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           Search results for: Mouse Anti-beta-Amyloid(1-40) Polyclonal Antibody, FITC conjugated,Isotype: IgG   

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#27617027   2016/09/12 Save this To Up

Chi-Ju-Di-Huang-Wan protects rats against retinal ischemia by downregulating matrix metalloproteinase-9 and inhibiting p38 mitogen-activated protein kinase.

Retinal ischemia is a retinal disorder related to retinal vascular occlusion, glaucoma, diabetic retinopathy and age-related macular degeneration. The study aimed to evaluate the protective effects and underlying mechanisms of Chi-Ju-Di-Huang-Wan (CJDHW) against retinal ischemia in rats.

1537 related Products with: Chi-Ju-Di-Huang-Wan protects rats against retinal ischemia by downregulating matrix metalloproteinase-9 and inhibiting p38 mitogen-activated protein kinase.

Human Serine threonine-pr Human Matrix metalloprote Rat matrix metalloprotein ELISA Human , Matrix Meta ELISA Human , Cartilage O Anti-Serine Threonine-Pro anti-ATM Protein Kinase p Anti-ATM Protein Kinase p Anti-ATM Protein Kinase p Anti-ATM Protein Kinase p Anti-ATM Protein Kinase S Mouse Anti-Human Matrix M

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#15896799   2005/06/15 Save this To Up

Removal of therapeutic anti-lymphocyte antibodies from human sera prior to anti-human leukocyte antibody testing.

Both monoclonal (e.g. Orthoclone (OKT3), rituximab) and polyclonal (e.g. ATGAM, Thymoglobulin (Thymo)) anti-lymphocyte Abs (ALAs) are used extensively in organ transplantation for immunosuppression induction, desensitization, and treatment of acute rejection. ALAs often interfere with post transplant immunologic monitoring. We describe a method that uses magnetic beads to selectively remove ALAs from patient serum. Rabbit anti-mouse Fc-specific (180 mug), or rabbit anti-mouse Fab-specific (180 microg), or rabbit anti-horse heavy and light chain-specific and rabbit anti-horse F(ab')2 (200 microg) (Jackson Immunoresearch) was adsorbed to 6.7 x 10(8) Dynabeads M-280 conjugated with sheep anti-rabbit IgG (Dynal Biotech). Fifty microliters of normal human serum (NHS) with 2 microg/ml of OKT3 or 100 microg/ml ATGAM, Thymo, or rituximab were incubated with conjugated beads for several incubations. NHS containing ALAs before and after treatment by the protocol were incubated with human lymphocytes and labeled with FITC-antibody to immunoglobulin of the species used to produce the particular ALA. Residual ALA was determined using flow cytometry. Average median channel for serum with or without ALA was 11.1 and 0.120, respectively for OKT3; 64.4 and 0.344 for ATGAM; 108.5 and 0.200 for Thymo; and 1022.5 and 11.4 for rituximab. Treatment lowered the median channel for serum with OKT3 to 0.103, 0.309 for ATGAM, 0.199 for Thymo, and 12.1 for rituximab. ALAs can be effectively removed from serum by the use of magnetic beads conjugated with Ab specific for ALA thereby permitting immunologic monitoring without interference.

1900 related Products with: Removal of therapeutic anti-lymphocyte antibodies from human sera prior to anti-human leukocyte antibody testing.

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#15366659   2004/09/15 Save this To Up

Production of IgY anti-mouse IgG antibodies from chicken eggs.

IgY technology offers several advantages over antibody production in mammals. In this study, we applied IgY technology for the production of anti-mouse IgG polyclonal antibodies and developed a FITC conjugate reagent. Two hens were immunized 3 times with mouse IgG, one via the pectoralis and the other via the calf muscles. Specific antibodies could be detected in the sera two weeks after the immunization, and maximum levels were reached at week 10. The hen which was immunized via the pectoralis muscle produced a much higher antibody response than the hen immunized via the calf muscle. In egg yolk, specific antibodies appeared 2 weeks after the first immunization, reached a plateau after week 11 and remained high until week 20. IgY were extracted from egg yolk by sodium sulfate precipitation. Approximately 40 mg of IgY could be extracted from a single egg. The extracted IgY was labeled with FITC. The so-produced antibody-FITC conjugate reacted to all mouse IgG isotypes and could be used to determine leukocyte sub-populations in blood samples by flow cytometry.

2304 related Products with: Production of IgY anti-mouse IgG antibodies from chicken eggs.

Rabbit Anti-Chicken IgY ( Mouse anti Human IgA anti Mouse anti Human IgE anti Mouse anti Human IgE anti Mouse anti Human IgE anti Mouse anti Human IgE anti Mouse anti Canine IgE ant Mouse anti Canine IgE ant Mouse anti Canine IgE ant Mouse anti Canine IgE ant Mouse anti Human IgG anti Mouse anti Human IgG anti

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#15020090   2004/03/15 Save this To Up

Dual enhancement of triple immunofluorescence using two antibodies from the same species.

Triple immunofluorescence method with two mouse monoclonal antibodies and another rabbit polyclonal antibody was established with catalyzed reporter deposition (CARD) amplification on thick floating sections from the rat cerebellum. One of the monoclonal antibodies (anti-calbindin), diluted maximally, probed with anti-mouse IgG-horseradish peroxidase (HRP) and amplified with Cy5-conjugated tyramide, immunolabeled cerebellar Purkinje cells and their arborization. Subsequently, a rabbit polyclonal IgG (anti-glial fibrillary acidic protein (anti-GFAP)), probed with anti-rabbit IgG-HRP, amplified with biotin-tyramide and visualized with fluorescein-isothiocyanate (FITC)-streptavidin, immunolabeled Bergmann's glia. Another mouse monoclonal IgG (anti-SNAP25), probed with anti-mouse IgG-rhodamine without CARD amplification, selectively visualized synaptic sites, because the maximal dilution of the other monoclonal antibody (anti-calbindin) was below the detection threshold of this anti-mouse IgG-rhodamine. Separation of the two signals (calbindin and SNAP25), each detected through mouse monoclonal antibody, was then based on the difference of sensitivity either with or without CARD amplification. Triple immunofluorescence is possible when just one of the three primary antibodies is from different species. Intensification of two of the three signals provides further advantages to examine immunolocalization of multiple epitopes on histological sections.

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#11483208   2001/08/02 Save this To Up

Resolution of rabbit polyclonal anti-fluorescein Fab (IgG) fragments into subpopulations differing in affinity and spectral properties of bound ligand.

Fab fragments derived from ten different IgG populations of hyperimmune rabbit polyclonal anti-fluorescein antibodies were further resolved into subfractions based on differences in time-dependent dissociation from an FITC-adsorbent in the presence of 0.1 M fluorescein at 4 degrees C. Fab fragments separated into subpopulations based on specific dissociation times of 0.1 day, 1.0 day, 10 days and 100 days from the adsorbent. Finally, after the 100 days elution step incubation with 6.0 M guanidine-HCl was included to determine total protein concentration of specific anti-fluorescein Fab fragments. Yields of specifically eluted Fab fragments ranged from 12.7 to 84.1% of the total Fab population originally incubated with the adsorbent. All Fab polyclonal populations and subpopulations analyzed quenched the fluorescence of the bound ligand by 90% or greater. None of the plots of protein concentration versus percent yield of the total specific antibody obtained for each of the five resolved fractions constituting a specific polyclonal population conformed to Gaussian distributions. All resolved Fab subpopulations retained bound fluorescein ligand that exhibited significant bathochromic shifts in absorbancy. Based on the extent of the red-shift the antibodies segregated into one of two general spectral families showing either a peak shift to 505-507 nm or to 518-520 nm. The red-shift to 518-520 nm appeared unique to rabbit anti-fluorescein antibodies, since corresponding large shifts have not been observed with antibodies derived from other species (e.g. mouse, rat, chicken, etc.). K(d) values determined for the resolved fractions confirmed a continuous progression in affinity from the 0.1day through the 100 days elution. Preliminary isoelectric focusing analyses revealed progressive selection for relatively more homogeneous fractions, especially in the 100 days resolved fraction.

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#10605505   2000/01/13 Save this To Up

Immunological and parasitological studies of Cryptosporidium muris, Tyzzer (1907).

Oocysts of C. muris and the events of excystation using 0.5% sodium hypochlorite as excystation medium were described with light microscope. The response of the immunocompetent BALB/c mice against infection was studied using sera of orally infected mice at different periods postinoculation by indirect immunofluorescence antibody test using 1:150 FITC conjugated rabbit serum antimouse polyclonal IgG. From the patterns of IFAT, it was suggested that the dominant antigen in C. muris was restricted to the apical complex of the sporozoites. Such antigen may play a role in the invasion of the host cell. Future analysis of such receptor molecules might constitute prime candidates as immunogens for a vaccine, the efficiency of which might cause inhibition of parasite invasion.

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#9701944   1998/09/16 Save this To Up

Immunocytochemical methods to study the distribution of Orientia tsutsugamushi in Leptotrombidium (Acari: Trombiculidae) chiggers.

Immunocytochemical methods were developed and tested for their ability to detect the distribution of Orientia tsutsugamushi in paraffin sections of adult chiggers (Leptotrombidium imphalum Vercammen-Grandjean & Langston). Rickettsial antigen was detected by application of a simple direct or amplified immunocytochemistry procedure and an indirect immunofluorescent procedure. In the direct procedure alkaline phosphatase conjugation to the mouse polyclonal antibody to the Karp strain was followed by the HistoMark Red test system to detect rickettsial antigen. The amplification procedure used a similar method but used an unlabeled primary antibody followed by secondary biotinylated antimouse IgG, streptavidin-alkaline phosphatase, and the HistoMark Red test system. The immunofluorescent procedure included a biotinylated secondary antibody followed by addition of a streptavidin-FITC conjugate. Specific tissue tropisms in infected chiggers were observed in the salivary glands, nervous tissue, and ovaries of adult female mites in all procedures; however, nonspecific fluorescence of the chigger limited definitive identification of tissue tropisms with the indirect immunofluorescent procedure.

1161 related Products with: Immunocytochemical methods to study the distribution of Orientia tsutsugamushi in Leptotrombidium (Acari: Trombiculidae) chiggers.

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#8876053   1997/01/21 Save this To Up

Localization by indirect immunofluorescence of nitric oxide synthase in mouse and human spermatozoa.

The localization of nitric oxide synthase was studied in mouse epididymal spermatozoa and freshly ejaculated human sperm. A rabbit antiserum against the neuronal isoform of the enzyme was used, and antibody binding was detected with a fluorescein isothiocyanate-conjugated polyclonal antibody specific for rabbit IgG. In mouse spermatozoa, the percentage of cells staining specifically ranged from 88% to 98%. Samples were examined after 0-, 90- and 150-min incubations in vitro. Three different patterns of staining were observed: (a) Pattern I, intense fluorescent staining localized in the acrosome and in a segment of the tail; (b) Pattern II, fluorescent staining localized only in the tail; and (c) Pattern III, faint fluorescent staining localized in the acrosomal cap and in the tail. The potential physiological significance of these patterns is discussed. Nitric oxide synthase was also localized in the acrosome of freshly ejaculated human sperm.

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#7741191   1995/06/08 Save this To Up

Demonstration of specific high-affinity Fc epsilon-receptors on the human basophil-like leukemia cell line KU812 by flow cytometry.

The specificity of IgE binding to a human basophil-like cell line (KU812) was studied by flow cytometry. Four IgE myeloma proteins, representing both light-chain types, one chimeric IgE protein, and polyclonal serum IgE blocked the direct binding of FITC-labeled IgE(DES) myeloma protein to KU812 cells in a dose-dependent and nearly equimolar way. Although not as efficiently as human IgE (from five to eight times less on a molar basis), both rat and mouse IgE blocked IgE(DES)-FITC binding to KU812 cells. In sharp contrast, all four human IgG subclasses, both IgA subclasses, and IgM myeloma proteins, as well as monomeric and heat-aggregated polyclonal human IgG, were unable to block significantly IgE(DES)-FITC binding to KU812 cells (< 0.5% on a molar basis). The cytophilic epitope on IgE was heat-susceptible (56 degrees C, 2 h), lost after reduction alkylation, and resident in the papain-derived Fc epsilon-fragment, but not in the papain-derived Fab epsilon- and Fc'epsilon-fragments nor in the pepsin-derived F(ab')2 epsilon- and Fc"epsilon-fragments. Washing and displacement experiments indicated that a major part of IgE reacted with high affinity to KU812 cells. The results indicate that the binding of IgE to KU812 cells is highly specific and involves the classical high-affinity Fc epsilon RI-receptor. Although the density of receptors is low, this human cell line offers a unique model to study IgE/Fc epsilon RI interactions.

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#7864993   1995/01/13 Save this To Up

Malaria vaccine research.

In our report "Activation of Raf as a result of recruitment to the plasma membrane" (3 June, p. 1463) (1), panels E and F of figure 1 on page 1464 were incorrect. The correct photographs appear below. In addition, the [See figure in the PDF file] second sentence of the legend to figure 1 should have read, "The Raf constructs were tagged at the COOH-terminus with a Glu-Glu epitope (MEYMPME) (24) for c-Raf, or at the NH(2)-terminus with both the Glu-Glu and the Myc (MEQKLISEEDL) (23) epitopes for RafCAAX"; the next-to-the-last sentence of the legend to figure 1 should have read, "The c-Raf constructs in (A through D) are Glu-Glu-tagged and were detected by using an anti Glu-Glu antibody, and the RafCAAX and Raf6QCAAX constructs used in E and F were detected by using the antibody to Raf COOH-terminal peptide"; and the third sentence of note 26 should have read, "After blocking with 5% milk in phosphate-buffered saline (M-PBS), cells were incubated with a mouse monoclonal antibody to Glu-Glu or a rabbit polyclonal antibody to a 20-amino acid COOH-terminal peptide of Raf-1 (Santa Cruz Biotechnology, Santa Cruz, California), washed, and incubated with donkey antibodies to mouse or rabbit IgG combined with Texas Red (Jackson) in M-PBS, washed, and mounted in FITC-Guard (Testog)."

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