The 2A3 monoclonal antibody reacts with trinitrophenol. Because trinitrophenol is not expressed by mammals this antibody is ideal for use as an isotype-matched control for rat IgG2a antibodies in most in vivo and in vitro applications.

This non-therapeutic biosimilar antibody uses the same variable regions from the therapeutic antibody Adalimumab making it ideal for research use. This Adalimumab biosimilar reacts with human TNFα (tumor necrosis factor-alpha) a multifunctional proinflammatory cytokine. TNFα belongs to the TNF superfamily of cytokines and signals through its two receptors, TNFR1 and TNFR2 which can be activated by both the soluble trimeric and membrane-bound and forms of TNFα. TNFα is primarily produced by macrophages in response to foreign antigens such as bacteria (lipopolysaccharides), viruses, and parasites as well as mitogens and other cytokines but can also be expressed by monocytes, neutrophils, NK cells, CD4 T cells and some specialized dendritic cells. TNFα is known to play key roles in a wide spectrum of biological processes including immunoregulation, cell proliferation, differentiation, apoptosis, antitumor activity, inflammation, anorexia, cachexia, septic shock, hematopoiesis, and viral replication. TNFα dysregulation has been implicated in a variety of diseases, including autoimmune diseases, insulin resistance, and cancer. Adalimumab blocks the interaction of TNFα with the TNFR1 (p55) and TNFR2 (p75) resulting in a down-regulation of the inflammatory response associated with autoimmune diseases.

This non-therapeutic biosimilar antibody uses the same variable regions from the therapeutic antibody Trastuzumab making it ideal for research use. This Trastuzumab biosimilar reacts with human HER2 (human epidermal growth factor receptor 2) also known as neu peptide, CD340, ErbB-2, and p185. HER2 is a 185 kDa transmembrane, receptor-like glycoprotein with intrinsic tyrosine kinase activity that is part of several cell surface receptor complexes. HER2 lacks an identified ligand however, the kinase can be activated in the absence of a ligand when overexpressed. HER2 is a proto-oncoprotein that is commonly overexpressed on a variety of different tumors. Approximately 40% of human breast cancers overexpress HER2. HER2 overexpression is associated with poorer overall survival rates, shorter times to disease progression, and increased resistance to chemotherapy. Because of these clinical characteristics anti-HER2 monoclonal antibody therapy is now a standard for the treatment of advanced breast cancers that overexpress HER2. Trastuzumab induces an immune-mediated response that triggers the internalization and downregulation of HER2.

This non-therapeutic biosimilar antibody uses the same variable regions from the therapeutic antibody Nivolumab making it ideal for research use. This Nivolumab biosimilar reacts with human PD-1 (programmed death-1) also known as CD279. PD-1 is a 50-55 kDa cell surface receptor encoded by the Pdcd1 gene that belongs to the CD28 family of the Ig superfamily. PD-1 is transiently expressed on CD4 and CD8 thymocytes as well as activated T and B lymphocytes and myeloid cells. PD-1 expression declines after successful elimination of antigen. Additionally, Pdcd1 mRNA is expressed in developing B lymphocytes during the pro-B-cell stage. PD-1’s structure includes a ITIM (immunoreceptor tyrosine-based inhibitory motif) suggesting that PD-1 negatively regulates TCR signals. PD-1 signals via binding its two ligands, PD-L1 and PD-L2 both members of the B7 family. Upon ligand binding, PD-1 signaling inhibits T-cell activation, leading to reduced proliferation, cytokine production, and T-cell death. Additionally, PD-1 is known to play key roles in peripheral tolerance and prevention of autoimmune disease. Induced PD-L1 expression is common in many tumors including squamous cell carcinoma, colon adenocarcinoma, and breast adenocarcinoma. PD-L1 overexpression results in increased resistance of tumor cells to CD8 T cell mediated lysis. PD-L1 overexpression results in increased resistance of tumor cells to CD8 T cell mediated lysis. In experimental models of melanoma, tumor growth can be transiently arrested via treatment with antibodies which block the interaction between PD-L1 and its receptor PD-1. For these reasons anti-PD-1 mediated immunotherapies are currently being used as cancer treatments. Nivolumab binds to PD-1 on activated immune cells to selectively block the interaction of PD-1 with its ligands.

This non-therapeutic biosimilar antibody uses the same variable regions from the therapeutic antibody Bevacizumab making it ideal for research use. This Bevacizumab biosimilar reacts with human VEGF (vascular endothelial growth factor). VEGF is a 45 kDa homodimeric, disulfide-linked glycoprotein that plays key roles in angiogenesis, vasculogenesis, and endothelial cell growth. It promotes mitogenesis, chemotaxis, and vascular permeability. Most tumors have a requirement for angiogenesis, and inhibition of VEGF biding to VEGF receptors has been the focus of several tumor therapeutic strategies. Bevacizumab neutralizes the biological activity of VEGF by preventing the interaction of VEGF with its receptors on the surface of endothelial cells, resulting in the inhibition of tumor growth.

This non-therapeutic biosimilar antibody uses the same variable regions from the therapeutic antibody Pembrolizumab making it ideal for research use. This Pembrolizumab biosimilar reacts with human PD-1 (programmed death-1) also known as CD279. PD-1 is a 50-55 kDa cell surface receptor encoded by the Pdcd1 gene that belongs to the CD28 family of the Ig superfamily. PD-1 is transiently expressed on CD4 and CD8 thymocytes as well as activated T and B lymphocytes and myeloid cells. PD-1 expression declines after successful elimination of antigen. Additionally, Pdcd1 mRNA is expressed in developing B lymphocytes during the pro-B-cell stage. PD-1’s structure includes a ITIM (immunoreceptor tyrosine-based inhibitory motif) suggesting that PD-1 negatively regulates TCR signals. PD-1 signals via binding its two ligands, PD-L1 and PD-L2 both members of the B7 family. Upon ligand binding, PD-1 signaling inhibits T-cell activation, leading to reduced proliferation, cytokine production, and T-cell death. Additionally, PD-1 is known to play key roles in peripheral tolerance and prevention of autoimmune disease. Induced PD-L1 expression is common in many tumors including squamous cell carcinoma, colon adenocarcinoma, and breast adenocarcinoma. PD-L1 overexpression results in increased resistance of tumor cells to CD8 T cell mediated lysis. PD-L1 overexpression results in increased resistance of tumor cells to CD8 T cell mediated lysis. In experimental models of melanoma, tumor growth can be transiently arrested via treatment with antibodies which block the interaction between PD-L1 and its receptor PD-1. For these reasons anti-PD-1 mediated immunotherapies are currently being used as cancer treatments. Pembrolizumab binds to PD-1 on activated immune cells to selectively block the interaction of PD-1 with its ligands.

This non-therapeutic biosimilar antibody uses the same variable regions from the therapeutic antibody Infliximab making it ideal for research use. This Infliximab biosimilar reacts with human TNFα (tumor necrosis factor-alpha) a multifunctional proinflammatory cytokine. TNFα exists as a soluble 17 kDa monomer, which forms homotrimers in circulation or as a 26 kDa membrane-bound form. TNFα belongs to the TNF superfamily of cytokines and signals through its two receptors, TNFR1 and TNFR2 which can be activated by both the soluble trimeric and membrane-bound and forms of TNFα. TNFα is primarily produced by macrophages in response to foreign antigens such as bacteria (lipopolysaccharides), viruses, and parasites as well as mitogens and other cytokines but can also be expressed by monocytes, neutrophils, NK cells, CD4 T cells and some specialized dendritic cells. TNFα is known to play key roles in a wide spectrum of biological processes including immunoregulation, cell proliferation, differentiation, apoptosis, antitumor activity, inflammation, anorexia, cachexia, septic shock, hematopoiesis, and viral replication. TNFα dysregulation has been implicated in a variety of diseases, including autoimmune diseases, insulin resistance, and cancer. Infliximab blocks the interaction of TNFα with the TNFR1 (p55) and TNFR2 (p75) resulting in a down-regulation of the inflammatory response associated with autoimmune diseases.

This non-therapeutic biosimilar antibody uses the same variable regions from the therapeutic antibody Atezolizumab making it ideal for research use. This Atezolizumab biosimilar reacts with human PD-L1 (programmed death ligand 1) also known as B7-H1 or CD274. PD-L1 is a 40 kDa type I transmembrane protein that belongs to the B7 family of the Ig superfamily. PD-L1 is expressed on T lymphocytes, B lymphocytes, NK cells, dendritic cells, as well as IFNγ stimulated monocytes, epithelial cells and endothelial cells. PD-L1 binds to its receptor, PD-1, found on CD4 and CD8 thymocytes as well as activated T and B lymphocytes and myeloid cells. Engagement of PD-L1 with PD-1 leads to inhibition of TCR-mediated T cell proliferation and cytokine production. PD-L1 is thought to play an important role in tumor immune evasion. Induced PD-L1 expression is common in many tumors and results in increased resistance of tumor cells to CD8 T cell mediated lysis. Atezolizumab blocks the interaction of PD-L1 with PD-1 and CD80.

The 29F.1A12™ monoclonal antibody reacts with mouse PD-1 (programmed death-1) also known as CD279. PD-1 is a 50-55 kDa cell surface receptor encoded by the Pdcd1 gene that belongs to the CD28 family of the Ig superfamily.

The 29F.1A12™ monoclonal antibody reacts with mouse PD-1 (programmed death-1) also known as CD279. PD-1 is a 50-55 kDa cell surface receptor encoded by the Pdcd1 gene that belongs to the CD28 family of the Ig superfamily.

经过多年筛选出针对Human IgE的单克隆抗体，与同类产品相比大幅度提高了检测灵敏度。用于人血清中sIgE、总IgE的检测，可明确体内是否存在过敏性疾病、免疫性疾病、感染等，为临床治疗提供有价值的信息。