Search results for: Mouse Anti-Estradiol-17-beta Antibodies
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Increased permeability of blood vessels after reversible electroporation is facilitated by alterations in endothelial cell-to-cell junctions.Delivery of electric field pulses, i.e. electroporation (EP), to tissues has been shown to have a blood flow modifying effect. Indeed, the diameter of blood vessels exposed to EP is immediately reduced resulting in blood flow abrogation, followed by an increase in vascular permeability. The main cause of the increased permeability remains unknown. The aim of this study was to determine whether the in vivo effects of EP on permeability of blood vessels are linked to the permeabilization of endothelial cells' membrane (EC) and/or disruption of cell-to-cell junctions. We used a dorsal window chamber model in C57Bl/6 mice coupled with multiphoton microscopy and fluorescently labelled antibodies against PECAM-1 (CD31) to visualize endothelial cell-to-cell junctions. Clinically validated EP parameters were used and behavior of cell-to-cell junctions, in combination with leakage of 70 kDa fluorescein isothiocyanate labelled dextran (FD), was followed in time. After EP, a constriction of blood vessels was observed and correlated with the change in the shape of ECs. This was followed by an increase in permeability of blood vessels for 70 kDa FD and a decrease in the volume of labelled cell-to-cell junctions. Both parameters returned to pre-treatment values in 50% of mice. For the remaining 50%, we hypothesize that disruption of cell-to-cell junctions after EP may trigger the platelet activation cascade. Our findings show for the first time in vivo that alterations in cell-to-cell junctions play an important role in the response of blood vessels to EP and explain their efficient permeabilization.
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Human IgG subtype cross-species reactivity to mouse and cynomolgus monkey Fcγ receptors.In therapeutic antibody discovery and early development, mice and cynomolgus monkey are used as animal models to assess toxicity, efficacy and other properties of candidate molecules. As more candidate antibodies are based on human immunoglobulin (IgG) subtypes, many strategies are pursued to simulate the human system in the test animal. However, translation rate from a successful preclinical trial to an approved drug is extremely low. This may partly be due to differences in interaction of human IgG based candidate molecules to endogenous Fcγ receptors of model animals in comparison to those of human Fcγ receptors. In this study, we compare binding characteristics of human IgG subtypes commonly used in drug development (IgG1, IgG2, IgG4) and their respective Fc silent versions (IgG1σ, IgG2σ, IgG4 PAA) to human, mouse and cynomolgus monkey Fcγ receptors. To control interactions between Fab and Fc domains, the test IgGs all have the same variable regions. We found distinct variations of interaction of human IgG subtypes to model animal Fcγ receptors in comparison to their human counterparts. Particularly, cynomolgus monkey Fcγ receptors show consistently tighter binding to human IgGs than human Fcγ receptors. Moreover, the presumably Fc silent human IgG4 PAA framework bound to cynomolgus monkey FcγRI with nanomolar affinity while only very weak binding was observed for the human FcγRI. Our results highlight the need for a thorough in vitro affinity characterization of candidate IgGs against model animal Fcγ receptors and careful design of preclinical studies.
1311 related Products with: Human IgG subtype cross-species reactivity to mouse and cynomolgus monkey Fcγ receptors.Rabbit Anti-TPST2 Polyclo Rabbit Anti-TPST2 Polyclo Rabbit Anti-PIWIL4 Polycl Rabbit Anti-PIWIL4 Polycl Rabbit Anti-EDG1 CD363 Po Rabbit Anti-EDG1 CD363 Po Rabbit Anti-GPR65 Polyclo Rabbit Anti-GPR65 Polyclo CD74 Host Mouse Species R Hsp90alpha Host Mouse Spe Nitrotyrosine Host Mouse Hsp27 FITC Host Mouse Spe
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Multiparametric Analysis of Myeloid Populations by Flow Cytometry.Flow cytometry is extensively used for the immune-profiling of leukocytes in tissue during homeostasis and inflammation. The multiparametric power of using fluorescently conjugated antibodies for specific surface and activation markers provides a comprehensive profile of immune cells. This chapter describes the identification and characterization of myeloid populations using flow cytometric analysis in an acute model of resolving inflammation. This model allows the examination of heterogenic populations across different systemic and tissue locations. We describe tissue processing, antibody staining, and analysis, which include a newly described viSNE tool to generate two-dimensional clustering within myeloid populations. We also reference the use of transgenic reporter mice on specific myeloid cells that provides enhanced specificity and profiling when defining myeloid heterogeneity.
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Generating a Battery of Monoclonal Antibodies Against Firefly Luciferase for Dot Blot Analysis, Western Blot Analysis, and Immunostaining of Cells in Culture and Paraffin Sections.Firefly luciferase (FLuc) is commonly used as a reporter gene PpyLuc1 in bioanalytical assays. We have produced five mouse-derived monoclonal antibodies (mAbs) that recognize FLuc. The mAbs, DSHB-LUC-2, DSHB-LUC-3, DSHB-LUC-9, DSHB-LUC-16, and DSHB-LUC-24, were generated by immunizing mice with purified 6xHIS-tagged FLuc (6xHis-FLuc) in suspension with an adjuvant. All five were validated by dot blots. Four of the mAbs provided strong signals in western blot analysis, and one a weak signal. All five were validated for immunostaining in fixed cell culture. Only one stained cells embedded in paraffin. The five mAbs are available at cost through the Developmental Studies Hybridoma Bank (DSHB), a nonprofit National Resource created by the National Institutes of Health.
2050 related Products with: Generating a Battery of Monoclonal Antibodies Against Firefly Luciferase for Dot Blot Analysis, Western Blot Analysis, and Immunostaining of Cells in Culture and Paraffin Sections.anti HSV (II) gB IgG1 (mo anti HCMV IE pp65 IgG1 (m anti HCMV gB IgG1 (monocl HIV1 integrase antibody, Rat Anti-Mouse Dendritic Rabbit Anti-Human Androge Goat Anti-Human Androgen Rabbit Anti-Rat Androgen Mouse Anti-Ca19.9 Sialyl Mouse Anti-Histone H4 Me1 Mouse Anti-Apolipoprotein Mouse Anti-Histone H4 Me3
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Eliminating Factor H-Binding Activity ofCspZ Combined with Virus-Like Particle Conjugation Enhances Its Efficacy as a Lyme Disease Vaccine.The spirocheteis the causative agent of Lyme disease, the most common tick-borne disease in the US and Europe. No potent human vaccine is currently available. The innate immune complement system is vital to host defense against pathogens, as complement activation on the surface of spirochetes results in bacterial killing. Complement system is inhibited by the complement regulator factor H (FH). To escape killing,produces an outer surface protein CspZ that binds FH to inhibit complement activation on the cell surface. Immunization with CspZ alone does not protect mice from infection, which we speculate is because FH-binding cloaks potentially protective epitopes. We modified CspZ by conjugating to virus-like particles (VLP-CspZ) and eliminating FH binding (modified VLP-CspZ) to increase immunogenicity. We observed greater bactericidal antibody titers in mice vaccinated with modified VLP-CspZ: A serum dilution of 1:395 (modified VLP-CspZ) vs 1:143 (VLP-CspZ) yielded 50% borreliacidal activity. Immunizing mice with modified VLP-CspZ cleared spirochete infection, as did passive transfer of elicited antibodies. This work developed a novel Lyme disease vaccine candidate by conjugating CspZ to VLP and eliminating FH-binding ability. Such a strategy of conjugating an antigen to a VLP and eliminating binding to the target ligand can serve as a general model for developing vaccines against other bacterial infectious agents.
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A reappraisal of CTLA-4 checkpoint blockade in cancer immunotherapy.It is assumed that anti-CTLA-4 antibodies cause tumor rejection by blocking negative signaling from B7-CTLA-4 interactions. Surprisingly, at concentrations considerably higher than plasma levels achieved by clinically effective dosing, the anti-CTLA-4 antibody Ipilimumab blocks neither B7 trans-endocytosis by CTLA-4 nor CTLA-4 binding to immobilized or cell-associated B7. Consequently, Ipilimumab does not increase B7 on dendritic cells (DCs) from either CTLA4 gene humanized (Ctla4) or human CD34stem cell-reconstituted NSG™ mice. In Ctla4mice expressing both human and mouse CTLA4 genes, anti-CTLA-4 antibodies that bind to human but not mouse CTLA-4 efficiently induce Treg depletion and Fc receptor-dependent tumor rejection. The blocking antibody L3D10 is comparable to the non-blocking Ipilimumab in causing tumor rejection. Remarkably, L3D10 progenies that lose blocking activity during humanization remain fully competent in inducing Treg depletion and tumor rejection. Anti-B7 antibodies that effectively block CD4 T cell activation and de novo CD8 T cell priming in lymphoid organs do not negatively affect the immunotherapeutic effect of Ipilimumab. Thus, clinically effective anti-CTLA-4 mAb causes tumor rejection by mechanisms that are independent of checkpoint blockade but dependent on the host Fc receptor. Our data call for a reappraisal of the CTLA-4 checkpoint blockade hypothesis and provide new insights for the next generation of safe and effective anti-CTLA-4 mAbs.
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ADAM17 is required for EGF-R-induced intestinal tumors via IL-6 trans-signaling.Colorectal cancer is treated with antibodies blocking epidermal growth factor receptor (EGF-R), but therapeutic success is limited. EGF-R is stimulated by soluble ligands, which are derived from transmembrane precursors by ADAM17-mediated proteolytic cleavage. In mouse intestinal cancer models in the absence of ADAM17, tumorigenesis was almost completely inhibited, and the few remaining tumors were of low-grade dysplasia. RNA sequencing analysis demonstrated down-regulation of STAT3 and Wnt pathway components. Because EGF-R on myeloid cells, but not on intestinal epithelial cells, is required for intestinal cancer and because IL-6 is induced via EGF-R stimulation, we analyzed the role of IL-6 signaling. Tumor formation was equally impaired in IL-6mice and sgp130Fc transgenic mice, in which only trans-signaling via soluble IL-6R is abrogated. ADAM17 is needed for EGF-R-mediated induction of IL-6 synthesis, which via IL-6 trans-signaling induces β-catenin-dependent tumorigenesis. Our data reveal the possibility of a novel strategy for treatment of colorectal cancer that could circumvent intrinsic and acquired resistance to EGF-R blockade.
1539 related Products with: ADAM17 is required for EGF-R-induced intestinal tumors via IL-6 trans-signaling.(3R,4S,5R,6S)-1-Aza-4-hyd Rabbit Anti-CD25 IL-2RA P Rabbit Anti-IL-12 Polyclo Rabbit Anti-IL-8 CXCL8 Po Rabbit Anti-intestinal FA Rabbit Anti-intestinal FA Rabbit Anti-IL-15 Polyclo Rabbit Anti-IL-9 Polyclon Rabbit Anti-IL-8 CXCL8 Po Rabbit Anti-IL-1 Beta IL- Rabbit Anti-IL-4I1 Polycl Rabbit Anti-IL-4I1 Polycl
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Targeting CD6 for the treatment of experimental autoimmune uveitis.CD6 is emerging as a new target for treating many pathological conditions in which T cells are integrally involved, but even the latest data from studies of CD6 gene engineered mice were still contradictory. To address this issue, we studied experimental autoimmune uveitis (EAU), a model of autoimmune uveitis, in wild-type (WT) and CD6 knockout (KO) mice.
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Microglial activation and amyloid-β clearance induced by exogenous heat-shock proteins.SPECIFIC AIMS We addressed the hypothesis that extracellular heat shock proteins (HSPs) induce microglial activation resulting in cytokine production and clearance of amyloid-β peptide (Aβ). The effects of exogenous HSP90, HSP70, and HSP32 on the production of interleukin 6 (IL-6) and tumor necrosis factor α (TNF-α) and the phagocytosis of Aβ(1-42) were studied in isolated microglial cultures from rat and Toll-like receptor 4 (TLR4) mutant mouse brains; levels of expression and localization of HSP90 were investigated in the brains of patients with Alzheimer's disease (AD). PRINCIPAL FINDINGS 1. Exogenous HSPs induce cytokine production In rat microglial culture, addition of HSP90, HSP70, or HSP32 markedly induced production of IL-6 or TNF-α in a concentration-dependent manner whereas HSP27 did not, even at 10 μg/ml (Fig. 1 ⤻ A, B). To exclude the possibility of endotoxin contamination, samples of HSPs and lipopolysaccharide (LPS) from E. coli were heat treated at 100°C for 20 min to inactivate protein but not LPS activity before incubation with the microglia. Heat treatment completely abolished HSP90-, HSP70-, and HSP32-related induction of IL-6 and TNF-α (Fig. 1C, D ⤻ ) but, as expected, did not affect the induction of cytokine production by LPS. In contrast, 10 μg/ml of polymyxin B, which is an LPS trapper and blocks LPS-induced cellular activation, completely abolished LPS-induced production of IL-6 and TNF-α but had no effect on cytokine production induced by HSP90, HSP70, or HSP32 (Fig. 1C, D ⤻ ). Thus, microglial activation by HSPs is unlikely to be due to endotoxin contamination. [Figure: see text] 2. Exogenous HSPs enhanced phagocytosis and clearance of Aβ(1-42) At 1 day after addition of Aβ(1-42) into the culture, it was phagocytosed into rat microglia in a concentration-dependent manner. At that time, aggregated peptides of Aβ(1-42) were also detected by immunoblotting with anti-Aβ antibody. Laser confocal microscopy showed Aβ immunoreactivity in small vesicles in some microglia. The amount of Aβ(1-42) in the microglia was significantly increased after the administration of 5 μg/ml of HSP90 (56 nM), HSP70 (71 nM), or HSP32 (156 nM) but not after administration of IL-6 or TNF-α (Fig. 2 ⤻ ). The number of microglia that phagocytosed Aβ(1-42) was markedly increased: after 3 days, the amount of Aβ(1-42) detected in the microglia was significantly decreased by treatment with these HSPs vs. vehicle (Fig. 2) ⤻ . Thus, exogenous HSPs significantly facilitated the phagocytosis and clearance of Aβ(1-42) by microglia. [Figure: see text] 3. The TLR4 pathway is involved in HSP-induced microglial activation To clarify the mechanism underlying the effects of exogenous HSPs on cytokine production and Aβ clearance, the degradation of nuclear factor (NF) -κB inhibitor (IκB), phosphorylation of p38 mitogen-activated protein kinase (MAPK), and influence of TLR4-mutation were assessed. In rat microglia, the administration of 5 μg/ml of HSPs significantly induced IκB degradation and p38 MAPK phosphorylation similar to the effect of LPS. In TLR4 mutant microglia, however, production of IL-6 and TNF-α and the enhancement of Aβ phagocytosis induced by HSPs were almost completely suppressed. TLR4 mutant microglia showed a marked reduction in HSP-induced IκB degradation and p38 MAPK phosphorylation. Thus, exogenous HSPs induce NF-κB and p38 MAPK activation through TLR4. 4. HSP90 associates with Aβ plaques in AD brain After in vitro incubation of Aβ(1-42) with HSPs, Aβ was immunoprecipitated by antibodies against HSP90, HSP70, or HSP32. When rat microglia were incubated with HSPs in the presence of Aβ(1-42), IL-6 and TNF-α were produced at levels similar to when cells were treated with HSP alone. The level of expression of HSP90 in cytosolic and membranous fractions of the temporal cortex of AD brains was significantly higher than that in age-matched controls. Consistent with our in vitro studies, HSP90 immunoreactivity was colocalized with Aβ immunoreactivity. Extracellular HSP90 immunoreactivity was observed close to the microglia that expressed the human leukocyte antigen DR, a marker of reactive microglia, in senile plaques. These immunocytochemical results suggest that extracellular HSP90 accumulates close to the microglia in senile plaques. CONCLUSIONS A characteristic of AD is the accumulation of fibrillar Aβ to form amyloid plaques. Understanding the balance of production and clearance of Aβ is the key to understanding amyloid plaque homeostasis. Microglia associated with the senile plaques are likely to play a major role in this process. We showed that HSPs, such as HSP90, HSP70, and HSP32, but not HSP27, induce the production of IL-6 and TNF-α. The effect of HSPs is mediated by NF-κB and/or p38 MAPK activation through TLR4. HSP90, HSP70, and HSP32 increased the amount of Aβ in the microglia after 1 day and decreased the amount after 3 days. Addition of Aβ(1-42) alone did not induce the production of IL-6 and TNF-α, but Aβ(1-42) at lower concentrations was taken up by microglia. Although production of IL-6 and TNF-α was induced by exogenous HSPs, these cytokines did not affect the phagocytosis of Aβ by microglia. Therefore, exogenous HSPs act directly via the TLR4 pathway to induce microglial activation and facilitate the phagocytosis and clearance of Aβ (Fig. 3 ⤻ ). We demonstrated that HSP90 was also significantly increased in both the cytosolic and particulate fractions of AD brains and that extracellular HSP90 is colocalized with Aβ plaques. HSP90, HSP70, and HSP32 bound to Aβ(1-42) in vitro and, in the presence of Aβ(1-42), induced cytokine production with a potency similar to that induced by treatment with HSP alone. These observations suggest that when these HSPs are found in the extracellular milieu, they may exert chaperone and regulatory effects on various immunocompetent cells present in regions where the neurons degenerate in AD. [Figure: see text] It has been reported that IL-6 immunoreactivity is observed in senile plaques and that the TNF-α level is elevated in sera from AD patients. Since IL-6 and TNF-α are known to be proinflammatory cytokines in the immune system, microglial activation and these cytokines had been considered to exacerbate neurodegeneration. However, since recent reports have shown that IL-6 and TNF-α inhibit neuronal cell death, these cytokines may actually play a neuroprotective role in the brain (Fig. 3) ⤻ . More recently, immunization with Aβ peptides was reported to reduce the Aβ burden in transgenic mice displaying Aβ plaques. Antibodies to Aβ administered peripherally enter the brain and increase Aβ clearance, a process mediated by Fc receptors in microglia. Our findings suggest that microglial Aβ clearance induced by exogenous HSPs is mediated by activation of NF-κB and/or p38 MAPK via the TLR4 pathway. Thus, HSP-induced clearance of Aβ is mediated by a mechanism different from the clearance by antibodies to Aβ. We believe that HSP-induced microglial activation participates in compensatory neuroprotection through the production of cytokines, enhancement of phagocytosis, and clearance of Aβ. HSPs may be another option (along with anti-Aβ antibodies) to investigate in the search for a therapeutic strategy for AD.To read the full text of this article, go to http://www.fasebj.org/cgi/doi/10.1096/fj.01-0530fje ; to cite this article, use FASEB J. (February 25, 2002) 10.1096/fj.01-0530fjeThe first two authors contributed equally to this work.
1191 related Products with: Microglial activation and amyloid-β clearance induced by exogenous heat-shock proteins.Human Heat shock proteins Heat Shock Protein 70 (H Heat Shock Protein 70 (H Low endotoxin heat shock Low endotoxin heat shock Low endotoxin heat shock Low endotoxin heat shock Standard grade heat shoc Standard grade heat shoc Standard grade heat shoc Standard grade heat shoc Standard grade heat shoc
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[Surveillance with sentinel mice in key water areas of schistosomiasis endemic regions in Yunnan Province, 2015].To carry out the surveillance with sentinel mice in the key water areas of schistosomiasis endemic regions in Yunnan Province, so as to establish and perfect the surveillance and forecast system of schistosomiasis.
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