Search results for: Mouse Anti-beta-Amyloid 1-42(CT) Polyclonal Antibody, PE-Cy3 Conjugated
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ELISA units, IgG subclass ratio and avidity determined functional activity of mouse anti-Pfs230 antibodies judged by a standard membrane-feeding assay with Plasmodium falciparum.The standard membrane-feeding assay (SMFA) is a functional assay that has been used to inform the development of transmission-blocking vaccines (TBV) against Plasmodium falciparum malaria. For Pfs230, a lead target antigen for TBV development, a few studies have tested either a single anti-Pfs230 polyclonal or monoclonal antibody (one antibody per study) at serial dilutions and showed a dose-dependent response. Further, there have been reports that the SMFA activity of anti-Pfs230 polyclonal and monoclonal antibodies were enhanced in the presence of complement. However, no analysis has been performed with multiple samples, and the impact of anti-Pfs230 antibody titers, IgG subclass profile and avidity were evaluated together in relation to transmission-reducing activity (TRA) by SMFA. In this report, a total of 39 unique anti-Pfs230 IgGs from five different mouse immunization studies were assessed for their ELISA units (EU), IgG2/IgG1 ratio and avidity by ELISA, and the functionality (% transmission-reducing activity, %TRA) by SMFA. The mice were immunized with Pfs230 alone, Pfs230 conjugated to CRM, or a mixture of unconjugated Pfs230 and CRM proteins using Alhydrogel or Montanide ISA720 adjuvants. In all studies, the Pfs230 antigen was from the same source. There was a significant correlation between EU and %TRA (p < 0.0001 by a Spearman rank test) for the anti-Pfs230 IgGs. Notably, multiple linear regression analyses showed that both IgG2/IgG1 ratio and avidity significantly affected %TRA (p = 0.003 to p = 0.014, depending on the models) after adjusting for EU. The results suggest that in addition to antibody titers, IgG2/IgG1 ratio and avidity should each be evaluated to predict the biological activity of anti-Pfs230 antibodies for future vaccine development.
1774 related Products with: ELISA units, IgG subclass ratio and avidity determined functional activity of mouse anti-Pfs230 antibodies judged by a standard membrane-feeding assay with Plasmodium falciparum.Mouse Anti-Plasmodium fal 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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Carbohydrate Specificity and Isotypes of Monoclonal and Polyclonal Antibodies to Conjugated Tetrasaccharide, a Synthetic Analogue of Repeating Unit of Capsular Polysaccharide of Streptococcus Pneumoniae Serotype 14.We studied carbohydrate specificity and isotypes of antibodies to BSA-conjugated tetrasaccharide, a repeating unit of the capsular polysaccharide of Streptococcus pneumoniae serotype 14, in mouse polyclonal sera and hybridoma-synthesized products. Natural IgM antibodies to the tetrasaccharide containing epitopes similar to surface carbohydrate structures of mammalian and human cells in low titers were determined in native mouse serum by ELISA using biotinylated tetrasaccharide and synthetic capsular polysaccharide as the solid-phase antigens. Polyclonal sera to the conjugated tetrasaccharide contained IgM and all subclasses of IgG antibodies, which were detected in a higher titer when the biotinylated tetrasaccharide was used as a solid phase antigen compared to synthetic capsular polysaccharide. Monoclonal antibodies to S. pneumoniae serotype 14 tetrasaccharide were identified in an equivalent titer using either biotinylated tetrasaccharide or synthetic capsular polysaccharide. Monoclonal antibodies obtained in vitro belonged to IgM isotype and cross-reacted with secondary full-size IgG antibodies. In the serum of mice inoculated with hybridoma, IgM and IgG2a antibodies recognizing the tetrasaccharide epitope in the structure of synthetic capsular polysaccharide were simultaneously determined.
1258 related Products with: Carbohydrate Specificity and Isotypes of Monoclonal and Polyclonal Antibodies to Conjugated Tetrasaccharide, a Synthetic Analogue of Repeating Unit of Capsular Polysaccharide of Streptococcus Pneumoniae Serotype 14.MOUSE ANTI BOVINE ROTAVIR Shiga Toxin 1 antibody, M Shiga Toxin 2 antibody, M Cholera toxin antibody, M Chlamydia pneumoniae anti Clostridium botulinum D T Clostridum difficile toxi Clostridum difficile toxi Clostridum difficile toxi Clostridum difficile toxi Clostridum difficile toxi Clostridum difficile toxi
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PEGylated pUR4/FUD peptide inhibitor of fibronectin fibrillogenesis decreases fibrosis in murine Unilateral Ureteral Obstruction model of kidney disease.Fibronectin is a blood and extracellular matrix glycoprotein that plays important roles in wound healing and fibrosis since it controls the deposition of collagen and other extracellular matrix molecules and is a substrate for infiltrating lymphocytes. Using a high-affinity fibronectin-binding peptide (FUD/pUR4) that inhibits fibronectin deposition into extracellular matrix (ECM), we tested the ability of a PEGylated FUD/pUR4 (PEG-FUD) to inhibit fibrosis in the Unilateral Ureteral Obstruction (UUO) kidney disease model. Fibronectin fibrillogenesis assays, using human fibroblasts and human proximal tubular epithelial cultures, showed that PEG-FUD can inhibit fibronectin fibrillogenesis in vitro with an IC50 similar to unconjugated FUD, in the order of 20-35 nM. In contrast, a mutated FUD (mFUD) conjugated to PEG that lacked activity did not inhibit fibronectin assembly, even at 20 μM. The in vivo activity of PEG-FUD was tested in the murine UUO model by daily subcutaneous injection of 12.5 mg/kg for 7 days until harvest at day 10. Control treatments included saline, PEG, unconjugated FUD, and PEG-mFUD. Immunoblotting studies showed that fibronectin was enriched in the extracellular matrix fractions of extracted UUO kidneys, compared to contralateral untreated kidneys. In vivo, PEG-FUD significantly decreased fibronectin by ~70% in UUO kidneys as determined by both IHC and immunoblotting, respectively. In contrast, neither PEG-mFUD, PEG, nor saline had any significant effect. PEG-FUD also decreased collagens I and III and CD45-expressing cells (leukocytes) by ~60% and ~50%, as ascertained by picrosirius red staining and IHC, respectively. Immunoblotting studies also showed that the fibronectin remaining after PEG-FUD treatment was intact. Utilizing a custom-made polyclonal antibody generated against pUR4/FUD, intact PEG-FUD was detected by immunoblotting in both the ECM and lysate fractions of UUO kidneys. No adverse reaction or event was noted with any treatment. In summary, these studies suggest that PEG-FUD reached the kidneys without degradation, and decreased fibronectin incorporation into interstitial tissue. Decreased fibronectin was accompanied by a decrease in collagen and leukocyte infiltration. We propose that PEG-FUD, a specific inhibitor of fibronectin assembly, may be a candidate therapeutic for the treatment of fibrosis in kidney diseases.
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Hapten-mediated recruitment of polyclonal antibodies to tumors engenders antitumor immunity.Uptake of tumor antigens by tumor-infiltrating dendritic cells is limiting step in the induction of tumor immunity, which can be mediated through Fc receptor (FcR) triggering by antibody-coated tumor cells. Here we describe an approach to potentiate tumor immunity whereby hapten-specific polyclonal antibodies are recruited to tumors by coating tumor cells with the hapten. Vaccination of mice against dinitrophenol (DNP) followed by systemic administration of DNP targeted to tumors by conjugation to a VEGF or osteopontin aptamer elicits potent FcR dependent, T cell mediated, antitumor immunity. Recruitment of αGal-specific antibodies, the most abundant naturally occurring antibodies in human serum, inhibits tumor growth in mice treated with a VEGF aptamer-αGal hapten conjugate, and recruits antibodies from human serum to human tumor biopsies of distinct origin. Thus, treatment with αGal hapten conjugated to broad-spectrum tumor targeting ligands could enhance the susceptibility of a broad range of tumors to immune elimination.
1538 related Products with: Hapten-mediated recruitment of polyclonal antibodies to tumors engenders antitumor immunity.Anti VGLUT-1 Rat, polyclo 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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Rapid and Sensitive Detection of Campylobacter jejuni in Poultry Products Using a Nanoparticle-Based Piezoelectric Immunosensor Integrated with Magnetic Immunoseparation.Campylobacter jejuni is one of the leading causes of foodborne human gastrointestinal diseases. Poultry and poultry products have been identified as the major transmission routes to humans for this pathogenic bacterium. The objective of this research was to develop a rapid and sensitive immunosensor for detection of C. jejuni in poultry products on the basis of a quartz crystal microbalance (QCM) using magnetic nanobeads (MNBs) for separation of target pathogen and gold nanoparticles for amplification of the measurement. A QCM sensor in a flow cell was prepared by immobilizing the mouse anti- C. jejuni monoclonal antibody (mAb) on the sensor surface to specifically capture C. jejuni. Rabbit anti- C. jejuni polyclonal antibody (pAb) was conjugated with MNBs to capture and separate C. jejuni from food matrices. MNB-pAb- C. jejuni complexes were injected into the flow cell to bind with the mAb immobilized on the QCM sensor surface. Goat anti-rabbit immunoglobulin G polyclonal antibody conjugated with gold nanoparticles was injected into the flow cell to bind with pAb on MNBs. Finally, resonant frequency was measured with a QCM analyzer, and the change in resonant frequency was correlated to the cell number of C. jejuni. The specificity of this immunosensor was confirmed with different strains of Campylobacter, Salmonella, and other foodborne pathogens commonly colonized in the broiler gastrointestinal tract. Samples of broiler carcass wash and ground turkey were spiked with C. jejuni at different concentrations for use in tests. Results showed that the QCM immunosensor could rapidly detect C. jejuni in poultry products, with a detection limit of 20 to 30 CFU/mL without preenrichment, and a total detection time of less than 30 min. Characteristics of C. jejuni captured by the antibody immobilized on the surface of the QCM sensor were visualized by using atomic force microscopy. This highly adaptive and flexible method could provide the poultry industry a more rapid, sensitive, and effective method for detection of major foodborne pathogens in poultry products.
2186 related Products with: Rapid and Sensitive Detection of Campylobacter jejuni in Poultry Products Using a Nanoparticle-Based Piezoelectric Immunosensor Integrated with Magnetic Immunoseparation.MarkerGeneTM in vivo lacZ Campylobacter jejuni anti Beta Amyloid (1 42) High Anti 3 DG imidazolone Mon Mouse Anti-Campylobacter EnzyChrom™ NAD NADH Ass EnzyChrom™ Kinase Assay Resorufin Oleate, Fluorog MarkerGeneTM Fluorescent Goat Anti-Campylobacter j Syringe pump can be contr Interleukin-34 IL34 (N-t
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Cyclic OmpC peptidic epitope conjugated to tetanus toxoid as a potential vaccine candidate against shigellosis.In earlier works we have described that mice immunized with outer membrane protein OmpC survive the challenge with live Shigella flexnerii 3a. We have also identified conformational epitope of this protein, that was recognized by mice antibodies. The aim of current work was to investigate whether synthetic OmpC epitope homologs can elicit immunological response sufficient in protecting mice against shigellosis. Several linear peptides containing RYDERY motif were synthesized and conjugated to poly-lysine. These conjugates appeared to be poor immunogens and to boost the immunological response an addition of the adjuvant (MPL) was required. Unfortunately, the MPL alone caused a very high immunological reaction that was masking response to peptidic epitope. Under those circumstances we used tetanus toxoid (TT) as the carrier protein for the peptides and the agent stimulating immunological response. Series of cyclic peptides, homologs of the OmpC main epitope were synthesized and conjugated to TT. The loop size in cyclic peptides varied by number of glycine residues, i.e., 1-3 residues added to the GLNRYDERYIGK motif. The linear GLNRYDERYIGC-TT was also prepared as the control. The latter conjugate gave the highest immunological response, followed by the cyclic-GGLNRYDERYIGC-TT and cyclic-GLNRYDERYIGC-TT. The third peptide, cyclic-GGGLNRYDERYIGC-TT, gave a very low response, although it was the most resistant to proteolysis. However, antibodies obtained against cyclic-GGLNRYDERYIGC-TT were more potent to recognize both OmpC and Shigella flexnerii 3a cells than the antibodies against linear GLNRYDERYIGC-TT. Furthermore, the monoclonal antibodies raised against linear GLNRYDERYIGC-TT showed 20-fold lower dissociation constant (KD) than the naturally occurring polyclonal antibodies from umbilical cord sera. Monoclonal antibodies also gave a weaker signal in electron microscope than mice and human polyclonal antibodies. In overall, our results point to cyclic peptides as better candidates for a vaccine development, since they are eliciting production of the higher affinity antibodies against Shigella cells and OmpC.
1796 related Products with: Cyclic OmpC peptidic epitope conjugated to tetanus toxoid as a potential vaccine candidate against shigellosis.Rat Anti Tetanus Toxoid I Goat Anti-Clostridium tet Clostridium botulinum D T Cell Meter™ JC 10 Mitoc Cell Meter™ JC 10 Mitoc Cell Meter™ NIR Mitocho Cell Meter™ NIR Mitocho Cell Meter™ Mitochondri Cell Meter™ Fluorimetri Cell Meter™ Fluorimetri Screen Quest™ Membrane Screen Quest™ Membrane
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Development of a Colloidal Gold-Based Immunochromatographic Assay for the Rapid Detection of .Edwardsiella Ictaluri is known as the etiological agent of enteric septicaemia of channel catfish, causing heavy economic losses in the aquaculture industry. In this study, a colloidal gold-based immunochromatography assay (GICA) was developed for rapid detection of E. ictaluri. Briefly, monoclonal antibody (MAbs) and polyclonal antibody (PAbs) against E. ictaluri were prepared. Sensitivity of MAbs and PAbs to E. ictaluri was analyzed by Dot ELISA. Mouse MAb5D11 against E. ictaluri was conjugated with the 20 nm colloidal gold particles as the detector. Rabbit PAbs of E. ictaluri and goat anti-mouse IgG antibody was sprayed on nitrocellulose membranes as test line (T) and control line (C) respectively. The minimum detectable amount of this method to E. ictaluri was 5 × 106 CFU/mL. Cross reactions wouldn't occur when detecting E. tarda, Aeromonas hydrophila, V. parahaemolyticus and other several common standard strains. The result could be got in only 5 to 10 minutes. It didn't need professional technologies and testing experience. So this assay was very suitable for basic departments of aquatic product companies.
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Generation and Characterization of Siglec-F-Specific Monoclonal Antibodies.Siglec-F (SF) is a surface glycoprotein expressed by mouse eosinophils and induces caspase- and mitochondria-dependent apoptosis after engagement with its cognate ligand or specific antibodies. This targeting eosinophils by monoclonal antibodies may help diverse diseases associated with increased frequency of eosinophils including allergy and asthma. In this paper, production of murine and rat monoclonal antibodies (mAbs) against Siglec-F has been addressed. Balb/c mice were immunized with siglec-F1 (SF1) and siglec-F2 (SF2) synthetic peptides conjugated to a carrier protein. Rats were immunized with Chinese hamster ovary CHO cells overexpressing Siglec-F (CHO-SF) or with Siglec-F-human immunoglobulin FC fusion protein (CHO-SF-Ig). Hybridomas were produced by standard protocol and screened for their reactivity by enzyme-linked immunosorbent assay (ELISA), western blotting (WB), and flow cytometry. In parallel, polyclonal antibodies were generated in New Zealand White rabbits immunized with SF1 and SF2 peptides. Three mouse and three rat mAbs were generated against synthetic peptides and SF-Ig, respectively. All mouse monoclonal and rabbit polyclonal antibodies reacted well with immunizing molecules in ELISA and detected specific band of Siglec-F in WB. However, they failed to detect native molecule in flow cytometry analysis. Quite the contrary, rat mAbs did not reacted with the denatured protein in WB, instead exhibited significant reactivity with CHO-SF cells in flow cytometry. Based on the heavily glycosylated nature of Siglec-F, it seems that generation of anti-SF antibodies able to detect native protein needs a properly folded molecule for immunization. Monoclonal antibodies reported here are invaluable tools for studying linear and conformation epitopes of SF and tracing mouse eosinophils.
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Field-usable lateral flow immunoassay for the rapid detection of a macluravirus, large cardamom chirke virus.A simple and rapid lateral flow immunoassay (LFIA) was developed by utilizing gold nanoparticles conjugated to a polyclonal antibody against coat protein of large cardamom chirke virus (LCCV). The LFIA based on the principle of sandwich immunoassay detected LCCV within ∼10 min and the result could be evaluated visually. The colloidal gold (CG) was made using 1% gold chloride solution. The LCCV IgG (1 μg/μl) and Mouse IgG (0.5 μg/μl) were conjugated with CG individually and coated onto a conjugate pad at 1:1 ratio. A sample extraction procedure was optimized in order to get adequate clear leaf sap of large cardamom leaf within few minutes. The sensitivity limit of the detection was 1:40 dilution of LCCV infected leaf sap. The diagnostic performance of LFIA was compared with ELISA using field samples. The LFIA was free from false positive as no visible test line was developed with healthy and potyviruses such as papaya ringspot virus and potato virus Y. The diagnostic specificity and sensitivity of LFIA was 100% and 90%, respectively. The Cohen's kappa coefficient (0.701) suggested a very good agreement between the ELISA and LFIA. Receiver operating characteristic analysis indicated that LFIA was a robust method as the area under the curve (0.950) is significantly (P <0.0001) broader.
2052 related Products with: Field-usable lateral flow immunoassay for the rapid detection of a macluravirus, large cardamom chirke virus.LATERAL FLOW ASSAY EZ PAN MarkerGeneTM Fluorescent MOUSE ANTI CANINE DISTEMP Rapid Microplate Assay K Recombinant Viral Antige Tick born encephalitis vi Rubella virus E1 mosaic r Rubella virus E2 recombin Rubella virus capsid (C) West Nile Virus Envelope West Nile Virus Pre M rec MOUSE ANTI BOVINE ROTAVIR
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Less is More: A Comparison of Antibody-Gold Nanoparticle Conjugates of Different Ratios.This comprehensive study is related to gold nanoparticles (GNPs) conjugated with antibodies. The goal of the study is to determine the minimal concentration of antibodies for conjugate synthesis when the conjugates have high antigen-capturing activity. Two systems were studied: gold nanoparticles conjugated with monoclonal antibodies (mAb-GNP) specific to Helicobacter pylori and gold nanoparticles conjugated with polyclonal antibodies (pAb-GNP) specific to mouse immunoglobulins. Several conjugates were synthesized with different GNP-to-antibody molar ratios (from 1:1 to 1:245) through nondirectional and noncovalent immobilization on a surface of GNPs with a diameter of 25.3 ± 4.6 nm. The maximal antigen-capturing activities and equilibrium constants of the conjugates correlate with the formation of a constant hydrodynamic radius of the conjugates for mAb-GNP (GNP to antibody molar ratio 1:58) and with the stabilizing concentration by flocculation curves for pAb-GNP (GNP to antibody molar ratio 1:116). The application of the conjugates to the lateral flow immunoassay shows that the antibody concentrations used for the conjugation can be reduced (below the stabilizing concentration) without losing activity for the mAb-GNP conjugates. The findings highlight that the optimal concentration of antibodies immobilized on the surface of GNPs is not always equal to the stabilizing concentration determined by the flocculation curve.
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