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           Search results for: Rat Anti-IAA Monoclonal Antibody, PE-Cy5.5 conjugated Isotype: IgG   

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#26661181   2016/04/01 Save this To Up

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.

2625 related Products with: Internalization of targeted quantum dots by brain capillary endothelial cells in vivo.

Human Brain Microvascular GFP Expressing Human Brai Human Small Intestine Mic Human Large Intestine Mic Human Internal Mammary Ar GFP Expressing Human Inte Mouse Brain Microvascular GFP Expressing Mouse Brai MarkerGeneTM in vivo lacZ anti HSV (II) gB IgG1 (mo anti HCMV IE pp65 IgG1 (m anti HCMV gB IgG1 (monocl

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#26316179   2015/11/17 Save this To Up

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.

1172 related Products with: On-bead antibody-small molecule conjugation using high-capacity magnetic beads.

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

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#25118216   2014/09/10 Save this To Up

Development of an anti-claudin-3 and -4 bispecific monoclonal antibody for cancer diagnosis and therapy.

Most malignant tumors are derived from epithelium, and claudin (CLDN)-3 and CLDN-4 are frequently overexpressed in such tumors. Although antibodies have potential in cancer diagnostics and therapy, development of antibodies against CLDNs has been difficult because the extracellular domains of CLDNs are too small and there is high homology among human, rat, and mouse sequences. Here, we created a monoclonal antibody that recognizes human CLDN-3 and CLDN-4 by immunizing rats with a plasmid vector encoding human CLDN-4. A hybridoma clone that produced a rat monoclonal antibody recognizing both CLDN-3 and -4 (clone 5A5) was obtained from a hybridoma screen by using CLDN-3- and -4-expressing cells; 5A5 did not bind to CLDN-1-, -2-, -5-, -6-, -7-, or -9-expressing cells. Fluorescence-conjugated 5A5 injected into xenograft mice bearing human cancer MKN74 or LoVo cells could visualize the tumor cells. The human-rat chimeric IgG1 monoclonal antibody (xi5A5) activated FcγRIIIa in the presence of CLDN-3- or -4-expressing cells, indicating that xi5A5 may exert antibody-dependent cellular cytotoxicity. Administration of xi5A5 attenuated tumor growth in xenograft mice bearing MKN74 or LoVo cells. These results suggest that 5A5 shows promise in the development of a diagnostic and therapeutic antibody for cancers.

1626 related Products with: Development of an anti-claudin-3 and -4 bispecific monoclonal antibody for cancer diagnosis and therapy.

Anti C Reactive Protein A MOUSE ANTI BOVINE ROTAVIR MONOBODIES (Monoclonal An MONOBODIES (Monoclonal An MONOBODIES (Monoclonal An MOUSE ANTI BORRELIA BURGD Anti CEL Monoclonal Antib Anti CEL Monoclonal Antib Anti CEL Monoclonal Antib Anti trimethyl Histone H3 Anti trimethyl Histone H3 Anti trimethyl Histone H3

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#23377501   2013/02/19 Save this To Up

An ultrasensitive electrochemical immunosensor platform with double signal amplification for indole-3-acetic acid determinations in plant seeds.

A label-free electrochemical immunosensor for ultra-sensitive detection of indole-3-acetic acid (IAA), a very important phytohormone, has been developed in this work. The detection strategy was mainly based on 4-aminophenylboronic acid, magnetic nanoparticles functionalized with horseradish peroxidase-conjugated goat anti-rat immunoglobulin G (HRP-IgG-Fe(3)O(4)) and rat monoclonal antibody against IAA-modified gold nanoparticles (anti-IAA-AuNPs). HRP-IgG-AuNPs was covalently assembled on the electrode surface through the specific chemical reaction between boronic acid and the vicinal diol in HRP-IgG. Then, anti-IAA-AuNPs was further assembled on the electrode via the interaction between IgG and antibody. Through the dual amplification of HRP-IgG-Fe(3)O(4) and anti-IAA-AuNPs, the trapping capacity of the immunosensor for IAA was significantly enhanced based on the promotion of the immunoreaction between antibody and antigen, which resulted in a large decrease of the electrochemical response of the redox probe, Fe(CN)(6)(3-), and an increase in sensitivity. The developed electrochemical immunosensor exhibited a wide linear range from 0.02 to 500 ng mL(-1) with a low detection limit of 0.018 ng mL(-1) (S/N = 3). Moreover, the proposed immunosensor showed acceptable selectivity, reproducibility, accuracy and stability. The IAA extracted from various seeds was successfully detected using the developed immunosensor. This assay method might provide an alternative strategy for the detection of various phytohormones.

1056 related Products with: An ultrasensitive electrochemical immunosensor platform with double signal amplification for indole-3-acetic acid determinations in plant seeds.

Rabbit Anti-IAA (Indole-3 Rabbit Anti-IAA (Indole-3 Rabbit Anti-IAA (Indole-3 Rabbit Anti-IAA (Indole-3 Rabbit Anti-IAA (Indole-3 Rabbit Anti-IAA (Indole-3 Rabbit Anti-IAA (Indole-3 Rabbit Anti-IAA (Indole-3 Rabbit Anti-IAA (Indole-3 Rabbit Anti-IAA (Indole-3 Rabbit Anti-IAA (Indole-3 Rabbit Anti-IAA (Indole-3

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#20429814   2011/05/19 Save this To Up

Targeting of ICAM-1-directed immunoliposomes specifically to activated endothelial cells with low cellular uptake: use of an optimized procedure for the coupling of low concentrations of antibody to liposomes.

Targeted delivery of therapeutics to the endothelium is an important goal in the treatment of inflammatory diseases. The aim of this work was to exploit the overexpression of intercellular adhesion molecule-1 (ICAM-1) on activated endothelial cells for the targeting of anti-ICAM-1-coupled immunoliposomes with the intent for further use as drug carriers. Immunoliposomes were prepared from using an optimized method for the coupling of low concentrations of antibody to liposomes, thereby preventing the loss of antibody through the derivatization, extraction, and activation process. This is especially suitable for limiting ligand conjugates that are isolated or synthesized in small quantities, such as monoclonal antibodies (mAbs). To investigate the functionality of the resulting immunoliposomes, the specificity of binding and cellular internalization studies of liposomes, either nonconjugated or conjugated with mAbs to ICAM-1 or to irrelevant IgG to high endothelial venule (HEV) cells, were analyzed by fluorescence microplate spectroscopy at 4 and 37°C. Immunoliposomes specifically directed against ICAM-1 were shown to bind selectively and specifically to tumor necrosis factor alpha-activated endothelial cells in vitro, with minimal cellular internalization. This study provides a novel delivery system that has the potential for targeting therapeutics to inflammatory tissue.

2520 related Products with: Targeting of ICAM-1-directed immunoliposomes specifically to activated endothelial cells with low cellular uptake: use of an optimized procedure for the coupling of low concentrations of antibody to liposomes.

FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu Shiga Toxin 1 antibody, M Shiga Toxin 2 antibody, M Cholera toxin antibody, M Clostridium botulinum D T Clostridum difficile toxi Clostridum difficile toxi Clostridum difficile toxi Clostridum difficile toxi

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#16423412   2006/03/06 Save this To Up

Co-clustering activating and inhibitory receptors: impact at varying expression levels of the latter.

Clustering the mast cell function-associated antigen (MAFA) has earlier been shown to inhibit mast cells' secretory response to the type 1 Fcepsilon receptor (FcepsilonRI) stimulus. MAFA is a type II membrane glycoprotein first identified on rat mast cells and contains an immunoreceptor tyrosine-based inhibitory motif (ITIM) in its cytosolic domain. This inhibition is induced already upon clustering MAFA alone. Still, the inhibitory capacity of MAFA-FcepsilonRI co-clustering has recently been characterized and co-clustered MAFA molecules were found to exhibit a markedly higher inhibition capacity than MAFA-clusters alone. We have now compared the inhibitory capacity of FcepsilonRI co-clustered MAFA on the secretory response of rat mucosal-type mast cells (RBL-2H3 line) expressing different levels of this inhibitory protein. Reacting these cells carrying an IgE class, 2,4 dinitrophenyl (DNP)-specific monoclonal antibody with DNP-conjugated F(ab')2 fragments of non-specific polyclonal mouse IgG causes clustering of the FcepsilonRI-IgE. Reaction of these cells with DNP-conjugated F(ab')2 fragments of the MAFA-specific, monoclonal antibody G63 co-aggregates MAFA together with the FcepsilonRI-IgE thereby producing FcepsilonRI-IgE-MAFA co-clusters. Results of measurements of the secretory responses of RBL-2H3 cells expressing higher or lower MAFA levels than those of unmodified cells provided further support to the notion that co-clustered MAFA molecules exhibit a markedly higher inhibition capacity than MAFA-clusters alone. The molecular basis for this enhanced inhibition is most probably the increased concentration of the inhibitory cell components in the immediate proximity of the co-clustered FcepsilonRI-MAFA.

1850 related Products with: Co-clustering activating and inhibitory receptors: impact at varying expression levels of the latter.

Activating Transcription Activating Transcription Activating Transcription Activating Transcription ATF3 Expression Media Products Expression Media Products Expression Media Products BACTERIOLOGY BACTEROIDES DNA (cytosine 5) methyltr Human Migration Inhibitor Human Beta-cell Attractin

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#16199376   2005/10/03 Save this To Up

Targeting of daunomycin using biotinylated immunoliposomes: pharmacokinetics, tissue distribution and in vitro pharmacological effects.

Biotinylated immunoliposomes were prepared by a non-covalent (biotin-streptavidin) coupling procedure and conjugated to the OX26 monoclonal antibody directed against the rat transferrin receptor. In vitro, these biotinylated immunoliposomes were used to by-pass P-glycoprotein in multidrug-resistant RBE4 brain capillary endothelial cells and thereby to achieve 2- to 3-fold higher intracellular accumulation of liposomal daunomycin as compared to free drug. The extent of cellular uptake of liposomal daunomycin was dose- and time-dependent, was inhibited by competition with unbound OX26 and was associated with a pharmacological (i.e. cytotoxic) effect. Cytotoxic effects of liposomal formulations of daunomycin, in contrast to the free drug, were apparent only after prolonged incubation periods being indicative of a slow intracellular unpacking and release of liposomal daunomycin. Pharmacokinetics and tissue distribution studies in the rat revealed brain accumulation of daunomycin in OX26-immunoliposomes to higher levels as compared to brain uptake of free daunomycin, or daunomycin incorporated within pegylated liposomes or within unspecific IgG(2a) isotype control immunoliposomes. Such OX26-mediated effects were not observed in other tissues such as spleen, liver, muscle or kidney.

1519 related Products with: Targeting of daunomycin using biotinylated immunoliposomes: pharmacokinetics, tissue distribution and in vitro pharmacological effects.

Mouse Anti-Human Interleu Mouse Anti-Human Interleu Alkaline Phospatase (ALP) Incu Tissue(square vessel Incu Tissue(square vessel Incu Tissue(square vessel Cultrex In Vitro Angiogen Human integrin aVb3, affi T-2 Toxin Mycotoxins ELIS Zearalenone Mycotoxins EL Multi organ carcinoma tis Multi organ carcinoma tis

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#15063802   2004/04/05 Save this To Up

Establishment and validation of an immunoenzymatic assay to determine mouse IgG levels based on a rat monoclonal antibody.

In this paper we describe an immunoenzymatic assay based on a rat monoclonal antibody (Ram kappa) developed to determine mouse IgG concentration, which is widely used for samples obtained on purification processes, like supernatant waste and the content of IgG in the vaccine (rHBsAg). This assay involves the use of a rat antibody-horseradish peroxidase-conjugated for the revealing of the antigen-antibody reaction. The rat antibody was produced in cell culture using a dialysis tube (DT). The immunoassay was standardized following several concepts, such as specificity, precision, and linearity. The result obtained permitted us to replace the use of polyclonal antibodies to determine the kappa light chain mouse antibodies by a rat monoclonal antibody of high sensibility and reproducibility. The assay permitted a reliable measurement of murine kappa Ig up to 0.68 ng/ml and was capable of quantifying 6.25 ng/ml. Due to the high frequency of the kappa light chain in mouse antibodies this system acquires a great application.

1540 related Products with: Establishment and validation of an immunoenzymatic assay to determine mouse IgG levels based on a rat monoclonal antibody.

Shiga Toxin 1 antibody, M Shiga Toxin 2 antibody, M Cholera toxin antibody, M Clostridium botulinum D T Clostridum difficile toxi Clostridum difficile toxi Clostridum difficile toxi Clostridum difficile toxi Clostridum difficile toxi Clostridum difficile toxi Clostridum difficile toxi Diphtheria toxin antibody

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#11123432   2001/01/26 Save this To Up

Effective cancer targeting using an anti-tumor tissue vascular endothelium-specific monoclonal antibody (TES-23).

Immunoconjugate targeting of solid tumors has not been routinely successful because the endo-thelial cells of blood vessels act as a physical barrier against the transport of macromolecules, such as antibodies. In the present study, we attempted to achieve tumor vascular targeting with an anti-tumor tissue endothelium-specific monoclonal antibody (TES-23). TES-23, an IgG1 monoclonal antibody raised against rat KMT-17 fibrosarcoma-derived endothelial cells, was covalently conjugated with neocarzinostatin (NCS) in a previous study. The TES-23-NCS conjugate induced tumor hemorrhagic necrosis, and showed marked anti-tumor effects against rat KMT-17 fibrosarcoma. This result prompted us to investigate whether this approach would be applicable to various other types of solid tumors. One hour after injection of (125)I-labeled TES-23 into BALB / c mice bearing Meth-A fibrosarcoma and Colon 26 adenocarcinoma, the tumor accumulation of TES-23 was greater than that of the control IgG. In the present study, we report the anti-tumor effects of this monoclonal antibody in mice bearing Meth-A fibrosarcoma. Mice treated with the immunoconjugate showed improved survival with no side effects. This result indicates that common antigens may be found in different kinds of tumor endothelial cells, and that TES-23 might recognize these antigens.

1008 related Products with: Effective cancer targeting using an anti-tumor tissue vascular endothelium-specific monoclonal antibody (TES-23).

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#10649788   2000/02/15 Save this To Up

Mab-ZAP: a tool for evaluating antibody efficacy for use in an immunotoxin.

Immunotoxins, consisting of antibodies coupled to toxins, are extremely useful tools in the elimination of specific cell populations in vitro and in vivo for research and therapeutic applications. The antibody is used to target the toxin to a specific cell population, which is distinguished by its cell-surface antigen. Not all antibodies are suitable for creating an immunotoxin, and large numbers of antibodies may need to be screened. This is a time-consuming and expensive process if each potential candidate must be conjugated to the toxin and purified. A faster and more economical way to identify potential targeting antibodies is to use a second immunotoxin, an anti-IgG antibody that is coupled to the toxin. The second immunotoxin eliminates the need to couple every candidate antibody to the toxin because it can simply be added to cells in culture with the antibody of interest. Using this method, many antibodies can be screened quickly and efficiently for their ability to internalize.

2040 related Products with: Mab-ZAP: a tool for evaluating antibody efficacy for use in an immunotoxin.

MOUSE ANTI BOVINE ROTAVIR MOUSE ANTI BORRELIA BURGD succinate-CoA ligase, GDP formin-like 1 antibody So succinate-CoA ligase, ADP Primary antibody Caspase Primary antibody FLIP An RABBIT ANTI GSK3 BETA (pS MOUSE ANTI CANINE DISTEMP MOUSE ANTI HUMAN CD15, Pr Analysis Tool for AAH-INF Analysis Tool for AAH-INF

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