQPGRSLKLSCAASGFTFSHYYMAWVRQAPKKGLEWVTSINYEGNSAYYGD SVKGRFTISRDNAKSTLYLQMDSLRSEDTATYYCATETLRESLDYWGQGVMVTVSS SEQ ID NO: 8 The sequence for the murine mAb1706 light chain variable region. DIQMTQSPSSMSVSLGDRVTITCRASQDIGNYLSWYQQKLGKSPKLMIHSASNLEVGVPSRFS GSRSGSDYSLTINTLESEDPGIYFCLQHKQFPRTFGGGTKLELK SEQ ID NO: 9 The sequence for the murine heavy chain variable region mAb1780. QVKLLQSGAALVKPGDSVKMSCKASDYTFTEYLIHWVKQSQGRSLEWIGYINPYSGGTVYNEK FKSKALTVDKFSSTAYMEFRRLTFEDSAIYYCARDGGYSDPLDYWGQGVMVTVSS SEQ ID NO: 10 nccLLn / Lznz / e / YiAi The procedure for the variant region of the cadena ligera mAb1780 murina. DTVLTQSPALAVSPGERVSISCRASEGLTSYMHWYQQKPGQQPKLLIYKASNLASGVPARFSG SGSGTDFTLTIDPVEADDAATYFCQQNWNDPWTFGGGTKLELK SEQ ID NO: 11 La secuencia para la region variant de cadena pesada mAb1773 murina. EVQLQQSLAELVRPGASVTLSCTASGFNIKNTYIHWVKQRPEQGLEWIGRIDPANGDTKHGPK FQGKATITADTSSNTAYLQFSSLTSEDTAIYYCFRYGIYPDHWGQGTPLTVSS SEQ ID NO: 12 The procedure for the variant region of the cadena ligera mAb1773 murina. QIVLTQSPALMSASPGEKVTMTCSASSSVNYIYWYQQKPRSSPKPWIYLTATLASGVPARFSG SGSGTSFSLTISRMEAEDAATYYCQQWNSYPYTFGGGTKLEIE SEQ ID NO: 13 La secuencia para la region variant de cadena pesada mAb1779 murina. QVKLLQSGAALVKPGDSVKMSCKASGYTFTDYIIHWVKQSHGKSLEWIGYFNPNSGGSNYNE NFKRKATLTADKSSSTAYLEFSRVTSEDSAIYYCGRRIAWDHWYFDFWGPGTMVTVSS SEQ ID NO: 14 The sequence for the murine mAb1779 light chain variable region. DIQMTQSPASLSASLGETVSIECLASEGISNDVAWYQQKSGRSPQLLVYAASRLQDGVPSRFS GSGSGTRYFFKISGMQPEDEADYFCQQGYKTPLTFGSGTKLEIK SEQ ID NO: 15. The light and heavy chain CDR sequences for each antibody are shown in Table 1. nccLLn / Lznz / e / YiAi Table 1. The sequences of the CDR regions in the heavy chain and light chain of each antibody Anticuerpo Heavy Chain Light Chain mAb1705 HCDR1 HYYMA SEQ ID NO: 16 LCDR1 RASQDIANYLS SEQ ID NO: 19 HCDR2 SISYEGDITYYGDSVKG SEQ ID NO: 17 LCDR2 GTSNLEV SEQ ID NO: 20 HCDR3 QTLRESFDY SEQ ID NO: 18 LCDR3 LQDKEFPRT SEQ ID NO: 21 mAb1706 HCDR1 HYYMA SEQ ID NO: 22 LCDR1 RASQDIGNYLS SEQ ID NO: 25 HCDR2 SINYEGNSAYYGDSVKG SEQ ID NO: 23 LCDR2 SASNLEV SEQ ID NO: 26 HCDR3 ETLRESLDY SEQ ID NO: 24 LCDR3 LQHKQFPRT SEQ ID NO: 27 mAb1780 HCDR1 EYLIH SEQ ID NO: 28 LCDR1 RASEGLTSYMH SEQ ID NO: 31 HCDR2 YINPYSGGTVYNEKFKS SEQ ID NO: 29 LCDR2 KASNLAS SEQ ID NO: 32 HCDR3 DGGYSDPLDY SEQ ID NO: 30 LCDR3 QQNWNDPWT SEQ ID NO: 33 mAb1773 HCDR1 NTYIH SEQ ID NO: 34 LCDR1 SASSSVNYIY SEQ ID NO: 37 HCDR2 RIDPANGDTKHGPKFQG SEQ ID NO: 35 LCDR2 LTATLAS SEQ ID NO: 38 HCDR3 YGIYPDH SEQ ID NO: 36 LCDR3 QQWNSYPYT SEQ ID NO: 39 mAb1779 HCDR1 DYIIH SEQ ID NO: 40 LCDR1 LASEGISNDVA SEQ ID NO: 43 HCDR2 YFNPNSGGSNYNENFKR SEQ ID NO: 41 LCDR2 AASRLQD SEQ ID NO: 44 HCDR3 RIAWDHWYFDF SEQ ID NO: 42 LCDR3 QQGYKTPLT SEQ ID NO: 45 The result of the Biacore activity detection can be found in Table nccLLn / Lznz / e / YiAi 2. Table 2. In vitro activity of murine IL-5 antibody Antibody Affinity Hull-5 (KD (M)) mAb1705 7.27E-11 mAb1706 3.83E-11 mAb1780 8.99E-11 mAb1773 1.29E-10 mAb1779 4.58E-10 nccLLn / Lznz / e / YiAi The results show that the murine antibodies of the present invention have a high affinity for the antigen. Example 4. Purification of recombinant IL-5 related proteins and purification of hybridoma antibodies and recombinant antibodies 4.1 Purification steps of the recombinant IL-5-Flag-His protein: The samples were centrifuged at high speed to remove impurities and concentrated to an appropriate volume. The NI-NTA affinity column (QIAGEN, Cat No. 30721) was equilibrated with PBS and washed with 2–5 times the column volume. After removing impurities, the cell expression supernatant sample was loaded onto the column. The column was washed with PBS until the A280 reading returned to baseline. The column was washed with PBS to remove contaminating proteins, and the sample was collected. The target protein was successively eluted with wash buffer (20 mM imidazole) and elution buffer (300 mM imidazole), and the elution peaks were collected. The collected eluate was further purified by ion exchange (Hiload 16 / 600 superdex 200 column). The column was equilibrated with approximately two columns' worth of PBS to ensure a pH of 7.4. The elution buffer comprising the identified target protein was concentrated and loaded, the sample was collected and verified by SDS-PAGE and LC-MS, and divided into aliquots for use. 4.2 Purification of antibodies expressed by hybridoma and Fe fusion protein The cell expression supernatant sample was centrifuged at high speed to remove impurities. The hybridoma expression supernatant was purified using the Protein G column, and the Fe fusion protein expression supernatant was purified using the Protein A column. The column was washed with PBS until the A280 reading dropped to baseline. The target protein was eluted with 100 mM acetic acid, pH 3.0, and neutralized with 1 M Tris-HCl, pH 8.0. After the eluted sample was adequately concentrated, it was further purified by PBS-equilibrated gel chromatography (GE), and the aggregate-free peak was collected and then aliquoted for use. Example 5. Humanization design of a human anti-IL-5 monoclonal antibody The humanization of the murine anti-human IL-5 monoclonal antibody was carried out as described in many references on the technique. In summary, the constant regions of the murine antibody were replaced with human constant regions, and the murine antibody's CDRs were grafted onto the human FR template with the highest homology, and a back mutation was performed on the amino acids in the FR region. By aligning against the germline gene database of the human antibody IMGT light and heavy chain variable region, the heavy and light chain variable region germlines that have high identity with each of the amino acid sequences of mAb-1705, mAb-1706, mAb1780, mAb1773, and mAb1779 antibodies were selected as templates. The murine antibody CDRs were grafted onto the corresponding human template to form a variable region in the order FR1-CDR1 FR2-CDR2-FR3-CDR3-FR4. The amino acid residues were determined and annotated according to Kabat's numbering criteria. Selection of human FR regions and reverse mutation of amino acids. Based on the typical structure of the murine VH / VL CDR antibody obtained, homologous sequences of the light chain (VL) and heavy chain (VH) variable regions were retrieved from the human germline database and ranked according to FR homology (from highest to lowest); the germline with the highest FR homology was selected as the master template. The CDR regions of the murine antibody were grafted onto the human template, and then the FR residues were mutated and the amino acid residues optimized to obtain the final humanized molecules. 5.1 Selection of the humanized framework for the mAb1705 hybridoma clone For h1705, IGHV3-23*04 was selected as the template for VH, and IGKV1-12*01 was selected as the template for VL. The CDRs of mAb1705 were grafted onto the human template; embedded residues and residues that interacted directly with the CDR region (identified using software) were reverse mutated. Various variable light-chain and heavy-chain lines were obtained from the humanized antibodies, as shown in Table 3. nccLLn / Lznz / e / YiAi Table 3. Template selection and reverse mutation design for h1705 h1705_VL h1705_VH h1705_VL.1 Grafted h1705_VH.1 Grafted h1705_VL.1A A43S, G66R h1705_VH.1A K98S h1705_VL.1B A43S, L47V, G66R, T69S, F71Y,Y87F h1705 VH.1B S49T, V93T, K98S nccLLn / Lznz / e / YiAi Note: Grafting represents that the murine antibody CDRs were grafted into the FR region sequence of the human germline. For example, according to the natural numbering of the amino acid sequence, A43S represents that A at position 43 of grafted was mutated back to S. Table 4. Combination of light and heavy chain variable regions of the humanized antibody h1705 h1705_VH.1 h1705_VH.1A h1705_VH.1B h1705_VL. 1 h1705-003 h 1705-004 h1705-005 h1705_VL.1A h1705-006 h 1705-007 h1705-008 h1705_VL.1B hl705-009 h1705-010 h1705-011 Note: This table shows the sequences obtained by various combinations of mutations. As indicated by h1705-007, the humanized murine antibody h1705-007 comprises two mutants, namely the light chain h1705_VL.1 A and the heavy chain h1705_VH.1 A, and so on. The specific sequences of the variable regions of the humanized antibody h1705 are as follows: h1705_VL.1 (SEQ ID NO: 46) DIQMTQSPSSVSASVGDRVTITCRASQDIANYLSWYQQKPGKAPKLLIYGTSNLEVGVPSRFSG SGSGTDFTLTISSLQPEDFATYYCLQDKEFPRTFGGGTKVEIK h1705_VL.1A (SEQ ID NO: 47) DIQMTQSPSSVSASVGDRVTITCRASQDIANYLSWYQQKPGKSPKLLIYGTSNLEVGVPSRFSG SRSGTDFTLTISSLQPEDFATYYCLQDKEFPRTFGGGTKVEIK h1705_VL.1B (SEQ ID NO: 48) DIQMTQSPSSVSASVGDRVTITCRASQDIANYLSWYQQKPGKSPKLVIYGTSNLEVGVPSRFSG SRSGSDYTLTISSLQPEDFATYFCLQDKEFPRTFGGGTKVEIK h1705_VH.1 (SEQ ID NO: 49) EVQLVESGGGLVQPGGSLRLSCAASGFTFSHYYMAWVRQAPGKGLEVWSSISYEGDITYYGD SVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAKQTLRESFDYWGQGTLVTVSS h1705_VH.1A (SEQ ID NO: 50) EVQLVESGGGLVQPGGSLRLSCAASGFTFSHYYMAWVRQAPGKGLEWVSSISYEGDITYYGD SVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCASQTLRESFDYWGQGTLVTVSS h1705_VH.1B (SEQ ID NO: 51) EVQLVESGGGLVQPGGSLRLSCAASGFTFSHYYMAWVRQAPGKGLEWVTSISYEGDITYYGD SVKGRFTISRDNSKNTLYLQMNSLRAEDTATYYCASQTLRESFDYWGQGTLVTVSS. Each of the light chain variable regions described above combined with the light chain constant region to form a light chain sequence, and each of the heavy chain variable regions combined with the heavy chain constant region to form a heavy chain sequence. The sequences of the constant region of the exemplary humanized antibody are shown below: constant region of heavy chain lgG1: ASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYS LSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPP KPKDTLYITREPEVTCVWDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRWSVLTV LHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGF YPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHN HYTQKSLSLSPGK SEQ ID NO: 52 Note: the underlined part represents M252Y, S254T, T256E mutations. constant kappa region of light chain: RTVAA PS VFIF P PSD EQ LKSGTAS VVC LLN NF YP R EA KVQ WKVD NA LQSG N SQ ESVTEQ DS KD STYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC SEQ ID NO: 53. 5.2 Selection of the humanized frame for the mAb1706 hybridoma clone For h1706, IGHV3-23*04 was selected as the template for VH, and IGKV1 12*01 was selected as the template for VL. The CDRs of the murine antibody mAb1706 were grafted onto the selected humanized template; the FR amino acids were reverse-mutated. The light-chain and heavy-chain variable regions of the humanized antibodies were obtained, as shown in Table 5. nccLLn / Lznz / e / YiAi Table 5. Template selection and reverse mutation design for h1706 h1706_VL h1706_VH h1706_VL.1 Grafted h1706_VH.1 Grafted h1706_VL.1A A43S h1706_VH.1 A K98T h1706_VL.1B A43S, L47M, F71Y, Y87F h1706_VH.1B S49T, V93T, K98T nccLLn / Lznz / e / YiAi Note: Grafting represents that the murine antibody CDRs were grafted into the FR region of the human germline. For example, according to the natural numbering of the amino acid sequence, A43S represents that A at position 43 of grafted was mutated back to S. The engineered humanized molecules were combined to form different antibodies, as shown in the following table, as shown in Table 6. Table 6. Combination of light and heavy chain variable regions of the humanized antibody h1706 h1706_VH.1 h1706_VH.1A h1706_VH.1B h1706_VL1 h1706-002 h 1706-003 h 1706-004 h1706_VL.1A h1706-005 h1706-006 h 1706-007 h1706_VL.1B h1706-008 h1706-009 h 1706-010 The specific sequences of the variable regions of the humanized antibody h1706 are as follows: h1706_VL1 (SEQ ID NO: 54) DIQMTQSPSSVSASVGDRVTITCRASQDIGNYLSWYQQKPGKAPKLLIYSASNLEVGVPSRFSG SGSGTDFTLTISSLQPEDFATYYCLQHKQFPRTFGGGTKVEIK h1706_VL.1A (SEQ ID NO: 55) DIQMTQSPSSVSASVGDRVTITCRASQDIGNYLSWYQQKPGKSPKLLIYSASNLEVGVPSRFSG SGSGTDFTLTISSLQPEDFATYYCLQHKQFPRTFGGGTKVEIK h1706_VL.1 B (SEQ ID NO: 56) DIQMTQSPSSVSASVGDRVTITCRASQDIGNYLSWYQQKPGKSPKLMIYSASNLEVGVPSRFS GSGSGTDYTLTISSLQPEDFATYFCLQHKQFPRTFGGGTKVEIK h1706_VH.1 (SEQ ID NO: 57) EVQLVESGGGLVQPGGSLRLSCAASGFTFSHYYMAWVRQAPGKGLEWVSSINYEGNSAYYG DSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAKETLRESLDYWGQGTMVTVSS h1706_VH.1A (SEQ ID NO: 58) EVQLVESGGGLVQPGGSLRLSCAASGFTFSHYYMAWVRQAPGKGLEWVSSINYEGNSAYYG DSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCATETLRESLDYWGQGTMVTVSS h1706_VH.1B (SEQ ID NO: 59) EVQLVESGGGLVQPGGSLRLSCAASGFTFSHYYMAWVRQAPGKGLEWVTSINYEGNSAYYGD SVKGRFTISRDNSKNTLYLQMNSLRAEDTATYYCATETLRESLDYWGQGTMVTVSS. Each of the light-chain variable regions described above combined with the light-chain constant region to form a light-chain sequence. Each of the heavy-chain variable regions combined with the heavy-chain constant region to form a heavy-chain sequence. 5.3 Selection of the humanized frame for the mAb1780 hybridoma clone For h1780, IGHV1-2*02 was selected as the template for VH, and IGKV311*01 was selected as the template for VL. The CDRs of the murine antibody mAb1780 were grafted onto the selected humanized template; the FR amino acids were reverse-mutated. The light-chain and heavy-chain variable regions of the humanized antibodies were obtained, as shown in Table 7. nccLLn / Lznz / e / YiAi Table 7. Template selection and backmutation design for h1780 h1780_VL h1780_VH h1780_VL.1 Grafted h1780_VH.1 Grafted h1780_VL.1A E1D, I2T h1780_VH.1A M70L, R72V, T74K h1780_VL.1B E1D, I2T, I57V, V84T, Y86F h1780_VH.1B M48I, V68A, M70L, R72V, T74K, L83F h1780_VH.1C R38K, M48I, R67K, V68A, M70L, R72V, T74K, L83F Note: Grafting represents that the murine antibody CDRs were grafted into the FR region of the human germline. For example, according to the natural numbering of the amino acid sequence, E1D represents that E at position 1 of grafted was mutated back to D. The engineered humanized molecules were combined to form different molecules as shown in the following table, as shown in Table 8. Table 8. Combination of light and heavy chain variable regions of the humanized antibody h1780 h1780_VH.1 h1780_VH.1A h1780_VH.1B h1780_VH.1C h1780_VL1 h 1780-007 h 1780-008 h 1780-009 h1780-010 h1780_VL.1A h1780-011 h 1780-012 h1780-013 h1780-014 h1780_VL.1B h 1780-015 h 1780-016 h1780-017 h1780-018 nccLLn / Lznz / e / YiAi Laser secuencias específicas de las regions Variables de anticuerpo humanizado H1780 son las siguientes: h1780_VL.1 (SEQ ID NO: 60) EIVLTQSPATLSLSPGERATLSCRASEGLTSYMHWYQQKPGQAPRLLIYKASNLASGIPARFSG SGSGTDFTLTISSLEPEDFAVYYCQQNWNDPWTFGGGTKVEIK h1780_VL.1A (SEQ ID NO: 61) DTVLTQSPATLSLSPGERATLSCRASEGLTSYMHWYQQKPGQAPRLLIYKASNLASGIPARFS GSGSGTDFTLTISSLEPEDFAVYYCQQNWNDPWTFGGGTKVEIK h1780_VL.1 B (SEQ ID NO: 62) DTVLTQSPATLSLSPGERATLSCRASEGLTSYMHWYQQKPGQAPRLLIYKASNLASGVPARFS GSGSGTDFTLTISSLEPEDFATYFCQQNWNDPWTFGGGTKVEIK h1780_VH.1 (SEQ ID NO: 63) EVQLVQSGAEVKKPGASVKVSCKASGYTFTEYLIHWVRQAPGQGLEWMGYINPYSGGTVYNE KFKSRVTMTRDTSISTAYMELSRLRSDDTAVYYCARDGGYSDPLDYWGQGTMVTVSS h1780_VH.1A (SEQ ID NO: 64) EVQLVQSGAEVKKPGASVKVSCKASGYTFTEYLIHWVRQAPGQGLEWMGYINPYSGGTVYNE KFKSRVTLTVDKSISTAYMELSRLRSDDTAVYYCARDGGYSDPLDYWGQGTMVTVSS h1780_VH.1B (SEQ ID NO: 65) EVQLVQSGAEVKKPGASVKVSCKASGYTFTEYLIHWVRQAPGQGLEWIGYINPYSGGTVYNEK FKSRATLTVDKSISTAYMEFSRLRSDDTAVYYCARDGGYSDPLDYWGQGTMVTVSS h1780_VH.1C (SEQ ID NO: 66) EVQLVQSGAEVKKPGASVKVSCKASGYTFTEYLIHWVKQAPGQGLEWIGYINPYSGGTVYNEK FKSKATLTVDKSISTAYMEFSRLRSDDTAVYYCARDGGYSDPLDYWGQGTMVTVSS. Each of the light-chain variable regions described above combined with the light-chain constant region to form a light-chain sequence. Each of the heavy-chain variable regions combined with the heavy-chain constant region to form a heavy-chain sequence. 5.4 Selection of the humanized frame for the hybridoma clone mAb1773 For h1773, IGHV3-73*01 was selected as the template for VH, and IGKV1 39*01 was selected as the template for VL. The CDRs of the murine antibody mAb1773 were grafted onto the selected humanized template; the amino acids were reverse-mutated. The light-chain and heavy-chain variable regions of the humanized antibodies were obtained, as shown in Table 9. In addition, N in h1773 HCDR2 (RIDPANGDTK HGPKFQG) was mutated to V (i.e., N55V) to form a heavy-chain variable region variant of HCDR2 (the sequence of the mutated HCDR2 is as shown in SEQ ID NO: 82: RIDPAVGDTKHGPKFQG). nccLLn / Lznz / e / YiAi Table 9. Template selection and reverse mutation design for h1773 h1773_VL h1773_VH h1773 VL.1 Grafted h1773 VH.1 Grafted h1773_VL.1A M4L, A42S, L45P, L46W h1773_VH.1A F29I, R72A, T97F + N55V h1773_VH.1B F29I, R38K, V48I, R72A, T97F+N55V Note: Grafting represents that the murine antibody CDRs were grafted into the FR region of the human germline. For example, according to the natural numbering of the amino acid sequence, M4L represents that M at position 4 of grafting was mutated back to L. The engineered humanized molecules were combined to form different molecules as shown in the following table, as shown in Table 10. Table 10. Combination of light and heavy chain variable regions of the humanized antibody h1773 h1773_VH.1 h1773_VH.1A h1773_VH.1B h1773_VL1 h 1773-002 h1773-003 h1773-004 h1773_VL.1A h 1773-005 h1773-006 h1773-007 Laser secuencias específicas de las regiones variables del anticuerpo humanizado h1773 son las siguientes: h1773_VL.1 (SEQ ID NO: 67) DIQMTQSPSSLSSASVGDRVTITCSSASSSVNYIYWYQQKPGKAPKLLIYLTATLASGVPSRFSGS GSGTDFTLTISSLQPEDFATYYCQQWNSYPYTFGGGTKVEIK h1773_VL.1A (SEQ ID NO: 68) DIQLTQSPSSLSASVGDRVTITCSASSSVNYIYWYQQKPGKSPKPWIYLTATLASGVPSRFSGS GSGTDFTLTISSLQPEDFATYYCQQWNSYPYTFGGGTKVEIK h1773_VH.1 (SEQ ID NO: 69) EVQLVESGGGLVQPGGSLKLSCAASGFTFSNTYIHWVRQASGKGLEWVGRIDPAVGDTKHGP KFQGRFTISRDDSKNTAYLQMNSLKTEDTAVYYCTRYGIYPDHWGQGTLVTVSS h1773_VH.1A (SEQ ID NO: 70) EVQLVESGGGLVQPGGSLKLSCAASGFTISNTYIHWVRQASGKGLEWVGRIDPAVGDTKHGP KFQGRFTISADDSKNTAYLQMNSLKTEDTAVYYCFRYGIYPDHWGQGTLVTVSS h1773VH.1B (SEQ ID NO: 71) EVQLVESGGGLVQPGGSLKLSCAASGFTISNTYIHWVKQASGKGLEWIGRIDPAVGDTKHGPK FQGRFTISADDSKNTAYLQMNSLKTEDTAVYYCFRYGIYPDHWGQGTLVTVSS. Each of the variable regions of the light chain described above was combined with the sequence of the constant region of the light chain as shown in SEQ ID NO: 53 to form the complete final light chain sequence. Each of the variable regions of the heavy chain was combined with the constant region of the heavy chain as shown in SEQ ID NO: 52 to form the complete final heavy chain sequence. 5.5 Selection of the humanized frame for the hybridoma clone mAb1779 For h1779, IGHV1-2*02 was selected as the template for VH, and IGKV1-33*01 was selected as the template for VL. The CDRs of the murine h1779 antibody were grafted onto the selected humanized template; the amino acids were reverse-mutated. The light-chain and heavy-chain variable regions of the humanized antibodies were obtained, as shown in Table 11. Table 11. Template selection and reverse mutation design for h1779 nccLLn / Lznz / e / YiAi h1779_VL h1779_VH h1779_VL.1 Grafted h1779_VH.1 Injeratdo + D89E h1779_VL.1A A43S h1779_VH.1A R72A,T74K + D89E h1779VL.1B A43S, I48V, F71Y h1779 VH.1B M48I, V68A, R72A, T74K + D89E h1779_VH.1C M48I, V68A, R72A, T74K, M81 L, L83F + D89E h1779_VH.1D R38K, M48I, R67K, V68A, R72A, T74K, M81L, L83F+ D89E Note: Grafting represents that the murine antibody CDRs were grafted into the FR region of the human germline. For example, according to the natural numbering of the amino acid sequence, A43S represents that A at position 43 of grafted was mutated back to S. The engineered humanized molecules were combined to form different molecules as shown in the following table, as shown in Table 12. nccLLn / Lznz / e / YiAi Table 12. Combination of light and heavy chain variable regions of the humanized antibody h1779 h1779_VH. 1 h1779_VH.1 A h1779_VH.1 B h1779_VH.1 C h1779_VH.1 D h1779_VL1 h1779-005 h 1779-006 h 1779-007 h1779-008 h 1779-009 h1779_VL. 1 A h 1779-010 h 1779-011 h1779-012 h1779-013 h 1779-014 h1779_VL. 1 B h 1779-015 h 1779-016 h 1779-017 h1779-018 h 1779-019 Laser secuencias específicas de las regiones variables del anticuerpo humanizado h1779 son las siguientes: h1779_VL.1 (SEQ ID NO: 72) DIQMTQSPSSSLSASVGDRVTITCLASEGISNDVAWYQQKPGKAPKLLIYAASRLQDGVPSRFSG SGSGTDFTFTISSLQPEDIATYYCQQGYKTPLTFGQGTKLEIK h1779_VL.1A (SEQ ID NO: 73) DIQMTQSPSSLSASVGDRVTITCLASEGISNDVAWYQQKPGKSPKLLIYAASRLQDGVPSRFSG SGSGTDFTFTISSLQPEDIATYYCQQGYKTPLTFGQGTKLEIK h1779 VL.1 B (SEQ ID NO: 74) DIQMTQSPSSLSASVGDRVTITCLASEGISNDVAWYQQKPGKSPKLLVYAASRLQDGVPSRFS GSGSGTDYTFTISSLQPEDIATYYCQQGYKTPLTFGQGTKLEIK h1779_VH.1 (SEQ ID NO: 75) EVQLVQSGAEVKKPGASVKVSCKASGYTFTDYIIHWVRQAPGQGLEWMGYFNPNSGGSNYN ENFKRRVTMTRDTSISTAYMELSRLRSEDTAVYYCARRIAWDHWYFDFWGQGTMVTVSS h1779 VH.1 A (SEQ ID NO: 76) EVQLVQSGAEVKKPGASVKVSCKASGYTFTDYIIHWVRQAPGQGLEWMGYFNPNSGGSNYN ENFKRRVTMTADKSISTAYMELSRLRSEDTAVYYCARRIAWDHWYFDFWGQGTMVTVSS h1779_VH.1B (SEQ ID NO: 77) EVQLVQSGAEVKKPGASVKVSCKASGYTFTDYIIHWVRQAPGQGLEWIGYFNPNSGGSNYNE NFKRRATMTADKSISTAYMELSRLRSEDTAVYYCARRIAWDHWYFDFWGQGTMVTVSS h1779_VH.1C (SEQ ID NO: 78) EVQLVQSGAEVKKPGASVKVSCKASGYTFTDYIIHWVRQAPGQGLEWIGYFNPNSGGSNYNE NFKRRATMTADKSISTAYLEFSRLRSEDTAVYYCARRIAWDHWYFDFWGQGTMVTVSS h1779 VH.1 D (SEQ ID NO: 79). EVQLVQSGAEVKKPGASVKVSCKASGYTFTDYIIHWVKQAPGQGLEWIGYFNPNSGGSNYNE NFKRKATMTADKSISTAYLEFSRLRSEDTAVYYCARRIAWDHWYFDFWGQGTMVTVSS. Each of the variable regions of the light chain, as described above, was combined with the sequence of the constant region of the light chain, as shown in SEQ ID NO: 53, to form a light chain sequence. Each of the variable regions of the heavy chain was combined with the constant region of the heavy chain, as shown in SEQ ID NO: 52, to form a heavy chain sequence. The full-length sequences of the exemplary humanized antibodies are as follows: Heavy chain h1705-008: EVQLVESGGGLVQPGGSLRLSCAASGFTFSHYYMAWVRQAPGKGLEWVTSISYEGDITYYGD SVKGRFTISRDNSKNTLYLQMNSLRAEDTATYYCASQTLRESFDYWGQGTLVTVSSAST KG PS VFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVT VPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTL YITREPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDW LNGKEYKCKVSNKALPAPIEKTISKAKGPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIA VEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQK SLSLSPGK SEQ ID NO: 83 cadena ligera h 1705-008: DIQMTQSPSSVSASVGDRVTITCRASQDIANYLSWYQQKPGSKSPKLLIYGTSNLEWGVPSRFSG SRSGTDFTLTISSLQPEDFATYYCLQDKEFPRTFGGGTKVEIKRT VAAPS V FIFPPSDEQLKSGT ASVVCLLNNFYPREAKVQWKVDNALQGSGNSQESVTEQDSKDSTYSLSSTLTLSKAYEKHKVY ACEVTHQGLSSPVTKSFNRGEC SEQ ID NO: 84 cadena pesada h 1706-009: EVQLVESGGGLVQPGGSLRLSCAASGFTFSHYYMAWVRQAPGKGLEWVSSINYEGNSAYYG DSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCATETLRESLDYWGQGTMVTVSSAST KG P SVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVV TVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDT LYITREPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQD WLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSD IAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQ KSLSLSPGK SEQ ID NO: 85 cadena ligera h 1706-009: DIQMTQSPSSVSASVGDRVTITCRASQDIGNYLSWYQQKPGKSPKLMIYSASNLEVGVPSRFS GSGSGTDYTLTISSLQPEDFATYFCLQHKQFPRTFGGGTKVEIKRTVAAPSVFIFPPSDEQLKS nccLLn / Lznz / e / YiAi GTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKH KVYACEVTHQGLSSPVTKSFNRGEC SEQ ID NO: 86 cadena pesada h 1780-017: EVQLVQSGAEVKKPGASVKVSCKASGYTFTEYLIHWVRQAPGQGLEWIGYINPYSGGTVYNEK FKSRATLTVDKSISTAYMEFSRLRSDDTAVYYCARDGGYSDPLDYWGQGTMVTVSSAST KG P SVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVV TVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDT LYITREPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQD WLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSD IAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQ KSLSLSPGK SEQ ID NO: 87 cadena ligera h 1780-017: DTVLTQSPATLSLSPGERATLSCRASEGLTSYMHWYQQKPGQAPRLLIYKASNLASGVPARFS GSGSGTDFTLTISSLEPEDFATYFCQQNWNDPWTFGGGTKVEIKRTVAAPSVFIFPPSDEQLKS GTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKH KVYACEVTHQGLSSPVTKSFNRGEC SEQ ID NO: 88 cadena pesada h 1773-007: EVQLVESGGGLVQPGGSLKLSCAASGFTISNTYIHWVKQASGKGLEWIGRIDPAVGDTKHGPK FQGRFTISADDSKNTAYLQMNSLKTEDTAVYYCFRYGIYPDHWGQGTLVTVSSASTKGPSVFP LAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPS SSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLYIT REPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLN GKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVE WESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSL SLSPGK SEQ ID NO: 89 cadena ligera h 1773-007: DIQLTQSPSSLSASVGDRVTITCSASSSVNYIYWYQQKPGKSPKPWIYLTATLASGVPSRFSGS GSGTDFTLTISSLQPEDFATYYCQQWNSYPYTFGGGTKVEIKRTVAAPSVFIFPPSDEQLKSGT ASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVY ACEVTHQGLSSPVTKSFNRGEC SEQ ID NO: 90 cadena pesada h 1779-014: EVQLVQSGAEVKKPGASVKVSCKASGYTFTDYIIHWVKQAPGQGLEWIGYFNPNSGGSNYNE NFKRKATMTADKSISTAYLEFSRLRSEDTAVYYCARRIAWDHWYFDFWGQGTMVTVSSASTK nccLLn / Lznz / e / YiAi GPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSS VVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPK DTLYITREPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQ DWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPS DIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYT QKSLSLSPGK SEQ ID NO: 91 light chain h 1779-014: DIQMTQSPSSLSASVGDRVTITCLASEGISNDVAWYQQKPGKSPKLLVYAASRLQDGVPSRFS GSGSGTDYTFTISSLQPEDIATYYCQQGYKTPLTFGQGTKLEIK RTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKD STYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC SEQ ID NO: 92; The Hu39D10 antibody against IL5 in WO2012083370A1 was used as a positive control in the present invention, and the heavy chain and light chain sequences thereof are shown in SEQ ID NO: 80 and SEQ ID NO: 81, respectively. The Hu39D10 heavy chain sequence EVQLVESGGGLVQPGGSLRLSCAVSGLSLTSNSVNWIRQAPGKGLEWVGLIWSNGDTDYNSA IKSRFTISRDTSKSTVYLQMNSLRAEDTAVYYCAREYYGYFDYWGQGTLVTVSSASTKGPSVF PLAPCSRSTSESTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVP SSSLGTKTYTCNVDHKPSNTKVDKRVESKYGPPCPPCPAPEFLGGPSVFLFPPKPKDTLMISR TPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNG KEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTLPPSQEEMTKNQVSLTCLVKGFYPSDIAVE WESNGQPENNYKTTPPVLDSDGSFFLYSRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSL SLSLGK SEQ ID NO: 80 The sequence for the Hu39D10 light chain DIQMTQSPSSLSASVGDRVTITCLASEGISSYLAWYQQKPGKAPKLLIYGANSLQTGVPSRFSG SGSATDYTLTISSLQPEDFATYYCQQSYKFPNTFGQGTKVEVKRTVAAPSVFIFPPSDEQLKSG TASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKV YACEVTHQGLSSPVTKSFNRGEC SEQ ID NO: 81 Example 6. Preparation of recombinant chimeric antibody and humanized antibody 1. Molecular cloning of recombinant chimeric antibody After positive antibody molecules were obtained by hybridoma screening, the gene sequences encoding variable regions were obtained by sequencing. Forward and reverse primers were designed based on the obtained sequences, and the sequenced gene was used as a template to construct each fragment of the nccLLn / Lznz / e / YiAi gene. VH / VK antibody was PCR-produced, and then inserted into the pHr expression vector (which has signal peptide and hlgGI / hkappa (CH1-Fc / CL fragment) of the constant region) by homologous recombination to construct a recombinant chimeric antibody full-length expression plasmid VH-CH1-Fc-pHr / VL-CL-pHr, to obtain five chimeric antibodies Ch1705, Ch1706, Ch1780, Ch1773, and Ch1779. 2. Molecular cloning of humanized antibodies The humanized antibody sequence was subjected to codon optimization, then the coding gene sequence was obtained with human codon preference; primers were designed to build each antibody VH / VK gene fragment by PCR, which was then inserted into the pHr expression vector (having the signal peptide and the hlgGI / hkappa (CH1-Fc / CL) constant region gene fragment) by homologous recombination to build a full-length expression plasmid of humanized antibody VH-CH1-Fc-pHr / VLCL-pHr. 3. Expression and Purification of Recombinant Chimeric Antibodies and Humanized Antibodies. The plasmid expressing the antibody's light or heavy chain was transfected separately into HEK293E cells. Six days later, the expression supernatant was collected, centrifuged at high speed to remove impurities, and purified using a protein A column. The column was washed with PBS until the A280 reading dropped to baseline. The target protein was eluted with acidic elution buffer, pH 3.0–pH 3.5, and neutralized with 1 M Tris-HCl, pH 8.0–9.0. The eluted sample was appropriately concentrated and further purified by gel chromatography. Using Superdex200 (GE) gel pre-equilibrated with PBS to remove aggregates, the monomer peaks were collected and aliquoted for use. The following test methods were used to verify the performance and beneficial effects of the antibodies of the present invention. Biological evaluation of in vitro activity Example test 1. The binding of murine IL-5 antibody to IL-5 from different species using the Biacore assay The affinity of the murine IL-5 antibody to be tested with human IL-5 was measured using a Biacore T200 (GE) instrument. The protein A biosensor chip was used to capture the molecules to be tested by affinity. The antigen (recombinant human and IL-5 cyno, prepared in Example 1) was then flowed across the chip's surface, and the reaction signal was detected under real-time conditions using the Biacore T200 instrument to obtain binding and dissociation curves. After dissociation in each experimental cycle, the biosensor chip was washed and regenerated with a glycine-hydrochloric acid regeneration solution (pH 1.5). GE's BIAevaluation software version 4.1 was used to fit the data to the Langmuir (1:1) model, and the affinity value was obtained and is shown in Table 13. nccLLn / Lznz / e / YiAi Table 13. Results of the affinity of murine IL-5 antibodies with IL-5 from different species using the BIAcore assay Antigen KD (M) mAb 1705 mAb 1706 mAb1780 mAb1773 mAb 1779 human IL-5 7.27E-11 3.83E-11 8.99E-11 1.29E-10 4.58E-10 IL-5 cyno 2.05E-10 2.77E-10 3.12E-10 4.76E-10 9.98 E-9 nccLLn / Lznz / e / YiAi This example proves that the antibodies mAb1705, mAb1706, mAb1780, mAb1773 and mAb1779 of the present invention have a high affinity for IL-5 from different species (human, monkey). Example Test 2. The affinity of humanized IL-5 antibody for IL-5 from different species using the Biacore assay The affinity of the humanized IL-5 antibody to be tested with human IL-5 was measured using a Biacore T200 (GE) instrument. The protein A biosensor chip was used for affinity capture of the molecules to be tested. The antigen (prepared in Example 1) was then flowed across the chip's surface, and the reaction signal was detected in real time using the Biacore T200 instrument to obtain binding and dissociation curves. After dissociation in each experimental cycle, the biosensor chip was washed and regenerated with a glycine-hydrochloric acid regeneration solution (pH 1.5). GE's BIAevaluation software version 4.1 was used to fit the data against the Langmuir (1:1) model, and the affinity value was obtained and is shown in Table 14. Table 14. Results of the affinity of humanized IL-5 antibodies to human IL-5 using the BIAcore assay KD(M) Antibody KD(M) Antibody h 1705-003 3.35E-09 h 1706-003 1.89E-11 h 1705-006 4.11E-09 h1706-006 1.73E-11 h 1705-009 4.55E-09 h1706-009 5.45E-11 h 1705-004 2.14E-11 h1780-017 7.78E-11 h 1705-007 2.21E-11 h1773-007 2.07E-10 h1705-010 2.05E-11 h1779-014 4.12E-10 h 1705-005 2.16E-11h 1705-008 3.42E-11h 1705-011 2.30E-11 The results show that all humanized IL-5 antibodies have a high affinity for human IL-5. Example Test 3. ELISA-based assay of murine IL-5 antibody to block IL-5 binding to the IL-5a receptor To identify the ability of the IL-5 antibody to block IL-5 binding to the extracellular region of the recombinantly expressed IL-5a receptor protein, an ELISA plate was coated with IL-5 (5 pg / ml in PBS) and incubated at 37°C for 1 hour. The coating was removed, and 200 µL / well of 5% skim milk blocking solution diluted with PBS was added and the plate was incubated for 2.5 hours at 37°C for blocking. After blocking, the blocking solution was removed, and the plate was washed 5 times with PBST buffer (pH 7.4 PBS comprising 0.05% Tween-20). 25 μI of IL-5Ra 10 pg / mi (in 1% BSA) labeled with a biotin titration kit (Tojin Chemical, LK03) was added, and then 25 μI of gradient diluted antibody was added (the antibody competed with IL-5Ro for IL-5 binding) and incubated at 37°C for 1 hour.After incubation, the reaction solution was removed from the microtiter plate, the plate was washed 5 times with PBST, 50 µL / well of streptavidin-peroxidase polymer (Sigma, S2438-250UG) diluted with sample dilution solution at 1:600 ​​was added and incubated for 1 hour at 37°C. The plate was washed 5 times with PBST, 50 µL / well of TMB chromogenic substrate (KPL, 52-00-03) was added and incubated at room temperature for 3-10 min; 50 µL / well of 1 M H2SO4 was added to stop the reaction; the NOVOStar microplate reader was used to read the absorbance value at 450 nm; The IC50 value of the IL-5 antibody was calculated to block the binding of IL-5 to IL-5Ra. The results are shown in Table 15. The antibodies of the present invention can effectively inhibit the binding of IL-5 to its receptor. Table 15. ELISA results of the murine IL-5 antibody to block IL-5 binding to the IL-5a receptor nccLLn / Lznz / e / YiAi mAb1705 mAb 1706 IC50 (pg / ml) 0.42 0.40 Example test 4. FACS-based assay of IL-5 antibody to block IL-5 binding to IL-5 receptor To identify the selected IL-5 antibody that can block the IL-5 receptor on the cell surface, a recombinant CHOS cell line that heavily expresses two IL-SRα / β receptors was constructed. This experiment demonstrated that IL-5 antibodies can block the binding of IL-5 to the recombinant IL-5α / β receptor on the surface of the CHOS cell line. The specific method was as follows: CD-CHO, comprising 100 ng / mL of G418 and 25 ng / mL of zeozine, was used to culture CHO-S-IL-5Ra and β cells. During cell culture, the concentration should not exceed 3 × 10⁶ cells / mL. Healthy IL-5Ra / 3-CHOS cells were centrifuged (at 1000 rpm, 5 min) and washed once with 10% FBS in PBS. The cells were counted, the cell concentration was adjusted to 4 × 10⁶ cells / mL, and 25 µL were removed and added to a 96-well round-bottom plate. The antibody to be tested was diluted with a PBS solution comprising 10% FBS. The initial concentration was 200 µg / ml and was diluted 1:10 for 8 gradient dilutions. 25 µL of IL-5 100 ng / ml labeled with a biotin titration kit (Tojin Chemical, LK03) were added and thoroughly mixed with 50 µL of antibody diluted to each concentration and added to a 96-well plate that had been added with cells, and incubated at 4°C for 1 hour.After incubation, the sample was centrifuged at 4°C (400 g, 5 min), and the supernatant was removed. The plate was washed with 200 μL of pre-cooled PBS by centrifugation, repeated twice. PE-avidin secondary antibody diluted to 1:1333 was added and incubated in the dark at 4°C for 40 min. It was centrifuged at 4°C (400 g, 5 min). The supernatant was removed, and 200 μL of pre-cooled PBS was added to pipette the cells. The plate was washed by centrifugation at 4°C three times. 100 μL of PBS was added, and the plate was read on the machine. The IC50 value of the IL-5 antibody to block the binding of IL-5 to IL-SRa / β was calculated according to the fluorescence signal value. The results are shown in Table 16 and Figure 1. Table 16. Results of the IL-5 antibody test to block IL-5 binding to IL-5Ra / p nccLLn / Lznz / e / YiAi IgG antibody hu39D10 h1705- 008 h1706- 009 h1780- 017 h1779- 014 IC50 (ng / ml) 8777 25.07 14.51 24.74 16 49.64 The results show that the antibodies h1705-008, h1706-009, h1780-017 and h1779-014 show a strong ability to block the binding of IL-5 to IL-5 receptors on the cell surface. Example test 5. The IL-5 antibody inhibits IL-5-induced TF1 cell proliferation IL-5 can induce TF-1 cell proliferation, and the IL-5 antibody can prevent IL-5 from stimulating TF-1 cell proliferation. Specifically: TF-1 cells (ATCC, CRL-2003) were cultured in RPMI1640 comprising 10% FBS and 2 ng / ml rhGM-CSF (LinkBio, Catalog No. 96-AF-300-03-20), placed in a 37°C, 5% CO2 incubator, with cell density not to exceed 1 x 10⁶ cells / ml. To detect antibodies, logarithmic-phase cells were washed with PBS three times and centrifuged at 800 rpm for 5 min; cell density was adjusted to 6000 cells / well / 90 µL with RPMI1640 (FBS: 2%, recombinant human IL-5: 10 ng / ml); Ten microliters of the gradient-diluted antibody to be tested were added to a 96-well culture plate. After 3 days of culture, 30 microliters of cell titer were added and mixed for detection. The IC50 was calculated based on the readings. The test results are shown in Table 17 below. Table 17. Results of the IL-5 humanized antibody test to inhibit IL-5-induced TF1 cell proliferation nccLLn / Lznz / e / YiAi Antibody IC50 (nM) Antibody IC50 (nM) Hu39D10 0.30 h 1706-003 0.31 h1705-004 0.30 h 1706-004 0.30 h1705-005 0.30 h 1706-006 0.34 h1705-007 0.25 h 1706-007 0.28 h1705-008 0.20 h 1706-009 0.25 h 1705-010 0.30 h 1773-007 0.38 h1705-011 0.28 h1780-017 0.16 h 1779-014 0.20 Example test 6. IL5 antibody test to inhibit IL5-induced eosinophil adhesion IL-5 can induce eosinophil differentiation, maturation, migration, and activation, leading to airway inflammation and asthma. This experiment is based on the principle that IL-5 cytokines can promote eosinophil adhesion and activation. Eosinophils were collected and purified from human peripheral blood to test the blocking effect of IL-5-specific antibodies on the IL-5 pathway and to detect the blocking effect of IL-5 antibodies on IL-5-mediated eosinophil adhesion in vitro. Specifically: human peripheral blood was diluted 5-fold with PBS containing 2 mM EDTA, and Percoll™ (1.088 density gradient) was used to isolate monocytes and granulocytes. The red blood cell layer comprising granulocytes was carefully aspirated, and a red blood cell lysis solution was used to remove the red blood cells. The remaining cells were counted, and magnetic separation beads (Miltenyi Biotec, Catalog No. 130-045-701) with CD16 antibody were added proportionally. The mixture was incubated for 30 min and flowed through the magnetic bead column. Subpopulations (mainly eosinophils) flowing directly through the column were collected by negative selection.Isolated eosinophils were counted and added to a 96-well cell culture plate pre-coated with IgG antibody, with approximately 1 x 104 cells per well; human IL-5 (20 ng / ml) and IL-5 antibody molecules were added at different concentrations (starting from 10 pg / ml, triple dilution, 10 concentration points); the cell culture plate was placed in a 5% CO2 incubator at 37°C and incubated for 1 hour, then the culture plate was removed and 0.3% CTAB was added to lyse the cells, and finally the TMB peroxidase reaction substrate was added to give color, development, and the OD450 absorbance value was read with a microplate reader.The reading value for the well added with IL-5 only was the maximum adsorption value; the well without IL-5 and antibody agent served as a background control; the inhibition value of the antibody agent at each concentration was calculated relative to the maximum adsorption value = (maximum adsorption value [antibody agent]) / (maximum adsorption value - background control value) χ 100%, and the IC50 was calculated. The results are shown in Table 18:. Table 18. The IL-5 antibody blocks IL-5-induced eosinophil adhesion nccLLn / Lznz / e / YiAi Hu39D10 h 1705-008 h1706- 009 h1780- 017 IC50 (ng / ml) 11.79 4.85 4.3 21.19 The results show that the humanized antibodies of the present invention exhibit a strong ability to inhibit IL5-mediated eosinophil adhesion. Example test 7. Evaluation of the specificity of the humanized IL-5 antibody with Th2 cytokine IL-5 was one of the Th2 cytokines. To verify that the IL-5 antibody only specifically targets IL-5 and does not cross-react with other cytokines, Fortebio was used to detect 12 types of Th2 and related cytokines, comprising IL2 (R&D, 202-IL010 / CF), IL4 (R&D, 204-IL-050 / CF), IL-5 (R&D, 205-IL-025 / CF), IFNgamma, IL6 (R&D, 7270-IL025 / CF), IL9 (R&D, 209 -IL-010 / CF), IL10 (R&D, 217-IL-025 / CF), IL13 (R&D, 213-ILB-025 / CF), IL25 (R&D, 8134-IL-025 / CF), IL31 (R&D, 2824-IL-010 / CF) and IL3 (203-IL-050 / CF) and GMCSF (R&D, 215-GM-010 / CF) that share α receptors with IL-5. Specifically: a protein A biosensor (PALL Fortebio, 18-5010) was used to capture the antibody, the capture signal was recorded, and then each cytokine was injected at 40 nM and the new binding signal was recorded. Finally, the binding signal with IL-5 was defined as 100%. The binding signals of other cytokines with antibodies were observed, and the results are shown in Figure 2. The results show that, among 12 related cytokines, the humanized IL-5 antibodies h1705-008 and h1706-009 only bind specifically to IL-5 and have no cross-reactivity with other Th2 cytokines. Biological evaluation of in vivo activity. Example test 8. Evaluation of IL-5 antibody efficacy in an OVA-induced mouse asthma model This test was based on the airway inflammatory response and airway remodeling to evaluate the efficacy of the IL-5 antibody in the BALB / c mouse model of ovalbumin (OVA) aerosol-induced asthma. Mice were randomly divided into 7 groups based on body weight, each group containing 10 mice: a normal control group (G1); a model group (G2); treatment groups receiving two antibodies to be tested, h1705-008 (G3 and G4) and h1706-009 (G5 and G6), at two doses (10 MPK and 2 MPK) of each antibody; and a control group receiving the positive antibody Hu39D10 (G7, 10 MPK). On days 1 and 14, all mice were sensitized by intraperitoneal injection of an allergenic solution. On days 28, 29, and 30, all six groups of mice (except the first group) were challenged with an aerosolized OVA challenge solution for 30 minutes. Two hours before the challenge, the second group (G2) was injected intraperitoneally with phosphate buffer, mice from the third group to the seventh group (G3-G7) were injected intraperitoneally with different doses of different antibodies (once a day, for three days).The antibodies to be tested were prepared fresh before each injection, and administration ended half an hour after antibody preparation. Mice in the first group (as a normal control group) were exposed to PBS aerosol for 30 minutes, and 2 hours before the phosphate exposure buffer was injected intraperitoneally once a day for three consecutive days. On day 31, the WBP system was used to test airway hyperreactivity in the animals. All animals were aerosolized to ingest methacholine at 2-fold incremental concentrations (1.5625, 3.125, 6.25, 12.5, 25, and 50 mg / mL), and enhanced respiratory pause values ​​were measured at the corresponding concentrations. The BALF was centrifuged at 300g at 4°C for 5 minutes. The supernatant was retained for cytokine analysis. After centrifugation, the cells were resuspended in 1.5 mL of PBS (comprising 1% BSA and 0.6 mM EDTA) for cell counting. A hemocytometer and trypan blue staining experiment were used to count the total number of cells in BALF. The cells were spread on a slide and stained with Wright's stain for 1 minute, then stained with Giemsa for 7 minutes to distinguish eosinophils, neutrophils, macrophages, and lymphocytes. Counting was performed under a light microscope. After washing, the lung tissue was collected and stained with a 10% neutral formaldehyde solution and then fixed in a 10% neutral formaldehyde solution. The fixed tissue was embedded in paraffin, trimmed, stained with hematoxylin and eosin (H&E), and annotated. The test results are shown in Figure 3, Figure 4A, and Figure 4B. nccLLn / Lznz / e / YiAi The results show that the antibody molecules h1705-008 and h1706-009 of the present invention can significantly improve lung function in a dose-dependent manner, whereas a high dose (10 mpk) of the positive compound cannot improve lung function (see Figure 3). Meanwhile, the two antibodies significantly reduce eosinophil levels and mucosal membrane thickness at the same dose (10 mpk) and exhibit a stronger capacity to reduce eosinophils than the positive antibody (see Figures 4A and 4B). In the same type of mouse asthma model, repeated experiments also verified that 1 mg / ml of h1705-008, h1706-009, and h1780-017 significantly reduces eosinophil levels in BalF compared to the positive antibody (see Figure 4C). Example test 9. Evaluation of the in vivo efficacy of the IL-5 antibody in a guinea pig model of acute asthma induced by exogenous human IL-5 In this experiment, male guinea pigs were selected to establish a model of acute asthma induced by human IL-5, to evaluate the inhibitory effect of five humanized IL-5 mAbs of the present invention on the increase in eosinophils in bronchial lavage fluid (BALF) from guinea pig lungs induced by human IL-5, and hu39D10 was used as the positive antibody. The guinea pigs were divided into 9 groups, each with 8-10 animals: normal control group, model group, hu39D10 group (1 mg / kg), h1705-008 group (1 mg / kg), h1706-009 group (1 mg / kg), h1780-017 group (1 mg / kg), h1773-007 group (1 mg / kg), and h1779-014 group (1 mg / kg). Guinea pigs in the model group and administration groups were injected into the trachea with 100 pl of human IL5 (comprising 5 pg of IL5 antigen) on day 1 for irritation, respectively; and the normal control group was injected with PBS into the trachea.The treatment group was injected intraperitoneally with 1 mg / kg of IL5 monoclonal antibody as previously described, 2 hours before irritation, with an administration volume of 5 ml / kg; the model group was administered with the corresponding IgG antibody, and the normal control group was administered intraperitoneally with PBS solvent. Guinea pigs were anesthetized 24 hours after tracheal injection to collect pulmonary bronchial lavage fluid. The cell concentration was adjusted to 5 x 10⁶ / ml, 15 ml were poured onto a slide and dried to fix; H&E staining was performed, and the total number of cells and eosinophils was counted under a 400x microscope, and the percentage of eosinophils was calculated. The results are shown in Figure 5A and Figure 5B, indicating that 5 humanized antibodies of the present invention significantly reduce the level of eosinophils in BALF. Selection and evaluation of the stability of the formulation ingredients. The exemplary preparation process for the pharmaceutical composition (formulation) of an antibody: nccLLn / Lznz / e / YiAi Step 1: A certain amount of purified anti-IL-5 antibody solution was taken and an antibody-free buffer (such as 30 mM acetic acid-sodium acetate buffer, pH 5.5) was used for solvent exchange (preferably by ultrafiltration). At least six times the volume was exchanged through an ultrafiltration membrane, and the protein was concentrated to approximately 120 mg / ml. A certain volume of sucrose stock solution was added and mixed to obtain a final concentration of 72 mg / ml sucrose. A certain volume of polysorbate 80 stock solution was added and mixed to obtain a final concentration of 0.4 mg / ml of polysorbate 80. Acetic acid-sodium acetate 10 mM pH 5.5 buffer was added to reach a certain volume, resulting in a protein concentration of 100 mg / ml (other formulations to be tested or stable formulations were prepared according to similar steps). The product was filtered and then analyzed using central control sampling to determine if it was free of pathogens. The stock solution was passed through a 0.22 µm PVDF filter and the filtrate was collected. Step 2: The volume was adjusted to 1.2ml, the filtrate was loaded into a 2ml vial with a stopper, and central control samples were taken at the beginning, middle, and end of the loading to detect the difference in loading volume. Step 3: The capping machine was started to apply aluminum caps and perform the capping. Step 4: A visual inspection was performed to confirm that the products were free of defects, such as incorrect loading. Vial labels were printed and affixed; carton labels were printed; the cartons were folded; and packaging and box labels were attached. Example test 10. Buffer system screening The h1705-008 formulations were prepared with a protein concentration of 100 mg / ml in a series of buffers at pH 5.0 to 6.5, wherein the stirring sample comprised 0.2 mg / ml of polysorbate 80 (PS80), and other samples comprised 0.05 mg / mL of PS80. The buffer systems were as follows: acetic acid-sodium acetate (AA) 10 mM pH 5.0, 5.5; succinic acid-sodium succinate (SA) 10 mM pH 5.0, 5.5, 6.0; citric acid-sodium citrate (GA) 10 mM pH 5.5, 6.0, 6.5; histidine hydrochloride (His) 10 mM pH 5.5, 6.0, 6.5; Phosphate (PB) 10 mM pH 6.0, 6.5. Each formulation was filtered, loaded, applied with a stopper, and capped. The samples were subjected to a forced degradation experiment; and appearance, SEC, CIEF serving as evaluation indicators. The results are shown in Table 19. Appearance data indicate that the samples underwent agitation (300 rpm, 25°C), and the samples at 40°C show varying degrees of particle formation. In general, the appearance is better at lower pH, with the acetic acid-sodium acetate and succinic acid-sodium succinate buffer systems being the best. SEC data show that the AA pH 5.5 group is slightly better at 40°C. CIEF data show that the AA pH 5.5, His pH 5.5, and CA pH 6.5 groups are slightly better at 40°C. Considering physical and chemical stability, AA pH 5.5 is preferable. Table 19. Screening results for pH and nccLLn / Lznz / e / YiAi buffer system Lot N B. Condition Appearance SEC (%) Neutral peak CIEF (%) 01 AA5.0 T0 clear 98.3 75.3 Agitation D4 clear 96.2 N / A 40°C-D13 Fine particle 94.8 62.3 02 AA5.5 T0 clear 98.0 75.4 Agitation D4 clear 96.0 N / A 40°C-D13 Small flocculent particles 95.4 64.2 03 SA5.0 T0 clear 98.2 74.9 Agitation D4 clear 96.5 N / A 40°C-D13 Fine particles+ 94.8 59.3 04 SA5.5 T0 clear 98.2 74.7 Agitation D4 Large quantity of small particles 96.2 N / A 40°C-D13 Small particles 94.8 62.1 05 SA6.0 T0 clear 97.9 75.8 Agitation D4 Clear, slightly opalescent 95.7 N / A 40°C-D13 Small particles 95.0 63.7 06 His5.5 T0 clear 98.2 75.7 Agitation D4 Clear, few particles 96.2 N / A 40°C-D13 Small particles 94.9 64.8 07 HIS6.0 T0 clear 98.3 74.6 Agitation D4 large number of particles 96.2 N / A 40°C-D13 medium particles 94.6 65.8 08 His6.5 TO clear 98.1 74.6 Agitation D4 severe opalescence 95.8 N / A 40°C-D13 Medium particles 94.3 62.3 09 CA5.5 TO clear 98.2 74.8 Agitation D4 Clear slightly opalescent N / AN / A. 40°C-D13 Fine particles 94.7 60.9 10 CA6.0 T0 clear 98.0 75.3 Agitation D4 evident opalescence, large quantity of particles N / AN / A 40°C-D13 Medium particles 94.6 61.5 11 CA6.5 T0 clear 97.9 74.6 Agitation D4 severe opalescence, large quantity of particles N / AN / A 40°C-D13 Small particles 95.0 64.4 12 PB6.0 T0 clear 98.0 74.4 Agitation D4 With particles N / AN / A 40°C-D13 Fine particles 94.3 63.0 13 PB6.5 T0 clear 97.9 74.7 Agitation D4 severe opalescence, large quantity of particles N / AN / A 40°C-D13 large particles 93.9 61.9 Note: N / A represents not detected, D represents the day and TO represents day 0. nccLLn / Lznz / e / YiAi Example test 11. Selection of excipients in formulations The h1705-008 formulations were prepared with a protein concentration of 100 mg / ml in 10 mM SA buffer (pH 5.0) comprising different types of excipients, as follows. In particular, the excipients were the following: 1) 0.1 mg / ml polysorbate 20 (PS20) 2) 0.1 mg / ml polysorbate 80 (PS80) 3) 50 mg / ml sucrose + 0.1 mg / ml PS80 4) 50 mg / ml trehalose + 0.1 mg / ml PS80 5) 50 mg / ml mannitol + 0.1 mg / ml PS80 6) 50 mg / ml sorbitol + 0.1 mg / ml PS80 7) 8 mg / ml arginine (Arg) + 0.1 mg / ml PS80 8) 8 mg / ml lysine (Lys) + 0.1 mg / ml PS80 9) 8 mg / ml glycine (Gly) + 0.1 mg / ml PS80 10) 8 mg / ml methionine (Met) + 0.1 mg / ml PS80 11)8 mg / ml proline (Pro) + 0.1 mg / ml PS80 12) 8 mg / ml of sodium chloride (NaCl) + 0.1 mg / ml of PS80. Each formulation was filtered, loaded, applied with a cap, and capped for use. The samples were subjected to a forced degradation experiment at 40°C; the results show (Table 20): there is no significant difference in the SEC test results. CE and CIEF between each sample group, Arg / Lys / NaCl groups have the poorest appearance and there are no significant differences between other groups. Sucrose, trehalose, mannitol, sorbitol, glycine, proline and methionine have favorable effects on protein stability. Table 20. Results of the excipient screening nccLLn / Lznz / e / YiAi Lot No. Condition Appearance SEC (%) Neutral peak ¡CIEF (%) EC-SDS (%) 1 DO clear 96.6 75.16 95.05 40°C D12 clear 94.29 59.24 93.53 2 DO clear 96.64 74.39 94.96 40°C D12 clear 94.33 58.99 93.31 3 DO clear 96.59 74.51 95.44 40°C D12 clear 94.33 58.33 93.3 4 DO clear 96.63 74.87 95.26 40°C D12 clear 94.43 58.14 93.68 5 DO clear 96.63 74.8 95.33 40°C D12 clear 94.47 59.79 93.43 6 DO clear 96.63 74.25 95.29 40°C D12 clear 94.39 58.04 93.41 7 DO clear and slight opalescence 96.6 74.31 95.19 40°C D12 opalescence, large quantity of particles 94.27 59.18 93.45 8 DO clear and slight opalescence 96.56 74.7 95.2 40°C D12 opalescence 94.26 59.62 93.56 9 DO clear 96.54 73.77 95.47 40°C D12 clear 94.38 58.82 93.56 10 DO clear 96.56 75.68 95.5 40°C D12 clear 94.45 59.57 93.71 11 DO clear 96.43 75.22 95.02 40°C D12 clear 94.47 61.1 95.32 12 DO Clear, opalescence 96.51 73.63 95.02 40°C D12 opalescence, large number of particles 93.99 60.51 93.21 Note: D represents a day. Example test 12. Surfactant detection The h1705-008 formulations were prepared comprising SA 10 mM pH 5.5, 70 mg / ml sucrose, 0.4 mg / ml PS20 or PS80, with a protein concentration of 100 mg / ml. The samples were placed at 4°C to investigate stability. The results are shown in Table 21. The results show that the PS80 group exhibits a clear appearance and no significant change in SEC, CE, and iCIEF at 4°C for 4 months, indicating favorable stability; whereas the PS20 group shows a large number of particles. Therefore, PS80 is better than PS20. Furthermore, the addition of PS80 to the formulation has a better stabilizing effect on h 1705-008, and the formulation's stability is improved. Table 21. Stability results of h1705-008 at 4°C nccLLn / Lznz / e / YiAi Group Time (M) Appearance SEC (%) CE-SDS non-reducing (%) Neutral peak iCIEF (%) PS80 0 clear 97.2 94.4 71.2 4 clear 97.6 95.0 71.6 PS20 0 clear 97.1 94.3 72.7 4 large amount of particles N / A / N / A Note: M represents month; N / A represents not detected. Test Example 13. Design and Selection of the DOE Formulation The Design of Experiments (DOE) was performed using 10 mM acetate buffer (AA) pH, protein concentration, and Tween concentration as variables. A series of formulations were designed based on the following factors and levels: pH from 5.0 to 5.8, PS80 concentration from 0.2 to 0.6 mg / mL, and h1705-008 antibody concentration from 80 to 120 mg / mL. The formulations are shown in Table 22. The samples were subjected to forced degradation at a high temperature of 40°C. Appearance, SEC, non-reducing EC, and CIEF were used as evaluation indicators. The results are shown in Table 23. Table 22. Screening experiment and design for DOE formulations Lot No. pH PS80 (mg / mL) Protein Content (mg / mL) 1 5.8 0.2 80 2 5.4 0.6 100 3 5.4 0.4 80 4 5.0 0.2 80 5 5.4 0.2 100 6 5.8 0.6 80 7 5.0 0.2 120 8 5.0 0.6 80 9 5.8 0.6 120 10 5.4 0.4 120 11 5.4 0.4 100 12 5.0 0.6 120 13 5.8 0.2 120 14 5.0 0.4 100 15 5.8 0.4 100 16 5.4 0.4 100 nccLLn / Lznz / e / YiAi Table 23. Results of the screening experiment of DOE formulations Lot No. Condition Appearance SEC (%) Neutral peak ¡CIEF (%) Non-reducing EC-SDS (%) 1 DO clear 98.9 63.9 93.8 40°C D15 clear 97.8 49.9 92.5 2 DO clear 98.9 64.5 93.8 40°C D15 clear 97.5 49.8 92.9 3 DO clear 98.9 64.3 94.0 40°C D15 clear 97.6 49.6 92.2 4 DO clear 99.0 63.6 93.9 40°C D15 clear 97.7 50.3 92.4 5 DO clear 98.9 63.4 93.8 40°C D15 clear 97.6 49.7 92.2 6 DO clear 98.9 63.5 93.9 40°C D15 clear 97.7 51.5 92.4 7 Clear 98.9 64.3 93.7 40°C D15 Clear 97.6 49.2 92.4 8 Clear 99.0 64.4 93.9 40°C D15 Clear 97.7 49.6 92.3 9 Clear 98.7 66.2 93.8 40°C D15 Clear 97.3 50.6 92.4 10 Clear 98.8 64.1 93.9 40°C D15 Clear 97.4 50.9 92.3 11 Clear 98.8 64.5 94.0 40°C D15 Clear 97.5 50.6 92.4 12 Clear 99.0 64.4 93.7 40°C D15 Clear 97.6 49.9 92.3 13 D clear 98.8 63.7 93.8 40°C D15 clear 97.4 50.8 92.6 14 D clear 99.0 63.6 93.9 40°C D15 clear 97.7 50.9 92.1 15 D clear 98.8 63.0 93.6 40°C D15 clear 97.6 51.1 92.4 16 D clear 98.8 64.9 93.8 40°C D15 clear 97.5 50.0 92.3 nccLLn / Lznz / e / YiAi Note: D stands for el día. The results show that the appearance of each formulation is clear; SEC, CE, and CIEF decrease within an acceptable range, at <2%, <2%, and approximately 14%, respectively; and the stability of one formulation is favorable; therefore, formulation 5 comprises a protein concentration of 80-120 mg / ml, 0.2-0.6 mg / ml of PS80, pH 5.0-5.8. The optimum formulation is: 100 mg / ml of protein, 0.4 mg / ml of PS80, pH 5.5. Example test 14. Stability test The h 1705-008 formulations were prepared comprising 10 mM AA pH 5.5, 70 mg / ml sucrose, and 0.4 mg / ml PS80, with a protein concentration of 100 mg / ml; and the samples were subjected to stability investigation at 4°C and 2°C. The results are shown in Table 24. The results show that under high-temperature conditions, SEC, CE, and CIEF decrease slightly in formulation h1705-008, but the decrease is within an acceptable range; there is no significant change in any of the indicators under other conditions. The formulation has favorable stability and can ensure the stability of h1705-008 at 4°C for 6 months. Table 24. Stability results of h1705-008 at 25°C and 4°C Condition Appearance SEC (%) Neutral peak iCIEF (%) CE-SDS non-reducing (%) T0 clear 98.0 59.8 94.5 25°C - M3 clear 97.6 55.2 93.4 25°C - M6 clear 96.7 51.7 91.7 4°C - M3 clear 98.5 59.7 94.6 4°C - M6 clear 98.7 60.0 94.0 nccLLn / Lznz / e / YiAi Note: M represents the month. Example test 15. Ionic strength screening Formulations of h 1705-008 were prepared, comprising a protein concentration of 100 mg / ml, 70 mg / ml of sucrose, and 0.4 mg / ml of PS80 in (sodium) acetate buffer with different ionic strengths. The pH of the buffers used for the exchange and the pH of the final formulations were measured. The results are shown in Table 25. The results show that the higher the ionic strength, the lower the pH drift. When the ionic strength is 30 mM, the pH drift is less than 0.1. Table 25. pH results of formulations with different ionic strengths Ionic Strength Buffer - pH Stock Solution of Formation - pH ΔρH 10mM 5.50 5.71 0.21 20mM 5.50 5.66 0.16 30mM 5.50 5.59 0.09 Example test 16. Screening of saccharide concentration The h 1705-008 formulations were prepared, comprising a protein concentration of 100 mg / ml, AA 30 mM pH 5.5, and PS80 0.4 mg / ml in the following buffers comprising sucrose at different concentrations. The osmotic pressure was determined. The results are shown in Table 26. The results show that the osmotic pressure is in an optimal isotonic range of 290 to 310 mosm, when the saccharide concentration is 70 to 75 mg / ml; according to the osmotic pressure data of groups of 70 mg / ml and 73 mg / ml, the osmotic pressure reaches the best value of approximately 300 mosm, when the saccharide concentration is 72 mg / ml. Table 26. Comparison of osmotic pressure in h1705-008 formulations with different concentrations of saccharides Saccharide concentration (mg / ml) 70 73 75 Osmotic pressure (mosm) 290 306 310 nccLLn / Lznz / e / YiAi Example test 17. Stability test of formulations Formulations of h 1705-008, comprising a protein concentration of 100 mg / ml, 30 mM AA pH 5.5, 72 mg / ml sucrose, and 0.4 mg / ml PS80, were prepared to investigate stability at 4°C and 25°C. The results are shown in Table 27. The results show that SEC, CE, and IEC decrease slightly in formulation h1705-008 under high-temperature conditions, but the decrease is within an acceptable range. There is no significant change in any of the indicators at 4°C, indicating that the formulations have favorable stability. Table 27. Stability of h1705-008 formulations Condition Appearance SEC (%) Neutral peak IEC (%) CE-SDS non-reducing (%) T0 clear 98.4 63.5 97.6 25°C - M3 N / A 96.8 55.0 96.5 4°C - M3 clear 98.4 61.9 97.3 Note: M represents the month, T represents the time, N / A represents not determined. Test Example 18. Additional Optional Formulations Furthermore, the present invention also provides additional formulations for anti-IL-5 antibody pharmaceutical formulations, comprising but not limited to: (1) 1 mg / ml anti-IL-5 antibody (h1705-008), 72 mg / ml sucrose, 0.4 mg / ml polysorbate 80 and 10 mM acetic acid-sodium acetate buffer at pH 5.5; (2) 100 mg / ml anti-IL-5 antibody (h1705-008), 72 mg / ml sucrose, 0.4 mg / ml polysorbate 80 and 20 mM acetic acid-sodium acetate buffer at pH 5.5; (3) 120 mg / ml anti-IL-5 antibody (h1705-008), 72 mg / ml sucrose, 0.4 mg / ml polysorbate 80 and 40 mM acetic acid-sodium acetate buffer at pH 5.5; (4) 100 mg / ml anti-IL-5 antibody (h1705-008), 80 mg / ml sucrose, 0.6 mg / ml polysorbate 80 and 30 mM acetic acid-sodium acetate buffer at pH 5.0; (5) 80 mg / ml anti-IL-5 antibody (h1705-008), 75 mg / ml sucrose, 0.6 mg / ml polysorbate 80 and 20 mM acetic acid-sodium acetate buffer at pH 5.4; (6) 100 mg / ml anti-IL-5 antibody (h1705-008), 80 mg / ml sucrose, 0.4 mg / ml polysorbate 80 and 30 mM acetic acid-sodium acetate buffer at pH 5.5; (7) 90 mg / ml anti-IL-5 antibody (h1705-008), 74 mg / ml sucrose, 0.5 mg / ml polysorbate 80 and 25 mM acetic acid-sodium acetate buffer at pH 5.6; (8) 90 mg / ml anti-IL-5 antibody (h1705-008), 76 mg / ml sucrose, 0.3 mg / ml polysorbate 80 and 35 mM acetic acid-sodium acetate buffer at pH 5.4; (9) 80 mg / ml anti-IL-5 antibody (h1705-008), 72 mg / ml sucrose, 0.4 mg / ml polysorbate 80 and 30 mM acetic acid-sodium acetate buffer at pH 5.6; (10) 100 mg / ml anti-IL-5 antibody (h1705-008), 72 mg / ml sucrose, 0.4 mg / ml polysorbate 80 and 40 mM acetic acid-sodium acetate buffer at pH 5.5; (11) 100 mg / ml anti-IL-5 antibody (h1705-008), 80 mg / ml sucrose, 0.4 mg / ml polysorbate 80 and 40 mM acetic acid-sodium acetate buffer at pH 5.5. Experimental results show that the IL-5 antibody formulations described above have favorable stability and can be applied to the preparation of IL-5 antibody agents. Example test 19. Illofilization of anti-IL-5 antibody formulations Antibody formulations h1705-008 were prepared, comprising 72 mg / ml sucrose, 0.4 mg / ml polysorbate 80, and a concentration of 100 mg / ml anti-IL-5 antibody in 30 mM acetic acid-sodium acetate buffer at pH 5.5. The antibody was loaded into 6 ml vials at a concentration of 2.15 ml / vial and placed in a lyophilization chamber for freeze-drying. The freeze-drying process comprises pre-freezing, primary drying, and secondary drying. After freeze-drying, the vials were vacuum-sealed and capped. The reconstituted samples were compared to the pre-freeze-dried counterparts. The results show that the reconstituted solutions can maintain favorable performance similar to that of the liquid formulations. nccLLn / Lznz / e / YiAi Table 28. Lyophilization steps for formulations Process parameters for lyophilization: Set temperature (°C) Degree of vacuum (mBar) Pre-freezing 5 N / A -45 N / A Primary drying -27 0.1 Secondary drying 25 0.1 25 0.01 Note: N / A means that the table was not applicable.

Claims

1. A pharmaceutical composition comprising an anti-IL-5 antibody or an antigen-binding fragment thereof, a buffer and a surfactant, wherein the buffer is any selected from the group consisting of acetic acid-sodium acetate, succinic acid-sodium succinate buffer, histidine hydrochloride and citric acid-sodium citrate, preferably acetic acid-sodium acetate buffer or succinic acid-sodium succinate buffer; wherein the anti-IL-5 antibody or its antigen-binding fragment comprises a heavy chain variable region and a light chain variable region selected from the group consisting of i) to vi): i) a heavy chain variable region comprising HCDR1, HCDR2 and HCDR3 as shown in the amino acid sequence SEQ ID NO: 16, 17 and 18, respectively, and a light chain variable region comprising LCDR1, LCDR2 and LCDR3 as shown in the amino acid sequence SEQ ID NO: 19, 20 and 21, respectively;(i) a heavy chain variable region comprising HCDR1, HCDR2 and HCDR3 as shown in the amino acid sequence SEQ ID NO: 22, 23 and 24, respectively, and a light chain variable region comprising LCDR1, LCDR2 and LCDR3 as shown in the amino acid sequence SEQ ID NO: 25, 26 and 27, respectively; (ii) a heavy chain variable region comprising HCDR1, HCDR2 and HCDR3 as shown in the amino acid sequence SEQ ID NO: 28, 29 and 30, respectively, and a light chain variable region comprising LCDR1, LCDR2 and LCDR3 as shown in the amino acid sequence SEQ ID NO: 31, 32 and 33, respectively; iv) a heavy chain variable region comprising HCDR1, HCDR2 and HCDR3 as shown in the amino acid sequence SEQ ID NO: 34, 35 and 36, respectively, and a light chain variable region comprising LCDR1, LCDR2 and LCDR3 as shown in the amino acid sequence SEQ ID NO: 37, 38 and 39, respectively;(v) a heavy chain variable region comprising HCDR1, HCDR2 and HCDR3 as shown in the amino acid sequence SEQ ID NO: 40, 41 and 42, respectively, and a light chain variable region comprising LCDR1, LCDR2 and LCDR3 as shown in the amino acid sequence SEQ ID NO: 43, 44 and 45, respectively; and (vi) a heavy chain variable region comprising HGDR1, HCDR2 and HGDR3 as shown in the amino acid sequence SEQ ID NO: 34, 82 and 36, respectively, and a light chain variable region comprising LCDR1, LCDR2 and LCDR3 as shown in the amino acid sequence SEQ ID NO: 37, 38 and 39, respectively.

2. The pharmaceutical composition according to claim 1, wherein the pH of the buffer is from approximately 5.0 to approximately 6.5, preferably from approximately 5.0 to approximately 5.8 and most preferably from approximately 5.

5. nccLLn / Lznz / e / YiAi 3. The pharmaceutical composition according to claim 1 or 2, wherein the buffer concentration is from approximately 10 mM to approximately 40 mM, preferably from approximately 20 mM to approximately 30 mM.

4. The pharmaceutical composition according to any one of claims 1 to 3, wherein the concentration of the anti-IL-5 antibody or the antigen-binding fragment thereof is from approximately 1 mg / ml to approximately 120 mg / ml, preferably from approximately 80 mg / ml to approximately 120 mg / ml, and most preferably approximately 100 mg / ml.

5. Pharmaceutical composition according to any of claims 1 to 4, wherein the surfactant is polysorbate 80.

6. The pharmaceutical composition according to claim 5, wherein the concentration of polysorbate 80 is from approximately 0.1 mg / ml to approximately 0.6 mg / ml, preferably from approximately 0.2 mg / ml to approximately 0.6 mg / ml, and more preferably from approximately 0.4 mg / ml.

7. The pharmaceutical composition according to any one of claims 1 to 6, further comprising a stabilizer, wherein the stabilizer is a saccharide or an amino acid, wherein the saccharide is selected from the group consisting of sucrose, trehalose, mannitol and sorbitol, preferably sucrose; wherein the amino acid is selected from the group consisting of glycine, methionine and proline.

8. The pharmaceutical composition according to claim 7, wherein the concentration of the saccharide is from approximately 50 mg / ml to approximately 80 mg / ml, preferably from approximately 70 mg / ml to approximately 75 mg / ml, and most preferably from approximately 72 mg / ml.

9. Pharmaceutical composition according to claim 7, wherein the concentration of the amino acid is approximately 8 mg / ml.

10. The pharmaceutical composition according to any one of claims 1 to 9, comprising the following components: from approximately 1 mg / ml to approximately 120 mg / ml of the anti-IL-5 antibody or the antigen-binding fragment thereof; acetic acid-sodium acetate buffer from approximately 10 mM to approximately 40 mM, the pH being from approximately 5.0 to approximately 6.5; and from approximately 0.1 mg / ml to approximately 0.6 mg / ml of polysorbate 80.

11. The pharmaceutical composition according to any one of claims 1 to 9, comprising: approximately 80 mg / ml to approximately 120 mg / ml of the anti-IL-5 antibody or the antigen-binding fragment thereof, sodium acetate acetic acid buffer of approximately 10 mM to approximately 30 mM, pH of approximately 5.0 to approximately 5.8, approximately 0.2 mg / ml to approximately 0.6 mg / ml of polysorbate 80, and approximately 70 mg / ml to approximately 80 mg / ml of sucrose; Preferably, the pharmaceutical composition comprises: approximately 100 mg / ml of anti-IL-5 antibody or the antigen-binding fragment thereof, approximately 30 mM of acetic acid-sodium acetate buffer, pH approximately 5.5, approximately 0.4 mg / ml of polysorbate 80, and approximately 72 mg / ml of sucrose.

12. Pharmaceutical composition according to any of claims 1 to 11, wherein the anti-IL-5 antibody or its antigen-binding fragment is a murine antibody, a chimeric antibody, or a humanized antibody.

13. The pharmaceutical composition according to claim 12, wherein the humanized anti-IL-5 antibody comprises a heavy chain variable region as shown in SEQ ID NO: 49, 57, 63, 69 or 75 or a variant thereof; the variant comprising from 1 to 10 reverse amino acid mutations in the sequence of the heavy chain variable region as shown in SEQ ID NO: 49, 57, 63, 69 or 75, respectively.

14. The pharmaceutical composition according to claim 13, wherein the variant is a variant as shown in any of the following: i) a variant comprising one or more reverse amino acid mutations selected from the group consisting of S49T, V93T and K98S in the variable region of the heavy chain as shown in SEQ ID NO: 49; ii) a variant comprising one or more reverse amino acid mutations selected from the group consisting of S49T, V93T and K98T in the variable region of the heavy chain as shown in SEQ ID NO: 57; iii) a variant comprising one or more reverse amino acid mutations selected from the group consisting of R38K, M48I, R67K, V68A, M70L, R72V, T74K and L83F in the variable region of the heavy chain as shown in SEQ ID NO: 63;(iv) a variant, comprising one or more reverse amino acid mutations selected from the group consisting of F29I, R38K, V48I, R72A and T97F in the heavy chain variable region as shown in SEQ ID NO: 69, and / or N55V mutation in HCDR2; (ov) a variant, comprising one or more reverse amino acid mutations selected from the group consisting of R38K, M48I, R67K, V68A, R72A, T74K, M81L, L83F and D89E in the heavy chain variable region as shown in SEQ ID NO:

75.

15. The pharmaceutical composition according to claim 14, wherein the humanized anti-IL-5 antibody comprises: a heavy chain variable region as shown in SEQ ID NO: 50 or 51; or a heavy chain variable region as shown in SEQ ID NO: 58 or 59; or a heavy chain variable region as shown in any one selected from the group consisting of SEQ ID NO: 64, 65 and 66; or a heavy chain variable region as shown in SEQ ID NO: 70 or 71; or a heavy chain variable region as shown in any one selected from the group consisting of SEQ ID NO: 76, 77, 78 and 79.

16. The pharmaceutical composition according to claim 12, wherein the humanized anti-IL-5 antibody comprises a light chain variable region as shown in SEQ ID NO: 46, 54, 60, 67 or 72, or a variant thereof; the variant comprising reverse mutations of 1 to 10 amino acids in the light chain variable region as shown in SEQ ID NO: 46, 54, 60, 67 or 72.

17. The pharmaceutical composition according to claim 16, wherein the variant is a variant as shown in any of the following: i) a variant comprising one or more reverse amino acid mutations selected from the group consisting of A43S, L47V, G66R, T69S, F71Y and Y87F in the light chain variable region as shown in SEQ ID NO: 46; ii) a variant comprising one or more reverse amino acid mutations selected from the group consisting of A43S, L47M, F71Y and Y87F in the light chain variable region as shown in SEQ ID NO: 54; iii) a variant comprising one or more reverse amino acid mutations selected from the group consisting of E1D, I2T, I57V, V84T and Y86F in the light chain variable region as shown in SEQ ID NO: 60;(iv) a variant, comprising one or more reverse amino acid mutations selected from the group consisting of M4L, A42S, L45P and L46W in the light chain variable region as shown in SEQ ID NO: 67; (ov) a variant, comprising one or more reverse amino acid mutations selected from the group consisting of A43S, I48V and F71Y in the light chain variable region as shown in SEQ ID NO: 72.; 18. The pharmaceutical composition according to claim 17, wherein the humanized anti-IL-5 antibody comprises: a light chain variable region as shown in SEQ ID NO: 47 or 48; or a light chain variable region as shown in SEQ ID NO: 55 or 56; or a light chain variable region as shown in SEQ ID NO: 61 or 62; or a light chain variable region as shown in SEQ ID NO: 68; or a light chain variable region as shown in SEQ ID NO: 73 or 74.

19. Pharmaceutical composition according to claim 12, wherein the humanized anti-IL-5 antibody comprises: i) a heavy chain variable region as shown in any of SEQ IDs 49, 50 and 51 or having 95% sequence identity with any of SEQ IDs 49, 50 and 51; and a light chain variable region as shown in any of SEQ IDs 46, 47 and 48 or having 95% sequence identity with any of SEQ IDs 46, 47 and 48; ii) a heavy chain variable region as shown in any of SEQ IDs 57, 58 and 59 or having 95% sequence identity with any of SEQ IDs 57, 58 and 59; and a variable light chain region as shown in any of SEQ ID NO: 54, 55 and 56 or having a 95% sequence identity with any of SEQ ID NO: 54, 55 and 56;(ii) a heavy chain variable region as shown in any of SEQ IDs NO: 63, 64, 65 and 66 or having 95% sequence identity with any of SEQ IDs NO: 63, 64, 65 and 66; and a light chain variable region as shown in any of SEQ IDs NO: 60, 61 and 62 or having 95% sequence identity with any of SEQ IDs NO: 60, 61 and 62; (iv) a heavy chain variable region as shown in any of SEQ IDs NO: 69, 70 and 71 or having 95% sequence identity with any of SEQ IDs NO: 69, 70 and 71; and a light-chain variable region as shown in any of SEQ IDs NO: 67 and 68 or having a 95% sequence identity with any of SEQ IDs NO: 67 and 68; ov) a heavy-chain variable region as shown in any of SEQ IDs NO: 75, 76, 77, 78 and 79 or having a 95% sequence identity with any of SEQ IDs NO: 75, 76, 77, 78 and 79;and a light chain variable region as shown in any of SEQ ID NO: 72, 73 and 74 or having 95% sequence identity with any of SEQ ID NO: 72, 73 and 74; preferably, the humanized anti-IL-5 antibody comprises: a) the heavy chain variable region as shown in SEQ ID NO: 51 and the light chain variable region as shown in SEQ ID NO: 47; b) the heavy chain variable region as shown in SEQ ID NO: 65 and the light chain variable region as shown in SEQ ID NO: 62; c) the heavy chain variable region as shown in SEQ ID NO: 58 and the light chain variable region as shown in SEQ ID NO: 56; nccLLn / Lznz / e / YiAi d) the heavy chain variable region as shown in SEQ ID NO: 71 and the light chain variable region as shown in SEQ ID NO: 68; oe) the heavy chain variable region as shown in SEQ ID NO: 79 and the light chain variable region as shown in SEQ ID NO: 73.; 20. The pharmaceutical composition according to any one of claims 1 to 19, wherein the anti-IL-5 antibody comprises the constant region or regions of the human antibody; preferably comprising: a human antibody heavy chain constant region as shown in SEQ ID NO: 52 and a human antibody light chain constant region as shown in SEQ ID NO:

53.

21. Pharmaceutical composition according to claim 20, wherein the anti-IL-5 antibody comprises: i) a heavy chain as shown in SEQ ID NO: 83 and a light chain as shown in SEQ ID NO: 84; i) a heavy chain as shown in SEQ ID NO: 85 and a light chain as shown in SEQ ID NO: 86; j) a heavy chain as shown in SEQ ID NO: 87 and a light chain as shown in SEQ ID NO: 88; iv) a heavy chain as shown in SEQ ID NO: 89 and a light chain as shown in SEQ ID NO: 90; v) a heavy chain as shown in SEQ ID NO: 91 and a light chain as shown in SEQ ID NO:

92.

22. Pharmaceutical composition according to any of claims 1 to 21, wherein the anti-IL-5 antibody is a monoclonal antibody or an antigen-binding fragment thereof that competes for binding to human IL-5 with the anti-IL-5 antibody or the antigen-binding fragment thereof according to any of claims 1 to 21.

23. A method for preparing the pharmaceutical composition according to any one of claims 1 to 22, comprising a step of replacing the anti-IL-5 antibody stock solution or the antigen-binding fragment thereof with a buffer, wherein the buffer is preferably acetic acid-sodium acetate buffer.

24. A lyophilized formulation comprising the anti-IL-5 antibody or the antigen-binding fragment thereof, obtained by lyophilization of the pharmaceutical composition according to any one of claims 1 to 22; preferably, the lyophilization comprises the steps of pre-freezing, primary drying, and secondary drying, successively.

25. A reconstituted solution comprising the anti-IL-5 antibody or its antigen-binding fragment, wherein the reconstituted solution is obtained by reconstitution of the lyophilized formulation according to claim 24. nccLLn / Lznz / e / YiAi 26. An article comprising a container, wherein the container comprises the pharmaceutical composition according to any one of claims 1 to 22, or the lyophilized formulation according to claim 24, or the reconstituted solution according to claim 25.

27. A method for treating an IL-5-mediated disease, comprising administering a therapeutically effective amount of the pharmaceutical composition according to any of claims 1 to 22, or the lyophilized formulation according to claim 24, or the reconstituted solution according to claim 25, or the article according to claim 26, to a subject in need;where IL-5-mediated disease is preferentially selected from the group consisting of asthma, chronic pneumonia, allergic rhinitis, allergic bronchopulmonary aspergillosis 10, eosinophilia, Churg-Strauss syndrome, atopic dermatitis, onchocerciasis dermatitis, intermittent angioedema, eosinophilic myalgia syndrome, eosinophilic gastroenteritis, worm infection, Hodgkin's disease, nasal polyps, Loeffler's syndrome, urticaria, hypereosinophilic bronchitis, nodular arteritis, sinusitis, eosinophilic esophagitis, allergic eosinophilic esophagitis, allergic conjunctivitis, onchocerciasis dermatitis, endometriosis 15 and spheroid-dependent bronchitis.