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           Search results for: Mouse Anti-Insulin(1D4:) Monoclonal Antibody, PE-Cy5.5 conjugated Isotype: IgG   

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Radiolabeling of the antibody IgG M75 for epitope of human carbonic anhydrase IX by Cu and Cu and its biological testing.

Human carbonic anhydrase IX is a membrane enzyme that is significantly expressed in some types of cancer cells, while copper radioisotopes offer wide range of diagnostic, therapeutic and theranostic properties. The work was focused on a new approach to the labelling of antibody IgG M75 for epitope human carbonic anhydrase IX with copper radioisotopes Cu and Cu and its in vivo testing in mice with inoculated colorectal cancer. Monoclonal antibody IgG M75 for epitope human carbonic anhydrase IX was successfully conjugated with copper-specific chelator "phosphinate" and labelled with Cu and Cu The obtained molecule has considerable potential as a radioimmuno pharmaceutical suitable for imaging of tumours expressing carbonic anhydrase IX by positron emission tomography (PET).

2220 related Products with: Radiolabeling of the antibody IgG M75 for epitope of human carbonic anhydrase IX by Cu and Cu and its biological testing.

Rabbit Anti-Cullin 5 CUL5 Analysis Tool for Custom Rabbit Anti-Cullin 5 CUL5 MOUSE ANTI HUMAN CD19 RPE Cullin-7 antibody Source Leptin ELISA Kit, Human A Carbonic anhydrase 9 anti Custom Human DR6 ELISA EL Androgen Receptor Ab-1 An Human Apolipoprotein AI E Custom Human FAP ELISA EL Mouse anti-human type II

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Human colorectal cancer antigen GA733-2-Fc fused to endoplasmic reticulum retention motif KDEL enhances its immunotherapeutic effects.

The aim of this is to compare the immunotherapeutic effects of human colorectal cancer antigen GA733-2 fused to the Fc fragment of antibody (GA733-2-Fc) and to Fc and endoplasmic reticulum (ER) retention motif KDEL (GA733-2-Fc-KDEL).

1223 related Products with: Human colorectal cancer antigen GA733-2-Fc fused to endoplasmic reticulum retention motif KDEL enhances its immunotherapeutic effects.

Human Vitronectin Total A Human Ovarian Cancer Anti Human Plasminogen Total A Human Antithrombin III to Human Dnak (HSP70) His ta stress-associated endopla Total Human uPA Antigen A Human Gastrointestinal Ca serologically defined col Human Breast Cancer Antig Human IgG (total) ELISA K Goat Anti-Human TEM8 Anth

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Immune suppression of food allergy by maternal IgG in murine models.

Most of the patients develop food allergy early in life. The factors related to parental immune condition might be one of the conceivable causes.

1240 related Products with: Immune suppression of food allergy by maternal IgG in murine models.

anti-Diazepam Binding Inh Mouse Anti Shigella boydi Mouse Anti P. aeruginosa Mouse Anti Salmonella typ Hamster AntiSerine Protea anti HCMV IE pp65 IgG1 (m Mouse AntiInfluenza A Tar Mouse Anti-Insulin-Like G anti-C1 inhibitor (4G12), Mouse AntiMRSA Target Ant HIV1 integrase antibody, DMPO, N1664A Host Mouse S

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Novel, Broadly Reactive Anticapsular Antibodies against Carbapenem-Resistant Klebsiella pneumoniae Protect from Infection.

Carbapenem-resistant (CR) sequence type 258 (ST258) has become an urgent health care threat, causing an increasing number of high-mortality infections. Its resistance to numerous antibiotics and threat to immunocompromised patients necessitate finding new therapies to combat these infections. Previous successes in the laboratory, as well as the conservation of capsular polysaccharide (CPS) among the members of the ST258 clone, suggest that monoclonal antibody (MAb) therapy targeting the outer polysaccharide capsule of could serve as a valuable treatment alternative for afflicted patients. Here, we isolated several IgG antibodies from mice inoculated with a mixture of CR CPS conjugated to anthrax protective antigen. Two of these MAbs, 17H12 and 8F12, bind whole and oligosaccharide epitopes of the CPS of clade 2 ST258 CR , which is responsible for the most virulent CR infections in the United States. These antibodies were shown to agglutinate all clade 2 strains and were also shown to promote extracellular processes killing these bacteria, including biofilm inhibition, complement deposition, and deployment of neutrophil extracellular traps. Additionally, they promoted opsonophagocytosis and intracellular killing of CR by human-derived neutrophils and cultured murine macrophages. Finally, when mice were intratracheally infected with preopsonized clade 2 CR , these MAbs reduced bacterial dissemination to organs. Our data suggest that broadly reactive anticapsular antibodies and vaccines against clade 2 ST258 CR are possible. Such MAbs and vaccines would benefit those susceptible populations at risk of infection with this group of multidrug-resistant bacteria. Carbapenem-resistant is an enteric bacterium that has been responsible for an increasing number of deadly outbreaks and hospital-acquired infections. The pathogen's resistance to numerous antibiotics, including new drugs, leaves few therapeutic options available for infected patients, who often are too sick to fight the infection themselves. Immunotherapy utilizing monoclonal antibodies has been successful in other medical fields, and antibodies targeting the outer polysaccharide capsule of these bacteria could be a valuable treatment alternative. This study presents two anticapsular antibodies, 17H12 and 8F12, that were found to be protective against the most virulent carbapenem-resistant clinical strains. These antibodies are shown to promote the killing of these strains through several extracellular and intracellular processes and prevent the spread of infection in mice from the lungs to distal organs. Thus, they could ultimately treat or protect patients infected or at risk of infection by this multidrug-resistant bacterium.

1872 related Products with: Novel, Broadly Reactive Anticapsular Antibodies against Carbapenem-Resistant Klebsiella pneumoniae Protect from Infection.

Chlamydia pneumoniae anti Anti C-Reactive Protein A Mouse Anti-C. pneumoniae Rabbit Anti-M. pneumoniae Rabbit Anti-M. pneumoniae Mouse Anti-K. pneumoniae Rabbit Anti-S. pneumoniae Mouse Anti-S. pneumoniae Guinea Pig Anti-S. pneumo Rabbit Anti-M. pneumoniae BACTERIOLOGY KLEBSIELLA P Rabbit Anti-Klebsiella sp

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Self-assembled particulate PsaA as vaccine against infection.

is a human pathogen responsible for the majority of childhood pneumonia and media otitis cases worldwide. The diversity of its capsular polysaccharides (CPS) results in more than 91 serotypes of which at least 23 are virulent. Various CPS conjugated to immunogenic carrier proteins are currently licensed and provide protection against the infection caused by the respective serotypes but not against new and emerging virulent serotypes. In this study, we considered the conserved protein antigen PsaA, the pneumococcal surface adhesin A, in order to overcome the limitations of CPS antigens. The PsaA was translationally fused to a polyhydroxybutyrate (PHB) synthase which mediated production of PsaA displayed on PHB inclusions in recombinant . This suggested that the PsaA fusion to the PHB synthase did not interfere with PHB synthase activity and its ability to mediate formation of nano-sized inclusions composed of a PHB core surrounded by the PHB synthase fused to PsaA. Isolated PHB beads showed a negative surface charge. Transmission electron microscopy analysis suggested that the PsaA fusion to the PHB synthase reduced the size of PHB beads from about 500 nm to 100 nm. The integrity and antigenicity of the fusion protein attached to isolated PHB beads was confirmed by SDS-PAGE, tryptic peptide fingerprinting analysis using MALDI-TOF-MS/MS and immunoblotting using a monoclonal anti-PsaA antibody. Mice immunized with PsaA displaying PHB beads produced high and specific IgG levels dominated by IgG1 isotype. While IgG1 titer were similar between soluble and insoluble PsaA, the IgG2 titers were strongly increased upon vaccination with insoluble PsaA i.e. PsaA displayed on PHB beads. Particulate PsaA-PHB beads elicited IgG antibodies recognizing PsaA in whole cell lysates of seven different serotypes of This study suggested that PHB beads are suitable carriers for PsaA in order to induce a significant and specific Th-2-type immune response.

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Cytosol/Particulate Separ Cytosol Particulate Separ Cytosol Particulate Separ Rabbit Anti-ASB12 Polyclo Mouse anti-porcine type I Caspase 8 Fluorometric As Caspase 5 Substrate WEHD Asenapine N-Oxide C17H16C Cell Meter™ Phosphatidy GST Colorimetric Activity Annexin V PE Apoptosis De Asparaginase Activity Ass

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Internalization of targeted quantum dots by brain capillary endothelial cells in vivo.

Receptors located on brain capillary endothelial cells forming the blood-brain barrier are the target of most brain drug delivery approaches. Yet, direct subcellular evidence of vectorized transport of nanoformulations into the brain is lacking. To resolve this question, quantum dots were conjugated to monoclonal antibodies (Ri7) targeting the murine transferrin receptor. Specific transferrin receptor-mediated endocytosis of Ri7-quantum dots was first confirmed in N2A and bEnd5 cells. After intravenous injection in mice, Ri7-quantum dots exhibited a fourfold higher volume of distribution in brain tissues, compared to controls. Immunofluorescence analysis showed that Ri7-quantum dots were sequestered throughout the cerebral vasculature 30 min, 1 h, and 4 h post injection, with a decline of signal intensity after 24 h. Transmission electron microscopic studies confirmed that Ri7-quantum dots were massively internalized by brain capillary endothelial cells, averaging 37 ± 4 Ri7-quantum dots/cell 1 h after injection. Most quantum dots within brain capillary endothelial cells were observed in small vesicles (58%), with a smaller proportion detected in tubular structures or in multivesicular bodies. Parenchymal penetration of Ri7-quantum dots was extremely low and comparable to control IgG. Our results show that systemically administered Ri7-quantum dots complexes undergo extensive endocytosis by brain capillary endothelial cells and open the door for novel therapeutic approaches based on brain endothelial cell drug delivery.

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GFP Expressing Human Brai Human Internal Mammary Ar Human Brain Microvascular Human Large Intestine Mic GFP Expressing Mouse Brai GFP Expressing Human Inte Human Small Intestine Mic MarkerGeneTM in vivo lacZ Mouse Brain Microvascular GFP Expressing Human Umbi Beta Amyloid (40) ELISA K Human Glomerular Microvas

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High treatment efficacy by dual targeting of Burkitt's lymphoma xenografted mice with a (177)Lu-based CD22-specific radioimmunoconjugate and rituximab.

Dual-targeted therapy has been shown to be a promising treatment option in recurrent and/or refractory B-cell non-Hodgkin's lymphoma (B-NHL). We generated radioimmunoconjugates (RICs) comprising either a novel humanized anti-CD22 monoclonal antibody, huRFB4, or rituximab, and the low-energy β-emitter (177)Lu. Both RICs were evaluated as single agents in a human Burkitt's lymphoma xenograft mouse model. To increase the therapeutic efficacy of the anti-CD22 RIC, combination therapy with unlabelled anti-CD20 rituximab was explored.

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Cytoskeleton Phospho-Spec MMP (Human) Antibody Arra Insulin Glucose Phospho-S p53 Signaling Phospho-Spe Apoptosis (Human) Antibod Cytokine (Mouse) Antibody Inflammation (Mouse) Anti Atherosclerosis (Mouse) A Cytokine (Human) Antibody AKT PKB Signaling Phospho Cytokine (Mouse) Antibody Inflammation (Human) Anti

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On-bead antibody-small molecule conjugation using high-capacity magnetic beads.

Antibodies labeled with small molecules such as fluorophore, biotin or drugs play an important role in various areas of biological research, drug discovery and diagnostics. However, the majority of current methods for labeling antibodies is solution-based and has several limitations including the need for purified antibodies at high concentrations and multiple buffer exchange steps. In this study, a method (on-bead conjugation) is described that addresses these limitations by combining antibody purification and conjugation in a single workflow. This method uses high capacity-magnetic Protein A or Protein G beads to capture antibodies directly from cell media followed by conjugation with small molecules and elution of conjugated antibodies from the beads. High-capacity magnetic antibody capture beads are key to this method and were developed by combining porous and hydrophilic cellulose beads with oriented immobilization of Protein A and Protein G using HaloTag technology. With a variety of fluorophores it is shown that the on-bead conjugation method is compatible with both thiol- and amine-based chemistry. This method enables simple and rapid processing of multiple samples in parallel with high-efficiency antibody recovery. It is further shown that recovered antibodies are functional and compatible with downstream applications.

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NanoLink™ 4FB Magnetic Protein A G L Magnetic Be MagnaLink™ Streptavidin Protein G Magnetic Beads NanoLink™ Streptavidin NanoLink™ Amino Magneti MagnaLink™ Amino Magnet Protein L Magnetic Beads NanoLink™ Streptavidin Protein A Magnetic Beads NanoLink™ Streptavidin MagnaLink™ 4FB Magnetic

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