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           Search results for: MOUSE ANTI HUMAN ALBUMIN-MONOCLONAL ANTIBODY   

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Antioxidative nanoparticles significantly enhance therapeutic efficacy of an antibacterial therapy against Listeria monocytogenes infection.

Acute inflammatory conditions such as sepsis lead to fatal conditions, including multiple organ failure. However, currently no definite treatments are available against these conditions. Therefore, several treatments, such as steroidal anti-inflammatory drugs, protease inhibitors, anti-human TNF-α monoclonal antibodies, and continuous hemodiafiltration (CHDF), are currently being investigated in order to decrease the blood cytokine level, which increases remarkably. However, these treatments are not always reliable and effective, and none have drastically improved survival rates. Reactive oxygen species (ROS) are signaling molecules responsible for the production of cytokines and chemokines that can mediate hyperactivation of the immune response. In addition to the abovementioned agents, various antioxidants have been explored for the removal of excess ROS during inflammation. However, the development of low-molecular-weight (LMW) antioxidants as therapeutic agents has been hampered by several issues associated with toxicity, poor pharmacokinetics, low bioavailability, and rapid metabolism. In the present study, we aimed to overcome these limitations through the use of antioxidative nanoparticles. Although treatment with antioxidative nanoparticles alone did not eliminate bacteria, combined treatment with an antibacterial agent was found to significantly improve survival rate of the treated mice as compared to the control group. More importantly, the antioxidative nanoparticles reduced oxidative tissue injury caused by the bacterial infection. Thus, our findings highlighted the effectiveness of combination treatment with antioxidative nanoparticles and an antibacterial agent to prevent severe inflammation caused by bacterial infection.

2763 related Products with: Antioxidative nanoparticles significantly enhance therapeutic efficacy of an antibacterial therapy against Listeria monocytogenes infection.

Mouse Anti-Listeria monoc Mouse Anti-Listeria monoc LISTERIA MONOCYTOGENES se Rabbit Anti-Listeria ATCC Rabbit Anti-Listeria ATCC Rabbit Anti-Listeria ATCC Rabbit Anti-Listeria ATCC FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu

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Chimeric antigen receptors with human scFvs preferentially induce T cell anti-tumor activity against tumors with high B7H6 expression.

B7H6 is emerging as a promising tumor antigen that is known to be expressed on a wide array of tumors and is reported to stimulate anti-tumor responses from the immune system. As such, B7H6 presents a good target for tumor-specific immunotherapies. B7H6-specific chimeric antigen receptors (CAR) based on a murine antibody showed successful targeting and elimination of tumors expressing B7H6. However, mouse single chain variable fragments (scFvs) have the potential to induce host anti-CAR responses that may limit efficacy, so human scFvs specific for B7H6 were selected by yeast surface display. In this study, we validate the functionality of these human scFvs when formatted into chimeric antigen receptors. The data indicate that T cells expressing these B7H6-specific human scFvs as CARs induced potent anti-tumor activity in vitro and in vivo against tumors expressing high amounts of B7H6. Importantly, these human scFv-based CARs are sensitive to changes in B7H6 expression which may potentially spare non-tumor cells that express B7H6 and provides the foundation for future clinical development.

1470 related Products with: Chimeric antigen receptors with human scFvs preferentially induce T cell anti-tumor activity against tumors with high B7H6 expression.

anti CD38 Hematopoietic p anti Transferrin receptor Human tumor cell array, 1 Mouse Anti-Human CD34 Tar anti CD7 All T cells Reco anti CD45 RA B cells, T c Human tumor cell array, 1 Mouse Anti-Human Mast Cel Mouse Anti-Human Mast Cel Mouse Anti-Human Fibrobla Goat Anti-Human Wilms tum FDA normal and tumor orga

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Mouse and human HSPC immobilization in liquid culture by CD43 or CD44-antibody coating.

Keeping track of individual cell identifications is imperative to the study of dynamic single cell behavior over time. Highly motile hematopoietic stem and progenitor cells (HSPCs) migrate quickly and do not adhere, and thus must be imaged very frequently to keep cell identifications. Even worse, they are also flushed away during medium exchange. To overcome these limitations, we tested antibody coating for reducing HSPC motility in vitro. Anti-CD43 and -CD44 antibody coating reduced cell motility of mouse and human HSPCs in a concentration dependent manner. This enables 2D colony formation without cell mixing in liquid cultures, massively increases time-lapse imaging throughput, and maintains cell positions also during media exchange. Anti-CD43, but not -CD44 coating reduces mouse HSPC proliferation with increasing concentrations. No relevant effects on cell survival or myeloid and megakaryocyte differentiation of hematopoietic stem cells and multipotent progenitors 1-5 (MPPs) were detected. Human umbilical cord hematopoietic CD34+ cell survival, proliferation and differentiation was not affected by either coating. This approach both, massively simplifies and accelerates continuous analysis of suspension cells, and enables the study of their behavior in dynamic rather than static culture conditions over time.

2314 related Products with: Mouse and human HSPC immobilization in liquid culture by CD43 or CD44-antibody coating.

Integrin β1 (CD29) Antib Rabbit Anti-intestinal FA Rabbit Anti-Orexin-A Poly Rabbit Anti-APIP Apaf1 In Rabbit Anti-APIP Apaf1 In Rabbit Anti-TNIP2 ABIN2 T Rabbit Anti-TNIP2 ABIN2 T Rabbit Anti-Cell death in Rabbit Anti-Cell death in Inhibitory mouse monoclo Anti AGO2 Human, Monoclon Anti AGO2 Mouse, Monoclon

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Tumor cell-intrinsic Tim-3 promotes liver cancer via NF-κB/IL-6/STAT3 axis.

T-cell immunoglobulin and mucin-domain containing-3 (Tim-3), mediating immune exhaustion in tumor microenvironment, has become a promising target for tumor therapy. However, the exact mechanisms for tumor cell-intrinsic Tim-3 in tumor development and its potential contribution in Tim-3-targeted therapy strategy have not been elucidated yet. In this study, we showed that human liver cancer tissues contained high ratio of Tim-3-expressing hepatocytes, and cytokines rich in tumor microenvironment and HBV involved in Tim-3 upregulation in malignant hepatocytes. We demonstrated that hepatocyte-specific Tim-3 overexpression enhances tumor cell growth, whereas Tim-3 inhibition on malignant hepatocytes by anti-Tim-3 antibodies or RNAi suppresses tumor growth both in vitro and in Tim-3 knockout mice. Mechanistically, the hepatocyte-Tim-3 receptor activates NF-κB phosphorylation, which in turn stimulates IL-6 secretion and STAT3 phosphorylation. Our results identify tumor cell-intrinsic functions of Tim-3 in tumorigenesis and suggest that blocking Tim-3 in tumor cells might contribute to the clinical efficacy of anti-Tim-3 antibody treatment in the future tumor therapy.

2421 related Products with: Tumor cell-intrinsic Tim-3 promotes liver cancer via NF-κB/IL-6/STAT3 axis.

Bone giant cell tumor tis Hygromycin B, EvoPure™, Hygromycin B, EvoPure™, Lung squamous cell carcin Liver cancer tissue array High density liver cancer Liver cancer tissue array Recombinant Human IL 4 Recombinant Viral antige Recombinant Viral antige Recombinant Viral Antige rHu IL 2 , 3MIU , Lot 200

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Safety evaluation of a human chimeric monoclonal antibody that recognizes the extracellular loop domain of claudin-2.

Claudin-2 (CLDN-2), a pore-forming tight-junction protein with a tetra-transmembrane domain, is involved in carcinogenesis and the metastasis of some cancers. Although CLDN-2 is highly expressed in the tight junctions of the liver and kidney, whether CLDN-2 is a safe target for cancer therapy remains unknown. We recently generated a rat monoclonal antibody (mAb, clone 1A2) that recognizes the extracellular domains of human and mouse CLDN-2. Here, we investigated the safety of CLDN-2-targeted cancer therapy by using 1A2 as a model therapeutic antibody. Because most human therapeutic mAbs are IgG1 subtype that can induce antibody-dependent cellular cytotoxicity, we generated a human-rat chimeric IgG1 form of 1A2 (xi-1A2). xi-1A2 activated Fcγ receptor IIIa in the presence of CLDN-2-expressing cells, indicating that xi-1A2 likely exerts antibody-dependent cellular cytotoxicity. At 24 h after its intravenous injection, xi-1A2 was distributed into the liver, kidney, and tumor tissues of mice bearing CLDN-2-expressing fibrosarcoma cells. Treatment of the xenografted mice with xi-1A2 attenuated tumor growth without apparent adverse effects, such as changes in body weight and biochemical markers of liver and kidney injury. These results support xi-1A2 as the lead candidate mAb for safe CLDN-2-targeted cancer therapy.

2716 related Products with: Safety evaluation of a human chimeric monoclonal antibody that recognizes the extracellular loop domain of claudin-2.

Monoclonal Anti-dEGF Rece Anti C Reactive Protein A Anti AGO2 Human, Monoclon Anti AGO2 Human, Monoclon Anti AGO2 Human, Monoclon Anti AGO2 Human, Monoclon Anti AGO2 Human, Monoclon Anti AGO2 Human, Monoclon Anti Human AGO3, Monoclon anti CD16 monoclonal anti anti CD20 monoclonal anti anti CD54 IgG2b k monoclo

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Microenvironmental regulation of the IL-23R/IL-23 axis overrides chronic lymphocytic leukemia indolence.

Although the progression of chronic lymphocytic leukemia (CLL) requires the cooperation of the microenvironment, the exact cellular and molecular mechanisms involved are still unclear. We investigated the interleukin (IL)-23 receptor (IL-23R)/IL-23 axis and found that circulating cells from early-stage CLL patients with shorter time-to-treatment, but not of those with a more benign course, expressed a defective form of the IL-23R complex lacking the IL-12Rβ1 chain. However, cells from both patient groups expressed the complete IL-23R complex in tissue infiltrates and could be induced to express the IL-12Rβ1 chain when cocultured with activated T cells or CD40Lcells. CLL cells activated in vitro in this context produced IL-23, a finding that, together with the presence of IL-23 in CLL lymphoid tissues, suggests the existence of an autocrine/paracrine loop inducing CLL cell proliferation. Interference with the IL-23R/IL-23 axis using an anti-IL-23p19 antibody proved effective in controlling disease onset and expansion in xenografted mice, suggesting potential therapeutic strategies.

2454 related Products with: Microenvironmental regulation of the IL-23R/IL-23 axis overrides chronic lymphocytic leukemia indolence.

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hPMSC transplantation restoring ovarian function in premature ovarian failure mice is associated with change of Th17/Tc17 and Th17/Treg cell ratios through the PI3K/Akt signal pathway.

Human placenta-derived mesenchymal stem cell (hPMSC) transplantation has been demonstrated to be an effective way of recovering ovarian function in mice with autoimmune induced premature ovarian failure (POF). But the exact mechanism remains unclear. The goal of the present study is to investigate the role of immune factors (T-helper 17 (Th17), cytotoxic T (Tc17) and regulatory T (Treg) cells) in the recovery of ovarian function and whether the phosphatidylinositol 3-kinase (PI3K)/Akt signal pathway is involved in the regulation.

2093 related Products with: hPMSC transplantation restoring ovarian function in premature ovarian failure mice is associated with change of Th17/Tc17 and Th17/Treg cell ratios through the PI3K/Akt signal pathway.

AKT PKB Signaling Phospho T-Cell Receptor Signaling Tissue array of ovarian g Akt Inhibitor, Isozyme Se AP-1 Reporter – HEK293 Wnt Signaling Pathway TCF JAK pathway ISRE reporter Cell cycle antibody array Signal transduction antib AKT Phospho-Specific Arra AMPK Signaling Phospho-Sp Cell Cycle Phospho-Specif

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Staphylococcal protein A contributes to persistent colonization of mice with.

persistently colonizes the nasopharynx of humans, which increases the risk for invasive diseases such as skin infection and bacteremia. Nasal colonization triggers IgG responses against staphylococcal surface antigens, however these antibodies cannot prevent subsequent colonization or disease. Here we describeWU1, a multi-locus sequence type ST88 isolate, that persistently colonizes the nasopharynx of mice. We report that staphylococcal protein A (SpA) is required for persistence ofWU1 in the nasopharynx. Compared to animals colonized by wild-type, mice colonized with the Δvariant mount increased IgG responses against staphylococcal colonization determinants. Immunization of mice with a non-toxigenic SpA variant, which cannot crosslink B cell receptors and divert antibody responses, elicits protein A-neutralizing antibodies that promote IgG responses against colonizingand diminish pathogen persistence.persistently colonizes the nasopharynx of about a third of the human population, thereby promoting community- and hospital-acquired infections. Antibiotics are currently used for decolonization of individuals at increased risk of infection. However, the efficacy of antibiotics is limited by recolonization and selection for drug-resistant strains. Here we propose a model whereby staphylococcal protein A (SpA), a B cell superantigen, modifies host immune responses during colonization to support continued persistence ofin the nasopharynx. We show that this mechanism can be thwarted by vaccine-induced anti-SpA antibodies that promote IgG responses against staphylococcal antigens and diminish colonization.

1683 related Products with: Staphylococcal protein A contributes to persistent colonization of mice with.

Anti C Reactive Protein A TOM1-like protein 2 antib Recombinant Human IFN-alp Recombinant Human IFN-alp Recombinant Staphylococca Recombinant Staphylococca Recombinant Staphylococca Rabbit Anti-Staphylococca MarkerGene™ Total Prote Rabbit Anti-Human Toll In Human Dnak (HSP70) His ta Toxoplasma gondii GRA8, r

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Dermaseptins as potential antirabies compounds.

Over the last 20 years, natural peptides playing a key role in defense mechanisms and innate immunity have been isolated from unicellular organisms. Amphibian skin secretes dermaseptins, 24-34 amino acids in length that have a wide antimicrobial spectrum incorporating yeast, fungi, protozoa, bacteria and enveloped viruses. The anti-rabies virus (RABV) activity of dermaseptins S3 (30aa) and S4 (28aa) from Phyllomedusa sauvagei has been investigated, and further dissected its molecular basis by comparing punctual mutation or deletion of S4 analogues. The results showed that: (1) S4 is more active than S3 against RABV infection, 89% versus 38% inhibition at 7.5 μM; (2) the 5 NH2-aa of S4 are crucial for its inhibitory potential (S4lost any inhibition) but the COOH terminus stabilizes the inhibitory potential (S4showed only 23% inhibition at 7.5 μM); (3) there is a correlation between viral inhibition and dermaseptin cytotoxicity, which remains however moderated for BSR cells (≤12% at 10 μM). A single mutation in position 4 (S4) slightly reduced cytotoxicity while keeping its antiviral activity, 97% at 7.5 μM. S4 and S4showed an antiviral activity in vitro when provided 1 h after infection. In vivo experiments in mice by intramuscular injection of non-toxic doses of dermaseptin S41 h post-infection by a lethal dose of RABV at the same site allowed more than 50% improvement in mice survival. This study highlights the potential interest of dermaseptins as non-expansive alternatives to rabies immunoglobulins for the treatment of rabies that continues to claim about 60,000 human lives per year worldwide, almost exclusively in developing countries.

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HAVCR1 (CD365) and its mouse ortholog are functional hepatitis A virus (HAV) cellular receptors that mediate HAV infection.

The Hepatitis A virus (HAV) cellular receptor 1 (HAVCR1), classified as CD365, was initially discovered as a HAV cellular receptor using an expression cloning strategy. Due to the lack of HAV receptor-negative replication-competent cells, it was not possible to fully prove that HAVCR1 was a functional HAV receptor. However, biochemistry, classical virology, and epidemiology studies further supported the functional role of HAVCR1 as a HAV receptor. Here, we show that an anti-HAVCR1 monoclonal antibody that protected African green monkey (AGMK) cells against HAV infection only partially protected monkey Vero E6 cells and human hepatoma Huh7 cells indicating that these two cell lines express alternative yet unidentified HAV receptors. Therefore, we focused our work on AGMK cells to further characterize the function of HAVCR1 as a HAV receptor. Advances in CRISPR/Cas9 technology allowed us to knock out HAVCR1 in AGMK cells. The resulting AGMK HAVCR1 KO cells lost susceptibility to HAV infection including HAV free viral particles (vpHAV) and exosomes purified from HAV-infected cells (exo-HAV). Transfection of HAVCR1 cDNA into AGMK HAVCR1 KO cells restored susceptibility to vpHAV and exo-HAV infection. Furthermore, transfection of the mouse ortholog of HAVCR1, mHavcr1, also restored the susceptibility of AGMK HAVCR1 KO cells to HAV infection. Taken together, our data clearly show that HAVCR1 and mHavcr1 are functional HAV receptors that mediate HAV infection. This work paves the way for the identification of alternative HAV receptors to gain a complete understanding of their interplay with HAVCR1 in the cell entry and pathogenic processes of HAV.HAVCR1, a HAV receptor, is expressed in different cell types including regulatory immune cells and antigen presenting cells. How HAV evades the immune response during a long incubation period of up to 4 weeks and the mechanism by which the subsequent necroinflammatory process clears the infection remain a puzzle that most likely involves the HAV-HAVCR1 interaction. Based on negative data, a recent paper from the Lemon and Maury laboratories (1) suggested that HAVCR1 is neither a functional HAV receptor nor required for HAV infection. However, our data based on regain of HAV-receptors function in HAVCR1 knockout cells transfected with the HAVCR1 cDNA disagree with their findings. Our positive data show conclusively that HAVCR1 is indeed a functional HAV receptor and lays the ground for the identification of alternative HAV receptors and how they interact with HAVCR1 in cell entry and pathogenesis of HAV.

1501 related Products with: HAVCR1 (CD365) and its mouse ortholog are functional hepatitis A virus (HAV) cellular receptors that mediate HAV infection.

Mouse Anti-Hepatitis A Vi Human anti hepatitis A vi Goat Anti-Hepatitis A Vir Hepatitis C Virus antibod Hepatitis B Virus antibod Hepatitis B Virus antibod Hepatitis C Virus antibod Hepatitis C Virus antibod Hepatitis C Virus antibod Hepatitis C Virus antibod Hepatitis C Virus antibod Hepatitis A Virus antibod

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