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Search results for: Monoclonal Anti-dEGF Receptor, Extracellular Domain produced in mouse Antibody

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#32102522   2020/02/01 To Up

Inhibitory Effect of Polyclonal Antibodies Against HER3 Extracellular Subdomains on Breast Cancer Cell Lines.

Human epidermal growth factor receptor 3 (HER3) is a unique member of the tyrosine kinase receptors with an inactive kinase domain and is the preferable dimerization partner for HER2 which lead to potent tumorigenic signaling.
Samaneh Mansouri-Fard, Mojgan Ghaedi, Mohammad-Reza Shokri, Tannaz Bahadori, Jalal Khoshnoodi, Forough Golsaz-Shirazi, Mahmood Jeddi-Tehrani, Mohammad Mehdi Amiri, Fazel Shokri

1357 related Products with: Inhibitory Effect of Polyclonal Antibodies Against HER3 Extracellular Subdomains on Breast Cancer Cell Lines.

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#31930453   2020/01/13 To Up

Production, characterization, and application of a monoclonal antibody specific for the extracellular domain of human P2X7R.

This paper focuses on the production of a high-affinity monoclonal antibody (mAb) that can efficiently detect and block purinergic ligand-gated ion channel 7 receptor (P2X7R). To achieve this goal, the extracellular domain of human P2X7R, P2X7R-ECD, was used as an immunogen for BALB/c mice, inducing them to produce spleen lymphocytes that were subsequently fused with myeloma cells. Screening of the resultant hybridoma clones resulted in the selection of one stable positive clone that produced a qualified mAb, named 4B3A4. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis demonstrated that the purity of the purified 4B3A4 mAb was above 85%, with prominent bands corresponding to molecular weights of 55 kDa (heavy chain) and 25 kDa (light chain), and the BCA assay showed that the concentration of the purified 4B3A4 mAb was 0.3 mg/mL. Western blot analysis revealed that the 4B3A4 mAb could specifically recognize and bind both P2X7R-ECD and the full-length P2X7R protein. Laser scanning confocal microscopy (LSCM) revealed that the 4B3A4 mAb specifically bound to P2X7R on the membrane of human peripheral blood mononuclear cells (PBMCs). P2X7R expression was significantly different between healthy individuals and people with certain cancers as determined by flow cytometry (FCM). In addition, the 4B3A4 mAb significantly reduced ATP-stimulated Ca entry and YO-PRO-1 uptake, which indicated that the 4B3A4 mAb effectively blocked P2X7R activity. These data indicate that the 4B3A4 mAb can be further used as not only an antibody to detect cell surface P2X7R but also as a therapeutic antibody to target P2X7R-related signaling pathways.
Mingxuan Li, Shuping Luo, Yunfang Zhang, Lina Jia, Chuanyu Yang, Xiaoxiang Peng, Ronglan Zhao

1308 related Products with: Production, characterization, and application of a monoclonal antibody specific for the extracellular domain of human P2X7R.

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#31395688   2019/08/08 To Up

Preclinical Development of the Anti-LAG-3 Antibody REGN3767: Characterization and Activity in Combination with the Anti-PD-1 Antibody Cemiplimab in Human -Knockin Mice.

In the tumor microenvironment, multiple inhibitory checkpoint receptors can suppress T-cell function, thereby enabling tumor immune evasion. Blockade of one of these checkpoint receptors, PD-1, with therapeutic antibodies has produced positive clinical responses in various cancers; however, the efficacy of this approach can be further improved. Simultaneously targeting multiple inhibitory checkpoint receptors has emerged as a promising therapeutic strategy. Here, we report the development and characterization of REGN3767, a fully human IgG4 antibody targeting LAG-3, another inhibitory receptor on T cells. REGN3767 binds human and monkey LAG-3 with high affinity and specificity and blocks the interaction of LAG-3 with its ligand, MHC class II. In an engineered T-cell/antigen-presenting cell bioassay, REGN3767 alone, or in combination with cemiplimab (REGN2810, human anti-PD-1 antibody), blocked inhibitory signaling to T cells mediated by hLAG-3/MHCII in the presence of PD-1/PD-L1. To test the activity of REGN3767 alone or in combination with cemiplimab, we generated human knockin mice, in which the extracellular domains of mouse and were replaced with their human counterparts. In these humanized mice, treatment with cemiplimab and REGN3767 showed increased efficacy in a mouse tumor model and enhanced the secretion of proinflammatory cytokines by tumor-specific T cells. The favorable pharmacokinetics and toxicology of REGN3767 in nonhuman primates, together with enhancement of antitumor efficacy of anti-PD-1 antibody in preclinical tumor models, support its clinical development.
Elena Burova, Aynur Hermann, Jie Dai, Erica Ullman, Gabor Halasz, Terra Potocky, Seongwon Hong, Matt Liu, Omaira Allbritton, Amy Woodruff, Jerry Pei, Ashique Rafique, William Poueymirou, Joel Martin, Douglas MacDonald, William C Olson, Andrew Murphy, Ella Ioffe, Gavin Thurston, Markus Mohrs

2320 related Products with: Preclinical Development of the Anti-LAG-3 Antibody REGN3767: Characterization and Activity in Combination with the Anti-PD-1 Antibody Cemiplimab in Human -Knockin Mice.

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#30058195   2018/08/26 To Up

Inhibition of tumor formation and metastasis by a monoclonal antibody against lymphatic vessel endothelial hyaluronan receptor 1.

Although cancer metastasis is associated with poor prognosis, the mechanisms of this event, especially via lymphatic vessels, remain unclear. Lymphatic vessel endothelial hyaluronan receptor 1 (LYVE-1) is expressed on lymphatic vessel endothelium and is considered to be a specific marker of lymphatic vessels, but it is unknown how LYVE-1 is involved in the growth and metastasis of cancer cells. We produced rat monoclonal antibodies (mAb) recognizing the extracellular domain of mouse LYVE-1, and investigated the roles of LYVE-1 in tumor formation and metastasis. The mAb 38M and 64R were selected from hybridoma clones created by cell fusion between spleen cells of rats immunized with RH7777 rat hepatoma cells expressing green fluorescent protein (GFP)-fused mouse LYVE-1 proteins and mouse myeloma cells. Two mAb reacted with RH7777 and HEK293F human embryonic kidney cells expressing GFP-fused mouse LYVE-1 proteins in a GFP expression-dependent manner, and each recognized a distinct epitope. On immunohistology, the 38M mAb specifically stained lymphatic vessels in several mouse tissues. In the wound healing assay, the 64R mAb inhibited cell migration of HEK293F cells expressing LYVE-1 and mouse lymphatic endothelial cells (LEC), as well as tube formation by LEC. Furthermore, this mAb inhibited primary tumor formation and metastasis to lymph nodes in metastatic MDA-MB-231 xenograft models. This shows that LYVE-1 is involved in primary tumor formation and metastasis, and it may be a promising molecular target for cancer therapy.
Yuta Hara, Ryota Torii, Shiho Ueda, Erina Kurimoto, Eri Ueda, Hiroshi Okura, Yutaka Tatano, Hideki Yagi, Yoshiya Ohno, Toshiyuki Tanaka, Kazue Masuko, Takashi Masuko

2767 related Products with: Inhibition of tumor formation and metastasis by a monoclonal antibody against lymphatic vessel endothelial hyaluronan receptor 1.

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#29708866   // To Up

The Characterization of Monoclonal Antibodies to Mouse TLT-1 Suggests That TLT-1 Plays a Role in Wound Healing.

Platelets play a vital role in hemostasis and inflammation. The membrane receptor TREM-like transcript-1 (TLT-1) is involved in platelet aggregation, bleeding, and inflammation, and it is localized in the α-granules of platelets. Upon platelet activation, TLT-1 is released from α-granules both in its transmembrane form and as a soluble fragment (sTLT-1). Higher levels of sTLT-1 have been detected in the plasma of patients with acute inflammation or sepsis, suggesting an important role for TLT-1 during inflammation. However, the roles of TLT-1 in hemostasis and inflammation are not well understood. We are developing the mouse model of TLT-1 to mechanistically test clinical associations of TLT-1 in health and disease. To facilitate our studies, monoclonal murine TLT-1 (mTLT-1) antibodies were produced by the immunization of a rabbit using the negatively charged region of the mTLT-1 extracellular domain PPVPGPREGEEAEDEK. In the present study, we demonstrate that two selected clones, 4.6 and 4.8, are suitable for the detection of mTLT-1 by western blot, immunoprecipitation, immunofluorescent staining, flow cytometry and inhibit platelet aggregation in aggregometry assays. In addition, we found that the topical administration of clone 4.8 delayed the wound healing process in an experimental burn model. These results suggest that TLT-1 plays an important role in wound healing and because both clones specifically detect mTLT-1, they are suitable to further develop TLT-1 based models of inflammation and hemostasis in vivo.
Barbara Manfredi, Jessica Morales-Ortíz, Lymarie M Díaz-Díaz, Liz Hernandez-Matias, Delmaliz Barreto-Vázquez, Javier Menéndez-Pérez, J Alejandro Rodríguez-Cordero, Juan C Villalobos-Santos, Edgardo Santiago-Rivera, Adriana Rivera-Dompenciel, Eunice L Lozada-Delgado, Madhavi Kuchibhotla, Kelvin Carrasquillo-Carrión, Abiel Roche-Lima, A Valance Washington

1057 related Products with: The Characterization of Monoclonal Antibodies to Mouse TLT-1 Suggests That TLT-1 Plays a Role in Wound Healing.

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#29453154   2018/02/03 To Up

Unique pharmacology of a novel allosteric agonist/sensitizer insulin receptor monoclonal antibody.

Insulin resistance is a key feature of Type 2 Diabetes (T2D), and improving insulin sensitivity is important for disease management. Allosteric modulation of the insulin receptor (IR) with monoclonal antibodies (mAbs) can enhance insulin sensitivity and restore glycemic control in animal models of T2D.
Simon A Hinke, Anne M Cieniewicz, Thomas Kirchner, Katharine D'Aquino, Rupesh Nanjunda, Jason Aligo, Robert Perkinson, Philip Cooper, Ken Boayke, Mark L Chiu, Steve Jarantow, Eilyn R Lacy, Yin Liang, Dana L Johnson, Jean M Whaley, Russell B Lingham, Anthony J Kihm

2593 related Products with: Unique pharmacology of a novel allosteric agonist/sensitizer insulin receptor monoclonal antibody.

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#28234558   2017/02/16 To Up

Preparation and Characterization of a Novel Monoclonal Antibody Against the Extracellular Domain of Human Transferrin Receptor.

Human transferrin receptor (hTfR1), a type II homodimeric transmembrane protein, is extensively expressed at low levels in most normal human tissues. However, the expression level of hTfR1 in some tumor tissues and the blood-brain barrier (BBB) is comparatively higher. Therefore, we developed an hTfR1 monoclonal antibody 2C9, which may be utilized to deliver drugs across the BBB through receptor-mediated endocytosis in the future. 2C9 was obtained by hybridoma cells fused by the SP2/0-Ag14 cell line and splenic B cells from hTfR1-immunized BALB/c mice. In this study, we used indirect ELISA, Western blot, and immunofluorescence to explore the characterization and application of MAb 2C9. The results showed that the affinity constant (K) of the MAb 2C9 produced from ascites was 2.85 × 10 M and its isotype is IgG2a (Kappa chain). Above all, this report provides a more comprehensive protocol to produce monoclonal antibodies against the extracellular domain of hTfR1.
Xiaorui Li, Ling Yang, Yue Yang, Ming Shao, Yu Liu

2246 related Products with: Preparation and Characterization of a Novel Monoclonal Antibody Against the Extracellular Domain of Human Transferrin Receptor.

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#28132803   2017/01/26 To Up

Combined blockade of Tim-3 and MEK inhibitor enhances the efficacy against melanoma.

Insights into the role of the mitogen-activated protein kinase (MAPK) pathway and immune checkpoints have led combined targeted therapy and immunotherapy to be a promising regimen. Trametinib, as a mitogen-activated extracellular signal-regulated kinase (MEK) inhibitor, has demonstrated effectiveness in patients with advanced melanoma. T cell immunoglobulin- and mucin-domain-containing molecule-3 (Tim-3), an immune checkpoint molecule, participates in multiple negative regulation of antitumor immunity. We for the first time to our knowledge reported the combination of trametinib and anti-Tim-3 monoclonal antibody (mAb) in treating B16-F10 melanoma mice. We discovered that trametinib remarkably promoted apoptosis and inhibited cell proliferation while inhibition of MEK improved the expression of Tim-3 and caused the decrease of CD8 T cells; to the contrary, anti-Tim-3 mAb enhanced antitumor immunity by stimulating CD8 T cells, thus the combined therapy produced potent antitumor effect cooperatively. Taken together, our study provides compelling evidence for combining trametinib and anti-Tim-3 mAb as a potential valuable regimen in treating melanoma.
Yang Liu, Pengcheng Cai, Ning Wang, Qianwen Zhang, Fenghua Chen, Liang Shi, Yang Zhang, Lin Wang, Lihua Hu

1120 related Products with: Combined blockade of Tim-3 and MEK inhibitor enhances the efficacy against melanoma.

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#28060819   2017/01/06 To Up

An Anti-Human Lutheran Glycoprotein Phage Antibody Inhibits Cell Migration on Laminin-511: Epitope Mapping of the Antibody.

The Lutheran glycoprotein (Lu), also known as basal cell adhesion molecule (B-CAM), is an Ig superfamily (IgSF) transmembrane receptor for laminin α5. Although Lu is not present in normal hepatocytes, its expression is significantly increased in hepatocellular carcinoma (HCC). In this study, we isolated thirteen phage antibodies to Lu from a phage library of peripheral blood from HCC patients, suggesting that these patients produced autoantibodies against endogenous Lu. To characterize the phage antibodies, we determined the Lu domains they recognize. The extracellular domain of Lu contains five IgSF domains, D1-D2-D3-D4-D5. The epitope of one phage antibody (A7) was localized to the D5 domain. The other phage antibodies recognized the D2 domain, which is also recognized by a function blocking mouse monoclonal antibody. One of the antibodies to D2 (C7) inhibited the binding of Lu to ligand, and it also prevented tumor cell migration on laminin-511 (LM-511). However, the C7 scFv purified from the periplasm fraction of bacteria did not exhibit the inhibitory effects, indicating that the scFv form could not sterically inhibit the binding of Lu to LM-511. We also identified the amino acid residues that form the epitope recognized by the C7 phage antibody. Mutagenesis studies showed that Arg247 is necessary for forming the epitope. The C7 phage antibody and its epitope may be useful for developing drugs to prevent HCC progression and/or metastasis.
Yurie Enomoto-Okawa, Yuka Maeda, Nozomi Harashima, Yumika Sugawara, Fumihiko Katagiri, Kentaro Hozumi, Kam Man Hui, Motoyoshi Nomizu, Yuji Ito, Yamato Kikkawa

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