ANTIBODY CAPABLE OF BINDING TO THYMIC STROMAL LYMPHOPOIETIN AND ITS USE.

Abstract

An antibody capable of binding to thymic stromal lymphopoietin and its use are described. An anti-TSLP antibody, comprising a murine antibody, a chimeric antibody, and a humanized antibody of the light-chain and heavy-chain variable regions of the anti-TSLP antibody and antigen-binding fragments thereof, or a pharmaceutically acceptable salt or solvent compound thereof, and its use as a medicament for treating asthma, particularly its use in the preparation of a drug for treating TSLP-positive diseases or conditions, are described.

Description

ANTIBODY CAPABLE OF BINDING TO THYMIC STROMAL LYMPHOPOIETIN AND ITS USE Field of Invention The present invention relates to the field of antibody agents. Specifically, the present invention relates to anti-TSLP antibody agents and their use. Background of the Invention The statements in this document provide background information relating to the present invention only and do not necessarily constitute prior art. Asthma is a serious, chronic inflammatory disease of the airways. There are approximately 334 million asthma sufferers worldwide, and around 30 million in China, where the mortality rate is much higher than in developed countries. As the environment deteriorates and air pollution increases, more people may suffer from this disease, which poses a serious threat to their lives and health. Thymic stromal lymphopoietin (TSLP) is an epithelial cell-derived cytokine produced in response to pro-inflammatory stimuli. It primarily promotes allergic inflammation through its activity on dendritic cells and mast cells. TSLP is a type of interleukin-7 (IL-7) similar cytokine, first discovered in conditioned mouse thymic stromal cell medium. TSLP is mainly expressed in pulmonary, cutaneous, and intestinal epithelial cells. TSLP consists of four α helices and two AB and CD loops. The molecule contains three disulfide bonds consisting of six cysteines, two N-glycosylation sites, and has a molecular weight of approximately 15–20 kDa. The TSLP receptor is a complex consisting of two moieties: TSLPR and IL7Ra. TSLP first binds to TSLPR with relatively low affinity, then recruits IL7Ra binding with high affinity, and finally activates the stat5 signaling pathways, etc., which leads to the maturation of CD cells and the differentiation of T cells. Myeloid dendritic cells (mCDs) are the primary effector cells of TSLP. TSLP acts on immature mCDs, which secrete the cytokines IL-8, eotaxin-2, TARC, and CDM, while also expressing high levels of OX40L. In the absence of IL-12, OX40L binds to native CD4+ T cells, leading to their differentiation into Th2 cells. Th2 cells then secrete Th2 cytokines such as IL-5, IL-4, IL-9, and TNF, inducing a Th2 inflammatory response in the body. Furthermore, TSLP can also induce mCDs to produce the cytokine IL-8, which in turn recruits neutrophils, leading to neutrophilic innate immune inflammation. TSLP can also induce CDs to produce eotaxin-2, which recruits eosinophils and works together with IL5 to rapidly put the body into the inflammatory state of eosinophil infiltration.TSLP also acts on mast cells and natural killer cells and mediates innate inflammation by inducing the production of IL-4, IL-6, IgE, etc. In short, TSLP can cause both innate and Th2 inflammation simultaneously, which in turn increases tissue mucus, remodels the airways, leading to tracheal stenosis and severe cellular fibrosis. This inflammation gradually progresses to the three major allergic diseases: asthma, dermatitis, and allergic rhinitis. Therefore, blocking TSLP is a potentially effective strategy for treating diseases such as asthma, allergic dermatitis, and others. Currently, anti-TSLP antibodies are described in documents WO2008155365, WO2009035577, WO2011056772, WO2016142426, and WO2017004149. However, no corresponding antibody is commercially available. Therefore, further development of an effective drug to treat TSLP-related diseases is necessary. Summary of the Invention The present invention provides an anti-TSLP antibody. In some embodiments, the anti-TSLP antibody as described above comprises an antibody heavy chain variable region and a light chain variable region, wherein: i) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 14, SEQ ID NO: 15 and SEQ ID NO: 47, respectively, and the light chain variable region comprises LCDR1, LCDR2 as shown in SEQ ID NO: 17, SEQ ID NO: 18, respectively, and LCDR3 as shown in SEQ ID NO: 48 or 55; where, the sequence of SEQ ID NO: 47 is EDYDYDGYAMDX1, the sequence of SEQ ID NO: 48 is QQWSSX2RT, the sequence of SEQ ID NO: 55 is QQSDX3X4RX5, where X1 is H or Y, X2 is N or D, X3 is N or S, X4 is V or G, X5 is G or E; or (i) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 20, SEQ ID NO: 21 and SEQ ID NO: 22, respectively, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 76, SEQ ID NO: 24 and SEQ ID NO: 25, respectively; frnofrLn / Lznz / e / YiAi where, the sequence of SEQ ID NO: 76 is RASESVDX6SGLSFMH, where, X6 is selected from N, S or Q; or ii) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 26, SEQ ID NO: 96 and SEQ ID NO: 28, respectively, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 29, SEQ ID NO: 118 and SEQ ID NO: 31, respectively; where, the sequence of SEQ ID NO: 96 is VIDPGX7X8DTNYNE, the sequence of SEQ ID NO: 118 is X9VX10X11X12X13T, where X7 is selected from N, Q and V, X8 is G or V; X9 is Y or E, X10 is selected from S, D and E, Xn is selected from N, Q, D and E, X12 is selected from H, Y, D and E, Xi3 is E or Y; or iv) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 32, SEQ ID NO: 33 and SEQ ID NO: 34, respectively, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 35, SEQ ID NO: 36 and SEQ ID NO: 37, respectively. In some embodiments, the anti-TSLP antibody as described above comprises a heavy chain variable region and a light chain variable region, where: (i) the variable heavy chain region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 14, SEQ ID NO: 15 and SEQ ID NO: 16, respectively, and the variable light chain region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 17, SEQ ID NO: 18 and SEQ ID NO: 19, respectively; or (ii) the variable heavy chain region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 14, SEQ ID NO: 15 and SEQ ID NO: 45, respectively, and the variable light chain region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 17, SEQ ID NO: 18 and SEQ ID NO: 46, respectively; or (ii) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 14, SEQ ID NO: 15 and SEQ ID NO: 45, respectively, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 17, SEQ ID NO: 18 and SEQ ID NO: 53, respectively;or iv) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 14, SEQ ID NO: 15 and SEQ ID NO: 45, respectively, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 17, SEQ ID NO: 18 and SEQ ID NO: 54, respectively; or frnofrLn / Lznz / e / YiAi; (v) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 20, SEQ ID NO: 21 and SEQ ID NO: 22, respectively, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 23, SEQ ID NO: 24 and SEQ ID NO: 25, respectively; or (vi) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 20, SEQ ID NO: 21 and SEQ ID NO: 22, respectively, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 70, SEQ ID NO: 24 and SEQ ID NO: 25, respectively; or vii) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 20, SEQ ID NO: 21 and SEQ ID NO: 22, respectively, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 71, SEQ ID NO: 24 and SEQ ID NO: 25, respectively;or viii) the variable region of the heavy chain comprises HCDR1 and HCDR3 as shown in SEQ ID NO: 26, SEQ ID NO: 28, respectively, and HCDR2 as shown in SEQ ID NO: 27, 93, 94 or 95, and the light chain variable region comprises LCDR1 and LCDR3 as shown in SEQ ID NO: 29, SEQ ID NO: 31, respectively, and LCDR2 as shown in SEQ ID NO: 30, 108, 109, 110, 111, 112, 113, 114, 115, 116 or 117.; In some embodiments, the anti-TSLP antibody as described above comprises a heavy chain variable region and a light chain variable region, where: a) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 26, SEQ ID NO: 27 and SEQ ID NO: 28, respectively, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 29, SEQ ID NO: 30 and SEQ ID NO: 31, respectively; or (b) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 26, SEQ ID NO: 93 and SEQ ID NO: 28, respectively, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 29, SEQ ID NO: 30 and SEQ ID NO: 31, respectively; or c) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 26, SEQ ID NO: 94 and SEQ ID NO: 28, respectively, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 29, SEQ ID NO: 30 and SEQ ID NO: 31, respectively; or d) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 26, SEQ ID NO: 95 and SEQ ID NO: 28, respectively, and the light chain variable region frnofrLn / Lznz / e / YiAi comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 29, SEQ ID NO: 30 and SEQ ID NO: 31, respectively; or (e) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 26, SEQ ID NO: 27 and SEQ ID NO: 28, respectively, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 29, SEQ ID NO: 108 and SEQ ID NO: 31, respectively; or f) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 26, SEQ ID NO: 27 and SEQ ID NO: 28, respectively, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 29, SEQ ID NO: 109 and SEQ ID NO: 31, respectively; or (g) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 26, SEQ ID NO: 27 and SEQ ID NO: 28, respectively, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 29, SEQ ID NO: 110 and SEQ ID NO: 31, respectively; or (h) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 26, SEQ ID NO: 27 and SEQ ID NO: 28, respectively, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 29, SEQ ID NO: 111 and SEQ ID NO: 31, respectively; or (i) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 26, SEQ ID NO: 27 and SEQ ID NO: 28, respectively, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 29, SEQ ID NO: 112 and SEQ ID NO: 31, respectively; or (j) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 26, SEQ ID NO: 27 and SEQ ID NO: 28, respectively, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 29, SEQ ID NO: 113 and SEQ ID NO: 31, respectively; or (k) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 26, SEQ ID NO: 27 and SEQ ID NO: 28, respectively, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 29, SEQ ID NO: 114 and SEQ ID NO: 31, respectively; or I) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 26, SEQ ID NO: 27 and SEQ ID NO: 28, respectively, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 29, SEQ ID NO: 115 and SEQ ID NO: 31, respectively; or frnofrLn / Lznz / e / YiAi (m) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 26, SEQ ID NO: 27 and SEQ ID NO: 28, respectively, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 29, SEQ ID NO: 116 and SEQ ID NO: 31, respectively; or n) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 26, SEQ ID NO: 27 and SEQ ID NO: 28, respectively, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 29, SEQ ID NO: 117 and SEQ ID NO: 31, respectively. In some anti-TSLP antibody modalities as described above, the anti-TSLP antibody is a murine antibody, a chimeric antibody, or a humanized antibody. In some embodiments of the anti-TSLP antibody as described above, the anti-TSLP antibody comprises a framework region or regions derived from a human antibody, or the anti-TSLP antibody comprises a light chain variable region and / or a heavy chain variable region, selected from those described in (a), (b), (c) or (d) below: a) the variable region of the heavy chain comprises HCDR1 and HCDR2 as shown in SEQ ID NO: 14, SEQ ID NO: 15, respectively, and HCDR3 as shown in SEQ ID NO: 16 or 45, and the frame regions thereof comprise (s) at most 10 reverse mutations, preferably the reverse mutation being selected from one or more of 38K, 48I, 67A, 69L, 71V and 73K; and / or the variable region of the light chain comprises LCDR1 and LCDR2 as shown in SEQ ID NO: 17, SEQ ID NO: 18, respectively, and LCDR3 as shown in SEQ ID NO: 19, 46, 53 or 54, and the frame region comprises at most 10 amino acid reverse mutations, preferably the reverse mutation being selected from one or more of 46P, 47W, 58V, 70S and 71Y; b) the variable region of the heavy chain comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 20, SEQ ID NO: 21 and SEQ ID NO: 22, respectively, and the frame region thereof comprises (s) at most 10 reverse mutations, preferably the reverse mutation being selected from one or more of 2A, 27F, 38K, 39H, 48I, 67A, 69L, 71V and 76R; and / or the variable region of the light chain comprises LCDR2 and LCDR3 as shown in SEQ ID NO: 24, SEQ ID NO: 25, respectively, and LCDR1 as shown in SEQ ID NO: 23, 70 or 71, and the frame region(s) thereof comprise at most 10 amino acid reverse mutations, preferably the reverse mutation being one or more of 1D, 4L, 43P, 48L and 58I; c) the variable region of the heavy chain comprises HCDR1 and HCDR3 as shown in SEQ ID NO: 26, SEQ ID NO: 28, respectively, and HCDR2 as shown in frnofrLn / Lznz / e / YiAi SEQ ID NO: 27, 93, 94 or 95, and the frame region(s) thereof comprise a maximum of 10 reverse mutations, preferably the reverse mutation is selected from one or more of 27Y, 28A, 38K, 48I, 66K, 67A, 69L, 80I and 82bR; and / or the variable region of the light chain comprises LCDR1 and LCDR3 as shown in SEQ ID NO: 29, SEQ ID NO: 31, respectively, and LCDR2 as shown in SEQ ID NO: 30, 108, 109, 110, 111, 112, 113, 114, 115, 116 or 117, and the frame region(s) thereof comprise(s) at most 10 reverse mutations, preferably the reverse mutation being selected from one or more of 1S, 43S, 67Y and 73F; or d) the variable region of the heavy chain comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 32, SEQ ID NO: 33 and SEQ ID NO: 34, respectively, and the frame region thereof comprises (s) at most 10 reverse mutations, preferably the reverse mutation being selected from one or more of 38K, 48I, 66K, 67A, 69L, 71V, 73K and 78A; and / or the light chain variable region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 35, SEQ ID NO: 36 and SEQ ID NO: 37, respectively, and the frame region(s) thereof comprise at most 10 reverse mutations, preferably the reverse mutation being selected from one or more of 43S, 45Q, 48V, 66V and 70Q. In some embodiments, the anti-TSLP antibody as described above comprises a heavy chain variable region and a light chain variable region, where: (i) the heavy chain variable region has at least 90%, 92%, 94%, 95%, 96%, 97%, 98% or 99% sequence identity with the heavy chain variable region as shown in amino acid sequence SEQ ID NO: 6, 42, 43, 44 or 50, and the light chain variable region has at least 90%, 92%, 94%, 95%, 96%, 97%, 98% or 99% sequence identity with the light chain variable region as shown in amino acid sequence SEQ ID NO: 7, 38, 39, 40, 41, 49, 51 or 52;or ii) the heavy chain variable region has at least 90%, 92%, 94%, 95%, 96%, 97%, 98% or 99% sequence identity with the heavy chain variable region as shown in amino acid sequence SEQ ID NO: 8, 62, 63, 64, 65, 66, 67, 68 or 69, and the light chain variable region has at least 90%, 92%, 94%, 95%, 96%, 97%, 98% or 99% sequence identity with the light chain variable region as shown in amino acid sequence SEQ ID NO: 9, 56, 57, 58, 59, 60, 61, 72, 73, 74 or 75;or (ii) the heavy chain variable region has at least 90%, 92%, 94%, 95%, 96%, 97%, 98% or 99% sequence identity with the heavy chain variable region as shown in amino acid sequence SEQ ID NO: 10, 85, 86, 87, 88, 89, 90, 91, 92 or 97, and the light chain variable region has at least 90%, 92%, 94%, 95%, 96%, 97%, 98% or 99% sequence identity with the light chain variable region as shown in amino acid sequence SEQ ID NO: 11, 77, 78, 79, 80, 81, 82, 83, 84, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107 or 119;or iv) the heavy chain variable region has at least 90%, 92%, 94%, 95%, 96%, 97%, 98% or 99% sequence identity with the heavy chain variable region as shown in amino acid sequence SEQ ID NO: 12, 126, 127, 128, 129, 130, 131 or 132, and the light chain variable region has at least 90%, 92%, 94%, 95%, 96%, 97%, 98% or 99% sequence identity with the light chain variable region as shown in amino acid sequence SEQ ID NO: 13, 120, 121, 122, 123, 124 or 125.; In some forms of the anti-TSLP antibody as described above, the anti-TSLP antibody is a humanized antibody, comprising a frame region or regions derived from a human antibody or a variant of the frame region thereof, said variant of the frame region having at most 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 reverse amino acid mutations in the light chain frame region(s) and / or heavy chain frame region(s) of the human antibody, respectively. In some anti-TSLP antibody variants as described above, the frame region variant comprises selected reverse mutations from those described in (a), (b), (c) or (d) below: a) one or more amino acid reverse mutations selected from the group consisting of 46P, 47W, 58V, 70S and 71Y comprising the frame region or regions of the variable region of the light chain as shown in SEQ ID NO: 38, 49, 51 or 52, and / or one or more amino acid reverse mutations selected from the group consisting of 38K, 48I, 67A, 69L, 71V and 73K comprising the frame region of the variable region of the heavy chain as shown in SEQ ID NO: 42 or 50; b) one or more amino acid reverse mutations selected from the group consisting of 1D, 4L, 43P, 48L and 58I comprising the frame region(s) of the variable region of the light chain as shown in SEQ ID NO: 56, 59, 72, 73, 74 or 75, and / or one or more amino acid reverse mutations selected from the group consisting of 2A, 27F, 38K, 39H, 48I, 67A, 69L, 71V and 76R comprising the frame region(s) of the variable region of the heavy chain as shown in SEQ ID NO: 62; c) one or more amino acid reverse mutations selected from the group consisting of 1S, 43S, 67Y and 73F comprising the framework region or regions of the light chain variable region as shown in SEQ ID NO: 77, 81, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107 or 119, and / or one or more amino acid reverse mutations selected from the group consisting of 27Y, 28A, 38K, 48I, 66K, 67A, 69L, 80I and 82bR comprising the frnQfrtn / Lznz / e / YiAi framework region or regions of the heavy chain variable region as shown in SEQ ID NO: 85, 90, 91, 92 or 97; d) one or more amino acid reverse mutations selected from the group consisting of 43S, 45Q, 48V, 66V and 70Q comprising the framework region or regions of the variable region of the light chain as shown in SEQ ID NO: 120, and / or one or more amino acid reverse mutations selected from the group consisting of 38K, 48I, 66K, 67A, 69L, 71V, 73K and 78A comprising the framework region of the variable region of the heavy chain as shown in SEQ ID NO: 126. In some embodiments, the anti-TSLP antibody as described above comprises a heavy chain variable region and a light chain variable region, where: (i) the amino acid sequence of the heavy chain variable region is as shown in SEQ ID NO: 6, 42, 43, 44 or 50, and the amino acid sequence of the light chain variable region is as shown in SEQ ID NO: 7, 38, 39, 40, 41, 49, 51 or 52; or (ii) the amino acid sequence of the heavy chain variable region is as shown in SEQ ID NO: 8, 62, 63, 64, 65, 66, 67, 68 or 69, and the amino acid sequence of the light chain variable region is as shown in SEQ ID NO: 9, 56, 57, 58, 59, 60, 61, 72, 73, 74 or 75; or iii) the amino acid sequence of the variable region of the heavy chain is as shown in SEQ ID NO: 10, 85, 86, 87, 88, 89, 90, 91, 92 or 97, and the amino acid sequence of the variable region of the light chain is as shown in SEQ ID NO: 11, 77, 78, 79, 80, 81, 82, 83, 84, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107 or 119;or iv) the amino acid sequence of the variable region of the heavy chain is as shown in SEQ ID NO: 12, 126, 127, 128, 129, 130, 131 or 132, and the amino acid sequence of the variable region of the light chain is as shown in SEQ ID NO: 13, 120, 121, 122, 123, 124 or 125.; In some embodiments, the anti-TSLP antibody as described above comprises a heavy chain variable region and a light chain variable region as shown below: (a) the sequence of the heavy chain variable region is as shown in SEQ ID NO: 6, and the sequence of the light chain variable region is as shown in SEQ ID NO: 7; frnofrLn / Lznz / e / YiAi (b) the sequence of the heavy chain variable region is as shown in SEQ ID NO: 42, 43 or 44, and the sequence of the light chain variable region is as shown in SEQ ID NO: 39, 40 or 41; (c) the sequence of the heavy chain variable region is as shown in SEQ ID NO: 43, and the sequence of the light chain variable region is as shown in SEQ ID NO: 38; (d) the sequence of the heavy chain variable region is as shown in SEQ ID NO: 50, and the sequence of the light chain variable region is as shown in SEQ ID NO: 49, 51 or 52; (e) the sequence of the heavy chain variable region is as shown in SEQ ID NO: 8, and the sequence of the light chain variable region is as shown in SEQ ID NO: 9; (f) the sequence of the heavy chain variable region is as shown in SEQ ID NO: 62, 63, 64 or 65, and the sequence of the light chain variable region is as shown in SEQ ID NO: 56, 57 or 58; (g) the sequence of the heavy chain variable region is as shown in SEQ ID NO: 64, 66, 67, 68 or 69, and the sequence of the light chain variable region is as shown in SEQ ID NO: 59, 60 or 61; (h) the sequence of the heavy chain variable region is as shown in SEQ ID NO: 64, and the sequence of the light chain variable region is as shown in SEQ ID NO: 72 or 73; (i) the sequence of the heavy chain variable region is as shown in SEQ ID NO: 69, and the sequence of the light chain variable region is as shown in SEQ ID NO: 74; (j) the sequence of the heavy chain variable region is as shown in SEQ ID NO: 10, and the sequence of the light chain variable region is as shown in SEQ ID NO: 11; (k) the sequence of the heavy chain variable region is as shown in SEQ ID NO: 85, and the sequence of the light chain variable region is as shown in SEQ ID NO: 77, 78, 102 or 104; (I) the sequence of the heavy chain variable region is as shown in SEQ ID NO: 86 or 88, and the sequence of the light chain variable region is as shown in SEQ ID NO: 77 or 78; frnofrLn / Lznz / e / YiAi (m) the sequence of the heavy chain variable region is as shown in SEQ ID NO: 87, and the sequence of the light chain variable region is as shown in SEQ ID NO: 77, 78, 79, 81, 82, 83, 84, 98, 99, 100, 101, 103, 105, 106 or 107; (n) the sequence of the heavy chain variable region is as shown in SEQ ID NO: 89, and the sequence of the light chain variable region is as shown in SEQ ID NO: 79, 81, 82, 83 or 84; (o) the sequence of the heavy chain variable region is as shown in SEQ ID NO: 90, 91 or 92, and the sequence of the light chain variable region is as shown in SEQ ID NO: 78; (p) the sequence of the heavy chain variable region is as shown in SEQ ID NO: 97, and the sequence of the light chain variable region is as shown in SEQ ID NO: 119; (q) the sequence of the heavy chain variable region is as shown in SEQ ID NO: 12, and the sequence of the light chain variable region is as shown in SEQ ID NO: 13; (r) the sequence of the heavy chain variable region is as shown in SEQ ID NO: 127, 128, 129, 130, 131 or 132, and the sequence of the light chain variable region is as shown in SEQ ID NO: 120, 121, 123, 124 or 125; or (s) the sequence of the heavy chain variable region is as shown in SEQ ID NO: 132, and the sequence of the light chain variable region is as shown in SEQ ID NO: 125. In some anti-TSLP antibody formulations as described above, the combinations of the light chain variable region and the heavy chain variable region of the antibodies are shown below: Table 1. Combinations of the light and heavy chain variable regions of the humanized mAb3 antibodies frnofrLn / Lznz / e / YiAi VH Antibody (SEQ ID NO) VL (SEQ ID NO) hu3-01 42 39 hu3-02 42 40 hu3-03 42 41 hu3-04 43 38 hu3-05 43 39 hu3-06 43 40 hu3-07 43 41 hu3-08 44 39 hu3-09 44 40 hu3-10 44 41 hu3-11 50 49 hu3-12 50 51 hu3-13 50 52 frnofrLn / Lznz / e / YiAi Table 2. Combinations of the light and heavy chain variable regions of humanized mAb119 antibodies VH Antibody (SEQ ID NO) VL (SEQ ID NO) hui 19-01 62 56 hui 19-02 63 56 hui 19-03 64 56 hui 19-04 65 56 hui 19-05 62 57 hui 19-06 63 57 hui 19-07 64 57 hui 19-08 65 57 hui 19-09 62 58 hu119-10 63 58 hui 19-11 64 58 hu119-12 65 58 hu119-13 64 59 hu119-14 66 59 hu119-15 67 59 hu119-16 68 59 hu119-17 69 59 hu119-18 64 60 hu119-19 66 60 huí 19-20 67 60 huí 19-21 68 60 huí 19-22 69 60 huí 19-23 64 61 huí 19-24 66 61 huí 19-25 67 61 huí 19-26 68 61 huí 19-27 69 61 huí 19-28 64 72 huí 19-29 64 73 huí 19-30 69 74 Table 3. Combinations of the light and heavy chain variable regions of humanized mAb179 antibodies Antibody VH (SEQ ID NO) VL (SEQ ID NO) egg 79-01 85 77 egg 79-02 85 78 egg 79-03 86 77 egg 79-04 86 78 egg 79-05 87 77 egg 79-06 87 78 egg 79-07 87 79 huí 79-08 87 81 huí 79-09 87 82 hu179-10 87 83 huí 79-11 87 84 hu179-12 88 77 hu179-13 88 78 hu179-14 89 79 hu179-15 89 80 hu179-1 89 81 hu179-17 89 82 hu179-18 89 83 hu179-19 89 84 hu 179-20 90 78 hui 79-21 91 78 hui 79-22 92 78 hui 79-23 85 102 hui 79-24 85 104 hu 179-25 87 98 escaped 79-26 87 99 escaped 79-27 87 100 escaped 79-28 87 101 escaped 79-29 87 103 escaped 79-30 87 105 escaped 79-31 87 106 escaped 79-32 87 107 jumped 79-33 97 119 frnofrLn / Lznz / e / YiAi Table 4. Combinations of the light and heavy chain variable regions of the humanized mAb199 antibodies Antibody VH (SEQ ID NO) VL (SEQ ID NO) hu199-01 127 120 hu199-02 127 121 hu199-03 127 122 hu199-04 127 123 hu199-05 127 124 hu199-06 127 125 hu199-07 128 120 hu199-08 128 121 hu199-09 128 122 hu199-1 hu199-11 128 124 hu199-12 128 125 hu199-13 129 120 hu199-14 129 121 hu199-15 129 122 hu199-16 129 123 hu199-17 129 124 hu199-18 129 125 hu199-19 130 120 hu199-20 130 121 hu199-21 130 122 hu199-22 130 123 hu199-23 130 124 hu199-24 130 125 hu199-25 131 120 hu199-26 131 121 hu199-27 131 122 hu199-28 131 123 hu199-29 131 124 hu199-30 131 125 hu199-31 132 120 hu199-32 132 121 hu199-33 132 122 hu199-34 132 123 hu199-35 132 124 hu199-36 132 125 frnQfrLn / Lznz / e / γΐΛΐ In some embodiments of the anti-TSLP antibody as described above, the antibody further comprises antibody constant region(s); preferably, the heavy chain constant region of the antibody constant regions is selected from the group consisting of human IgG1, IgG2, IgG3, and IgG4 constant regions and conventional variants thereof, and the light chain constant region of the antibody constant regions is selected from the group consisting of human antibody κ and λ chain constant regions and conventional variants thereof; more preferably, the antibody comprises the heavy chain constant region as shown in the sequence SEQ ID NO: 133, and the constant region of the light chain as shown in the sequence SEQ ID NO: 134. In some forms, the anti-TSLP antibody as described above comprises a heavy chain and a light chain as shown below: (a) The amino acid sequence of the heavy chain is as shown in SEQ ID NO: 135 or has at least 90%, 92%, 94%, 95%, 96%, 97%, 98% or 99% sequence identity with the same, and the amino acid sequence of the light chain is as shown in SEQ ID NO: 136 or has at least 90%, 92%, 94%, 95%, 96%, 97%, 98% or 99% sequence identity with the same; (b) the amino acid sequence of the heavy chain is as shown in SEQ ID NO: 137 or has at least 90%, 92%, 94%, 95%, 96%, 97%, 98% or 99% sequence identity with the same, and the amino acid sequence of the light chain is as shown in SEQ ID NO: 138 or has at least 90%, 92%, 94%, 95%, 96%, 97%, 98% or 99% sequence identity with the same; (c) the amino acid sequence of the heavy chain is as shown in SEQ ID NO: 139 or has at least 90%, 92%, 94%, 95%, 96%, 97%, 98% or 99% sequence identity with the same, and the amino acid sequence of the light chain is as shown in SEQ ID NO: 140 or has at least 90% sequence identity with the same; or (d) the amino acid sequence of the heavy chain is as shown in SEQ ID NO: 141 or has at least 90%, 92%, 94%, 95%, 96%, 97%, 98% or 99% sequence identity with the same, and the amino acid sequence of the light chain is as shown in SEQ ID NO: 142 or has at least 90%, 92%, 94%, 95%, 96%, 97%, 98% or 99% sequence identity with the same. In some forms, the anti-TSLP antibody as described above comprises a heavy chain and a light chain as shown below: (a) the amino acid sequence of the heavy chain is as shown in SEQ ID NO: 135, and the amino acid sequence of the light chain is as shown in SEQ ID NO: 136; (b) the amino acid sequence of the heavy chain is as shown in SEQ ID NO: 137, and the amino acid sequence of the light chain is as shown in SEQ ID NO: 138; (c) the amino acid sequence of the heavy chain is as shown in SEQ ID NO: 139, and the amino acid sequence of the light chain is as shown in SEQ ID NO: 140; or (d) the amino acid sequence of the heavy chain is as shown in SEQ ID NO: 141, and the amino acid sequence of the light chain is as shown in SEQ ID NO: 142. In some modalities, the antibody is competitively bound to human TSLP with the anti-TSLP antibody as described above or an antigen-binding fragment thereof. frnofrLn / Lznz / e / YiAi In another aspect, the present invention also provides a nucleic acid molecule encoding the anti-TSLP antibody as described above. In another aspect, the present invention also provides an expression vector comprising the nucleic acid molecule as described above. In another aspect, the present invention also provides a host cell comprising the nucleic acid molecule as described above or the expression vector as described above, preferably the cell being a bacterial cell, a fungal cell, an animal insect cell, or a mammalian cell. In some embodiments, the present invention provides a method for preparing the TSLP antibody as described above. In some embodiments, the present invention provides a pharmaceutical composition containing a therapeutically effective amount of the anti-TSLP antibody as described above, or the nucleic acid molecule as described above, or the host cell as described above, as well as one or more acceptable pharmaceuticals, vehicles, diluents, buffers, or excipients. Preferably, the therapeutically effective amount means 0.1-3000 mg or 1-1000 mg of the anti-TSLP antibody as described above contained in a unit dose of the composition. In some embodiments, the present invention provides a method for the immunodetection or determination of TSLP in vitro or ex vivo, comprising a step of using the anti-TSLP antibody as described above. In some embodiments, the present invention provides for the use of the anti-TSLP antibody as described above in the preparation of reagents for the immunodetection of human TSLP. In some embodiments, the present invention provides an anti-TSLP antibody as described above for use in immunodetection or determination of TSLP. In some embodiments, the present invention provides a kit comprising the anti-TSLP antibody as described above. In some embodiments, the present invention provides for the use of the anti-TSLP antibody as described above, or the nucleic acid molecule as described above, or the host cell as described above, or the pharmaceutical composition as described above, in the preparation of a medicament for treating TSLP-related diseases, wherein TSLP-related diseases include, but are not limited to: asthma, idiopathic pulmonary fibrosis, atopic dermatitis, allergic conjunctivitis, allergic rhinitis, allergic sinusitis, urticaria, Netherton syndrome, eosinophilic esophagitis, food allergy, allergic diarrhea, eosinophilic gastroenteritis, allergic bronchopulmonary aspergillosis, allergic fungal sinusitis, chronic pruritus, cancer, breast cancer, colon cancer, lung cancer, ovarian cancer, prostate cancer, rheumatoid arthritis, chronic obstructive pulmonary disease, systemic sclerosis,Multiple sclerosis, keloidosis, ulcerative colitis, nasal polyposis, chronic eosinophilic pneumonia, eosinophilic bronchitis, celiac disease, Churg-Strauss syndrome, eosinophilic myalgia syndrome, hypereosinophilic syndrome, eosinophilic granulomatosis with polyangiitis, inflammatory bowel disease, scleroderma, interstitial lung disease, fibrosis caused by chronic hepatitis B or C, radiation-induced fibrosis, and fibrosis caused by wound healing. In some embodiments, the present invention provides a method for treating TSLP-related diseases, comprising administering to a subject a therapeutically effective amount of the anti-TSLP antibody as described above, or the nucleic acid molecule as described above, or the host cell as described above, or the pharmaceutical composition as described above;asthma, idiopathic pulmonary fibrosis, atopic dermatitis, allergic conjunctivitis, allergic rhinitis, allergic sinusitis, urticaria, Netherton syndrome, eosinophilic esophagitis, food allergy, allergic diarrhea, eosinophilic gastroenteritis, allergic bronchopulmonary aspergillosis, breast cancer, allergic fungal sinusitis, colon cancer, lung cancer, ovarian cancer, prostate cancer, rheumatoid arthritis, chronic obstructive pulmonary disease, systemic sclerosis, multiple sclerosis, keloidosis, ulcerative colitis, nasal polyposis, chronic eosinophilic pneumonia, eosinophilic bronchitis, celiac disease, Churg-Strauss syndrome, eosinophilic myalgia syndrome, hypereosinophilic syndrome, eosinophilic granulomatosis with polyangiitis, inflammatory bowel disease, scleroderma, interstitial lung disease, fibrosis caused by chronic hepatitis B or C, radiation-induced fibrosis and fibrosis caused by wound healing. In some embodiments, the present invention provides an anti-TSLP antibody for use as a medicament, wherein the anti-TSLP antibody is used in the treatment of TSLP-related diseases, wherein the TSLP-related disease includes, but is not limited to: asthma, idiopathic pulmonary fibrosis, atopic dermatitis, allergic conjunctivitis, allergic rhinitis, allergic sinusitis, urticaria, Netherton syndrome, eosinophilic esophagitis, food allergy, allergic diarrhea, eosinophilic gastroenteritis, allergic bronchopulmonary aspergillosis, allergic fungal pruritus, breast cancer, colon cancer, lung cancer, ovarian cancer, prostate cancer, rheumatoid arthritis, chronic obstructive pulmonary disease, systemic sclerosis, multiple sclerosis, keloidosis, ulcerative colitis, nasal polyposis, chronic eosinophilic pneumonia, eosinophilic bronchitis, celiac disease, Churg-Strauss syndrome, and other related conditions. eosinophilic myalgia,hypereosinophilic syndrome, eosinophilic granulomatosis with polyangiitis, inflammatory bowel disease, scleroderma, interstitial lung disease, fibrosis caused by chronic hepatitis B or C, radiation-induced fibrosis, and fibrosis caused by wound healing. Description of the Figures Figure 1: The result of the antibody blocking the binding activity of TSLP to the TSLP receptor. Figure 2: The result of the antibody blocking the binding activity of TSLP to the cell surface TSLP receptor. Figure 3: The antibody inhibits TSLP-induced BaF3 cell proliferation activity. Figure 4A shows the antibody activity of inhibiting TSLP-induced production of the chemokine TARC; Figure 4B shows the antibody activity of inhibiting TSLP-induced production of the chemokine OPG. Figure 5A shows the antibody activity of inhibiting the production of the Th2 cytokine IL-13; Figure 5B shows the antibody activity of inhibiting the production of the Th2 cytokine IL-4; Figure 5C shows the antibody activity of inhibiting the production of the Th2 cytokine TNF-α; Figure 5D shows the antibody activity of inhibiting the production of the Th2 cytokine IL-5. Detailed Description of the Invention Detailed description of the invention Terminology To facilitate understanding of the present invention, certain technical and scientific terms are specifically defined below. Unless clearly defined otherwise herein, all other technical and scientific terms used herein have the meanings commonly understood by those skilled in the art to which the present invention pertains. The three-letter codes and one-letter codes for amino acids used in the present invention are as described in J. biol. chem, 243, p. 3558 (1968). Thymic stromal lymphopoietin (TSLP) is a type I cytokine with four bundles of alpha helix, also known as an epithelial cell-derived cytokine produced in response to pro-inflammatory stimuli. It is closely related to interleukin-7 (IL-7), initiates allergic reactions by stimulating dendritic cells (DCs), and is an important factor in regulating the immune response in the human body. The term TSLP includes variants, isoforms, homologs, orthologs, and paralogs of TSLP. The antibody described in the present invention refers to an immunoglobulin. Generally, the intact antibody is a tetrapeptide chain structure composed of two identical heavy chains and two identical light chains linked by interchain disulfide bonds. The constant regions of immunoglobulin heavy chains exhibit different amino acid compositions and sort orders, thus exhibiting different antigenicity. Consequently, immunoglobulins can be divided into five types, or referred to as immunoglobulin isotypes, namely IgM, IgD, IgG, IgA, and IgE, and the corresponding heavy chains are the μ chain, δ chain, γ chain, o chain, and ε chain, respectively. The same type of Ig can be further divided into different subclasses based on differences in the amino acid composition of the hinge region and the number and position of the heavy chain disulfide bonds.For example, IgG can be divided into IgG1, IgG2, IgG3, and IgG4. The light chain is divided into a κ chain or a λ chain based on the difference in the constant region. Each of the five Ig types can have either a κ chain or a λ chain. The sequence of approximately 110 amino acids near the N-terminal end of the antibody's heavy and light chains varies considerably and is known as the variable region (Fv region); the remaining amino acid sequence near the C-terminal end is relatively stable and is the constant region. The variable region includes three hypervariable regions (HVRs) and four frame regions (FRs) with relatively conservative sequences. The three hypervariable regions determine antibody specificity and are also known as complementarity-determining regions (CDRs). Each light-chain (VL) and heavy-chain (VH) variable region consists of three CDRs and four FRs. The order from the amino terminus to the carboxy terminus is FR1, CDR1, FR2, CDR2, FR3, CDR3, FR4. The three light-chain CDRs are referred to as LCDR1, LCDR2, and LCDR3; the three heavy-chain CDRs are referred to as HCDR1, HCDR2, and HCDR3. The antibodies of the present invention include murine antibodies, chimeric antibodies, and humanized antibodies. The term "murine antibody" in the present invention refers to a monoclonal antibody against human TSLP prepared according to current knowledge and skill. During preparation, the TSLP antigen is injected into the test subject, and hybridomas expressing antibodies with the desired sequence or functional properties are then isolated. In a preferred embodiment of the present invention, the murine anti-TSLP antibody or its antigen-binding fragment may further comprise a constant region of murine κ, λ, or variants thereof, or further comprise a constant region of murine lgG1, lgG2, lgG3, or variants thereof. The term chimeric antibody refers to an antibody formed by fusing the variable region of a murine antibody with the constant region of a human antibody, which can alleviate the immune response induced by murine antibodies. Establishing a chimeric antibody requires first establishing a hybridoma that secretes specific murine monoclonal antibodies, then cloning the variable region gene from the murine hybridoma cells, and then cloning the constant region gene from the human antibody as needed. The murine variable region gene is then joined with the human constant region gene to form a chimeric gene, which is inserted into an expression vector. Finally, the chimeric antibody molecule is expressed in a eukaryotic or prokaryotic system.In a preferred embodiment of the present invention, the light chain of the TSLP chimeric antibody further comprises a light chain constant region of a human κ, λ chain or a variant thereof. The heavy chain of the TSLP chimeric antibody further comprises the heavy chain constant region of human lgG1, lgG2, lgG3, lgG4 or a variant thereof, preferably comprising the heavy chain constant region of lgG1, lgG2 or lgG4, or lgG1, lgG2 or lgG4 variants with amino acid mutations (e.g., L234A and / or L235A mutations, and / or S228P mutations). The term humanized antibody, also known as a CDR-grafted antibody, refers to an antibody produced by grafting murine CDR sequences into the framework of human antibody variable regions. In other words, it is an antibody produced using different types of human germline antibody framework sequences. It can overcome the heterogeneous reaction induced by chimeric antibodies because it carries a large number of murine protein components. Such framework sequences can be obtained from public DNA databases or published references that include germline antibody gene sequences. For example, germline DNA sequences of the human light chain and heavy chain variable region genes can be found in the VBase human germline sequence database (available online at www.mrccpe.com.ac.uk / vbase), as well as in Kabat, EA, et al.1991, Sequences of Proteins of Immunological Interest, 5th edition. To avoid the decrease in activity caused simultaneously by the decrease in immunogenicity, the framework sequence of the variable region of the human antibody can undergo minimal or reverse mutations to maintain activity. The humanized antibody of the present invention also includes humanized antibodies in which CDR affinity maturation is performed by yeast presentation. frnofrLn / Lznz / e / YiAi CDR grafting can result in reduced affinity of the produced antibody or its antigen-binding fragment for the antigen due to changes in the residues of the structure in contact with the antigen. Such interactions can result from somatic cell hypermutation. Therefore, it may still be necessary to graft such amino acids from the donor framework into the humanized antibody framework. Amino acid residues involved in the binding of non-human antigens and antibodies, or antigen-binding fragments thereof, can be identified by examining the sequence and structure of the variable region of the animal monoclonal antibody. Residues in the CDR donor framework that differ from the germline can be considered related.If the nearest germline cannot be determined, the sequence can be compared to the consensus sequence of a subclass of animal antibody sequences with a high percentage of similarity. The rare frame remnants are thought to be the result of somatic cell hypermutation and thus play an important role in binding. In one embodiment of the present invention, the antibody or antigen-binding fragment thereof may further comprise the light chain constant region of the human or murine κ, λ chain or a variant thereof, or further comprise the heavy chain constant region of human or murine lgG1, lgG2, lgG3, lgG4 or a variant thereof; preferably comprising the heavy chain constant region of human lgG1, lgG2 or lgG4, or variants of lgG1, lgG2 or lgG4 with amino acid mutations (e.g., L234A / L235A mutation, S228P mutation, YTE mutation). The conventional variant of the human antibody heavy chain constant region and the human antibody light chain constant region described in the present invention refers to the heavy chain constant region or light chain constant region variant described in the prior art and does not change the structure and function of the antibody variable region. Exemplary variants include heavy chain constant region variants of lgG1, lgG2, lgG3, or lgG4 with site-directed modifications and amino acid substitutions in the heavy chain constant region. Specific substitutions include YTE mutations, L234A and / or L235A mutations, S228P mutations, and / or mutations to obtain a knob-in-hole structure (resulting in the antibody heavy chain having a combination of knob-Fe and hole-Fc) known in the art.It has been confirmed that these mutations give the antibody new properties, but do not change the function of the antibody's variable region. Human antibody (HuMAb), human-derived antibody, fully human antibody, and all-human antibody can be used interchangeably, and can refer to antibodies derived from humans or antibodies obtained from a genetically modified organism that has been engineered to produce specific human antibodies in response to antigen stimulation and can be produced by any method known in the art. In some technologies, elements of human heavy chain and light chain gene loci are introduced into cell lines of organisms derived from embryonic stem cell lines, in which the endogenous heavy chain and light chain gene loci are altered targets. Transgenic organisms can synthesize human antibodies specific to human antigens, and the organisms can be used to produce hybridomas that secrete human antibodies.A human antibody can also be an antibody in which the heavy and light chains are encoded by nucleotide sequences derived from one or more human DNA sources. A fully human antibody can also be constructed using gene or chromosome transfection and phage presentation technology, or constructed using in vitro activated B cells, all of which are known techniques. The terms full-length antibody, intact antibody, complete antibody, and whole antibody are used interchangeably in this document and refer to an antibody in a substantially intact form, as distinct from the antigen-binding fragments defined below. These terms specifically refer to an antibody whose light chain and heavy chain comprise a constant region. The antibody of the present invention includes full-length antibody and antigen-binding fragments thereof. In some embodiments, the full-length antibody of the present invention includes antibodies formed by linking the variable region of the light chain to the constant region of the light chain and by linking the variable region of the heavy chain to the constant region of the heavy chain, as shown in the light and heavy chain combination lines in Tables 1 to 4 below. Practitioners may select different antibody-derived light chain constant regions and heavy chain constant regions according to actual needs, for example, human antibody-derived light chain constant regions and heavy chain constant regions. The term antigen-binding fragment or functional antibody fragment refers to one or more antibody fragments that retain the ability to bind specifically to an antigen (e.g., TSLP). Full-length antibody fragments have been shown to be capable of performing the antigen-binding function of antibodies.Examples of the binding fragment included in the term antigen-binding fragment of an antibody include (i) Fab fragment, a monovalent fragment consisting of VL, VH, CL, and CH1 domains; (ii) F(ab')2 fragment, a bivalent fragment comprising two Fab fragments linked by a disulfide bridge in the hinge region; (ii) Fd fragment, consisting of VH and CH1 domains; (iv) Fv fragment, consisting of VH frnofrLn / Lznz / e / YiAi and VL domains of one arm of the antibody; (v) dsFv, a stable antigen-binding fragment formed by interchain disulfide bonds between VH and VL; (vi) diabody, bispecific antibody, and multispecific antibody, comprising fragments such as scFv, dsFv, Fab, etc.Furthermore, although the two VL and VH domains of the Fv fragment are encoded by separate genes, recombination methods can be used to join them using synthetic linkers so that it can be produced as a single protein chain in which the VL and VH regions pair to form a monovalent molecule (referred to as single-stranded Fv (scFv); see, for example, Bird et al. (1988) Science 242: 423-426; and Huston et al. (1988) Proc. Nati. Acad. Sci USA 85: 5879-5883). Such single-stranded antibodies are also included under the term antigen-binding fragment of an antibody. Such antibody fragments are obtained using conventional techniques known to those skilled in the art and are selected in the same manner as for intact antibodies. The antigen-binding fragment can be produced by recombinant DNA technology or by enzymatic or chemical fragmentation of intact immunoglobulin.Antibodies can be antibodies of different isotypes, for example, IgG (for example, subtypes lgG1, lgG2, lgG3 or lgG4), lgA1, lgA2, IgD, IgE or IgM. Fab is an antibody fragment that has a molecular weight of approximately 50,000 and has antigen-binding activity among the fragments obtained by treating IgG antibody molecules with papain (which cleaves the amino acid residue at position 224 of the H chain), in which approximately half of the N-terminal H chain and the entire L chain are linked by disulfide bonds. F(ab')2 is an antibody fragment that has a molecular weight of approximately 100,000 and has antigen-binding activity and comprises two Fab regions connected at the hinge position between the fragments obtained by digesting the lower part of the two disulfide bonds at the hinge, IgG region with the enzyme pepsin. Fab' is an antibody fragment that has a molecular weight of approximately 50,000 and has antigen-binding activity obtained by cleaving the disulfide bond in the hinge region of F(ab')2. The Fab' of the present invention can be produced using reducing agents, for example, dithiothreitol, to treat the F(ab')2 of the present invention that specifically recognizes the TSLP and binds to the amino acid sequence of the extracellular domain or three-dimensional structure thereof. In addition, Fab' can be produced by inserting the DNA encoding the Fab' fragment of the antibody into a prokaryotic expression vector or a eukaryotic expression vector and introducing the vector into a prokaryotic or eukaryotic organism to express Fab'. frnofrLn / Lznz / e / YiAi The term single-stranded antibody, single-stranded Fv, or scFv refers to molecules comprising an antibody heavy chain variable domain (or region, VH) and an antibody light chain variable domain (or region, VL) connected by a linker. Such scFv molecules may have the general structure: NH2-VL-linker-VH-COOH or NH2VH-linker-VL-COOH. Suitable linkers in the prior art consist of repeated GGGGS amino acid sequences or variants thereof, for example, using 1 to 4 repeated variants (Holliger et al. (1993), Proc. Nati. Acad. Sci. USA 90: 6444-6448). Other linkers that may be used in the present invention are described in Alfthan et al. (1995), Protein Eng. 8: 725-731, Choi et al. (2001), Eur. J. Immunol. 31: 94-106, Hu et al. (1996), Cancer Res. 56: 3055-3061, Kipriyanov et al. (1999), J. Mol. Biol. 293: 41-56 and Roovers et al. (2001), Cancer Immunol. A diabody is an antibody fragment in which scFv or Fab is dimerized and is an antibody fragment with bivalent antigen-binding activity. In bivalent antigen-binding activity, the two antigens can be the same or different. Bispecific antibody and multispecific antibody refer to an antibody that can simultaneously bind to two or more antigens or antigenic determinants, including scFv or Fab fragments that can bind to TSLP. The diabody of the present invention can be produced by the following steps: obtaining the VH and VL encoding cDNA from the monoclonal antibody of the present invention that specifically recognizes human TSLP and binds to the amino acid sequence of the extracellular or three-dimensional structure domain thereof, constructing the scFv encoding DNA such that the amino acid sequence length of the peptide linker is 8 residues or less, inserting the DNA into a prokaryotic or eukaryotic expression vector, and then introducing the expression vector into a prokaryotic or eukaryotic organism to express the diabody. dsFv is obtained by joining VH and VL polypeptides in which one amino acid residue of each is replaced by a cysteine ​​residue via disulfide bonds between the cysteine ​​residues. The amino acid residues substituted with cysteine ​​residues can be selected according to known methods (Protein Engineering, 7, 697 (1994)) based on the prediction of the three-dimensional structure of the antibody. The full-length antibody or antigen-binding fragment of the present invention can be produced by the following steps: obtaining the VH and VL encoding cDNA of the monoclonal antibody of the present invention that specifically recognizes human TSLP and binds to the amino acid sequence, extracellular domain, or three-dimensional structure thereof, constructing the DNA encoding the full-length antibody or the frnofrLn / Lznz / e / YiAi antigen-binding fragment, inserting the DNA into a prokaryotic expression vector or a eukaryotic expression vector, and then introducing the expression vector into a prokaryotic or eukaryotic organism for expression. The term amino acid difference or amino acid mutation refers to the presence of amino acid changes or mutations in the variant protein or polypeptide compared to the original protein or polypeptide, including the appearance of 1, 2, 3 or more amino acids, insertion, deletion or acid substitution based on the original protein or polypeptide. The term antibody frame or FR region refers to a remnant of the VL or VH variable domain, which serves as a scaffold for the antigen-binding loop (CDR) of the variable domain. Essentially, it is a variable domain without a CDR. The term complementarity-determining region (CDR) or hypervariable region refers to one of the six hypervariable regions in the variable domain of an antibody that primarily contributes to antigen binding. Generally, there are three CDRs (HCDR1, HCDR2, HCDR3) in each heavy-chain variable region and three CDRs (LCDR1, LCDR2, LCDR3) in each light-chain variable region. Any of a variety of well-known schemes can be used to determine the amino acid sequence boundaries of CDRs, including Kabat's numbering rules (see Kabat et al. (1991), Protein Sequences of Immunological Interest, 5th edition, Public Health Service, National Institutes of Health, Bethesda, MD), Chothia numbering rules (see Al-Lazikani et al., (1997) JMB 273: 927-948), and ImmunoGenTics (IMGT) numbering rules (Lefranc MP, Immunologist, 7, 132-136 (1999); Lefranc, MP, et al., Dev. Comp. Immunol., 27, 55-77 (2003)), etc.For example, in the classic format, following Kabat's rule, the amino acid residue numbers of the CDRs in the variable domain of the heavy chain (VH) are 31–35 (HCDR1), 50–65 (HCDR2), and 95–102 (HCDR3); the amino acid residue numbers of the CDRs in the variable domain of the light chain (VL) are 24–34 (LCDR1), 50–56 (LCDR2), and 89–97 (LCDR3). Following Chothia's rule, the amino acid residue numbers of the CDRs in VH are 26–32 (HCDR1), 52–56 (HCDR2), and 95–102 (HCDR3); and the amino acid residue numbers in VL are 26–32 (LCDR1), 50–52 (LCDR2), and 91–96 (LCDR3). By combining the Kabat and Chothia definitions of RDAs, the RDAs consist of amino acid residues 26-35 (HCDR1), 50-65 (HCDR2) and 95-102 (HCDR3) in human VH and amino acid residues 24-34 (LCDR1), 50-56 (LCDR2) and 89-97 (LCDR3) in human VL.Following IMGT rules, the amino acid residue numbers of the CDRs in VH are approximately 26–35 (CDR1), 51–57 (CDR2), and 93–102 (CDR3), and the amino acid residue numbers of the CDRss in VL are approximately 27–32 (CDR1), 50–52 (CDR2), and 89–97 (CDR3). Following IMGT rules, the CDR regions of an antibody can be determined using the IMGT / DomainGap Align program. The term epitope or antigenic determinant refers to a site on an antigen where an immunoglobulin or antibody binds specifically (e.g., a specific site on TSLP molecules). Epitopes typically include at least 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15 consecutive or non-consecutive amino acids in a unique spatial conformation. See, for example, Epitope Mapping Protocols in Methods in Molecular Biology, vol. 66, GE Morris, Ed. (1996). The terms specific binding, selectively binding, selectively binding, and specifically binding all refer to the binding of an antibody to an epitope on a predetermined antigen. Generally, an antibody binds with an affinity (KD) of approximately less than 10⁻⁸ M, for example, approximately less than 10⁻⁹ M, 10⁻¹¹ M, 10⁻¹² M, or less. The term KD refers to the dissociation equilibrium constant of a specific antibody-antigen interaction. Generally, the antibody of the present invention binds to TSLP with an affinity (KD) of approximately less than 10⁻⁷M, for example, approximately less than 10⁻⁸M or 10⁻⁹M. In the present description, the affinity of the antibody against the cell surface antigen is determined by the FACS or Biacore method to determine the KD value. When the term competition is used in the context of antigen-binding proteins (e.g., neutralizing antigen-binding protein or neutralizing antibody) competing for the same epitope, it refers to competition between antigen-binding proteins, which is determined by the following assay: In the assay, the antigen-binding proteins to be tested (e.g., antibodies or functional immunological fragments thereof) prevent or inhibit (e.g., reduce) the specific binding of a reference antigen-binding protein (e.g., a reference ligand or antibody) to a common antigen (e.g., TSLP antigen or fragment thereof).Numerous types of competitive binding assays can be used to determine whether one antigen-binding protein competes with another; these assays are, for example, solid-phase direct or indirect radioimmunoassay (RIA), solid-phase direct or indirect enzyme immunoassay (EIA), sandwich competition assay (see, for example, Stahli et al., 1983, Methods in Enzymology 9: 242-253); solid-phase direct biotin-avidin EIA (see, for example, Kirkland et al., 1986, J. Immunol. 137: 3614-3619), solid-phase direct tipping assay, solid-phase direct tipping sandwich assay (see, for example, Harlow and Lañe, 1988, Antibodies, A Laboratory Manual, Cold Spring Harbor Press); Direct solid-phase titration RIA with markers 1-125 (see, for example, Morel et al., 1988, Molec. Immunol. 25: 7-15); direct solid-phase biotin-avidin EIA frnofrLn / Lznz / e / YiAi (see, for example, Cheung, et al., 1990, Virology 176: 546-552); and directly label RIA (Moldenhauer et al., 1990, Scand. J. Immunol. 32: 77-82). Generally, the assays involve the use of either unlabeled test antigen-binding proteins and labeled reference antigen-binding proteins to bind purified antigens attached to a solid surface or cells. Competitive inhibition is measured by measuring the amount of label bound to the solid surface or cells in the presence of the test antigen-binding protein. The test antigen-binding protein is usually present in excess.Antigen-binding proteins identified by competitive assays (competitive antigen-binding proteins) include antigen-binding proteins that bind to the same epitope as the reference antigen-binding protein; and antigen-binding proteins that bind to adjacent epitopes that are sufficiently close to the binding epitope of the reference antigen-binding protein, the two epitopes spherically preventing binding to each other. Generally, when the competitive antigen-binding protein is present in excess, it will inhibit (i.e., reduce) the specific binding of the reference antigen-binding protein to the common antigen by at least 40–45%, 45–50%, 50–55%, 55–60%, 60–65%, 65–70%, 70–75%, or 75% or more. In some cases, the binding is inhibited by at least 80-85%, 85-90%, 90-95%, 95-97% or 97% or more. The term nucleic acid molecule used in this document refers to a DNA molecule and an RNA molecule. The nucleic acid molecule can be single-stranded or double-stranded and is preferably double-stranded DNA or single-stranded mRNA or modified mRNA. When a nucleic acid is placed in a functional relationship with another nucleic acid sequence, the nucleic acid is operatively linked. For example, if a promoter or enhancer affects the transcription of a coding sequence, then the promoter or enhancer is operatively linked to the coding sequence. The identity of the amino acid sequence refers to the percentage of amino acid residues that are identical between the first and second sequences when the amino acid sequences are aligned (introducing spaces where necessary) to achieve the maximum percentage of sequence identity. Conservative substitutions are not considered part of the sequence identity. To determine the percentage of amino acid sequence identity, alignment can be achieved in a variety of ways within the technical scope of the technique, for example, using publicly available computer software such as BLAST, BLAST-2, ALIGN, ALIGN-2 Software, or Megalign (DNASTAR). Experts in the technique can determine the appropriate parameters for measuring alignment, including any algorithms needed to achieve maximum alignment across the entire length of the sequences being compared. frnofrLn / Lznz / e / YiAi The term expression vector refers to a nucleic acid molecule capable of carrying another nucleic acid to which it has been attached. In one embodiment, the vector is a plasmid, which refers to a circular loop of double-stranded DNA to which additional DNA segments can be attached. In another embodiment, the vector is a viral vector to which additional DNA segments can be attached to the viral genome. The vectors described herein can replicate autonomously in the host cell into which they have been introduced (e.g., bacterial vectors with a bacterial origin of replication and mammalian episomal vectors) or can integrate into the host cell's genome after being introduced, so that they replicate along with the host genome (e.g., non-episomal mammalian vectors). Methods for producing and purifying antibodies and antigen-binding fragments are well known in the prior art, such as the Antibody Experiment Technical Guide, Coid Spring Harbor, Chapters 5-8 and 15. For example, mice can be immunized with human TSLP or a fragment thereof, and the resulting antibodies 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 add one or more human FR regions to non-human CDR regions. Human FR germline sequences can be obtained from the ImmunoGeneTics (IMGT) website http: / / imgt.cines.fr comparing the human antibody variable region germline gene database IMGT and MOE software or can be obtained from The Immunoglobulin FactsBook, 2001ISBN012441351. The term host cell refers to a cell into which an expression vector has been introduced. Host cells can include bacteria, microorganisms, plant cells, or animal cells. Bacteria that can be readily transformed include members of the Enterobacteriaceae family, for example, strains of Escherichia coli or Salmonella; Bacillaceae, for example, Bacillus subtilis; and Streptococcus pneumoniae, Streptococcus pneumoniae, and Haemophilus influenzae. Suitable microorganisms include Saccharomyces cerevisiae and Pichia pastoris. Suitable animal host cell lines include CHO (Chinese hamster ovary cell line), 293 cells, and NS0 cells. The genetically modified antibodies or antigen-binding fragments of the present invention can be prepared and purified using conventional methods. For example, the cDNA sequences encoding the heavy and light chains can be cloned and recombined into a GS expression vector. Recombinant immunoglobulin expression vectors can stably transfect CHO cells. As a previously recommended technique, mammalian expression systems can lead to the frnQfrtn / Lznz / e / YiAi glycosylation of antibodies, particularly at the highly conserved N-terminal sites of the Fe region. Stable clones are obtained by expressing antibodies that bind specifically to human TSLP. Positive clones are expanded in serum-free bioreactor medium to produce antibodies. The medium in which the antibodies are secreted can be purified using conventional techniques.For example, using a Sepharose FF A or G column with adjusted buffer for purification. Non-specifically bound components are removed by washing. Bound antibodies are then eluted using the pH gradient method, and antibody fragments are detected and collected by SDS-PAGE. The antibodies can be filtered and concentrated using conventional methods. Soluble mixtures and polymers can also be removed using conventional methods, such as molecular sieves and ion exchange. The resulting product should be frozen immediately, for example, at -70 °C, or lyophilized. Administering, giving, and treating, when applied to animals, humans, experimental subjects, cells, tissues, organs, or biological fluids, refers to the contact of the exogenous drug, therapeutic agent, diagnostic agent, or composition with the animals, humans, subjects, cells, tissues, organs, or biological fluids. Administering, giving, and treating may refer, for example, to treatment, pharmacokinetics, diagnosis, research, and experimental methods. Cell treatment includes contacting reagents with cells and contacting reagents with fluids, where the fluids are in contact with the reagent. Administering, giving, and treating also refers to treating, for example, cells by means of reagents, diagnostics, 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, preventive or prophylactic measures, research, and diagnostic applications. Treatment refers to administering an internal or external therapeutic agent, for example, a composition comprising any of the binding compounds of the present invention, to a patient with 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 amount effective to relieve one or more disease symptoms in the patient or treated population, to induce the regression of such symptoms, or to inhibit the development of such symptoms to any clinically measurable degree. The amount of therapeutic agent that is effective in relieving 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, body weight, and the drug'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 routinely used by physicians or other healthcare professionals to evaluate the severity or progression of symptoms. Although the modalities of the present invention (e.g., frnofrLn / Lznz / e / YiAi treatment methods or products) may not be effective in relieving the target disease symptom(s) in every patient, as determined by any statistical testing method known in the art, such as the Student's t-test, chi-square test, Mann-Whitney U test, Kruskal-Wallis test (H-test), Jonckheere-Terpstra test, and Wilcoxon signed-rank test, they should reduce the target disease symptoms in a statistically significant number of patients. Conservative modification, or conservative substitution, refers to substituting amino acids in a protein with other amino acids that have similar characteristics (e.g., charge, side chain size, hydrophobicity / hydrophilicity, backbone conformation, and stiffness, etc.) so that changes can be made frequently without altering the protein's biological activity. Those skilled in the art know that, generally speaking, a single amino acid substitution in a non-essential region of a polypeptide does not substantially change biological activity (see, for example, Watson et al. (1987) Molecular Biology of the Gene, The Benjamin / Cummings Pub. Co., p. 224, (fourth edition)). Furthermore, substituting amino acids with similar structures or functions is unlikely to alter biological activity.Exemplary conservative substitutions are indicated in the Exemplary Conservative Substitutions of Amino Acids table below. Table 5. Conservative substitutions of exemplary amino acids frnofrLn / Lznz / e / YiAi Original Residue Conservative Substitution Ala(A) Gly; Ser Arg(R) Lys; His Asn(N) Gln; His; Asp Asp(D) Glu; Asn Cys(C) Ser; To the; Val Gln(Q) Asn;Glu Glu(E) Asp; Gln Gly(G) Ala His(H) Asn;Gln lle(l) Leu; Val Leu(L) He; Val Lys(K) Arg; His Met(M) Leu; He; Tyr Phe(F) Tyr; Met; Leu Pro(P) Ala Ser(S) Thr Thr(T) Ser Trp(W) Tyr; Phe Tyr(Y) Trp; Phe Val(V) He;Leu frnofrLn / Lznz / e / YiAi Effective quantity or effective dose refers to the amount of a drug, compound, or pharmaceutical composition necessary to achieve any or the most beneficial or desired therapeutic results. For preventive use, beneficial or desired results include the elimination or reduction of risk, the reduction of severity, or the delay of the onset of disease, including the biochemical, histological, and / or behavioral symptoms of the disease, its complications, and intermediate pathological phenotypes that appear during the disease development process. For therapeutic applications, beneficial or desired results include clinical outcomes, such as reducing the incidence of various disorders related to the target antigen of the present invention, improving one or more symptoms of the disorder, or reducing the dosage of other agents needed to treat the disorder., enhance the therapeutic effect of another agent and / or delay the progression of the patient's disorders related to the target antigen of the present invention. Exogenous refers to substances produced outside of organisms, cells, or human bodies depending on the circumstances. Endogenous refers to substances produced within cells, organisms, or human bodies depending on the circumstances. Homology refers to the sequence similarity between two polynucleotide sequences or two polypeptides. When positions in the two compared sequences are occupied by the same monomer subunit of base or amino acid—for example, if every position in two DNA molecules is occupied by adenine—then the molecules are homologous at that position. The percentage of homology between two sequences is a function of the number of matching or homologous positions shared by the two sequences divided by the total number of compared positions (χ 100). For example, in optimal sequence alignment, if 6 out of 10 positions in the two sequences match or are homologous, then the two sequences are 60% homologous; if 95 out of 100 positions in the two sequences match or are homologous, then the two sequences are 95% homologous. Generally, when aligning two sequences, comparisons are made to determine the maximum percentage of homology.For example, the comparison can be performed using the BLAST algorithm, where the algorithm parameters are selected to give the maximum match between each sequence across the entire length of each reference sequence. The following references refer to the BLAST algorithm, which is often used for sequence analysis: BLAST ALGORITHMS: Altschul, SF et al., (1990) J. Mol. Biol. 215: 403-410; Gish,. W. et al., (1993) Nature Genet. 3: 266-272; Madden, TL et al., (1996) Meth. Enzymol. 266: 131-141; Altschul, SF et al., (1997) Nucleic Acids Res. 25: 3389-3402; Zhang, J. et al., (1997) Genome Res. 7: 649-656. Other conventional BLAST algorithms, such as those provided by NCBI BLAST, are also well known to experts in the technique. The terms "cell," "cell line," and "cell culture," as used herein, may be used interchangeably, and all these terms encompass the progeny. Therefore, the words "transformant" and "transformed cell" include primary test cells and cultures derived from them, regardless of the number of passages. It should also be understood that, due to deliberate or unintentional mutations, all progeny may not be exactly the same in terms of DNA content. Mutant progeny with the same biological function or activity as that selected in the original transformed cells is included. This is clearly visible from the context when a different term is used. Polymerase chain reaction, or POR, as used herein, refers to a procedure or technique in which a trace amount of a specific nucleic acid residue, RNA and / or DNA, is amplified, as described, for example, in U.S. Patent No. 4,683,195. Generally, sequence information must be obtained from the end or outside the target region so that oligonucleotide primers can be designed. These primers are sequence-identical to the corresponding template strand to be amplified. The 5' terminal nucleotides of the two primers may be identical to the ends of the material to be amplified. POR can be used to amplify specific RNA sequences, specific DNA sequences from total genomic DNA, and cDNA sequences transcribed from total cellular RNA, phage or plasmid sequences, etc. For general information, see Mullis et al. (1987) Port of Coid Spring, Symp. Ouant. Biol.51: 263; Erlich ed., (1989) PCR TECHNOLOGY (Stockton Press, NY). The PCR used in this document is considered an example, but not the only example, of a nucleic acid polymerase reaction method for amplifying a nucleic acid test sample, and the method includes the use of nucleic acids known as primers and nucleic acid polymerases to amplify or produce a specific nucleic acid residue. Isolated refers to a purified state, and in this case means that the designated molecule is substantially free of other biomolecules, for example, nucleic acids, proteins, lipids, carbohydrates, or other materials, such as cell debris and growth medium. Generally, the term isolated is not intended to mean the complete absence of these materials or the absence of water, buffer, or salt, unless they are present in an amount that significantly interferes with the experimental or therapeutic use of the compound as described herein. frnofrLn / Lznz / e / YiAi Optionally means that the event or environment described below may occur, but does not have to occur, and this description includes occasions when the event or environment does or does not occur. Pharmaceutical composition means a mixture containing one or more of the compounds described in this document, or physiologically / pharmaceutically acceptable salts or prodrugs thereof, and other chemical components, for example, physiologically / pharmaceutically acceptable vehicles and excipients. The purpose of the pharmaceutical composition is to facilitate delivery to organisms, thereby promoting the absorption of the active ingredient and thus its biological activity. The term pharmaceutically acceptable vehicle refers to any inactive substance suitable for use in a formulation for the delivery of antibodies or antigen-binding fragments. The vehicle may be an anti-adherent, binder, coating agent, disintegrant, filler or diluent, preservative (such as an antioxidant, antibacterial, or antifungal agent), sweetener, absorption retardant, wetting agent, emulsifier, buffer, etc. Pharmaceutically acceptable vehicles include water, ethanol, polyols (e.g., glycerol, propanediol, polyethylene glycol, etc.), dextrose, vegetable oil (e.g., olive oil), saline solution, buffer, buffered saline solution, and isotonic agents, such as sugar, polyol, sorbitol, and sodium chloride. Furthermore, the present invention includes agents for the treatment of TSLP-related diseases, comprising the anti-TSLP antibody of the present invention or its antigen-binding fragment as an active ingredient. There is no limitation regarding the TSLP-related disease in the present invention, provided it is a TSLP-related disease. For example, the therapeutic response induced by the molecule of the present invention can be achieved by binding to human TSLP and then blocking the binding of TSLP to its receptors, or by killing cells that overexpress TSLP. Furthermore, the present invention relates to methods for immunodetection or determination of the target antigen (e.g., TSLP), reagents for immunodetection or determination of the target antigen (e.g., TSLP), methods for immunodetection or determination of cells expressing the target antigen (e.g., TSLP), and diagnostic agents for diagnosing diseases related to cells positive for the target antigen (e.g., TSLP), which includes the antibody or antibody fragment of the present invention as an active ingredient, which specifically recognizes the target antigen (e.g., human TSLP) and binds to the amino acid sequence of the extracellular domain or three-dimensional structure thereof. frnofrLn / Lznz / e / YiAi In the present invention, the method used for detecting or measuring the quantity of the target antigen (e.g., TSLP) can be any known method. For example, it includes immunodetection or measurement methods. Immunodetection or measurement methods are methods for detecting or measuring the amount of antibody or antigen using labeled antigens or antibodies. Examples of immunodetection or measurement methods include radioimmunoassay (RIA), enzyme immunoassay (EIA or ELISA), fluorescence immunoassay (FIA), luminescence immunoassay, Western blot, physicochemical methods, etc. The TSLP-related diseases mentioned above can be diagnosed by detecting or measuring cells that express TSLP using the antibody or antibody fragment of the present invention. To detect cells expressing the polypeptide, known immunodetection methods can be used, preferably immunoprecipitation, fluorescent cell staining, immunohistochemical staining, etc. In addition, a fluorescent antibody staining method using the FMAT8100HTS system (Applied Biosystem) can be used. In the present invention, there is no particular limitation for the in vivo sample used for the detection or measurement of the target antigen (e.g., TSLP), provided that it has the possibility of comprising cells expressing the target antigen (e.g., TSLP), e.g., histocyte, blood, plasma, serum, pancreatic juice, urine, feces, tissue fluid, or culture fluid. Depending on the required diagnostic method, the diagnostic agent containing the monoclonal antibody or antibody fragment thereof of the present invention may also contain reagents for performing the antigen-antibody reaction or reagents for detecting the reaction. Reagents used for performing the antigen-antibody reaction include buffers, salts, etc. Reagents used for detection include reagents commonly used in immunodetection or measurement methods, for example, labeled second antibodies that recognize the monoclonal antibody, antibody fragment thereof, or conjugate thereof, and corresponding label substrates, etc. The foregoing specification presents details of one or more embodiments of the present invention. Although any method and material similar or identical to those described herein may be used to implement or test the present invention, preferred methods and materials are described below. The other features, purposes, and advantages of the present invention will be obvious from the specification and the claims. In the specification and the claims, unless clearly indicated otherwise in the context, the singular form includes instances of the plural referent. Unless otherwise defined, all technical and scientific terms used herein have the general meanings understood by those skilled in the art to which the present invention pertains. All patents and publications cited in the specification are incorporated by reference.The following examples are presented to more fully illustrate preferred embodiments of the present invention. These examples should not be construed as limiting the scope of the present invention in any way, and the scope of the present invention is defined by the claims. Examples The following examples are incorporated for a further description of the present invention, but these examples do not limit the scope of the present invention. Experimental methods under conditions not specified in the examples or test examples of the present invention generally follow conventional conditions, or in accordance with the conditions recommended by the manufacturer of the raw material or basic product. See Sambrook et al., Molecular Cloning: A Laboratory Manual, Coid, Spring Harbor; Current Protocols in Molecular Biology, Ausubel et al., Greene Publishing Associates, Wiley Interscience, NY. Reagents from unspecified sources are commercially available, conventional reagents. Example 1. TSLP expression and TSLP receptor Sequences encoding His- and cyno-tagged human TSLP, IgG1-Fe-tagged human TSLP, and cyno-tagged TSLP, as well as extracellular domain sequences of the TSLP receptor, were loaded into the phr vector to construct expression plasmids, which were then transfected into HEK293. The specific transfection steps were as follows: the day before, HEK293E cells were seeded in Freestyle expression medium (containing 1% FBS) at 0.8 × 10⁶ / mL, placed on a constant-temperature shaker at 37°C (120 rpm), and cultured for 24 hours. After 24 hours, the transfection plasmid and PEI transfection reagent were sterilized using 0.22 µm filters. Then, the transfection plasmid was set to 100 pg / 100 mi of cells and the PEI (1 mg / mi) to plasmid mass ratio was 3:1.Taking as an example the transfection of 200 ml of HEK293E cells, 10 ml of Opti-MEM and 200 pg of plasmid were taken, mixed well, and allowed to stand for 5 min; another 10 ml of Opti-MEM and 600 pg of PEI were taken, mixed well, and allowed to stand for 5 min. The plasmid and PEI were mixed well and allowed to stand for 15 min, preferably not exceeding 20 min. The plasmid and PEI mixture was slowly added to 200 ml of HEK293E cells and placed on a shaker at 8% CO2, 120 rpm, and frnofrLn / Lznz / e / YiAi. 37SC for culture. On day 3 post-transfection, the culture was supplemented with 10% of the volume of supplemented medium. Until day 6 post-transfection, samples were taken and centrifuged at 4500 rpm for 10 min to collect the cell supernatant. The supernatant was filtered and purified to obtain TSLP receptor proteins and recombinant TSLP using Example 2. The purified proteins could be used in the experiments in each example below. The relevant sequences are as follows. 1. Amino acid sequence of the his-labeled human TSLP antigen (huTSLPhis) MFPFALLYVLSVSFRKIFILOLVGLVLTYDFTNCDFEKIKAAYLSTISKDLITYMS GTKSTEFNNrVSCSNRPHCLTElQSLTFNPFAGCASLAKEMFAMKTKAALAIW CPGYSETQINATQAMKK.ARKSKVTTNKCLEQVSQLQGLWRRFNRPLLKQQGS SD YKDDDDKHHHHHH Note: The underlined part is the signal peptide sequence; the italicized part is the Flag-His6 label. SEC ID NO: 1 2. Secuencia de aminoácidos del antígeno TSLP humano marcado con Fe (huTSLP-Fc) M FPFA L LY VLS VSFRKI FILQLVGLVLT YDFT NC DFE ΚIK AAYLS TIS KDL IT YMS GTKSTEFNNTVSCSNRPHCLTEIQSLTFNPTAGCASLAKEMFAMKTKAALAIW CPGYSETQINATQAMKKARKSKVTTNKCLEQVSQLQGLWRRFNRPLLKQQ / 9 / 7 KNQ VSL1CL VKGE YPSDIA YEWESNGQPENNYKrrPPVLDSüGSEELYSKLTVDKSRWQQGNVESCSVMHEALH NH YTQKSESLSPGK Note: Subrayada está la secuencia del péptido señal; The cursive part is the etiqueta of the human world. SEC ID NO: 2 3. Secuencia de aminoácidos del antígeno cyno TSLP marcado con his (cynoTSLP-his) METDTLLLWVLLLWVPGSTGYDFTNCDFOKIEADYLRTISKDLITYVISGTKST DFNNTVSCSNRPHCLTEIQSLTFNPTPRCASLAKEMFARKTKATLALWCPGYSE TQINATQAMKKARKSKVTTNKCLEQVSQLLGLWRFIRTLLKQQGSÓDrKDD DDKHHHHHH Note: Underlined is the signal peptide sequence; the part in italics is the flag-His6 label. frnofrLn / Lznz / e / YiAi SEC ID NO: 4. Amino acid sequence of the Fe-labeled cyno TSLP antigen (cynoTSLP-Fc) METDTLLLWVLLLWVPGSTGYDFTNCDFOKIEADYLRTISKDLITYMSGTKST DFNNTVSCSNRPHCLTEIQSLTFNPTPRCASLAKEMFARKTKATLALWCPGYSE TQINATQAMKKARKSKVTTNKCLEQVSQLLGLWRRFIRTLLKQQ£> / £G / ?MZ1£ PKSSDKTHTCPPCPAPELLGGPSVELEPPKPKDTLMISRI PEVTCVVVDVSHEDPE VKEN WYVDG VE VHNA KTKPREEQ EQUIPMENT V VS VLTVLHQD WLNGKE YKCK VSNK ALPAPIEKIISKAKGQPREPQVYILPPSRÜELIKNQVSL1CLVKGEYPSDIAVEWES NGQPENNYKTΓPPVLDSDGSEELYSKLΊ'VDKSR^VQQGNVESCSVMHEAL·HNHYΊ' QKSLSLSPGK Note: Underlined is the signal peptide sequence; the part in italics is the Fe label of the human-linker. SEC ID NO: 4 5. Amino acid sequence of the extracellular domain of the Fe-labeled human TSLP receptor (human-TSLPR-Fc-ECD): GAAEGVQIOllYFNLETVOVTWNASKYSRTNLTFHYRFNGDEAYDQCTNYLL QEGHTSGCLLDAEQRDDILYFSIRNGTHPVFTASRVVMVYYLKPSSPKHVRFSW HQDAVTVTCSDLSYGDLLYEVOYRSPFDTEWOSKQEMTCWTIEGLDAEKCY SFWVRVKAMEDVYGPDTYPSDWSEVTCWQRGEIRDACAETPTPPKPKLSKD / EGRMDEPKSSDKTHTCPPCPAPELLGGPSVFLEPPKPKDTLMISRTPEVTCVVVDV SHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYK CKVSNKALPAPIEKTISKAKGQPREPQVYI LPPSRDELl KNQVSLTCLVKGFYPSD1A VEWESNGQPENNYKnPPVLDSDGSEFLYSKLTVDKSRWQQGNVESCSVMHEALH ΝΗΥΊ QKSLSLSPGK Note: The underlined part is the extracellular domain of human TSLPR and the italicized part is the human ligand Fe tag. SEC ID NO: 5 Example 2. Purification of recombinant TSLP receptor and TSLP (TSLPR) proteins 2.1 Purification of recombinant TSLP proteins labeled with His from each species Cell expression supernatant samples were centrifuged at high speed to remove impurities and filtered. Nickel columns were equilibrated with PBS and washed with 10 times the column volume. The filtered supernatant samples were applied to the columns. The columns were washed with PBS containing 30 mM imidazole until the A280 reading dropped to baseline. Target proteins were then eluted with PBS containing 300 mM imidazole, and the elution peaks were collected. The proteins were concentrated and exchanged in PBS and divided into frnQfrtn / Lznz / e / YiAi aliquots for use after being identified as correct by LC-MS. His-labeled human TSLPs and cyno-labeled TSLPs were obtained. 2.1 Purification of human Fe-labeled TSLP from each species and recombinant proteins of the extracellular domain of the human TSLP receptor Cell expression supernatant samples were centrifuged at high speed to remove impurities. The recombinant antibody expression supernatant was purified using Protein A columns. The columns were washed with PBS until the A280 reading returned to baseline. Target proteins were eluted with 100 mM acetate buffer, pH 3.5, and neutralized with 1 M Tris-HCl, pH 8.0. The resulting proteins were concentrated and exchanged into fresh solutions, then aliquoted for use after being identified as correct by electrophoresis and LC-MS. Example 3. Construction and identification of recombinant TSLP receptor and IL7Ra receptor cell lines To screen for antibodies that can block TSLP binding to the TSLP receptor, CHO-K1 and BaF3 cell lines were constructed that simultaneously express both the human TSLP receptor and human IL7Ra (TSLPR / IL7Ra). Lentiviruses were used to package the TSLPR / IL7Ra target gene, which was then cloned into the target cell lines to form stable, high-expression cell lines. First, the human TSLPR and IL7Ra genes were cloned into the pCDH-CMV-MCS-EF1-pure and pCDH-CMV-MCS-EF1-Neo plasmids (SBI, CD500B-1), respectively. The lentivirus infection method was then used to insert human TSLPR into CHO-K1 and BaF3 cell lines, which were cultured under the selection pressure of puromycin 10 pg / mL (Gibco, USA) for three weeks. A second round of infection was then performed. The human IL7Ra gene was inserted into cell lines and screened with 1 mg / mi of G418 (Gibco, USA) and 10 pg / mi of puromycin for two to three weeks.Finally, the CHO-K1 and BaF3 monoclonal cell lines with high simultaneous expression of TSLPR and IL7Ra were selected by the flow sorting method. Example 4. Preparation and screening of human anti-TSLP antibodies Human anti-TSLP monoclonal antibodies were produced by immunizing 6- to 8-week-old female SJL white laboratory mice (Beijing Charles River Laboratory Animal Technology Co., Ltd., Animal Production License No.: SCXK (Beijing) 2012-0001). Housing environment: SPF level. After purchase, the mice were kept in a laboratory environment for 1 week, with a 12 / 12-hour light / dark cycle, temperature 20–25°C, and humidity 40–60%. Mice that had become acclimated to the environment were immunized with recombinant proteins huTSLP-Fc (25 pg), huTSLPhis (12.5 pg), and cyno TSLP-his (12.5 pg) and the adjuvant TiterMax, Alum, or CpG. After 4-5 immunizations, mice with high serum antibody titers and titers that tended to plateau were selected and sacrificed. Spleen cells were collected and fused with myeloma cells.Splenic lymphocytes and Sp2 / 0 myeloma cells (ATCC® CRL-8287TM) were fused to obtain hybridoma cells using PEG-mediated optimized fusion steps. For initial selection, ELISA binding assays for human and cyno TSLP, assays blocking the binding of human TSLP to its receptor TSLPR, and experiments inhibiting TSLP-induced BaF3 cell proliferation were performed. After transferring hybridoma cells to 24-well plates, the supernatant was re-screened. Hybridoma clones were obtained after two rounds of subcloning of the selected positive clones and were used for antibody production; purification was performed using affinity methods. Monoclonal hybridoma cell lines No. 3, No. 119, No. 179, and No. 199, which showed good activity after screening, were obtained, and hybridoma cells were harvested in the logarithmic growth phase. RNA was extracted using NucleoZol (MN), and reverse transcription was performed (PrimeScript™ Reverse Transcriptase, Takara, cat. # 2680A). The cDNA obtained by reverse transcription was amplified by PCR using a mouse Ig-Primer Set (Novagen, TB326 Rev. B 0503) and sent to a sequencing company for analysis. Murine anti-TSLP antibodies were obtained after sequencing: mab3, mab119, mab179, and mab199 sequences. The amino acid sequence of their variable regions is as follows: > sequence of the variable region of the murine heavy chain mab3: E VQLQQSGP VL VKPGAS VKMSCKA SG ΥΊ DDYMNIV VKQSHGKSLE W1G11SPYN GGISYNQKFKGKAILTVDKSSSIA YMELNSLTSEDSA VYYCARED YDYDG ​​YAMDH WGQGTSVTVSS SEC ID NO: 6 > sequence of the variable region of the mab3 murine light cycle: O1VLSOSPA1LSASPGEKVTMTCRASSSVSYMHWYOQKPGSSPKPW1YATSNLASGV PARFSGSGSGlSYSLnSRVEAEDAAlYYCOOWSSNRlFGGGlKLElK SEC ID NO: 7 frnofrLn / Lznz / e / YiAi > sequence of the variable region of the murine weight cycle mab119: QAYL QQSGAEL VRPGASVKMSCKASGFAF'ΓΓYNlyΠ±WVKHΊPGQGL E^^ΊGAlYPG NGETS YNQKFKDRA TLTVDKSSRTA YMQLSSLTSEDSA VYFCAREDD YGEG YFD V WGAG1TVTVSS SEQ ID NO: 8 > Sequence of the variable region of the mab119 murine light cycle: DIVLTQSPASLA VSLGQRA TISCRASESVDNSGLSFMHWYQQKPGOPPRLLLYRASN LGSGIPARFSGSGSGTDFILTLNP VETDD VA TYYCOQINTDPLTFGA GTKLELK SEC ID NO: 9 > sequence of the variable region of the murine weight cycle mab179: OVOLOQSGAELVRPGTSVKVSCKASGYAFTNYUEWVKORPGOGLEWIGVIDPGN GDTNYNENFKGKATLTADKSSSTA Y1ELSRLTSEDSA VYFCAREDNTGTAFDYWGQ GTEUVSS SEC ID NO: 10 > sequence of the variable region of the murine light chain mab179: YES VMTQTPKFLL VSA GOR VTISCKA SOS VSSD V!W YQQKPGOSPKLLl YYVSNH YTG VPDRFTGSG YGIDFTFHSSVQAEDLA VYFCOQHHRFPLTFGAGTKLELK SEC ID NO: 11 > sequence of the variable region of the murine heavy chain mab199: QVQL·QQSGPQL·VRPGASVKlSCKASGYSFTny2MH\VVKQRPGQGL·EWIGMΠ2PS DSEIJIJQKFKDKATLTVDKSSSTA YMQLSSPTSEDSA VYYCARTLDG YYDYWGOG ΊΊLTVSS SEC ID NO: 12 > sequence of the variable region of the murine light chain mab199: DIOMTQSPASLSASVGEIVTH CRASENIYSYLAWYOOKOGKSPQLLVYFAKTLAEG VPSRFSGSVSGTOFSLKINSLQPEDFGSYYCOHHYGTPWl FGGGl KLEIK SEC ID NO: 13 The amino acid sequences of the CDR regions obtained according to Kabat's numbering rules are shown in the following table: frnofrLn / Lznz / e / YiAi Tab 6. Secuencias de regiones CDR de cadena pesada y cadena ligera de anticuerpos de clones de hibridoma Anticuer po Cadena pesada Cadena ligera mab3 HCDR1 DDYMN SEQ ID NO: 14 LCDR1 RASSSVSYMH SEQ ID NO: 17 HCDR2 IISPYNGGTSYNQKFKG SEQID NO: 15 LCDR2 ATSNLAS SEQ ID NO: 18 HCDR3 EDYDYDGYAMDH SEQID NO: 16 LCDR3 QQWSSNRT SEQ ID NO: 19 mabll9 HCDR1 TYNMH SEQID NO: 20 LCDR1 RASESVDNSGLSFMH SEQ ID NO: 23 HCDR2 AIYPGNGETSYNQKFKD SEQID NO: 21 LCDR2 RASNLGS SEQ ID NO: 24 HCDR3 EDDYGEGYFDV SEQID NO: 22 LCDR3 QQINTDPLT SEQ ID NO: 25 mabl79 HCDR1 NYLIE SEQID NO: 26 LCDR1 KASQSVSSDVT SEQ ID NO: 29 HCDR2 VIDPGNGDTNYNENFKG SEQID NO: 27 LCDR2 YVSNHYT SEQ ID NO: 30 HCDR3 EDNTGTAFDY SEQID NO: 28 LCDR3 QQHHRFPLT SEQ ID NO: 31 mabl99 HCDR1 TYWMH SEQID NO: 32 LCDR1 RASENIYSYLA SEQ ID NO: 35 HCDR2 MIDPSDSETTLIQKFKD SEQID NO: 33 LCDR2 FAKTLAE SEQ ID NO: 36 HCDR3 TLDGYYDY SEQID NO: 34 LCDR3 QHHYGTPWT SEQ ID NO: 37 Chimeric antibodies were formed by joining the variable light and heavy chain regions of the aforementioned murine antibody with the constant light and heavy chain regions of the human antibody (such as the kappa constant region as shown in SEQ ID NO: 134 and the lgG1-YTE constant region as shown in SEQ ID NO: 133) . The chimeric antibody corresponding to the mab3 clone was named Ch3, and so on for other antibodies. Example 5. Humanization design of anti-human TSLP monoclonal antibodies To reduce the immunogenicity of murine antibodies, selected mab3, mab119, mab179, and mab199 antibodies with excellent in vivo and in vitro activity were humanized. The humanization of the murine monoclonal antibodies was performed according to methods published in numerous art documents. Briefly, human antibody constant domains were used to replace parental constant domains (murine antibody), human germline antibody sequences were selected based on homology between murine and human antibodies, and CDR grafting was performed. Then, based on the three-dimensional structure of the murine antibody, the VL and VH amino acid residues were reverse-mutated, and the murine antibody constant regions were replaced with human constant regions, resulting in the final humanized molecule. 5.1 Selection and reverse mutations of human FR regions for mab3 (1) Selection and reverse mutations of human FR regions For mab3, the humanized VH template was IGHV1-3*01 + IGHJ6*01, and the humanized VL template was IGKV3-20 + IGKJ4*01. The mab3 CDRs were grafted into the human template, and the variable region sequences obtained after grafting are as follows: hu3 VL-CDR grafted: VLTQ SPATL SLSPGERATL SCRASSSVSYMHW AND QQKPGQAPRLLIY ATS NLASG1PARFSGSGSGTDFTLTISRLEPEDFAVYYCQOWSSNRTFGGGTKVEIK SEC ID NO: 38 hu3 VH-CDR grafted: EVQLVQSGAEVKKPGASVKVSCKASGYTFTDDYMNWVRQAPGQRLEW MGIISPYNGGTSYNOKFKGRVTITRDTSASTAYMELSSLRSEDTAVYYCARED YDYDGYAMDHWGOGTTVTVSS frnQfrLn / Lznz / e / Ywi SEC ID Ns: 42 The reverse mutation design of the humanized antibody mab3 is shown in the following table: frnofrLn / Lznz / e / YiAi Table 7. Back mutations of the humanized antibody mab3 hu3 VL hu3VLl Grafted hu3VH hu3VHl Grafted hu3VL2 L46P, F71Y hu3VH2 I69L, R71V, T73K hu3VL3 L46P, L47W, I58V, F71Y hu3VH3 R38K, M48I, V67A, I69L, R71V, T73K hu3VL4 L46P, L47W, I58V, D70S, F71Y Note: grafted represents the grafting of murine antibody CDR sequences into the FR region sequences of the human germline. L46P represents that, according to the Kabat numbering system, the L at position 46 is mutated back to P. The sequences of the variable regions of the humanized antibody mab3 are as follows: > hu3VL1 (grafted hu3 VL-CDR) EIVLTOSPATLSLSPGERATLSCRASSSVSYMHWYOOKPGOAPRLLIYATSNLA SGIPARFSGSGSGTDFTLTISRLEPEDFAVYYCOQWSSNRTFGGGTKVEIK .hir,vi·, SEQ ID NO: 38 EIVLTOSPATLLSLSPGERATLSCRASSSVSYMHWYOOKPGOAPRPLIYATSNLA SGIPARFSGSGSGTDYTLTISRLEPEDFAVYYCQQWSSNRTI GGGTKVEIK SEQ ID NO: 39 15' hu3VL3 eivltospatlslspgeratlscrasssvsymhwyookpgoaprpwiyatsnia SGVPARFSGSGSGTDYT1.TISRI.EPEDFAVYYCOQWSSNRTFGGGTKVEIK SEQ ID NO: 40 • hu3VL4 EIVI.TQSPATLSLSPtiERATLStRASSSVSYMHWYOOKPGOAPRPWlYATSNLA SGVPARFSGSGSGTSYTLTISRI.F.PF.DFAVYYCOOWSSNRTFGGGTKVF.IK SEQ ID NO: 41 >hu3VHl (hu3 VH-CDR included) EVQLVQSGAEVKKPGASVKVSCKASGYTI•TDDYMNWVRQAPGORLEWMGU SPYNGG I SYNQKFKGRVnTRDI SASTAYMELSSLRSEDTAN YYCAREDYDYD GYAMDHWGQGTT\ TYSS SEQ ID NO: 42 > hu.3VH2 E\ QLVQSGAEVKKPGASVKVSCKASGYTFTDDYMN\V\ RQAPGQRLEWMGH SPYNGGTSYNQKFKGRX TLTVDKSASIAYMELSSLRSEDIAVYYCAREDYDY DGYAMDHWGQG Γ ΓΜΙ VSS SEQ ID NO: 43 > hu3VH3 E\ Q1 \QSGAEX KKPGASVKVSCKASGY I FTDDYMNWVKQAPGORLEW1GI1 SPYNGGISYNOKFKGRAI LTVDKSAS F AYMELSSLRSED TAVAYCARIÍDYDY DGYAMDHWGOGTTVTVSS SEQ ID NO: 44 Note: Single underline represents CDR regions and double underline represents reverse mutation sites. The aforementioned variable light and heavy chain regions were combined with sequences from the human germline light and heavy chain constant regions to form the final complete light and heavy chain sequences, thereby obtaining the antibody with a full-length sequence. By way of example, for the humanized antibody mab3 in the present invention, the heavy chain constant region is the lgG1-YTE constant region shown in SECTION ID NO: 133, and the light chain constant region is the kappa chain constant region shown in SECTION ID NO: 134, but these can also be replaced with other constant regions known in the art. The sequences of the heavy and light chain variable regions of the obtained humanized mab3 antibodies are shown in the following table: Table 8. The sequences of the variable region of the heavy and light chain of the humanized antibody mab3 frnofrLn / Lznz / e / YiAi Antibody and VH (SEQ ID No.) VL (SEQ ID No.) hu3-01 42 39 hu3-02 42 40 hu3-O3 42 41 hu3-04 43 38 hu3-05 43 39 hu3-06 43 40 hu3-07 43 41 hu3-08 44 39 hu3-09 44 40 hu3-10 44 41 The binding activity of the humanized antibody mab3 to human TSLP was detected by the ELISA method, and the results showed that the humanized antibodies mab3 have a very good binding capacity to human TSLP. (2) Point mutation to the hu3 antibody Screening revealed hotspots in the MDH sequence of HCDR3 and the NTR sequence of LCDR3 of the humanized mab3 antibody. Therefore, the corresponding hotspots were mutated. The sequences of the CDR regions of the humanized mab3 antibodies obtained after mutation are as follows: frnQfrtn / Lznz / e / YiAi Table 9. HCDR3 and LCDR3 sequences after mutation hu3 HCDR3-H110Y EDYDYDGYAMDY SEQ ID NO: 45 hu3LCDR3-N93D QQWSSDRT SEQ ID NO: 46 Note: The positions of the mutation sites in Table 9 are numbered according to the natural order of the sequences in the variable region. It can be concluded that the CDR sequences of the humanized antibody mab3 are as follows: Table 10. CDR after mutation of the humanized antibody mab3. Heavy chain Light chain HCDR1 DDYMN SEQ ID NO: 14 LCDR1 RASSSVSYMH SEQ ID NO: 17 HCDR2 IISPYNGGTSYNQKFK G SEQ ID NO: 15 LCDR2 ATSNLAS SEQ ID NO: 18 HCDR3 (general formula) EDYDYDGYAMDX1 SEQ ID NO: 47 LCDR3 (general formula 1) QQWSSX2RT SEQ ID NO: 48 Where, X1 is selected from H or Y, X2 is selected from N or D. As an example, the CDRs and the heavy and light chain variable regions of the humanized antibody hu3-11 obtained after the mutation are as follows: Table 11. CDR regions of hu3-11 Heavy Chain Light Chain HCDR1 DDYMN SEQ ID NO: 14 LCDR1 RASSSVSYMH SEQ ID NO: 17 HCDR2 IISPYNGGTSYNQK FKG SEQ ID NO: 15 LCDR2 ATSNLAS SEQ ID NO: 18 HCDR3-H110Y EDYDYDGYAMDY SEQ ID NO: 45 LCDR3-N93D QQWSSDRT SEQ ID NO: 46 frnofrLn / Lznz / e / YiAi > hu3-11 light chain variable region (hu3VL4-N93D) EIVLTOSPATLSLSPGERATLSCRASSSVSYMHWYOOKPGOAPRPWIYATSNLA SGYPARF SG SG SGTSYTLTTSRLEPEDFAVYYCOQWSSDRTFGGGTK VETK SEC ID N.2: 49 > Variable heavy chain region of hu3-11 (hu3VH2-H110Y) EVOLVOSGAEVKKPGASVKVSCKASGYTFTDDYMNWVROAPGORLEWMGII SPYNGGTSYNQKFKGRVTLTVDKSASTAYMELSSLRSEDTAVYYCAREDYDY DGYAMDYWGOGTTVTVSS SEQ ID NO: 50 The variable regions of the light and heavy chain after the hotspot mutation recombined with sequences from the constant region of the human germline light and heavy chain to form complete light and heavy chain sequences, thus obtaining the antibody with a full-length sequence. The binding activity of the antibody obtained after mutation in human TSLP was detected using the ELISA method. The results showed that the affinity activity of hu3-11 for human TSLP is still high, indicating that hotspot mutations in HCDR3 and LCDR3 of the humanized antibody mab3 do not affect antibody activity. (3) Affinity maturation of the hu3-11 antibody The hu3-11 molecule underwent affinity maturation. The affinity maturation process was as follows: Construction of the yeast library: Degenerate primers were designed and the engineered mutant amino acids were introduced into the antibody hu3-11 scFv mutant libraries by the PCR method, with the size of each library being approximately 109. The constructed yeast libraries were verified for their diversity by the sequencing method. In the first round of screening, approximately 5 × 10¹⁰ cells from the mutant hu3-11-scFv and biotinylated TSLP-Fc protein libraries (1–10 pg / ml) were incubated in 50 ml of 0.1% bovine serum albumin (BSA) containing phosphate-buffered saline (PBSA) for 1 hour at room temperature. The mixture was then washed with 0.1% PBSA to remove unbound antibody fragments. Next, 100 µL of streptomycin beads (Milenyi Biotec, Auburn, CA) were added to the biotinylated TSLP-Fc-bound hu3-11-scFv antibody mutant libraries, and the mixture was loaded into the AutoMACS system for sorting. Cells with high affinity for TSLP-Fc were collected from the antibody library and induced at 250 rpm and 20sC for 18 h. The resulting enriched library was then subjected to the second round of screening against biotinylated recombinant TSLP-Fc protein. For the third and fourth rounds of selection, cells from the previous round's library were incubated with biotinylated recombinant TSLP-Fc protein (0.1–1 pg / mi) and 10 pg / mi mouse anti-cMyc antibody (9E10, sigma) in 0.1% PBSA at room temperature for 1 h. The mixture was washed with 0.1% PBSA to remove unbound antibody fragments. Goat anti-mouse Alexa488 (A-11001, Life Technologies) and streptavidin PE (S-866, Life Technologies) were added, and the mixture was incubated at 4°C for 1 h. The mixture was again washed with 0.1% PBSA to remove unbound antibody fragments. Finally, high-affinity antibodies were selected by FACS detection (BD FACSAria™ FUSION). The hu3-11-scFv mutant libraries underwent two rounds of MACS screening and two rounds of FACS screening using biotinylated TSLP-Fc antigen. Approximately 400 individual yeast clones were then selected for culture and expression induction. Binding of individual yeast clones to TSLP-Fc antigen was detected using FACS, and high-affinity individual yeast clones were selected and subjected to sequencing verification. The sequenced clones were compared and analyzed. After removing redundant sequences, the non-redundant sequences were converted into full-length antibodies for mammalian cell expression. The sequences of the variable regions of the light chain obtained by affinity maturation are as follows: frnofrLn / Lznz / e / YiAi >hu3VL5 E1VLTOSPATLSLSPGERATLSCRASSSVSYMHWYQQKPGQAPRPWIYATSNLA SGVPARFSGSGSGTSYTLTISRLEPEDFAVYYCQQSDNVRGFGGGTKVEIK SEQ ID NO: 51 >hu3VL65EIVLTOSPATLSLSPGERATLSCRASSSVSYMHWYOOKPGOAPRPWIYATSNLA SGyPARFSGSGSGTSYTLTISRLEPEDFAVYYCQQSDSGREFGGGTKVEIK SEQ ID NO: 52 The light chain variable regions obtained were recombined with the heavy chain variable regions of the humanized antibody mab3 to obtain a novel humanized antibody mab3. For example, huVL5 and huVL6 were combined with hu3VH2-H110Y respectively to obtain the novel antibody molecules hu3-12 and hu3-13, which are shown in detail below: frnQfrin / Lznz / e / YiAi Table 12. Antibodies obtained by affinity maturation Antibody hu3VH hu3VL hu3-12 hu3VH2-H110Y hu3VL5 hu3-13 hu3VH2-H110Y hu3VL6 The CDR sequences of the humanized mab antibody obtained after affinity maturation are shown below: Table 13. CDR of antibodies of the humanized mab3 antibody obtained by affinity maturation Antibody Heavy chain Light chain hu3-12 HCDR1 DDYMN SEQ ID NO: 14 LCDR1 RASSSVSYMH SEQ ID NO: 17 HCDR2 IISPYNGGTSYNQKFKG SEQ ID NO: 15 LCDR2 ATSNLAS SEQ ID NO: 18 HCDR3H110Y EDYDYDGYAMDY SEQ ID NO: 45 LCDR3-V1 QQSDNVRG SEQ ID NO: 53 hu3-13 HCDR1 DDYMN SEQ ID NO: 14 LCDR1 RASSSVSYMH SEQ ID NO: 17 HCDR2 IISPYNGGTSYNQKFKG SEQ ID NO: 15 LCDR2 ATSNLAS SEQ ID NO: 18 HCDR3- H110Y EDYDYDGYAMDY SEQ ID NO: 45 LCDR3-V2 QQSDSGRE SEQ ID NO: 54 frnofrLn / Lznz / e / YiAi The newly obtained humanized mab3 antibody was subjected to ELISA to detect its binding activity to human TSLP. The results showed that hu3-12 and hu3-13 still have a high binding capacity to human TSLP. This demonstrated that changes in LCDR3 would not affect the activity of the hu3 antibody series. In summary, the CDRs of the humanized antibody mab3 have the sequences shown below: Table 14. General formula sequences of the CDR regions of the humanized antibody mab3 Heavy chain Light chain HCDR1 DDYMN SEQ ID NO: 14 LCDR1 RASSSVSYMH SEQ ID NO: 17 HCDR2 IISPYNGGTSYNQKFKG SEQ ID NO: 15 LCDR2 ATSNLAS SEQ ID NO: 18 HCDR3 (general formula) EDYDYDGYAMDXi SEQ ID NO: 47 LCDR3 (general formula 2) QQSDX3X4RX5 SEQ ID NO: 55 Where, Xi is H or Y, X3 is N or S, X4 is V or G, Xs is G or E. The combinations of variable regions of the light and heavy chain of the humanized antibody mab3 after hotspot mutation and affinity maturation are shown in the following table: Table 15. Antibody sequences after affinity maturation VH Antibody (SEQ ID NO) VL (SEQ ID NO) hu3-11 50 49 hu3-12 50 51 hu3-13 50 52 5.2 Selection and reverse mutations of human FR regions for mab119 For mab119, IGHV1-69*02 and HJ6*01 were selected as templates for VH, and IGKV4-1*01 and IGKJ2*01, as well as IGKV3-11*01 and IGKJ2*01, were selected as templates for VL. The CDR regions of the murine antibody were grafted into the selected humanized templates, and the FR regions were reverse-mutated to obtain different light-chain and heavy-chain variable regions. The variable region sequences obtained by CDR grafting are as follows: >hull9-VL CDR (Grafted, IGKV4-l*01) DI VMTQSPDSLAVSLGERATINCRASESVDNSGLSFMHWY00KPGQPPKLL1Y RASNLGSGVPDRFSGSGSGTDFTITISSLOAEDVAVYYCOQINTDPITFGOGTK LEIK SEQ ID NO: 56 >hull9VL4 (Grafted, IGKV3-ll*01) EIV LTQS PATL SLS PGER AT LSCRASESVDNSGLSFMHW YQQ K PGQ APR LLIY R ASNLGSGIPARFSGSGSGTDFTITISSLEPEDFAVYYCOQINTDPITFGOGTKLEI K SEQ ID NO: 59 >hull9-VH CDR (Grafted, IGHVl-69*02) EVQLVQSGAEVKKPGSSVKVSCKASGGTFFSTYNMHWVRQAPGQGLEWMGA IYPGNGETSYNQKFKDRVT1TADKSTSTAYMELSSLRSEDTAVYYCAREDDYG EGYFDVWGOGTTVT VSS SEQ ID NO: 62 The reverse mutations of the humanized antibody mab119 are shown in the following table: Table 16. Retromutations of mab119 hu119VL hu119VH hu119VL1 Grafted (IGKV4-1 *01) hu119VH1 Grafted (IGHV1-69*02) hu119VL2 Grafted (IGKV4-1 *01 )+M4L hu119VH2 G27F, I69L, A71V hu119VL3 Grafted (IGKV4- 1*O1)+I48L, V58I hu119VH3 G27F, M48I, V67A, I69L, A71V hu119VL4 Grafted (IGKV3-11 *01) hu119VH4 G27F, R38K, Q39H, M48I, V67A, I69L, A71V hu119VL5 Grafted (IGKV3-11 *01) +A43P, I48L hu119VH5 M48I, V67A, I69L, A71V hu119VL6 Grafted (IGKV311 *01 )+E1 D, A43P, I48L hu119VH6 V2A, G27F, M48I, V67A, I69L, A71V hu119VH7 M48I, V67A, I69L, A71V, S76R hu119VH8 V2A, G27F, M48I, V67A, I69L, A71V, S76R Note: For example, M4L represents that, according to the Kabat numbering system, M at position 4 mutates back to L. Graft represents that the murine CDR antibody is implanted into the FR region sequence of the human germline. The specific sequences of the variable regions of the humanized antibody mab119 are as follows:> huí 19VL1 (grafted (IGKV4-1* 01)) DIVMTOSPDSLAVSLGERATINCRASESVDNSGLSFMHWYOQKPGOPPKLLIY RASNLGSGVPDRFSGSGSGTDFTLTISSLQAF.DVAVYYCOQINTDPLTFGOGTK LEIK SEQ ID NO: 56 >hu119VL2 DIVLTOSPDSLAVSLGERATINCRASESVDNSGLSFMHWYOQKPGOPPKLLIY RASNLGSGVPDRFSGSGSGTDFTLTISSLOAEDVAVYYCOQINTDPLTFGOGTK LEIK SEQ ID NO: 57 >hu119VL3 DIVMTOSPDSLAVSLGERATINCRASESVDNSGLSFMHWYOOKPGOPPKLLLY RASNLGSG1PDRFSGSGSGTDFTLT1SSLOAEDVAVYYCOQ1NTDPLTFGOGTKL E1K SEQ ID NO: 58 >hu119VL4 (Grafted, IGKV3-11 *01) EIVLTQSPATLSLSPGERATLSCRASESVDNSGLSFMHWYQQKPGQAPRLLIYR ASNLGSGIPARFSGSGSGTDFTLTISSLEPEDFAVYYCOQ1NTDPLTFGOGTKLE1 K SEQ ID NO: 59 >hu119VL5 EIVLTOSPATLLSLSPGERATLSCRASESVDNSGLSFMHWYOQKPGOPPRLLLYR ASNLGSGIPARFSGSGSGTDFTLTISSLEPEDFAVYYCQQINTDPLTFGOGTKLEI K frnofrLn / Lznz / e / YiAi SEQ ID NO: 61 >hull9VHl (Injertado) EVQLVQSGAEVKKPGSSVKVSCKASGG FFSTYNMHW 'VRQAPGQGLEWMGA lYPGNGEISYNQKFKDRVIUADKS'l STAYMELSSLRSED IAVYYCAREDDYG EGYFDVWGQGTTVTVSS SEQ ID NO: 62 >hu I 19VH2 E\ QLVQSGAEVKKPGSSVKVSCKASGF TFSTYNMHW VRQAPGQGLEWMGA!. YPGNGETSYNOKFKDRVTLTVDKSTSTAYMEI.SSERSEDTAVY YCAREDDYG EGYFDVWt jQ( JTT VT VSS SEQ ID NO: 63 huí 19VH3 E\ QL\QSGAEVKKPGSSVKVSCK ASGETFSTYNMHW VKHAPGOGLEWIGAI YPGNGETSYNQKFKDRATLTVDKSTSTAYMEI.SSLRSEDTAVYYCAREDDYG EGYFDVWGOGTTVTVSS SEQ ID NO: 64 huí 19VH4 F.VOLVOSGAEVKKPGSSVKVSCKASGFTFSTYNMHWVKHAPGOGLEWIGAI YPGNCiETSYNQKFKDRATLTVDKSTSTAYMELSSLRSEDTAVYYOAREDDYC; EGYFDVWGQGTTVTVSS SEQ ID NO: 65 >hul 19VH5 EVQLVQSGAEVKKPGSSVKVSKKASCiGTFSTjQAlHWVRQAPGQGLEWIGAJ YPGNGE rSYNOKFKDRA rL rVDKS rS I AYMELSSLRSED I AVYYCAREDDYG EGYFDVWGOGTTVTVSS SEQ ID NO: 66 huí 19\Ή6 EAOLVOSGAEVKKPGSSVKVSCKASGHESTYNMHWVROAPGOGLEW1GA1 YPGNGETSYNOKFKDRATLTVDKSTSTAYMELSSLRSEDTAWYCAREDDYG EGYFDVWGOGTTVTVSS SEQ ID NO: 67 -huí 19VH7 E VQIΛQSGAEVKKPGSSVKVSCKASGGTFFSTYNMIIWVRQ APGQGI EW1GAl YPGNGETSYNQKFKDRAIL I VDKS FRIAYMELSSLRSED1 A\ YYCAREDDYG EGYFDVWGQGTTVTVSS SEQ ID NO: 68 huí 19VH8 EAQLVQSGAEVKKPGSSVKVSCKASGFTFSTYNMHWVRQAPGQGLEWIGAI YPGNGE I SYNQKFKDRA1L I VDKS IRI AYMELSSLRSED l AWYCAREDDYG EGYFDVWGOGTTVTVSS SEQ ID NO: 69 Note: Single underlining represents variable regions and double underlining represents reverse mutations. The variable light and heavy chain regions mentioned above were combined with sequences from the human germline light and heavy chain constant regions to form the final complete light and heavy chain sequences, thus obtaining the antibody with a full-length sequence. By way of example, for the humanized antibody mab119 in the present invention, the heavy chain constant region is the lgG1-YTE constant region shown in SECTION ID NO: 133, and the light chain constant region is the kappa chain constant region shown in SECTION ID NO: 134, but these can also be replaced with other constant regions known in the art. The heavy and light chain variable regions of the humanized antibody mab119 are shown in Table 17. Table 17. Variable regions of heavy and light chain of the humanized antibody mab119 frnofrLn / Lznz / e / YiAi VH Antibody (SEQ ID NO) VL (SEQ ID NO) hu119-01 62 56 huí19-02 63 56 huí19-03 64 56 huí 19-04 65 56 huí 19-05 62 57 huí 19-06 63 57 huí 19-07 64 57 huí 19-08 65 57 huí 19-09 62 58 hu119-10 63 58 huí 19-11 64 58 hu119-12 65 58 hu119-13 64 59 hu119-14 66 59 hu119-15 67 59 hu119-16 68 59 hu119-17 69 59 hu119-18 64 60 hu119-19 66 60 huí 19-20 67 60 huí119-21 68 60 huí19-22 69 60 huí19-23 64 61 huí 19-24 66 61 huí 19-25 67 61 I ran away 19-26 68 61 I fled 19-27 69 61 frnofrLn / Lznz / e / YiAi The binding activity of the humanized antibody to human TSLP was detected using the ELISA method, and the results showed that the humanized mab119 antibodies can specifically bind to human TSLP. (2) Mutations of huí 19 A hotspot was detected in the DNS LCDR1 sequence of the humanized antibody mab119; therefore, the corresponding site was mutated to N31S or N31Q. The LCDR1 sequences obtained after mutation are as follows: Table 18. LCDR1 after mutation of the humanized antibody mab119 site huí 19 LCDR1-N31S RASESVDSSGLSFMH SEQ ID NO: 70 huí 19 LCDR1-N31Q RASES VDQSGLSFMH SEQ ID NO: 71 Note: The positions of the mutation sites in Table 19 are numbered according to the natural order. As an example, the mutant sequences huí 19VL2, huí 19VL6 obtained after the mutation are as follows: Ιηι 119VL2-N31S DÍVn.TOSPDSLAVSLGERATTNCRASESVDSSGLSrMIIWYOOKPGOPPKLLIYR ASNLGSGVPDRFSGSGSGIDE TLTISSLQ.AEDVAV AND YCQQINTDPLTFGOG IKL EIK SEQ ID NO: 72 >hul 19VL2-N31Q DIVLTQSPDSLAVSLGERAT1NCR.ASESVDQSGLSFMHWYQQKPGQPPKLL1Y RASNLGSGVTDRFSGSGSGTDFTLTISSLOAEDVAVYYCOQINTDPLTFGOGTK LEIK SEQ ID NO: 73>hu 119VL6-N3 1S DIVLTOSPATLLSLSPGERATLSCRASESX DSSGLSFMHWYOOKPGOPPRLLLYR ASNLGSGIPARFSGSGSGI DF I El ISSLEPEDFAVYYCOQINTDPLTFGOGI KLEI K SEQ ID NO: 74>hul 19VL6-N3 1Q DIVLTQSPAI LSLSPGERAI LSCRASESVDQSGLSFMHWYOOKPGOPPRLLLYR ASNEGSGIPARFSGSGSGTDFTETISSEEPEDFAVYYCQQINTDPETFGQGTKEEI K SEQ ID NO: 75 Note: The simple subrayado represents regional variables and the double subrayado represents different variables. The resulting hu119VL2 and hu119VL6 mutants were combined with hu119VH to obtain novel humanized hu119 antibodies. For example, hu119VL2-N31S and hu119VL2-N31Q were combined with hu119VH3 to obtain the hu19-28 and hu19-29 antibodies, respectively; hu119VL3-N31S was combined with hu119VH8 to obtain the hu19-30 antibody. The following are exemplary combinations of variable regions of the mutated antibodies: Table 19. Combinations of variable regions of the humanized antibody after the frnQfrtn / Lznz / e / YiAi hotspot mutation hu119VH huí19VL huí 19-28 hu119VH3 huí 19VL2-N31S huí 19-29 hu119VH3 huí 19VL2-N31Q huí 19-30 hu119VH8 huí 19VL6-N31S The affinity of the antibody obtained after the mutation with human TSLP was detected using the ELISA method. The results showed that the huí 19-28 and huí 19-29 antibodies still have a relatively high affinity with human TSLP, demonstrating that the N31S and N31Q mutations of LCDR2 will not affect the activity of the anti-TSLP antibody. In summary, the CDRs of the humanized antibody mab119 have the sequences shown below: EnQELn / Lznz / e / YiAi Table 20. CDR of the humanized antibody mab119 HCDR1 TYNMH SEQ ID NO: 20 LCDR1- general formula RASESVDXeSGLSFMH SEQ ID NO: 76 HCDR2 AIYPGNGETSYNQKFKD SEQ ID NO: 21 LCDR2 RASNLGS SEQ ID NO: 24 HCDR3 EDDYGEGYFDV SEQ ID NO: 22 LCDR3 QQINTDPLT SEQ ID NO: 25 Where, Xe is selected from N, S and Q. 5.3. Humanization of mab179 (1) Template selection and reverse mutations for humanization of the murine antibody mab179 For mab179, IGHV1-69*02 and IGHJ6*01 were selected as templates for VH, and IGKV4-1*01 and IGKJ2*01 or IGKV2-29*02 and IGKJ2*01 were selected as templates for VL. The CDR regions of the murine antibody were grafted into the selected humanized templates, and the FR regions were reverse-mutated to obtain light-chain and heavy-chain variable regions with different sequences. The sequences of the humanized variable region and the reverse mutations are as follows: >hu179VL1 (Grafted (IGKV4-1*01)) DIVMTOSPDSLAVSLGERAnNCKASOSVSSDVTWYOQKPGOPPKLLlYYVSN HYTG\ PDRFSGSGSG I DETLT1SSLOAED\ AVY YCQQHHRFPLI FGQG I KLE1K SEQ ID NO: 77 >hu179VL5 (Grafted (IGKV2-29*02)) DIVM TQTPLSLSVIPGQPAS1SCKASQSVSSDVTW YLQKPGQSPQLL1Y YVSNH YTGVPDRESGSGSG I OF I LKISRVEAEDVGVYYCQQHHREPLTEGQGTKLE1K SEQ ID NO: 81 >hu179\ / H1 (Grafted) E VQLVQSG AE VKKPGSS VK V SCKASGGTF SNYLIEW VRQ APGQGLE WMG VI DPGNGDTNYNENFKGRVTITADKSTSTAYMELSSLRSEDTAW YCAREDNTGT AFDYWGOGTTVTVSS SEQ ID NO: 85 Table 21. Templates and reverse mutations for the humanization of mab179 hu179VL1VL hu179VH hu179VL1 Grafted (IGKV4-1*01) hu179VH1 Grafted (IGHV1-69*02) hu179VL2 Grafted (IGKV4-1*01) P43S hu179VH2 G27Y, I69L hu179VL3 Grafted (IGKV4-1*01) P43S,L73F hu179VH3 G27Y, M48I, V67A, I69L, M80I hu179VL4 Grafted (IGKV4-1*01) D1S,P43S hu179VH4 G27Y,R38K, M48I, R66K, V67A, I69L, M80I, S82bR hu179VL5 Grafted (IGKV229*02) hu179VH5 G27Y.T28 A, M481, V67 A, 16 9L hu179VL6 Grafted (IGKV229*02), D1S hu179VL7 Grafted (IGKV229*02) D1S,L73F hu179VL8 Grafted (IGKV229*02) D1S,S67Y Note: For example, P43S represents that, according to the Kabat numbering system, P at position 43 is mutated back to S. Graft represents that the murine antibody CDRs are implanted into the FR region sequences of the human germline. The variable regions of the humanized antibody mab179 are shown below: > hu179VL1 (Grafted (IGKV4-1 * 01)) DIVMTQSPDSLAVSLGERATINCKASQSVSSDVTWYOQKPGQPPKEL1YYVSN HYTGVPDRFSGSGSGTDFTLTISSLOAEDVAWYCQOHHRFPLTFGOGTKLEIK SEQ ID NO: 77 >hul79VL2 DIVMTOSPDSLAVSLGERATINCKASQSVSSDVTWYOOKPGOSPKLLIYYVSN HYTGVPDRFSGSGSGTDFTLTISSLOAEDVAVYYCOOHHRFPLTFGOGTKLEIK. SFQIDNO: 78 hu 179 VL3 DIVMTOSPDSLAVSLGERATINCKASOSVSSDVTWYOOKPGQSPKLLIYYVSN HYTGVPDRFSGSGSGTDFTFTISS1.OAF.DVAVYYCOQHHRFPI.TFGOGTKLEIK SFQIDNO: 79 hii 179 VL4 S1VM IOSPDSLAVSLGERAHNCKASQSVSSDVTW YQQKPGQSPKLL1YYVSN HYTGVPDRFSGSGSGTDFTLTISSEQAEDVAVYYCOOΗHRFPI TFGOGTK1.F,IK SFQIDNO: 80>hul79VL5 (Injertado (IGKV2-29*02)) DIVMTOTPLLSSVTPGOPASISCKASOSVSSDVTWYLOKPGOSPOLLIYYVSNH YTGVPDRFSGSGSGTDFTEKISRVEAEDVGVYYCOQHHRFPETFGOGTKEEIK SEQ ID NO: 81 >hu!79VL6 SIVM TQTPLSLSV I PGOPAS1SCKASOSVSSDV'I WYLOKPGOSPOLLlYYVSSIH YTGVPDRFSGSGSGTDFTEKISRVEAEDVGVYYCOQHHRFPETFGOGTKEEIK SFQIDNO: 82 >hu!79VL7 S1VMTOTPLSLSVTPGOPASISCKASOSVSSDVTWYLOKPGOSPOLLIYYVSNH YTGVPDRFSGSGSGTDFTFKISRVFAEDVGVYYCOQHHRFPETFGOGTKLFIK SFQIDNO: 83 >hu!79VL8 SI VMTOPLSLSVTPGOPASISCK ASOSVSSDVTWYLOKPGOSPOEIJYYVSNH YTGVPDRFSGSGYGTDFTIKISRVEAEDVGVYYCOOHHRFPITFGOGTKl.F.IK SFQIDNO: 84>hul79VHl (Injertado) EVOEVOSGAFVKKPGSSVKVSCKASGGTFSNYEIFWVROAPGOGI.FAVMGVI DPGNGDTNYNENFKGRVTITADKSTSTAYMELSSLRSF.DTAVYYCAREDNTGT AFDYWGQGTTVTVSS frnofrLn / Lznz / e / YiAi SEQ ID NO: 85 >hul79VH2 EVQLVQSGAFVKKPGSSVKVSCKASGYTFSNYL1EWVRQAPGQGLEWMGV1 DPGNGDTNYNENFKGRVTLTADKSTSTAYMELSSLRSEDTAVYYCAREDNTG TAFDYWGOC ÍTTVTVSS SEQ ID NO: 86 hii 179VI13 E VQ LVQ SG AEVKK PG SSVKV SC KA SG YT F SNYLIEW V RQ A PGQGL E WK i VID PGNGDTNYNENFKGRA IL IADKS IS FAYIELSSLRSED IA\ YYCAREDNTGIA FDYWGQGI T\ I VSS SEQ ID NO: 87 h1117QVI14 EVQLVQSGAEVKKPGSSVKVSCKASGY TFSNYLIEWX KOAPGOGLEW1GVID PGNGDTNYNENFKGKATLTADKS IS EAY1ELSRLRSEDI AVYYCAREDNTGI A FDYWGOGTTVTVSS SEQ ID NO: 88 >hu 1 79VH5 E\ QI VOSGAF VK KPGSSVK VSCK ASGYAFSNYI.IF. W\ROAPGOGI EWIGVID PGNGDTNYNENFKGRATLTADKSTSTAYMELSSLRSEDTAVYYCAREDNTGT AFDYWGOGTT VT VSS SEQ ID NO: 89 Note: The simple sub-company represents the CDR and the double sub-company represents the different positions in the market. The variable light and heavy chain regions mentioned above were combined with sequences from the human germline light and heavy chain constant regions to form the final complete light and heavy chain sequences, thus obtaining the antibody with a full-length sequence. By way of example, for the humanized antibody mab199 in the present invention, the heavy chain constant region is the lgG1-YTE constant region shown in SECTION ID NO: 133, and the light chain constant region is the kappa chain constant region shown in SECTION ID NO: 134, but these can also be replaced with other constant regions known in the art. frnofrLn / Lznz / e / YiAi Table 22. Combinations of heavy and light chain variable regions of the humanized antibody mab179 Antibody VH (SEQ ID NO) VL (SEQ ID NO) huí 79-01 85 77 huí 179-02 85 78 huí 79-03 86 77 huí 179-04 86 78 huí 79-05 87 77 huí 79-06 87 78 huí 79-07 87 79 hu 179-08 87 81 huí 79-09 87 82 hu179-10 87 83 hu179-11 87 84 hu179-12 88 77 hu179-13 88 78 hu179-14 89 79 hu179-15 89 80 hu179-16 89 81 hu179-17 89 82 hu179-18 89 83 hu179-19 89 84 The affinity of the humanized antibody mab179 with human TSLP was detected using the ELISA method, and the results showed that the humanized antibodies mab179 have a very good affinity with human TSLP. (2) Mutations of the hu179 antibody Through screening, hotspots were found in the HCDR2 and LCDR2 sequences of the humanized antibody mab179. Therefore, the corresponding hotspots were mutated to eliminate the risk of modification of the molecule. In one of the models, the HCDR2 GNG of hu179VH1 underwent amino acid mutation, and the sequences of hu179VH1 after the mutation are: hu179VH1- N55Q F.VQEVQSGAF.VKKPGSSVK VSCKASGGTFSNYIJEWVRQAPGQGEEWMGVl DPGOGDTNYNENFKGRVTITADKSTSTAYMELSSLRSEDTAVWCAREDNTGT15AFDYWGOGTTVTVSS SEQ ID NO: 90 hu!79VHl- N55V EVQLVQSGAEVKKPGSSVKVSCKASGGTFSNYLIEWVRQAPGQGLEWMGVI DPGVGDTNYNENFKGRVTITADKSTSTAYMELSSLRSEDTAVYYCAREDNTGT AFDYWGOGTTVTVSS SEQ ID NO: 91 hu!79VHl- G56V EVOLVOSGAEVKKPGSSVKVSCKASGGTFSNYL1EWVROAPGOGLEWMGV1 DPGNVDTNYNENFKGRVnTADKSTSTAYMELSSLRSED TAVYYCAREDNTGT AFDYWGOGTTVTVSS SEQ ID NO: 92 Note: The single underlined portion represents the CDRs and the double underlined portion represents the reverse mutation sites. The sequences of the HCDR2 regions of the humanized antibody mab179 obtained after the mutation are as follows: frnofrLn / Lznz / e / YiAi Table 23. HCDR2 mutants of the humanized antibody mab179 hu179 HCDR2-N55Q VIDPGQGDTNYNENFKG SEQ ID NO: 93 hu179 HCDR2-N55V VIDPGVGDTNYNENFKG SEQ ID NO: 94 hu179 HCDR2-G56V VIDPGNVDTNYNENFKG SEQ ID NO: 95 Note: The positions of the mutation sites in Table 24 are numbered according to the natural order. The CDR regions of the humanized antibody mab179 can be obtained from above and are shown below: Table 24. CDR of the humanized antibody mab179 after the mutation HCDR1 NYLIE SEQ ID NO: 26 LCDR1 KASQSVSSDVT SEQ ID NO: 29 HCDR2 (general formula) VIDPGX7XeDTNYNENFKG SEQ ID NO: 96 LCDR2 YVSNHYT SEQ ID NO: 30 HCDR3 EDNTGTAFDY SEQ ID NO: 28 LCDR3 QQHHRFPLT SEQ ID NO: 31 Where, X7 is selected from N, Q or V, X8 is selected from G or V. frnQfrin / Lznz / e / YiAi The hu179VH1 mutants obtained after mutation were combined with the humanized hu179VL to obtain novel humanized mab179 antibodies. The exemplary antibodies from a combination of hu179VH1 and hu179VL2 mutants are as follows: Table 25. Combinations of the antibody variable regions after mutation Variable region hu179VH1-N55Q huí79VH1-N55V hu179VH1-G56V hu179VL2 hu 179-20 huí 79-21 huí 79-22 The affinity of the antibody obtained after mutation with human TSLP was detected using the ELISA method. The results showed that the antibodies after the HCDR2 mutation still maintain a relatively high affinity with human TSLP. This showed that the N55Q, N55V, and G56V point mutations of HCDR2 in the humanized antibody mab179 do not significantly affect the antibody's affinity activity with TSLP. Using the same method, N55Q, N55V, and G56V point mutations (numbered in natural order) were introduced into hu179VH2, hu179VH3, hu179VH4, and hu179VH5, respectively, and the resulting heavy and light chain variable regions were recombined to produce novel humanized mab179 antibodies. The mutated sequence of hu179VH3 is shown below as an example: >hu 179VH3-N55 V EVQI .VQSG AE VKKPGSS VK VSCK A SGYTrSNYLIEW VRQ APGQGITAV1G VID PGVGDTNYNENFKG RATL TA DKSTS ΤΑ YIE LS SLRSE DTAV YYCAR EDNTGTA FDYWGOG II VI VSS SEO ID NO: 97 Note: The single underlined portion represents the CDRs and the double underlined portion represents the reverse mutation sites. In some other examples, the LCDR2 of the humanized antibody mab179 underwent an amino acid mutation. For example, the sequences of hu179VL2 after the mutation are as follows: >hul79VL2-Y50E DIVMTQSPDSLAVSLGERATINCKASOSVSSDVTWYQOKPGOSPKLLIYF.VSN I lYTGVPDRFSGSGSGTDFTLTISSLOAEDVAVWCQQI HIRFPLTFGOGTKLEIK SEQ ID NO: 98 >hul79VL2-S52D DIVMTQSPDSLAVSLGERATINCKASQSVSSDVTWYOQKPGOSPKLLIYYVDN 1IYTGVPDRFSGSGSGTDFTLTISSLOAEDVAVYYCQQIII IRFPLTFGOGTKLEIK SEQ ID NO: 99 hu I 79VL2-S52E DIVVITQSPDSLAVSLGFRATINCKASOSVSSDVTWYOOKPGQSPKLLIYYVEN IIYTGVPDRFSGSGSGTDFTLTISSLOAEDVAVYYCOQ1II IRFPLTFGOGTKLEIK SEQ ID NO: 100 >hu!79VL2-N53Q D1VM rOSPDSLAVSLGERAriNCKASQSVSSDV rWYOQKPGOSPKLLIYYVSQ HYTGVPDRFSGSGSGTDFTLTISSLOAEDVAWYCOQHHRFPLTFGOGTKLEIK SEQ ID NO: 101 >hu!79VL2-N53D DIVMTOSPDSLAVSLGERAT1NCKASOSVSSDVTWYOOKPGQSPKLLIYYVSD HYTGVPDRFSGSGSGTDFT1.TISSLQAEDVAVYYCQQHHRFPLTFGQGTK1.EIK SEQ ID NO: 102 >hul79VL2-N53E DIVMTOSPDSLAVSLGEAnNCKASQSVSSDVTWYOOKPGQSPKLLIYYVSE HYTGVPDRFSGSGSGTDFTLTISSLOAEDVAWYCOQHHRFPLTFGOGTKLEIK SEQ ID NO: 103 >hul79VL2-H54Y DI VMTQSPDSL AVSLGER ATI NCKASQSVSSDVTW YQQK PGQSPK LLIYYVSN YYTGVPDRFSGSGSGTDFTLTISSLQAEDVAVYYCQQHHRFPLTFGQGTKLEIK SEQ ID NO: 104 frnofrLn / Lznz / e / YiAi >hu!79VL2-H54D DIVMTQSPDSLAXSLGERATINCKASQSX'SSDX TWYQQKPGOSPKLL1YYXSN DYTGX PDRFSGSGSGTDFTLTISSI.OAF.DVAXWCOQHFIRFPITFGOGTKI.EIK SEQ ID NO: 105 >hul79VL2-H54E5divmtospdslavslgeraunckasqsvssdvt WYOOKPGOSPKLLIYYX SN EYTGVPDRFSGSGSGTDFTI.TISSl.OAEDVAVYYCQQHHRFPLTFGOGTKI.F.IK SEQ ID NO: 106 >hul79VL2-Y55E DI\'M IOSPDSLAVSLGERAHNCKASQSVSSDV I WYQQKPGOSPKLLIYYX SN HETGX'PDRFSGSGSGTDFTI.TISSLOAEDXAXYYCOOHHRFPLTFGOGTKI.F.IK SEQ ID NO: 107 Note: The single underlined portion represents the CDRs and the double underlined portion represents the reverse mutation sites. frnQfrLn / Lznz / e / γΐΛΐ The sequences of the humanized LCDR2 antibody mab179 obtained after the mutation are as follows: Table 26. LCDR2 mutants of the humanized antibody mab179 Mutant Sequence hu179 LCDR2-Y50E EVSNHYT SEQ ID NO: 108 hu179 LCDR2-S52D YVDNHYT SEQ ID NO: 109 hu179 LCDR2-S52E YVENHYT SEQ ID NO: 110 hu179LCDR2-N53Q YVSQHYT SEQ ID NO: 111 hu179 LCDR2-N53D YVSDHYT SEQ ID NO: 112 hu179 LCDR2-N53E YVSEHYT SEQ ID NO: 113 hu179 LCDR2-H54Y YVSNYYT SEQ ID NO: 114 hu179 LCDR2-H54D YVSNQYT SEQ ID NO: 115 hu179 LCDR2-H54E YVSNEYT SEQ ID NO: 116 hu179 LCDR2-Y55E YVSNHET SEQ ID NO: 117 frnofrLn / Lznz / e / YiAi It can be seen from the above that the general LCDR2 formula of the humanized antibody mab179 is: X9VX10X11X12X13T (SEQ ID NO: 118), where X9 is selected from Y or E, X10 is selected from S, D or E, Xn is selected from N, Q, D or E; X12 is selected from H, Y, D or E; X13 is selected from E or Y. The CDR regions of the humanized antibody mab179 are those shown in the following table: Table 27. CDR of the humanized antibody mab179 HCDR1 NYLIE SEQ ID NO: 26 LCDR1 KASQSVSSDVT SEQ ID NO: 29 HCDR2 VIDPGX7XsDTNYNENFK G SEQ ID NO: 96 LCDR2 31 Where, X7 is selected from N, Q or V, X8 is selected from G or V; X9 is selected from Y 10 or E; X10 is selected from S, D or E; Xn is selected from N, Q, D or E; X12 is selected from H, Y, D or E; X13 is selected from E or Y. The hu179VL2 mutants obtained after mutation were combined with the humanized hu179 heavy chain variable regions to obtain novel humanized mab179 antibodies. As an example, the hu179VL2 mutants were combined with 15 hu179VH1, hu179VH3, and the CDRs, and the combinations of the heavy and light chain variable regions of the resulting humanized mab179 antibodies are shown below: Table 28. The sequences of the CDR regions of the humanized antibody mab179 after the LCDR2 mutation HCDR1 NYLIE SEQ ID NO: 26 LCDR1 KASQSVSSDVT SEQ ID NO: 29 HCDR2 VIDPGNGDTNYNENFKG SEQ ID NO: 27 LCDR2 XsVXeXzXeXsT SEQ ID NO: 118 HCDR3 EDNTGTAFDY LCDR3 QQHHRFPLT SEQ ID NO: 28 SEQ ID NO: 31 Where, X5 is selected from Y or E; X6 is selected from S, D or E; X7 is selected from N, Q, D or E; X8 is selected from H, Y, D or E; X9 is selected from E or Y. Table 29. Combinations of heavy and light chain variable regions of the humanized antibody mab179 after the LCDR2 frnofrLn / Lznz / e / YiAi mutation VH Antibody (SEQ ID NO) VL (SEQ ID NO) huí 79-23 85 102 huí 79-24 85 104 huí 79-25 87 98 huí 79-26 87 99 huí 79-27 87 100 huí 79-28 87 101 huí 79-29 87 103 huí 79-30 87 105 huí 79-31 87 106 huí 79-32 87 107 The affinity of humanized mab179 antibodies obtained after LCDR2 mutation for human TSLP was detected using the ELISA method. The results showed that the antibodies obtained after the LCDR2 hotspot mutation still have relatively good affinity for human TSLP. This indicates that the LCDR2 hotspot mutation does not affect the binding activity of humanized mab179 antibodies. Using the same method, N53Q, N53D, N53S, H54Y, Y50E, S52D, S52E, N53E, H54D, H54E, and Y55E mutations were introduced into the LCDR2 region of hu179VL3, hu179VL4, hu179VL5, hu179VL6, hu179VL7, and hu179VL8. The light chain variable regions and the heavy chain variable regions after mutation were combined to form novel humanized monoclonal antibodies (mab). In one modality, the sequence of hu179VL8 after mutation is shown below: hul79VL8-N53E: SIVMTOTPLSLSVTPGOPASISCKASQSVSSDVTWYLOKPGOSPOLLIYYVSEH YTGVPDRFSGSGYGTDFT1 KISRVF.AEDVGVYYCOQHHRFPLTFGOGTKLEIK SEQ ID NO: 119 The mutation-obtained hu179VL8-N53E and hu179VH3-N55V antibodies were combined to obtain a new antibody molecule, hu179-33, whose CDR sequences are shown below: frnofrLn / Lznz / e / YiAi Table 30. CDR regions of the hu179-33 antibody HCDR1 NYLIE SEQ ID NO: 26 LCDR1 KASQSVSSDVT SEQ ID NO: 29 HCDR2-N55V VIDPGVGDTNYNENFKG SEQ ID NO: 94 LCDR2-N53E YVSEHYT SEQ ID NO: 113 HCDR3 EDNTGTAFDY SEQ ID NO: 28 LCDR3 QQHHRFPLT SEQ ID NO: 31 Biacore detected the binding activity of antibodies obtained after mutation in human TSLP. The exemplary binding activity of the antibodies is shown below: Table 31. Affinity of huí 79-33 with human TSLP Antibody Affinity to huTSLP KD (M) AMG157 8.12E-12 hul79-33 9.03E-13 The results showed that the huí79-33 antibody has a relatively high specific binding activity to human TSLP. This indicated that hotspot point mutations in both HCDR2 and LCDR2 will not affect the affinity of the humanized antibody mab179 for human TSLP. It can be seen that in the humanized antibody molecule mab179, mutations of N55Q, N55V, and G56V in HCDR2 and mutations of N53Q, N53D, N53S, H54Y, Y50E, S52D, S52E, N53E, H54D, H54E, and Y55E in LCDR2 will not affect the antibody's binding to human TSLP, meaning they will not affect the activity of anti-TSLP antibodies. 5.4 Selection and reverse mutations of human FR regions for the mab199 antibody For mab199, IGHV1-46*01 and HJ6*01 were selected as templates for VH, and IGKV1-39*01 and IGKJ4*01 were selected as templates for VL. The CDR regions of the murine antibody were grafted into the selected humanized templates, and the FR region was reverse-mutated to obtain variable light-chain and heavy-chain regions with different sequences. The reverse mutations are shown in Table 32. Table 32. Reverse mutation design for mab199 hul99VL hul99VH hul99VLl Grafted hul99VHl Grafted hul99VL2 I48V hul99VH2 R71V, T73K, V78A hul99VL3 A43S, K45Q, I48V, D70Q. hul99VH3 M69L, R71V, T73K, V78A hul99VL4 G66V hul99VH4 M48I, V67A, M69L, R71V, T73K, V78A hul99VL5 I48V, G66V hul99VH5 R38K, M48I, R66K, V67A, M69L, R71V, T73K, V78A hul99VL6 A43S, K45Q, I48V, G66V, D70Q. hul99VH6 R38K, R66K, R71V, T73K, V78A hul99VH7 R38K, R67K, M69L, R71V, T73K, V78A Note: For example, I48V represents that, according to the Kabat numbering system, I at position 48 mutates back to V. Graft represents that murine antibody CDRs 5 are implanted into the FR region sequences of the human germline. The variable regions of the humanized antibody mab199 are shown below: >hu199VL1 (Grafted D1QMTQSPSSLSASVGDRVH TCRASEN1YSYLAW YOOKPGK APKLLIYFAKTL AEGVPSRFSGSGSGTDFTLTISSLOPEDFATYYCQHHYGTPWTFGGGTKVEIK SEQ ID NO: 120 0 hulWX 1.2 DIOMTOSPSSLSASVGDRVTITCRASENIYSYLAWYOOKPGKAPKLLVYFAKT LAEGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQHHYGTPWTFGGGTKVEIK SEQ ID NO: 121 >hu 199VL3 DIOMTOSPSSLSASVGDRVTITCRASENIYSYLAWYOOKPGKSPOLLVYFAKT5LAEGVPSRFSGSGSGTQFTLT1SSLOPEDFATYYCQHHYGTPWTFGGGTKVE1K SEQ ID NO: 122 >hul99VL4 DIQMTQSPSSI.S AS VGDRVTITCRASENTYSYLAWYQQKPGK APKLLI YFAKTL AEGVPSRFSGSVSGTDFTLTISSLOPEDFATYYCQHHYGTPWTFGGGTKVEIK SEQ ID NO: 123 >hu 199VL5 DIOMTOSPSSLSASVGDRVTITCRASENIYSYLAWYOOKPGKAPKLLVYFAKT LAEGVPSRFSGSVSGTDFTLHSSLOPEDFATYYCQHHYGTPWTFGGGTKVE1K SEQ ID NO: 124 >hu!99VL6 DIOMTOSPSSLSASVGDRVTITCRASENIYSYLAWYOOKPGKSPOELWFAKT LAEGVPSRFSGSVSGTOFTLTISSLOPEDFATYYCQHHYGTPWTFGGGTKVEIK SEQ ID NO: 125 >hul99VHl (Injertado) EVQLVQSGAEVKKPGASVKVSCKASGYTF TTYWMHWVRQAPGQGLEWMG MIDPSDSETTLIQKFKDRVTMTRDTSTSTWMELSSLRSEDTAVYYCARTLDG YYDYWGOGTTVTVSS SEQ ID NO: 126 > hul99VH2 EVOLVOSGAEVKKPGASVKVSCKASGYTFTTYWMHWVROAPGOGLEWMG MlDPSDSEnLlQKFKDRVTMTVDKSTSTAYMELSSLRSEDTAVYYCARTLDG YYDYWGOGTTVT V S S SEQ ID NO: 127 > huI99VH3 EVQLVQSGAEVKKPGASVKVSCKASGYTFTTYWMHWVRQAPGQGLEWMG MIDPSDSETTLIQKFKDRVTLTVDKSTSTAYMELSSLRSEDTAVYYCARTLDG YYDYWGOGTTVTVSS SEQ ID NO: 128 > hu 199VH4 EVQLVQSGAEVKKPGASVKVSCKASGY 1F FTYWMHWVRQAPGQGLEW1GM IDPSDSETTLIQKFKDRATLTVDKSTSTAYMELSSLRSEDTAVYYCARTLDGY YDYWGOGTTVTVSS frnofrLn / Lznz / e / YiAi SEQ ID NO: 129 >hul99VH5 EVOLVOSGAEVKKPGASVKVSKASGYTF TTYWMHWVKOAPGOGLEWIGM IDPSDSETTL1QKFKDKATLTVDKS T STA YM EL SS L RS E DTAV YYCA RTLDGY YDYWGQGTTVTVSS SEQ ID NO: 130 > hul99VH6 EVQLVQSGAEVKKPGASVKVSKASGYTFFTYWMHWVKQAPGQGLEWVÍG MIDPSDSETTLIQKFKDKVTMTVDKSTSTA YMEL S SLR SEDTAV Y YC ARTLDG Y YDYWGQGTTVTVSS SEQ ID NO: 131 > hul99VH7 EVQLVQSGAEVKKPGASVKVSCKASGYTFFTTYWMUWVKQAPGQGLEWMG MIDPSDSETTLIQKFKDKVTLTVDKSTSTAY MELSSLRSE DTAV Y YC A RTLDG Y YDYWGQGTTVTVSS SEQ ID NO: 132 Note: The simple sub-company represents the CDR and the double sub-company represents the different positions in the market. The aforementioned variable light and heavy chain regions were combined with sequences from the human germline light and heavy chain constant regions to form the final complete light and heavy chain sequences, thereby obtaining the antibody with a full-length sequence. For the humanized mab199 antibodies, unless otherwise clearly described in the present invention, the light chain constant region is the constant region shown in SEQ ID NO: 134, and the heavy chain constant region is the constant region shown in SEQ ID NO: 133. The humanized mab199 antibodies obtained are shown below: Table 33. Sequences of light and heavy chain variable regions of the humanized antibodies mab199 VH Antibody (SEQ ID NO) VL (SEQ ID NO) huí 99-01 127 120 huí 99-02 127 121 huí 99-03 127 122 huí 99-04 127 123 huí 99-05 127 124 huí 99-06 127 125 huí 99-07 128 120 huí 99-08 128 121 huí 99-09 128 122 huí 99-10 128 123 huí 99-11 128 124 hu199-12 128 125 hu199-13 129 120 hu199-14 129 121 hu199-15 129 122 hu199-16 129 123 hu199-17 129 124 hu199-18 129 125 hu199-19 130 120 huí 99-20 130 121 huí 99-21 130 122 huí 99-22 130 123 huí 99-23 130 124 hu 199-24 130 125 ran away 99-25 131 120 ran away 99-26 131 121 ran away 99-27 131 122 ran away 99-28 131 123 ran away 99-29 131 124 ran away 99-30 131 125 ran away 99-31 132 120 ran away 99-32 132 121 ran away 99-33 132 122 ran away 99-34 132 123 ran away 99-35 132 124 ran away 99-36 132 125 frnofrLn / Lznz / e / YiAi The activity of humanized mab199 antibodies that block the binding of TSLP to the TSLP receptor was detected using the ELSA method, and the detection results are as follows: Table 34. The activity of the humanized antibody mab199 that blocks the binding of TSLP to the TSLP receptor Antibody IC50 (nM) Antibody IC50 (nM) Antibody IC50 (nM) Antibody IC50 (nM) huí 99-01 0.1912 hu199-10 0.3910 hu199-191 0.6584 huí 99-28 0.4619 huí 99-02 0.2193 hu199-11 0.3648 hu199-20 0.4001 huí 99-29 0.5543 huí 99-03 0.2077 hu199-12 0.3700 hu199-21 0.5353 huí 99-30 0.3493 huí 99-04 0.4242 hu199-13 0.2395 hu199-22 0.3449 huí 99-31 0.3044 huí 99-05 0.4726 hu199-14 0.3112 hu199-23 0.3370 huí 99-32 0.2870 huí 99-06 0.3806 hu199-15 0.2866 hu199-24 0.4960 huí 99-33 0.2055 huí 99-07 0.2834 hu199-16 0.7367 hu199-25 0.2460 hu 199-34 0.7107 huí 99-08 0.2828 hu199-17 0.6111 hu199-26 0.3651 huí 99-35 0.4849 huí 99-09 0.2732 hu199-18 0.4806 hu199-27 0.3544 huí 99-36 0.7273 Ch199 0.4266 The results showed that humanized mab199 antibodies still have a relatively high activity in blocking the binding of TSLP to the TSLP receptor. 5.5 Antibody constant regions The constant region of the heavy chain of the humanized antibody and the chimeric antibody can be selected from the group consisting of the constant regions of IgG1, IgG2, IgG4, and variants thereof. By way of example, the constant region of IgG1-YTE was used in the present invention, and its sequence is as shown in SEQ ID NO: 133. The constant region of the light chain can be selected from the constant regions of the human κ or λ chain, or variants thereof. By way of example, the constant region of the human κ chain was used in the present invention, and its sequence is as shown in SEQ ID NO: 134. > IgG 1-YTE heavy chain constant region: ASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTF PAVLQSSGLYSLSSVVTVPSSSLG FQTYICNVNHKPSNTKVDKKVEPKSCDK Γ htcppcpapellggpsvflfppkpkdtlyitrepevtcvvvdvshedpevkfn WYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNK ALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVE WESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEA LHNHYTQKSLSESPGK SEQ ID NO: 133 Note: Underlining refers to engineered mutations M252Y, S254T, T256E > κ light chain constant region: RTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQ ESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTFIQGLSSPVTKSFNRGE C SEQ ID NO: 134 The humanized light and heavy chain variable regions of the present invention were recombined with the previous constant regions to obtain the full-length frnQfrin / Lznz / e / YiAi sequences of the heavy and light chains. For example, the antibody sequences are as follows: heavy chain of the hu3-13 antibody: EVQLVQSGAEVKKPGASVKVSCKASGYTFTDDYMNWVRQAPGQRLEWMG.il SPYNGGTSYNQKFKGRXI LTVDKSASTAYMELSSLRSED IAVYYCAREDYDY DGYAMDYWGOGTTVΓVSSA5·7KGP5V / ^7J¿4 / ,55W575¢;G7A4LGCLVK£>r / ·7J¿7, VI VSWNSGALlSGVHTFPA VLQSSGLYSLSSVVl VPSSSLG7Q1 YICNVNHKPSNTKV DKKVEPKSCDK11HCPPCPAPELLGGPSVFLFPPKPKD1LYITREPEVICVVVDVS HEDPEVKFNWYVDGVEVHNAK1KPREEQYNSTYRVVSVLTVLHQDWLNGKEYKC KVSNCALPAPIEKTISKGQQPREPQVYI LPPSRDELl KNQVSLTCLVKGFYPSDIA VEWESNGQPINNYKn PPVLDSDGFFFLYSKLIVDKSRWQQGNVFSCSVMHEAL HNH YTQKSLSLSPGK SEQ ID NO: 135 hu3-13 antibody light chain: EIVLTOSPATLSLSPGERATLSCRASSSVSYMHWYOOKPGOAPRPWIYATSNLA SGVPARFSGSGSGTSYTLTISRLEPEDFAVYCQQSDSGREFGGGTKVEIK / ? / VA A PS VFIFPPSDEQLKSG TA SVVCLLNNFYPREA K VQ WK VDNALQSGNSQES V1EQD skdstyslsstltlskadyekhkvyagevthoglsspvtksfnrgeg SEQ ID NO: 136 heavy chain of the antibody fled 19-30 EAQLVQSGAEVKKPGSSVKVSCKASGFTFSTYNMHWVRQAPGQGEEWIGAI YPGNGETSYNQFKDRATLTVDKSTRTAYMELSSLRSEDTAWYCAREDDYG EGYFDVWGOGTTVTVSS45 / XG / ,5V / -POAP55K5 / 5GG744LGC¿VWr / - / ?¿PV7 VSWNSGALlSCiVH'FFPAVLQSSGLYSLSSVVl VPSSSLG!QI YICNVNHKPSN'EKVD KKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLYITREPEVrCVVVDVSH EDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLIV'LHQDWLNGKEYKCK VSNKALPA P1EKEISKAKGQPREPQVYLLPPSRDEll KNQ VSLTCLVKGFYPSDIA V EWESNGQPENNYKPl PPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALH NHY1QKSLSLSPGK frnofrLn / Lznz / e / YiAi SEQ ID NO: 137 days old Sunday 19-30 DIVLTOSPATLLSLSPGERATLSCRASESVDSSGLSFMHWYOOKPGOPPRLLLYR ASNLGSGIPARFSGSGSGTDFTLTISSLEPEDFAVYYCOQINTDPLTFGOGTKLEI K / ? / VA A ps vfifppsdeqlksgta SVVCLLNNFYPREAKVQ wk vdna lqsgnsqes VTEQDSKDSTYSl.SSTLTI.SKADYEKHKVYACEVTUQGl.SSPVTKSFNRGEC SEQ ID NO: 138 square meters from 79-33 EVOLVOSGAEVKKPGSSVKVSCKASGYTFSNYLIEWVROAPGOGLEWIGVID PGYGDTNYNENFKGRATLTADKS TS TAY1ELSSLRSEDIAVY YCAREDNTGTA FDYWGQGTT VTVS SAS / KGPS VFPLA PSSKSl SGG1AALGCL VKD YFPEP VTVSIV NSGALTSGVHTFPAVLQSSGLYSLSSSVVTVPSSSSLGTQTYICNVNHKPSNTKVDKKV EPKSCDKnnCPPCPAPEEEGGPSVFl.FPPKPKDTEYITREPEVTCVVVDVSHEDP EVKFNWYVDGVEVHNACTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSN CALPAPIEKTISKAKGQPREPQVYrLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWE SNGQPENNYKFrPPVLDSDGSFFLYSKLrVDKSRWQQGNVFSCSVMHEALHNHYT QKSLSLSPGK SEQ ID NO: 139 fugitive antibody light chain 79-33 SIVMTOTPLSLSV rPGOPASlSCKASOSVSSDVTWYLOKPGOSPOLLlYYVSEH YTG\ PDRFSGSGYGTDF rLKlSRVEAEDVGVYYCQQHHRFPLTGQGTKLEIK R TVAAPS VFIFPPSDEQLKSG TA S VVCLLNNF YPREA KVQ WK VDNALQSGNSQES V TEQDSKDSTYSLSSTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC frnofrLn / Lznz / e / YiAi SEQ ID NO: 140 heavy chain of the fugitive antibody 99-36 EVQLVQSGAEVKCPGASVKVSCKASGYTFTTYWMHWVKQAPGQGLEWMG MIDPSDSETTLIOKFKDKVTLTYDKSTSTAYMELSSLRSEDTAVYCARTLDG YYDYWGQGI TVTVSSAS7KGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPPVTVS WNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSSLGTQIYICNVNHKPSNTKVDKK VEPKSCDKTHTCPPCPPAPELLGGPSVFLFPPKPKDILYHREPEVTCVVVDVSHED PEVKFNWYVDGVEVHNACTKPREEQYNSTYRVVSVETVEHQDWENGKEYKCKVS NKALLPAPlEKnSKAKGQPREPQVYTLPPSRDELl KNQVSLTCLVKGFYPSDIAVEW ESNGQPENN ΥΚΊΊΊΊSDΡWSKLDGWQLDG VFSCSVMHEALHNH Y TQKSLSLSPGK SEQ ID NO: I4l light chain of the fugitive antibody 99-36: DIOMTOSPSSLSASVGDRVTITCRASENIYSYL AWYOOCPGKSPOLLVYFACT LOWVPSRFSGSVSGTOFTLTISSLOPEDFATYYCOHHYGTPWTFGGGTKVEIK R 7 VA APS VF1FPPSDEQLKSGTAS VVCLLNNF YPREA K VQ WK VDNALQSGNSQES V TEQDSKDSTYSLSSTLLSKADYEKHKVYACEVTHQGLSSPVl KSFNRGEC SEQ ID NO: I42 Note: The underlined part represents CDR and the italicized part represents the constant region. AMG157 was used as a positive control for the present invention, and its sequence is as shown in SEQ ID NO: 143 and SEQ ID NO: 144. Heavy chain sequence of AMG157 OMOLVESGGGVVQPGRSLRLSCAASGFTFRTYGMHWVRQAPGKGLEWVAV IWYDGSNKHYADSVKGRFTITRDNSKNTLNLQMNSLRAEDTAVYYCARAPO WELVHEAFDIWGQGTMVTVSSAS TKGPS VFPL APCSRSTSTALL VGCL YFPEPTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSNFGTQTYTCN VDHKPSNTKVDKTVERKCCVECPPCPAPPVAGPSWLFPPKPKDTLMISRTPE VTCVVVDVSHEDPEVOFNWYVDGVVHNACTKPREEQFNSVSTVLTV HQDWLNGKEYKCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTKN QVSLTCLVKGFYPSDIAVEWESNGQPENNYCTTPPMLDSDGSFFLYSKLTXD KSRWQQGNVFSCSVMHEALHNHYTOXSLSLSPGK SEQ ID NO: 143 AMG157 light chain sequence SYVLTOPPSVSVAPGOTAR1TCGGNNLGSKS\HWYOOKPGOAPVLVVYDDS DRPSW1PERFSGSNSGNTATTLTISRGEADYCQVWDSSSDHVVFGGGT KLTVLGQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGCAAPSVDSSPAVDS VKAGVETTTPSKQSNNKYAASYLSLTPEQWKSHRSYSCQVTHEGSTVEKTV APTECS SEQ ID NO: I44 Furthermore, when testing antibody activity, the present invention also used the human TSLP receptor and human IL7Ra to construct cell lines, and their sequences are as follows: The full-length amino acid sequence of the human TSLP receptor: MGRLVLLWGAAVFLLGGWMALGOGGAAEGVOIOIIYFNLETVOVTWNASK YSRTNLTFHYRFNGDEAYDQCTNYLLQEGHTSGCLLDAEQRDDILYFSIRNGT HPVFTASRWMVYYLKPSSPKHVRFSWHQDAVTVTCSDLSYGDLLYEVQYRSP FD TEWQSKQENTCN V HEGLDAEK.CYSFWVRVKAMEDVYGPD TYPSDWSEV TCWQRGE1RDACAETPTPPKPKLSKFILISSLAILLMVSLLLLSLWKLWRVKKF LIPSVPDPKS1FPGLFEIHQGNFQEWITDTQNVAHLHKMAGAEQESGPEEPLVV QLAKTEAESPRMLDPQTEEKEASGGSLQLPHQPLQGGDVVT1GGFTFVMNDR SYVAL SEO ID Ne: 145 Note: The underlined part refers to the signal peptide. The full-length amino acid sequence of human IL7Ra (Uniprot ID: P16871) MTILGTTFGMVFSLLQVVSGESGYAONGDLEDAELDDYSFSCYSOLEVNGSO HSLTCAFEDPDVNTTNLEFE1CGALVEVKCLNFRKLQE1YFIETKKFLL1GKSN1 CVKVGEKSLTCKKIDLTTIVKPEAPFDLSVIYREGANDFVVTFNTSHLQKKYV KVLMHDVAYRQEKDENKWTHVNLSSTKLTLLQRKLQPAAMYEIKVRSIPDHY FKGFWSEWSPSYYFRTPEINNSSGEMDPILLTISILSFFSVALLVILACVLWKKRI KPIVWPSLPDHKKTLEHLCKKPRKNLNVSFNPESFLDCQIHRVDDIQARDEVE GFLQDTFPQQLEESEKQRLGGDVQSPNCPSEDVVITPESFGRDSSLTCLAGNVS ACDAPILSSSRSLDCRESGKNGPHVYQDLLLSLG TTNSTLPPPFSLQSG1LTLNP VAQGQPILTSLGSNQEEAYVTMSSFYQNQ frnQfrin / Lznz / e / YiAi SEC ID Ns: 146 Note: The underlined part refers to the signal peptide. The antibodies of the present invention can be cloned, expressed, and purified using conventional gene cloning and recombinant expression methods. Test Examples: Biological Evaluation of In Vitro Activity Example Test 1: ELSA Detection of the Binding of Anti-TSLP Antibodies to Human TSLP Human TSLP-his (SEQ ID NO: 1) was diluted to 1 pg / ml with pH 7.4 PBS buffer (Shanghai BasalMedia, B320), added at 100 pg / well to 96-well microtiter plates (Corning, CLS3590-100EA), and incubated overnight at 4°C. After discarding the liquid, 200 µL / well of blocking solution containing 5% skim milk (Bright Dairy skim milk powder) diluted in PBS was added, and the plates were incubated at 37°C for 2 hours for blocking. After blocking was complete, the blocking solution was discarded, and the plates were washed three times with PBST buffer (0.1% PBS containing Tween-20, pH 7.4). The antibodies to be tested and the positive antibody AMG157 at different concentrations diluted with the sample diluent were added at 100 µL / well and incubated in an incubator at 37°C for 1 hour. After incubation, the plates were washed with PBST 3 times.HRP-labeled goat anti-mouse secondary antibody (Jackson Immuno Research, 115-035-003) diluted with sample diluent to 100 µL / well was added and incubated at 37°C for 1 hour. After washing the plate with PBST 6 times, 50 µL / well of TMB chromogenic substrate (KPL, 52-00-03) was added and incubated at room temperature for 10–15 min. Then, 50 µL / well of 1 M H₂SO₄ was added to stop the reaction. The absorbance value was read using a NOVOStar microplate reader at 450 nm. The EC50 value of the TSLP-binding antibodies was calculated, and the results are shown in the following table. Table 35. Results of the binding activity of antibodies to human TSLP frnofrLn / Lznz / e / YiAi EC50 Antibody (nM) EC50 Antibody (nM) EC50 Antibody (nM) Ch3 0.4929 hu119-14 0.345 hui 79-09 0.1573 hu3-01 0.8494 hu119-15 0.3497 hui 79-10 0.19 hu3-02 0.6285 hu119-16 0.366 hui 79-11 0.1369 hu3-03 0.5545 hu119-17 0.3515 hu179-12 0.1437 hu3-04 0.4353 hu119-18 0.3455 hu179-13 0.2011 hu3-05 0.5168 hu119-19 0.3533 hu179-14 0.2053 hu3-06 0.594 huí 19-20 0.3412 hu179-15 0.2035 hu3-07 0.3853 huí 19-21 0.3987 hu179-16 0.2287 hu3-08 0.4687 huí 19-22 0.351 hu179-17 0.218 hu3-09 0.4941 huí 19-23 0.3404 hu179-18 0.2458 hu3-10 0.3879 huí 19-24 0.3446 hu179-19 0.1616 hu3-12 0.1519 huí 19-25 0.3575 huí 79-20 0.7077 hu3-13 0.1477 huí 19-26 0.3782 huí 79-21 0.9784 Ch119 0.851 huí 19-27 0.3347 huí 79-22 0.7519 hu119-01 0.107 huí 19-28 0.2648 huí 79-23 0.997 hu119-02 0.1938 huí 19-29 0.2729 huí 79-24 0.6358 hu119-03 0.1593 huí 19-28 0.2648 huí 79-25 0.1313 huí 19-04 0.1881 huí 19-29 0.2729 huí 79-26 0.2006 hu119-05 0.1445 Ch179 0.2023 huí 79-27 0.1799 hu119-06 0.2206 huí 79-01 0.1248 huí 79-28 0.0906 hu119-07 0.2132 huí 79-02 0.1697 huí 79-29 0.2041 hu119-08 0.2015 huí 79-03 0.138 huí 79-30 0.246 hu119-09 0.1492 huí 79-04 0.1886 huí 79-31 0.2012 hu119-10 0.2329 huí 79-05 0.1416 huí 79-32 0.145 huí 19-11 0.174 huí 79-06 0.2188 Oh 199 0.5157 hu119-12 0.2034 huí 79-07 0.4478 AMG157 0.7219 hu119-13 0.3438 huí 79-08 0.1615 The results showed that the antibodies of the present invention have very good binding activity with human TSLP. Example Test 2: Biacore Detection of the Affinity of Humanized Anti-TSLP Antibodies with Different TSLP Species The affinity of the humanized TSLP antibodies to be tested with white and human TSLP was detected using a Biacore T200 instrument (GE). The molecules to be tested were captured by affinity using Protein A biosensor chips (Cat. # 29127556, GE). The antigens (huTSLP-his, 10 cynoTSLP-his, prepared in Example 1) were then allowed to flow across the chip surface, and the reaction signal was detected in real time using the Biacore T200 instrument to obtain binding and dissociation curves. After dissociation was complete for each experimental cycle, the biosensor chips were washed and regenerated with a glycine-hydrochloric acid regeneration solution (pH 1.5, cat. BR-1003-54, GE). The data were fitted to a model of Langmuir (1:1) using BIAevaluation software version 4.1, GE to obtain the affinity value, as shown in the following table. Table 36. The affinity of anti-TSLP antibodies with TSLP from different species frnofrLn / Lznz / e / YiAi Antibody Affinity to huTSLP KD (M) Affinity to Cyno TSLP KD (M) AMG157 8.12E-12 9.22E-12 hui 79-33 9.03E-13 3.04E-11 hu3-13 1.0E-12 3.40E-10 hui 19-30 5.0E-12 1.95E-09 hui 99-36 10.5E-12 1.72E-11 The results showed that the anti-TSLP antibodies of the present invention have a relatively high affinity for human TSLP and can also bind to cyno TSLP. Example Test 3: ELISA-Based Experiment of Anti-TSLP Antibodies Blocking TSLP Binding to the TSLP Receptor The TSLP receptor has two subunits, TSLPR and IL7R, of which TSLPR is a TSLP-specific receptor and IL7R is a common receptor for both TSLP and IL7. TSLP binds first to TSLPR and then to IL7R. This test example was used to identify whether TSLP antibodies can block the binding of TSLP to the extracellular domain of the recombinantly expressed TSLPR receptor protein. ELISA plates were coated with human TSLPR-Fc-ECD (2 pg / mL, SEQ ID NO: 5) and incubated overnight at 4°C. After discarding the coating, a blocking solution of 200 pL / well (5% skim milk diluted in PBS) was added, and the plates were incubated at 37°C for 2 hours to achieve blocking. After blocking, the blocking solution was discarded, and the plates were washed three times with PBST buffer (PBS containing 0.05% Tween-20, pH 7.4). Biotin-labeled huTSLP-Fc antigen was prepared at 3 nM, and the antibodies to be tested were diluted from 200 nM. The antigen and antibody were mixed 1:1, then incubated at 37°C for 15 min, added at 100 µL per well to microtiter plates, and incubated at 37°C for 1 h. The plates were washed with PBST three times. Streptavidin-peroxidase polymer diluted 1:4000 with the sample diluent was added at 100 µL / well and incubated at 37°C for 1 h.After washing the plates with PBST 5 times, 100 µL / well of TMB chromogenic substrate (KPL, 52-00-03) was added and incubated at room temperature for 3–10 min. Then, 100 µL / well of 1M H₂SO₄ was added to stop the reaction. The absorbance value was read using a NOVOStar microplate reader at 450 nm. The IC50 value of the TSLP antibodies blocking TSLP binding to TSLPR was calculated, and the results are shown in Table 37 and Figure 1. Table 37. Results of blocking antibody activity. frnQFLn / Lznz / e / YiAi Antibody hui 79-33 hui 19-30 hu3-13 hu199-36 IC50 (nM) 0.5038 0.5192 0.4975 0.5693 The results showed that all antibodies of the present invention can strongly inhibit the binding of TSLP to its receptor TSLPR. Example Test 5: FACS-Based Experiment of the TSLP Antibody Blocking the Binding of TSLP to the TSLP Receptor This test example was used to identify whether anti-TSLP antibodies can respectively block the binding of TSLP to TSLPR / IL7R receptors on the surface of the CHOK1 cell line. The detailed method was as follows: CHOK1-TSLPR / IL7R cells were cultured with DME / F12 containing 10% FBS, 1 mg / ml G418, and 10 pg / ml puromycin. Healthy CHOK1-TSLPR / IL7R cells were centrifuged (1000 rpm, 5 min) and washed once with 2% FBS in PBS. The cells were counted and adjusted to a cell concentration of 1 x 10⁶ / ml. Fifty microliters of cells were added to 96-well round-bottom plates. The antibodies to be tested were diluted with 2% BSA-containing PBS solution, starting at 20 nM and diluted in eight 1:4 gradients. Biotin-labeled TSLP-Fc antigen was prepared at 2 nM. The antigen and antibody were mixed 1:1 and incubated at 37°C for 15 min. The mixture was added at 50 µL per well to 96-well plates where the cells were plated and incubated at 4°C for 1 hour. After incubation, the plates were centrifuged at 4°C (800 g, 5 min) and the supernatant was discarded.The plates were washed twice with 200 µL of pre-cooled PBS by centrifugation. PE-SA secondary antibody diluted 1:1000 was added, and the plates were incubated at 4°C in the dark for 40 min. The plates were then centrifuged at 4°C (800 g, 5 min), and the supernatant was discarded. 200 µL of pre-cooled PBS was added to inflate the cells, which were washed by centrifugation at 4°C three times. 100 µL of PBS was added, and the plate was loaded into the plate reader. The IC50 value of the antibodies against TSLP that block the binding of TSLP to TSLPR / IL7R was calculated based on the fluorescence signal strength. The results are shown in Table 38. Table 38. Results of antibodies that block cell surface TSLPR AMG157 antibody huí 79-33 huí 19-30 hu3-13 huí 99-36 IC50 (nM) 0.2068 0.1867 0.1368 0.1325 0.2270 The results showed that all antibodies of the present invention can relatively strongly block the binding of TSLP to TSLPR / IL7R on the cell surface. Example Test 6: Anti-TSLP Antibodies Inhibited TSLP-Induced Chemokine Production TSLP can induce the maturation of naïve myeloid dendritic cells (mDCs) and the secretion of the thymus activation regulator chemokine (TARC) and osteoprotegerin (OPG), thereby further mediating the innate and adaptive immune inflammatory response. This test example was used to verify that the obtained antibodies can block TSLP-induced chemokine production by mDCs, thereby blocking the development of innate and adaptive inflammatory responses. Naive myeloid dendritic cells (DCs) were isolated and purified from human peripheral blood mononuclear cells (PBMCs) using the magnetic bead sorting method (CD1c (BDCA-1) + Dendritic Cell Isolation Kit, Miltenyi Biotec). The obtained DCs were seeded into 96-well cell culture plates. Serially diluted antibody samples and human TSLP (huTSLP-his, final concentration 50 ng / mL) were pre-incubated for approximately 45 minutes (37°C) and then added to each well of the cell culture containing DCs to stimulate the DCs in vitro. The plates were placed in a culture incubator for 48 hours. The cell culture supernatant was collected and appropriately diluted, and then the chemokine content was detected using the ELISA method.TARC was detected using the R&D Company's CCL17 / TARC Human Quantikine ELISA kit; OPG content was detected using the R&D Company's CCL22 / CDM Human Quantikine ELISA kit, and the results are shown in Figure 4A - Figure 4B. The results showed that all antibodies of the present invention can significantly inhibit TSLP-induced TARC and OPG chemokine production, indicating that the antibodies of the present invention can block the emergence of innate and adaptive inflammatory responses. Example Test 7. Anti-TSLP Antibodies Blocked Native TSLP-Induced BaF3-TLSPR / IL7R Cell Proliferation BaF3-hTSLPR / hlL7R cells can proliferate under stimulation by native TSLP. The binding of antibodies to native TSLP reduces the stimulatory effect of TSLP on BaF3-hTSLPR / hlL7R cells. NHLF cells (BeNa Culture Collection BNCC340764) and HLF1 cells (BeNa Culture Collection BNCC337730) were cultured until 80% cell growth was reached, and the supernatant was discarded. Human lung fibroblasts, NHLF (BeNa Culture Collection BNCC340764) and HLF1 (BeNa Culture Collection BNCC337730) were stimulated with 10 ng / ml of human IL1-β (Sino Biological GMP-10139-HNAE), 20 ng / ml of IL13 (R&D 213-ILB-005), and 20 ng / ml of TNF-α (PEPROTECH 300-01 A) for 72 hours to induce native TSLP production. Once stimulation was complete, the cell supernatant was collected and centrifuged at 4500 rpm for 5 min to remove cell debris. The supernatant was then collected, concentrated approximately 10-fold using concentration columns, and filtered for later use. BaF3-hTSLPR / hlL17R cells were cultured in RPMI1640 with 10% FBS (10 ng / mL mlL3, R&D 213-ILB-005), adjusted to a density of 1 x 10⁴ cells / ml, and cultured at 37°C, 5% CO2 incubator in the logarithmic growth phase. Cells were harvested, centrifuged at 800 rpm / min for 5 min, and the supernatant discarded. Cells were washed three times with PBS to remove cytokines that stimulate their proliferation in the culture medium. Cells were resuspended in RPMI1640 with 4% FBS, seeded in 96-well plates at 4000 cells / 50 µL / well, and cultured in an incubator for 2 h. The antibodies to be tested were serially diluted using native TSLP at a ratio of 10 times, with an initial antibody concentration of 100 nM, resulting in 3 dilution gradients: 100 nM, 10 nM, and 1 nM.Fifty milliliters per well of the diluted antibody / antigen mixture were added to the cells, with final antibody concentrations of 50 nM, 5 nM, and 0.5 nM. The plates were incubated in a 5% CO2 incubator at 37°C for 72 h. Then, 30 µL of CelITiter-Glo (Promega) was added to each well and incubated in the dark at room temperature for 10 minutes. Cells were detected using the luminescence program with the Cytation5 cell imager. The results are shown in the following table. Table 39. Results of anti-TSLP antibodies that inhibit cell proliferation BaF3TLSPR / IL7R bnQbtn / Lznz / e / YiAi AMG157 antibody hui 79-33 hu3-13 hui 19-30 IC50 (nM) 3.379 0.02279 0.2888 1.533 The results showed that all the antibodies obtained in the present invention can significantly inhibit native TSLP activity to stimulate BaF3 proliferation, especially huí 79-33, whose activity was more than 100 times that of AMG157. Example Test 8: Experiment of anti-TSLP antibodies that inhibit TSLP-induced proliferation of BaF3 cells overexpressing TSLPR / IL7R TSLP can bind to TSLPR / IL7R on the surface of BaF3, thereby promoting BaF3 proliferation. This test example was used to identify whether the antibodies of the present invention can block TSLP activity to induce BaF3 proliferation. Specifically, BaF3 cells overexpressing TSLPR / IL7R were cultured in RPMI1640 with 10% FBS and 2 ng / mL rhlL3 (MultiSciences, Catalog No. 96-AF-300-03-20), in a 37°C incubator with 5% CO2, at a cell density not exceeding 1 x 10⁶ cells / mL. Upon antibody detection, logarithmic-phase cells were washed three times with PBS and centrifuged at 800 rpm for 5 min. The cell density was adjusted to 8000 cells / well / 90 µL using RPMI1640 (2% FBS, recombinant human TSLP-Fc: 40 ng / mL). Ten microliters of serially diluted antibody to be tested were added to 96-well plates and cultured for 2 days. Thirty microliters of cell titer were added and mixed for detection. The IC50 was calculated based on the reading. The results are shown in Table 40 and Figure 3. Table 40. Inhibition of BaF3 cell proliferation activity by frnofrLn / Lznz / e / YiAi antibodies AMG157 antibody hui 79-33 hui 19-30 hu3-13 hu199-36 IC50 (nM) 0.5730 0.4092 0.4305 0.4436 0.4769 The results showed that all antibodies of the present invention have a relatively strong ability to inhibit TSLP-mediated BaF3 cell proliferation. Example Test 9: Humanized anti-TSLP antibodies blocked TSLP-induced differentiation of native CD4+ T cells into Th2 cells TSLP can induce the maturation of primary myeloid CDm cells. Mature CDm cells highly express the OX40 ligand, which can bind to OX40 on the surface of native CD4+ T cells, thereby differentiating the native CD4+ T cells into Th2 cells. These Th2 cells produce immune response-related factors such as IL4, IL5, and IL13, leading to a Th2 inflammatory response in the body. This test example was used to determine whether the antibodies obtained in the present invention can block TSLP-induced Th2 cell differentiation. Naive myeloid dendritic cells (MDs) were separated and purified from human peripheral blood mononuclear cells (PBMCs) using the magnetic bead sorting method (CD1c (BDCA-1) + Dendritic Cell Isolation Kit, Miltenyi Biotec). The resulting MDs were seeded into 96-well cell culture plates. Serially diluted antibody samples and recombinant human TSLP-expressed antibodies (huTSLP-his, final concentration 50 ng / mL) were pre-incubated (37°C) for approximately 45 minutes and then added to each well of the cell culture containing MDs, respectively, and cultured at 37°C for 24 hours. Mature MDs after stimulation were harvested and washed twice with PBS. Native CD4+CD45RA+ T cells were extracted from PBMCs using the magnetic bead sorting method (Myltenyi Biotec).Native T cells obtained by separation and mature CDm cells were mixed and seeded in 96-well cell culture plates in a 5:1 ratio and co-cultured for 6 days. The cells were harvested and seeded in 96-well plates pre-coated with anti-CD3 (10 pg / ml), and anti-CD28 (1 pg / ml) was added to re-stimulate the differentiated T cells. The cells were cultured for 24 hours, and the cell culture supernatant was collected. Th2-related cytokines secreted by the cells in the supernatant were detected. ELISA. Cytokines IL-4 and IL-5 were detected using ELISA kits from R&D, and TNF-α and IL-13 were detected using ELISA kits from NeoBioscience. The results are shown in Figure 5A - Figure 5D. The results showed that the antibodies obtained in the present invention can significantly inhibit the production of Th2 cytokines IL4, IL5, IL13 and TNF-α, which 15 indicates that the antibodies obtained in the present invention can block TSLP-induced Th2 cell differentiation.

Claims

1. An anti-TSLP antibody comprising a heavy chain variable region and a light chain variable region, wherein: i) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 14, SEQ ID NO: 15 and SEQ ID NO: 47, respectively, and the light chain variable region comprises LCDR1, LCDR2 as shown in SEQ ID NO: 17, SEQ ID NO: 18, respectively, and LCDR3 as shown in SEQ ID NO: 48 or 55; wherein, the sequence in SEQ ID NO: 47 is EDYDYDGYAMDX1, the sequence in SEQ ID NO: 48 is QQWSSX2RT, the sequence in SEQ ID NO: 55 is QQSDX3X4RX5, wherein X1 is H or Y, X2 is N or D, X3 is N or S, X4 is V or G, X5 is G or E; or i) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 20, SEQ ID NO: 21 and SEQ ID NO: 22, respectively, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 76, SEQ ID NO: 24 and SEQ ID NO: 25, respectively;where, the sequence of SEQ ID NO: 76 is RASESVDX6SGLSFMH, where, X6 is selected from N, S and Q; or (ii) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 26, SEQ ID NO: 96 and SEQ ID NO: 28, respectively, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 29, SEQ ID NO: 118 and SEQ ID NO: 31, respectively; where, the sequence of SEQ ID NO: 96 is VIDPGX7X8DTNYNE, the sequence of SEQ ID NO: 118 is X9VX10X11X12X13T, where X7 is selected from N, Q and V, X8 is G or V; X9 is Y or E, X10 is selected from S, D and E, X11 is selected from N, Q, D and E, X12 is selected from H, Y, D and E, X13 is E or Y;or iv) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 32, SEQ ID NO: 33 and SEQ ID NO: 34, respectively, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 35, SEQ ID NO: 36 and SEQ ID NO: 37, respectively.; 2. Anti-TSLP antibody according to claim 1, comprising a heavy chain variable region and a light chain variable region, wherein: i) the heavy chain variable region comprises HCDR1 and HCDR2 as shown in SEQ ID NO: 14, SEQ ID NO: 15, respectively, and HCDR3 as shown in SEQ ID NO: 16 or 45, and the light chain variable region comprises LCDR1 and LCDR2 as shown in SEQ ID NO: 17, SEQ ID NO: 18, respectively, and LCDR3 as shown in SEQ ID NO: 19, 46, 53 or 54; or i) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 20, SEQ ID NO: 21 and SEQ ID NO: 22, respectively, and the light chain variable region comprises LCDR2 and LCDR3 as shown in SEQ ID NO: 24 and SEQ ID NO: 25, respectively, and LCDR1 as shown in SEQ ID NO: 23, 70 or 71;or iii) the variable region of the heavy chain comprises HCDR1 and HCDR3 as shown in SEQ ID NO: 26 and SEQ ID NO: 28, respectively, and HCDR2 as shown in SEQ ID NO: 27, 93, 94 or 95, and the light chain variable region comprises LCDR1 and LCDR3 as shown in SEQ ID NO: 29 and SEQ ID NO: 31, respectively, and LCDR2 as shown in SEQ ID NO: 30, 108, 109, 110, 111, 112, 113, 114, 115, 116 or 117.; 3. Anti-TSLP antibody according to claim 2, comprising a heavy chain variable region and a light chain variable region, wherein: i) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 14, SEQ ID NO: 15 and SEQ ID NO: 45, respectively, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 17, SEQ ID NO: 18 and SEQ ID NO: 54, respectively; or i) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 14, SEQ ID NO: 15 and SEQ ID NO: 45, respectively, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 17, SEQ ID NO: 18 and SEQ ID NO: 53, respectively;(i) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 20, SEQ ID NO: 21 and SEQ ID NO: 22, respectively, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 70, SEQ ID NO: 24 and SEQ ID NO: 25, respectively; or (iv) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 20, SEQ ID NO: 21 and SEQ ID NO: 22, respectively, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 71, SEQ ID NO: 24 and SEQ ID NO: 25, respectively; ov) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 26, SEQ ID NO: 94 and SEQ ID NO: 28, respectively, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 29, SEQ ID NO: 113 and SEQ ID NO: 31, respectively;or frnofrLn / Lznz / e / YiAi vi) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 26, SEQ ID NO: 94 and SEQ ID NO: 28, respectively, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 29, SEQ ID NO: 30 and SEQ ID NO: 31, respectively; or vii) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 14, SEQ ID NO: 15 and SEQ ID NO: 16, respectively, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 17, SEQ ID NO: 18 and SEQ ID NO: 19, respectively; or viii) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 14, SEQ ID NO: 15 and SEQ ID NO: 45, respectively, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 17, SEQ ID NO: 18 and SEQ ID NO: 46, respectively;or ix) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 20, SEQ ID NO: 21 and SEQ ID NO: 22, respectively, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 23, SEQ ID NO: 24 and SEQ ID NO: 25, respectively; ox) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 26, SEQ ID NO: 27 and SEQ ID NO: 28, respectively, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 29, SEQ ID NO: 30 and SEQ ID NO: 31, respectively; ox¡) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 26, SEQ ID NO: 93 and SEQ ID NO: 28, respectively, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 29, SEQ ID NO: 30 and SEQ ID NO: 31, respectively;or xii) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 26, SEQ ID NO: 95 and SEQ ID NO: 28, respectively, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 29, SEQ ID NO: 30 and SEQ ID NO: 31, respectively; or xiii) the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 26, SEQ ID NO: 27 and SEQ ID NO: 28, respectively, and the light chain variable region comprises LCDR1, LCDR3 as shown in SEQ ID NO: 29, SEQ ID NO: 31, respectively, and LCDR2 as shown in SEQ ID NO: 108, 109, 110, 111, 112, 113, 114, 115, 116 or 117. frnofrLn / Lznz / e / YiAi; 4. Anti-TSLP antibody according to any of claims 1 to 3, wherein the anti-TSLP antibody is a murine antibody, a chimeric antibody, or a humanized antibody.

5. Anti-TSLP antibody according to claim 4, wherein the anti-TSLP antibody comprises the framework region or regions derived from a human antibody, wherein the anti-TSLP antibody comprises the light chain variable region and / or the heavy chain variable region, selected from those described in (a), (b), (c) or (d) below: (a) the heavy chain variable region comprises HCDR1 and HCDR2 as shown in SEQ ID NO: 14 and SEQ ID NO: 15, respectively, and HCDR3 as shown in SEQ ID NO: 16 or 45, and the framework regions thereof comprise (s) at most 10 reverse mutations, preferably the reverse mutation being selected from one or more of 38K, 48I, 67A, 69L, 71V and 73K;and / or the variable region of the light chain comprises LCDR1 and LCDR2 as shown in SEQ ID NO: 17 and SEQ ID NO: 18, respectively, and LCDR3 as shown in SEQ ID NO: 19, 46, 53 or 54, and the frame region the same comprise at most 10 amino acid reverse mutations, preferably the reverse mutation being selected from one or more of 46P, 47W, 58V, 70S and 71Y; b) the variable region of the heavy chain comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 20, SEQ ID NO: 21 and SEQ ID NO: 22, respectively, and the frame region thereof comprises (s) at most 10 reverse mutations, preferably the reverse mutation being selected from one or more of 2A, 27F, 38K, 39H, 48I, 67A, 69L, 71V and 76R;and / or the variable region of the light chain comprises LCDR2 and LCDR3 as shown in SEQ ID NO: 24 and SEQ ID NO: 25, respectively, and LCDR1 as shown in SEQ ID NO: 23, 70 or 71, and the frame region(s) thereof comprise at most 10 amino acid reverse mutations, preferably the reverse mutation being selected from one or more of 1D, 4L, 43P, 48L and 58L; c) the variable region of the heavy chain comprises HCDR1 and HCDR3 as shown in SEQ ID NO: 26 and SEQ ID NO: 28 respectively, and HCDR2 as shown in SEQ ID NO: 27, 93, 94 or 95, and the frame its region or regions comprise at most 10 reverse mutations, preferably the reverse mutation is selected from one or more of 27Y, 28A, 38K, 48I, 66K, 67A, 69L, 80I and 82bR;and / or the variable region of the light chain comprises LCDR1 and LCDR3 as shown in SEQ ID NO: 29 and SEQ ID NO: 31, respectively, and LCDR2 as shown in SEQ ID NO: 30, 108, 109, 110, 111, 112, 113, 114, 115, 116 or 117, and the frame region or regions thereof comprise at most 10 reverse mutations, preferably the reverse mutation being selected from one or more of 1S, 43S, 67Y and 73F; or frnofrLn / Lznz / e / YiAi d) the variable region of the heavy chain comprises HCDR1, HCDR2 and HCDR3 as shown in SEQ ID NO: 32, SEQ ID NO: 33 and SEQ ID NO: 34, respectively, and the frame region thereof comprises (s) at most 10 reverse mutations, preferably the reverse mutation being selected from one or more of 38K, 48I, 66K, 67A, 69L, 71V, 73K and 78A;and / or the variable region of the light chain comprises LCDR1, LCDR2 and LCDR3 as shown in SEQ ID NO: 35, SEQ ID NO: 36 and SEQ ID NO: 37, respectively, and the frame region thereof comprises (s) at most 10 reverse mutations, preferably the reverse mutation being selected from one or more of 43S, 45Q, 48V, 66V and 70Q.; 6. Anti-TSLP antibody according to claim 4, comprising a heavy chain variable region and a light chain variable region, wherein: i) the heavy chain variable region has at least 90% sequence identity with the heavy chain variable region as shown in the amino acid sequence SEQ ID NO: 6, 42, 43, 44 or 50, and the light chain variable region has at least 90% sequence identity with the light chain variable region as shown in the amino acid sequence SEQ ID NO: 7, 38, 39, 40, 41, 49, 51 or 52;or i) the heavy chain variable region has at least 90% sequence identity with the heavy chain variable region as shown in amino acid sequence SEQ ID NO: 8, 62, 63, 64, 65, 66, 67, 68 or 69, and the light chain variable region has at least 90% sequence identity with the light chain variable region as shown in amino acid sequence SEQ ID NO: 9, 56, 57, 58, 59, 60, 61, 72, 73, 74 or 75; or (ii) the heavy chain variable region has at least 90% sequence identity with the heavy chain variable region as shown in the amino acid sequence SEQ ID NO: 10, 85, 86, 87, 88, 89, 90, 91, 92 or 97, and the light chain variable region has at least 90% sequence identity with the light chain variable region as shown in the amino acid sequence SEQ ID NO: 11, 77, 78, 79, 80, 81, 82, 83, 84, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107 or 119;or iv) the heavy chain variable region has at least 90% sequence identity with the heavy chain variable region as shown in amino acid sequence SEQ ID NO: 12, 126, 127, 128, 129, 130, 131 or 132, and the light chain variable region has at least 90% sequence identity with the light chain variable region as shown in amino acid sequence SEQ ID NO: 13, 120, 121, 122, 123, 124 or 125. frnofrLn / Lznz / e / YiAi; 7. Anti-TSLP antibody according to claim 6, comprising a heavy chain variable region and a light chain variable region, wherein: i) the amino acid sequence of the heavy chain variable region is as shown in SEQ ID NO: 6, 42, 43, 44 or 50, and the amino acid sequence of the light chain variable region is as shown in SEQ ID NO: 7, 38, 39, 40, 41, 49, 51 or 52; or i) the amino acid sequence of the variable region of the heavy chain is as shown in SEQ ID NO: 8, 62, 63, 64, 65, 66, 67, 68 or 69, and the amino acid sequence of the variable region of the light chain is as shown in SEQ ID NO: 9, 56, 57, 58, 59, 60, 61, 72, 73, 74 or 75;or ii) the amino acid sequence of the variable region of the heavy chain is as shown in SEQ ID NO: 10, 85, 86, 87, 88, 89, 90, 91, 92 or 97, and the amino acid sequence of the variable region of the light chain is as shown in SEQ ID NO: 11, 77, 78, 79, 80, 81, 82, 83, 84, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107 or 119; or iv) the amino acid sequence of the variable region of the heavy chain is as shown in SEQ ID NO: 12, 126, 127, 128, 129, 130, 131 or 132, and the amino acid sequence of the variable region of the light chain is as shown in SEQ ID NO: 13, 120, 121, 122, 123, 124 or 125.; 8. The anti-TSLP antibody according to claim 7 comprises a heavy chain variable region and a light chain variable region as follows: a) the sequence of the heavy chain variable region is as shown in SEQ ID NO: 50, and the sequence of the light chain variable region is as shown in SEQ ID NO: 52; b) the sequence of the heavy chain variable region is as shown in SEQ ID NO: 50, and the sequence of the light chain variable region is as shown in SEQ ID NO: 51; c) the sequence of the heavy chain variable region is as shown in SEQ ID NO: 69, and the sequence of the light chain variable region is as shown in SEQ ID NO: 74; d) the sequence of the heavy chain variable region is as shown in SEQ ID NO: 64, and the sequence of the light chain variable region is as shown in SEQ ID NO: 73;or frnofrLn / Lznz / e / YiAi e) the sequence of the heavy chain variable region is as shown in SEQ ID NO: 97, and the sequence of the light chain variable region is as shown in SEQ ID NO: 119; of) the sequence of the heavy chain variable region is as shown in SEQ ID NO: 91, and the sequence of the light chain variable region is as shown in SEQ ID NO: 78; og) the sequence of the heavy chain variable region is as shown in SEQ ID NO: 132, and the sequence of the light chain variable region is as shown in SEQ ID NO: 125.; 9. Anti-TSLP antibody according to any of claims 1 to 8, wherein the antibody further comprises an antibody heavy chain constant region and a light chain constant region; preferably, the heavy chain constant region is selected from the group consisting of human IgG1, IgG2, IgG3 and IgG4 constant regions and conventional variants thereof, the light chain constant region is selected from the group consisting of human antibody κ and λ chain constant regions and conventional variants thereof; more preferably, the antibody comprises a heavy chain constant region as shown in sequence SEQ ID NO: 133, and a light chain constant region as shown in sequence SEQ ID NO:

134.

10. Anti-TSLP antibody according to claim 9, wherein the antibody comprises a heavy chain and a light chain as follows: a) the amino acid sequence of the heavy chain is as shown in SEQ ID NO: 135 or has at least 90% sequence identity with it, and the amino acid sequence of the light chain is as shown in SEQ ID NO: 136 or has at least 90% sequence identity with it; b) the amino acid sequence of the heavy chain is as shown in SEQ ID NO: 137 or has at least 90% sequence identity with it, and the amino acid sequence of the light chain is as shown in SEQ ID NO: 138 or has at least 90% sequence identity with it;oc) the amino acid sequence of the heavy chain is as shown in SEQ ID NO: 139 or has at least 90% sequence identity with it, and the amino acid sequence of the light chain is as shown in SEQ ID NO: 140 or has at least 90% sequence identity with it; od) the amino acid sequence of the heavy chain is as shown in SEQ ID NO: 141 or has at least 90% sequence identity with it, and the amino acid sequence of the light chain is as shown in SEQ ID NO: 142 or has at least 90% sequence identity with it.

11. An isolated anti-TSLP antibody, which competitively binds to human TSLP with the anti-TSLP antibody according to any of claims 1 to 10.

12. Nucleic acid molecule encoding the anti-TSLP antibody according to any of claims 1 to 11.

13. Host cell comprising the nucleic acid molecule according to claim 12.

14. A pharmaceutical composition containing a therapeutically effective amount of the anti-TSLP antibody according to any one of claims 1 to 11, or the nucleic acid molecule according to claim 12, or the host cell according to claim 13, as well as one or more pharmaceutically acceptable vehicles, diluents, buffers or excipients.

15. A method for the immunodetection or determination of TSLP in vitro or ex vivo, comprising a step of using the anti-TSLP antibody according to any of claims 1 to 11.

16. A kit comprising the anti-TSLP antibody according to any of claims 1 to 11.

17. A method for treating TSLP-related diseases, comprising administering to a subject a therapeutically effective amount of the anti-TSLP antibody of any of claims 1 to 11, or the nucleic acid molecule of claim 12, or the host cell of claim 13, or the pharmaceutical composition of claim 14, preferably wherein the TSLP-related disease is selected from the group consisting of: asthma, idiopathic pulmonary fibrosis, atopic dermatitis, allergic conjunctivitis, allergic rhinitis, allergic sinusitis, urticaria, Netherton syndrome, eosinophilic esophagitis, food allergy, allergic diarrhea, eosinophilic gastroenteritis, allergic bronchopulmonary aspergillosis, allergic fungal sinusitis, chronic pruritus, cancer, breast cancer, colon cancer, lung cancer, ovarian cancer, prostate cancer, rheumatoid arthritis, chronic obstructive pulmonary disease, systemic sclerosis, multiple sclerosis,Keloidosis, ulcerative colitis, nasal polyposis, chronic eosinophilic pneumonia, eosinophilic bronchiolitis, celiac disease, Churg-Strauss syndrome, eosinophilic myalgia syndrome, hypereosinophilic syndrome, eosinophilic granulomatosis with polyangiitis, inflammatory bowel disease, scleroderma, interstitial lung disease, fibrosis caused by chronic hepatitis B or C, radiation-induced fibrosis, and fibrosis caused by wound healing.