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           Search results for: Rabbit Anti-beta-Amyloid(1-42) Polyclonal Antibody, PE-Cy3 Conjugated   

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#28948470   2017/09/26 Save this To Up

A synthetic peptide derived from domain III envelope glycoprotein of Dengue virus induces neutralizing antibody.

Dengue virus (DENV) is an arthropod-borne human pathogen that represents a severe public health threat in both endemic and non-endemic regions. So far, there is no licensed vaccine or specific drugs available for dengue fever. A fifteen-amino-acid-long peptide that includes the NGR motif was chemically synthesized and conjugated with keyhole limpet hemocyanin. A standard immunization protocol was followed for the production of polyclonal antibodies by immunizing rabbits against the synthetic peptide. The immune response elicited high-titer polyclonal antibodies with the reactivity of the anti-peptide antibody against both synthetic peptide and four serotypes of DENV confirmed by DOT-ELISA. Neutralizing activity of anti-peptide antibody was found to be cross-reactive and effective resulting in 60% reduction of infectivity at 1:200 dilution in all four serotypes of DENV. Our findings have the potential to further improve our understanding of virus-host interactions and provide new insights into neutralizing antibodies and could also be used as a drug target.

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HIV type O envelope antig HIV 2 gp36 envelope antig fibronectin type III and to M-Calpain (E.C. 3.4.2 Anti-Dengue Virus Antibod Herpes Simplex Virus 1 (H EZH2 KMT6 Control Peptid GFP control peptide anti West Nile Virus Envelope Monoclonal antibody Anti Measles Virus Nucleoprote Measles Virus nucleoprote

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#28727765   2017/07/20 Save this To Up

Defining the target and the effect of imatinib on the filarial c-Abl homologue.

Previously we demonstrated the micro- and macrofilaricidal properties of imatinib in vitro. Here we use electron and multiphoton microscopy to define the target of imatinib in the adult and microfilarial stages of Brugia malayi and assess the effects of pharmacologically relevant levels of imatinib on the adult parasites.

1371 related Products with: Defining the target and the effect of imatinib on the filarial c-Abl homologue.

BACTERIOLOGY BACTEROIDES TCP-1 theta antibody Sour Recombinant Thermostable Recombinant Thermostable Recombinant Thermostable Recombinant Human PKC the Recombinant Human PKC the Recombinant Human PKC the Single Strand DNA Ligase, Single Strand DNA Ligase, Thermostable TDG Enzyme & Thermostable TDG Kit

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#28724261   2017/07/20 Save this To Up

Development of a sandwich enzyme-linked immunosorbent assay for dTMP-GH fusion protein by rational immunogen selection.

dTMP-GH is a chimeric protein containing a tandem dimer of thrombopoietin mimetic peptide (dTMP) fused to human growth hormone (hGH) prepared previously by our team. It shows significant bioactivity in promoting thrombocytopoiesis, but detection of intact dTMP-GH in plasma is still a challenge due to the presence of endogenous hGH. In this study, a rabbit polyclonal antibody with high affinity to dTMP was obtained with a BSA-conjugated immunogen composed of 20 amino acids sequence spanning two TMP and the linker. A monoclonal antibody termed as 3B2 was screened out by using immunizing mice with whole dTMP-GH, which was proved to simultaneously interact with rhGH, TMP-GH, and dTMP-GH, respectively. In this study, we developed a specific and sensitive sandwich enzyme-linked immunosorbent assay (ELISA) with two antibodies (one polyclonal and one HRP-conjugated monoclonal) to quantify dTMP-GH. The polyclonal antibody and HRP-conjugated monoclonal antibody 3B2 were applied as the capture antibody and detection antibody, respectively. A good correlation between ELISA and bicinchoninic acid (BCA) assay in the quantification of diluted dTMP-GH was observed (r(2) = 0.996). Meanwhile, the standard curve of this ELISA method was found in a linear relationship between 0.2 and 10 ng/mL in the presence of rabbit plasma. In vivo experiments demonstrate that the newly developed method is effective to detect dTMP-GH in rabbits, which paves the way for further pharmacokinetic evaluation.

1354 related Products with: Development of a sandwich enzyme-linked immunosorbent assay for dTMP-GH fusion protein by rational immunogen selection.

Mouse Anti-RSV Fusion Pro Bone Morphogenetic Protei anti FAS IgG1 (monoclonal Recombinant Human c-jun A Recombinant Human c-jun A Recombinant Human c-jun A Recombinant Chicken GH An Recombinant Chicken GH An Recombinant Chicken GH An Recombinant Sheep GH Anta Recombinant Sheep GH Anta Recombinant Sheep GH Anta

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#28679076   2017/07/05 Save this To Up

Development of a tree shrew-specific interferon-gamma assay.

Tree shrews (Tupaia belangeri) are small squirrel-like mammals closely related to primates. Due to their susceptibility to several human viruses, tree shrews have been proposed as potential animal models for the study of human viral infections. However, there are no standardized assays currently available for the detection of tree shrew-specific interferon (IFN)-γ, a major cytokine secreted during the antiviral immune response. Herein, we developed a novel enzyme-linked immunosorbent assay (ELISA) for the quantification of IFN-γ in tree shrew serum samples. Tree shrew-specific IFN-γ was expressed in Escherichia coli via fusion with glutathione S-transferase (GST-TS-IFN-γ) to obtain recombinant IFN-γ. To generate anti-IFN-γ monoclonal antibodies, mice were immunized with the GST-TS-IFN-γ recombinant fusion protein, and hybridoma cell lines were established. Similarly, anti-IFN-γ polyclonal antibodies were obtained from immunized rabbits, purified, and conjugated to horseradish peroxidase (HRP). Based on the results obtained from the antibody matching test, we optimized the monoclonal antibody (1:2000) and the HRP-conjugated polyclonal antibody (1:8000) as coating and detection antibodies, respectively. Titration curves were generated with recombinant IFN-γ to develop a sensitive sandwich ELISA; the lowest detection limit of the assay was 20 ng/ml. We also tested mitogen-stimulated tree shrew blood samples in this ELISA, and found significantly higher levels of IFN-γ in the stimulated versus the unstimulated samples. Most importantly, our ELISA system detected native IFN-γ in serum samples from 50 healthy tree shrews. We have thus developed a novel ELISA, and have demonstrated the first ELISA-based measurement of IFN-γ in tree shrew serum samples.

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Custom Immunoassay Develo Rat anti mouse Interferon Mouse Anti-Insulin-Like G Gamma Glutamyl Transferas Rat monoclonal anti mouse Hamster anti mouse Interf Peptoid Ligand Assay Deve Interferon-γ | Interfer Rapid Microplate Assay K Actin, Muscle Specific; Actin, Muscle Specific; PSA (Prostate Specific A

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#28335696   2017/03/24 Save this To Up

Development and initial evaluation of a lateral flow dipstick test for antigen detection of Entamoeba histolytica in stool sample.

Entamoeba histolytica infection remains a public health concern in developing countries. Early diagnosis of amoebiasis can avoid disease complications, thus this study was aimed at developing a test that can rapidly detect the parasite antigens in stool samples. Rabbits were individually immunized with recombinant pyruvate phosphate dikinase (rPPDK) and E. histolytica excretory-secretory antigens to produce polyclonal antibodies. A rapid dipstick test was produced using anti-rPPDK PAb lined on the dipstick as capture reagent and anti-EhESA PAb conjugated to colloidal gold as the detector reagent. Using E. histolytica-spiked in stool sample of a healthy individual, the detection limit of the dipstick test was found to be 1000 cells ml(-1). Meanwhile when rPPDK was spiked in the stool sample, the minimum concentration detected by the dipstick test was 0.1 μg ml(-1). The performances of the dipstick, commercial Techlab E. histolytica II enzyme-linked immunosorbent assays (ELISA) and real-time PCR were compared using 70 stool samples from patients infected with Entamoeba species (n = 45) and other intestinal pathogens (n = 25). When compared to real-time PCR, the diagnostic sensitivity of the dipstick for detection of E. histolytica was 65.4% (n = 17/26); while the diagnostic specificity when tested with stool samples containing other intestinal pathogens was 92% (23/25). In contrast, Techlab E. histolytica II ELISA detected 19.2% (5/26) of the E. histolytica-positive samples as compared to real-time PCR. The lateral flow dipstick test produced in this study enabled rapid detection of E. histolytica, thus it showed good potential to be further developed into a diagnostic tool for intestinal amoebiasis.

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H. Pylori antigen test ca Malaria pan antigen test, Malaria pf antigen test, Malaria pf pv antigen tes Beta Amyloid (40) ELISA K Beta Amyloid (1 42) ELISA Glucose Assay With the La LATERAL FLOW ASSAY EZ PAN Mouse Anti-Insulin-Like G HIV 1 intergase antigen. DNA (cytosine 5) methyltr anti H inh human blood an

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#27981588   2016/12/16 Save this To Up

A highly specific competitive direct enzyme immunoassay for sterigmatocystin as a tool for rapid immunochemotaxonomic differentiation of mycotoxigenic Aspergillus species.

A simplified method to produce specific polyclonal rabbit antibodies against sterigmatocystin (STC) was established, using a STC-glycolic acid-ether derivative (STC-GE) conjugated to keyhole limpet haemocyanin (immunogen). The competitive direct enzyme immunoassay (EIA) established for STC had a detection limit (20% binding inhibition) of 130 pg ml(-1) . The test was highly specific for STC, with minor cross-reactivity with O-methylsterigmatocystin (OMSTC, 0·87%) and negligible reactivity with aflatoxins (<0·02%). STC-EIA was used in combination with a previously developed specific EIA for aflatoxins (<0·1% cross-reactivity with STC and OMSTC), to study the STC/aflatoxin production profiles of reference strains of Aspergillus species. This immunochemotaxonomic procedure was found to be a convenient tool to identify STC- or aflatoxin-producing strains.

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MOUSE ANTI BOVINE ROTAVIR MOUSE ANTI BORRELIA BURGD NATIVE HUMAN PROLACTIN, P RABBIT ANTI GSK3 BETA (pS 10x ELISA WASH BUFFER, Pr 10X PHOSPHATE BUFFERED SA PERMANENT AQUEOUS MOUNTIN MOUSE ANTI CANINE DISTEMP MOUSE ANTI HUMAN CD15, Pr NATIVE HUMAN PROLACTIN, P MOUSE ANTI HUMAN CD19 RPE MOUSE ANTI HUMAN CD15, Pr

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#27940044   2016/12/12 Save this To Up

Immunochromatographic detection of the heat-labile enterotoxin of enterotoxigenic Escherichia coli with cross-detection of cholera toxin.

Here, we report the development of an immunochromatographic test strip that can detect heat-labile enterotoxin (LT) produced by enterotoxigenic Escherichia coli. Five types of monoclonal antibody (mAb)-producing hybridomas were isolated: three mAbs were A subunit specific and two were B subunit specific. Four mAbs also cross-reacted with both LT proteins derived from swine and human E. coli strains, but only one mAb 57B9 additionally cross-reacted with cholera toxin. Thus, mAb 57B9 was used to form a gold colloid-conjugated antibody for the immunochromatographic test by combination with polyclonal anti-LT rabbit IgG. This test strip detected not only LT in the culture supernatant of LT gene-positive strains, but also cholera toxin in the culture supernatant of Vibrio cholerae. These results indicate that this test strip is suitable for the diagnosis of both enterotoxigenic E. coli and V. cholerae infection.

1184 related Products with: Immunochromatographic detection of the heat-labile enterotoxin of enterotoxigenic Escherichia coli with cross-detection of cholera toxin.

Mouse Anti-E. coli heat-l Mouse Anti-E. coli heat-l Mouse Anti-E. coli Labile Mouse Anti-E. coli Labile MarkerGene™ FDG Bacteri Ofloxacin CAS Number [824 Syringe pump can be contr Casein ELISA Kit Milk ca Detection Buffer A&B Anti Detection Buffer C&D Anti ESCHERICHIA COLI clinical ESCHERICHIA COLI 0111 NM

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#27626291   2016/09/29 Save this To Up

Synthesis and Characterization of Site-Selective Orbitide-BSA Conjugate to Produce Antibodies.

Bioactive flax cyclic peptides (orbitides and linusorbs) were site-specifically ligated through methionine with bovine serum albumin (BSA) to produce immunogenic compounds. In this study, modified flaxseed immunosuppressant orbitides (linusorbs or LOs) containing hydroxyl (OH) groups were synthesized for use as haptens. These compounds were extensively characterized by (1)H nuclear magnetic resonance (NMR), (13)C NMR, high-performance liquid chromatography-tandem mass spectrometry, and Fourier transform infrared spectroscopy. The haptens were conjugated to BSA, and the extent of hapten incorporation was determined by matrix-assisted laser desorption and ionization, liquid chromatography-electrospray ionization-mass spectrometry, and sodium dodecyl sulfate polyacrylamide gel electrophoresis. The BSA hapten complexes were used to elicit polyclonal antibody (pAbs) production in rabbits. A competitive indirect enzyme-linked immunosorbent assay (CI-ELISA) was developed that used orbitide-specific pAbs and horseradish peroxidase (HRP) conjugates. The LO assay detection limit was approximately 0.01 μg/mL (ppm), and thus, ELISA can be used for the detection of LOs in tissue and plant samples. The pAbs can be used to detect and quantify LOs in flax and flaxseed samples, to verify the presence of LOs in flaxseed containing foods, and for the detection of LOs in tissue samples, wastes, and body fluids of animals fed flaxseed.

2602 related Products with: Synthesis and Characterization of Site-Selective Orbitide-BSA Conjugate to Produce Antibodies.

Viral antibodies, anti-R 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

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#27494306   2016/09/16 Save this To Up

Facile Preparation of Stable Antibody-Gold Conjugates and Application to Affinity-Capture Self-Interaction Nanoparticle Spectroscopy.

Protein-nanoparticle conjugates are widely used for conventional applications such as immunohistochemistry and biomolecular detection as well as emerging applications such as therapeutics and advanced materials. Nevertheless, it remains challenging to reproducibly prepare stable protein-nanoparticle conjugates with highly similar optical properties. Here we report an improved physisorption method for reproducibly preparing stable antibody-gold conjugates at acidic pH using polyclonal antibodies from a wide range of species (human, goat, rabbit, mouse, and rat). We find that gold particles synthesized using citrate alone or in combination with tannic acid are similar in size but display variable colloidal stability when conjugated to polyclonal antibodies. The variability in conjugate stability is due to differences in the pH and composition of the original gold colloid, which prevents reproducible preparation of stable antibody conjugates without additional purification of the particles prior to conjugation. Sedimentation-based purification of gold particles synthesized using different methods enabled reproducible generation of antibody-gold conjugates with high stability and similar plasmon wavelengths. We also find that antibody conjugates prepared using our improved procedure display excellent performance when applied to a high-throughput immunogold assay (affinity-capture self-interaction nanoparticle spectroscopy, AC-SINS) for identifying monoclonal antibodies with low self-association, high solubility, and low viscosity. The stable antibody conjugates prepared with various types of gold colloid result in robust and reproducible AC-SINS measurements of antibody self-association using extremely dilute (microgram per mL) and unpurified antibody solutions. We expect that this improved methodology will be useful for reproducibly preparing stable antibody-gold conjugates for diverse applications.

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TOM1-like protein 2 antib TOK-1 alpha antibody Sour TOM1L1 antibody Source Ra PRDX1 Antibody Peptide-af Rabbit Anti-CLCA4 Polyclo Rabbit Anti-GPR78 Polyclo MOUSE ANTI BOVINE ROTAVIR Anti AGO2 Human, Monoclon Anti AGO2 Mouse, Monoclon Anti AGO2 Human, Monoclon Anti AGO2 Mouse, Monoclon Shiga Toxin 1 antibody, M

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#27721695   2016/10/10 Save this To Up

Production of Polyclonal Antibody against Grapevine fanleaf virus Movement Protein Expressed in Escherichia coli.

The genomic region of Grapevine fanleaf virus (GFLV) encoding the movement protein (MP) was cloned into pET21a and transformed into Escherichia coli strain BL21 (DE3) to express the protein. Induction was made with a wide range of isopropyl-β-D-thiogalactopyranoside (IPTG) concentrations (1, 1.5, and 2 mM) each for duration of 4, 6, or 16 h. However, the highest expression level was achieved with 1 mM IPTG for 4 h. Identity of the expressed protein was confirmed by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) followed by Western blotting. The expressed 41 kDa protein was purified under denaturing condition by affinity chromatography, reconfirmed by Western blotting and plate-trapped antigen enzyme-linked immunosorbent assay (PTA-ELISA) before being used as a recombinant antigen to raise polyclonal antibodies in rabbits. Purified anti-GFLV MP immunoglobulines (IgGs) and conjugated IgGs detected the expressed MP and GFLV virions in infected grapevines when used in PTA-ELISA, double antibody sandwich-ELISA, and Western blotting. This is the first report on the production of anti-GFLV MP polyclonal antibodies and application for the virus detection.

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Rabbit Anti-APIP Apaf1 In Rabbit Anti-APIP Apaf1 In Rabbit Anti-APIP Apaf1 In Rabbit Anti-APIP Apaf1 In Rabbit Anti-APIP Apaf1 In Rabbit Anti-APIP Apaf1 In Rabbit Anti-APIP Apaf1 In Rabbit Anti-APIP Apaf1 In Rabbit Anti-APIP Apaf1 In Rabbit Anti-APIP Apaf1 In Rabbit Anti-APIP Apaf1 In Rabbit Anti-APIP Apaf1 In

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