Search results for: SHEEP ANTI ERYTHROSIN-POLYCLONAL ANTIBODY
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High seroprevalence of Rift Valley fever phlebovirus in domestic ruminants and African Buffaloes in Mozambique shows need for intensified surveillance.Introduction: Rift Valley fever (RVF) is an arthropod-borne disease that affects both animals and humans. RVF phlebovirus (RVFPV) is widespread in Africa and Arabian Peninsula. In Mozambique, outbreaks were reported in South; seroprevalence studies performed in livestock and water buffaloes were limited to central and south regions. We evaluated the seroprevalence of RVFPV among domestic ruminants and African buffaloes from 7 of 10 provinces of Mozambique, to understand the distribution of RVFPV and provide data for further RVF control programs. Materials and methods: A total of 1581 blood samples were collected in cattle, 1117 in goats, 85 in sheep and 69 in African buffaloes, between 2013 and 2014, and the obtained sera were analyzed by ELISA. Results and discussion: The overall seroprevalence of RVFPV domestic ruminants and African buffaloes was 25.6%. The highest was observed in cattle (37.3%) and African buffaloes (30.4%), which were higher than in previous studies within Mozambique. In south and central regions, the overall seroprevalences were higher (14.9%-62.4%) than in the north. Conclusion: This study showed the presence of anti-RVFPV antibodies in animals from all sampled provinces, suggesting that RVFPV is actively circulating among domestic ruminants and African buffaloes in Mozambique, therefore surveillance should be intensified.
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Full-house glomerular deposits: beware the sheep in wolf's clothing.The 2012 Systemic Lupus International Collaborating Clinics criteria propose the classification of systemic lupus erythematosus (SLE) by biopsy-confirmed lupus nephritis plus circulating antinuclear antibody or anti-double-stranded DNA antibody. Application of this stand-alone renal criterion to a cohort of patients with "full-house" glomerular deposits resulted in mistaken classification of SLE in some cases with antinuclear antibody. More precise biopsy criteria using a constellation of characteristic features are needed to optimize the kidney biopsy standard for lupus nephritis.
Recombinant Sheep Interfe Thermal Shaker with cooli Sheep interleukin 2 recep Sheep Anti-Human C1-Inact Sheep Anti-Human hCG (Int Sheep Anti-Human Indoleam Sheep Anti-Theophylline 3 FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu
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Effects of active immunization with newly modified GnRH peptides on spermatogenesis and production performance of Holstein bulls.Immunocastration via vaccination against gonadotropin-releasing hormone (GnRH) is an effective alternative to surgical castration in livestock. In this study, male mice were immunized with eight GnRH peptide derivatives. Two, which exhibited highly significant effects in mice, and one which exhibited the least significant effects were selected for active immunization of 13 month-old bulls. The effects of these GnRH vaccines on sexual development and meat quality in bulls were evaluated by examining testis length, serum hormone and GnRH antibody concentrations, observation of sexual behavior and testicular tissue sections, and evaluation of meat quality indexes. The results indicated that anti-GnRH titers increased rapidly (P < 0.05) and serum follicle stimulating hormone (FSH), luteinizing hormone (LH), and testosterone (T) concentrations decreased sharply after booster immunization (P < 0.05), while testis volumes were lower (P < 0.01), testicular growth was arrested and spermatogenesis inhibited in Group C GnRH-treated versus control bull groups. Meat quality was not significantly different in immunocastrates relative to bulls in the control group. Our collective results provide a scientific basis to further clarify the mechanisms underlying GnRH-mediated regulation of livestock reproduction, and contribute to the development of an efficient, safe and reversible immune castration vaccine.
2463 related Products with: Effects of active immunization with newly modified GnRH peptides on spermatogenesis and production performance of Holstein bulls.CAR,CAR,Constitutive acti Ofloxacin CAS Number [824 Bcl-2 Oncoprotein; Clone Bcl-2 Oncoprotein; Clone c-erbB-2 Oncoprotein c-erbB-2 Oncoprotein c-erbB-3 Oncoprotein; Cl c-erbB-3 Oncoprotein; Cl c-erbB-2 Oncoprotein; Cl c-erbB-2 Oncoprotein; Cl c-erbB-2 Oncoprotein; Cl c-erbB-2 Oncoprotein; Cl
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Humoral immune response against two surface antigens of Chlamydia pecorum in vaccinated and naturally infected sheep.Chlamydia pecorum is a globally recognised livestock pathogen due to the significant clinical and economic impact it poses to livestock producers. Routine serological diagnosis is through a complement fixation test (CFT), which is often criticised for cross-reactivity, poor sensitivity and specificity. Although serology remains the preferred method in veterinary diagnostic laboratories, serological assays based on surface antigens of C. pecorum have not been established until now. In this study, we evaluated the use of two chlamydial recombinant protein antigens (PmpG and MOMP-G) by a direct IgG ELISA method for detection of ovine anti-chlamydial antibodies. Using the Pepscan method we then identified B cell epitopes across PmpG and MOMP-G proteins, in lambs with (a) naturally occurring asymptomatic C. pecorum infections (b) C. pecorum-associated polyarthritis and (c) recombinant PmpG and MOMP-G vaccine. Plasma IgG antibodies to PmpG in natural infection of lambs were detected earlier in infection than CFT and served as an acute phase marker. Antibodies to MOMP-G IgG were significantly heightened in lambs with C. pecorum-associated polyarthritis. PmpG and MOMP-G specific B-cell epitope mapping revealed epitope responses in immunised lambs cluster with some of the epitope responses in naturally infected lambs. B-cell epitope mapping further revealed that lambs with polyarthritis recognised several unique PmpG (50% frequency, peptide 8, 25, 40, 41 and 50) and MOMP (50% frequency, peptide 50) epitopes in comparison to asymptomatic infections. The findings of this study will have implications towards improved serodiagnosis of C. pecorum infections in livestock and inform the downstream development of alternative peptide-based antigens for future C. pecorum vaccine studies.
1528 related Products with: Humoral immune response against two surface antigens of Chlamydia pecorum in vaccinated and naturally infected sheep.anti HSV (II) gB IgG1 (mo anti HCMV IE pp65 IgG1 (m anti HCMV gB IgG1 (monocl Rat TGF-beta-inducible ea Rat TGF-beta-inducible ea Recombinant Sheep Interfe Anti beta3 AR Human, Poly rHIV gp36, insoluble Anti rHIV gp36, soluble Antige rHIV gp41, soluble Antige Sheep interleukin 2 recep Mouse Anti-P. falciparum
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Expression and evaluation of recombinant P32 protein based ELISA for sero-diagnostic potential of capripox in sheep and goats.The study is aimed to develop and evaluate a recombinant P32 protein based ELISA for sero-monitoring and sero-surveillance using known and random/suspected serum samples for capripox infections from sheep and goats. Truncated P32 gene of goatpox virus (with an ORF of 750 bp) was expressed in E. coli BL-21 CodonPlus (DE3)-RIPL cells using pET32a vector and characterized by SDS-PAGE analysis and confirmed by western blotting as 48 kDa polyhistidine-tagged fusion protein. The protein was purified under denaturing conditions using 8M urea and characterized by SDS-PAGE and immunoblotting. The purified protein was used for optimizing ELISA in a chequerboard titration method using anti-GTPV serum as known positive. The optimized conditions were found to be 300 ng of protein/well, 1:10 dilution of antibody, 1:10000 dilution of rabbit anti-goat/sheep conjugate with 3% skim milk powder and 2% gelatin in phosphate buffer saline containing tween-20 as blocking buffer. The expressed protein was specific only for goatpox virus and sheeppox virus but did not react with related viruses of sheep and goats namely orf virus, peste de petits ruminants virus, bluetongue virus and foot and mouth disease virus. The optimized ELISA was evaluated using pre-vaccinated, post-vaccinated and also post-challenge sera. The assay was found to have a diagnostic specificity of 100/98.7% and sensitivity of 97.1/98.1% when compared to whole virus antigen based ELISA/SNT by receiver operating characteristic (ROC) analysis. The optimized ELISA is able to determine the progression of antibody response against GTPV and SPPV following vaccination and challenge in sheep and goats. The rP32 protein based ELISA was evaluated using random field serum samples (n = 1008) suspected for sheeppox and goatpox and it has shown positivity rate as 24.4%. The rP32 protein based ELISA was found to be specific and sensitive for sero-evaluation of sheeppox virus and goatpox virus following vaccination and infection in sheep and goats.
2789 related Products with: Expression and evaluation of recombinant P32 protein based ELISA for sero-diagnostic potential of capripox in sheep and goats.Recombinant Sheep Interfe Recombinant Human Androge Bone Morphogenetic Protei Recombinant Influenza HA Recombinant Influenza HA Recombinant Influenza HA Recombinant Sheep GH Prot Recombinant Sheep GH Prot Recombinant Sheep GH Prot Recombinant Sheep GH Anta Recombinant Sheep GH Anta Recombinant Sheep GH Anta
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Evaluation of UMELISA® T4 NEONATAL and UMELISA® T4 using polystyrene plates coated with anti-thyroxine (T4) monoclonal antibodies.Congenital hypothyroidism is one of the most common preventable causes of mental retardation. The Center of Immunoassay has developed the UMELISA® T4 NEONATAL and UMELISA® T4 to determine neonatal T4 levels in dried blood and serum samples. Both reagent kits use the same polystyrene plates coated with anti-thyroxine (T4) polyclonal antibodies as solid phase. This work shows the re-standardization of the UMELISA® T4 NEONATAL and UMELISA® T4 using plates coated with anti-T4 monoclonal antibodies (T4Mabs). Polystyrene plates of the modified assays were firstly coated with polyclonal IgG sheep-anti-mouse IgG for 18 hours. T4Mabs were added to the plates and incubated for 2 hours at room temperature. Different performance parameters were evaluated and correlation studies with the commercial kits done. Using polystyrene plates coated with T4Mabs increases the slope of the calibration curve in the clinical interest zone. The assay conjugates work twice diluted in respect to the ones of the commercial kits. Recovery percentages (90.8-110.7 for UMELISA® T4 NEONATAL and 92.1-109.3 for UMELISA® T4) and intra (7.2-7.6 for UMELISA® T4 NEONATAL and 6.9-7.2 for UMELISA® T4) and inter (7.4-8.5 for UMELISA® T4 NEONATAL and 7.1-8.5 for UMELISA® T4) coefficients of variation were similar to the ones described for the commercial kits. Limits of detection and quantification were 9.0 and 21.1 nmol/L for UMELISA® T4 NEONATAL, and 8.9 and 20.5 nmol/L for UMELISA® T4, respectively. The results also showed high overall concordance between assays (n = 244, r = 0.92, ρc = 0.91 for UMELISA® T4 NEONATAL and n = 492, r = 0.92, ρc = 0.9 for UMELISA® T4). The analytical sensibility of UMELISA® T4 NEONATAL and UMELISA® T4 is improved by using polystyrene plates coated with T4Mabs, without affecting the precision and accuracy of the results.
1530 related Products with: Evaluation of UMELISA® T4 NEONATAL and UMELISA® T4 using polystyrene plates coated with anti-thyroxine (T4) monoclonal antibodies.Rabbit Anti-Thyroxine (T4 Sheep Anti-Thyroxine (T4) Mouse Anti-Human Thyroxin Rabbit Anti-T4 L-Thyroxin Rabbit Anti-T4 L-Thyroxin Rabbit Anti-T4 L-Thyroxin Rabbit Anti-T4 L-Thyroxin Rabbit Anti-T4 L-Thyroxin Rabbit Anti-T4 L-Thyroxin Rabbit Anti-T4 L-Thyroxin Rabbit Anti-T4 L-Thyroxin Rabbit Anti-T4 L-Thyroxin
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Purification and biochemical characterization of a 22-kDa stable cysteine- like protease from the excretory-secretory product of the liver fluke Fasciola hepatica by using conventional techniques.This study describes the purification and characterization of a stable protease activity isolated from Fasciola hepatica adult worms maintained in vitro by employing acetone precipitation (40-60%) followed by a gel filtration through Sephadex G-100 and DEAE- cellulose ion exchange column. Through this three-step purification, the enzyme was purified 11-fold with a specific activity of 1893.9U/mg and 31.5% recovery. After the final ultrafiltration step, the purification fold was increased up to 13.1 and the overall activity yield reached a rate of 18.8%. The MW of the purified protease was estimated by reducing SDS-PAGE to be 22kDa while the proteolytic activity detection was carried out by zymography on non-denaturing SDS-PAGE containing the casein as substrate. Using this substrate, the protease showed extreme proteolytic activity at pH 5.5 and temperature 35-40°C and was highly stable over a wide range of pH, from 5.0 to 10.0. In addition to its preference for the Z-Phe-Arg-AMC fluorogenic substrate resulting in maximum proteolytic activity (99.7%) at pH 7.0, the pure protease exhibited highest cleavage activity against hemoglobin and casein substrates at pH 5.5 (85.6% and 82.8%, respectively). The Km values obtained for this protease were 5.4, 13, 160 and approximately 1000μM using respectively the fluorogenic substrate Z-Phe-Arg-AMC, hemoglobin, casein and albumin. The protease activity was completely inhibited either by E-64 inhibitor (5mM) or iodoacetamide (10mM), indicating its cysteine nature. The usefulness of the purified protease as an antigen was studied by immunoblotting. Thus, sera from sheep experimentally infected with F. hepatica recognized the protease band at 2 weeks post-infection (WPI) and strongly at 7 WPI. The early detection of antibodies anti- F. hepatica suggests the application of this molecule as a specific epitope for the serodiagnosis of fascioliasis disease.
1445 related Products with: Purification and biochemical characterization of a 22-kDa stable cysteine- like protease from the excretory-secretory product of the liver fluke Fasciola hepatica by using conventional techniques.HCV core recombinant anti HCV core recombinant anti HCV core recombinant anti HCV core recombinant anti HCV NS3 recombinant antig HBV surface recombinant a HBV surface recombinant a TCP-1 theta antibody Sour Bovine Serum Albumin (BSA Rabbit anti PKC theta (Ab Rabbit anti PKC theta (Ab Rabbit anti PKC theta (Ab
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Generation of High-Sensitivity Monoclonal Antibodies Specific for Homoserine Lactones.A number of bacteria use a class of chemical compounds called acyl-homoserine lactones (AHLs) as quorum sensing (QS) signals to coordinate their behavior at the population level, including pathogens like Pseudomonas aeruginosa. Blocking QS using antibodies is an attractive strategy for infection control as this process takes a central role in P. aeruginosa infections. Here the methods involved in the generation of high sensitivity anti-QS monoclonal antibodies from an immunized sheep phage display antibody library are described. A panel of AHL compounds conjugated to carrier proteins are used for sheep immunization and a phage display antibody library is constructed using the immune repertoire of sheep as a source of antibody genes. High sensitivity single chain antibody fragments (scFv) are isolated from the library using "smart selection strategies" and reformatted into single chain antibodies (scAbs). The resultant monoclonal antibodies: (1) recognize HSL compounds at low nanomolar concentrations; (2) have the potential to reduce virulence gene expression in P. aeruginosa; and (3) offer protection in a nematode model of infection.
2783 related Products with: Generation of High-Sensitivity Monoclonal Antibodies Specific for Homoserine Lactones.MOUSE ANTI BOVINE ROTAVIR MOUSE ANTI BORRELIA BURGD Rat monoclonal anti mouse Rat monoclonal anti mouse MOUSE ANTI CANINE DISTEMP MOUSE ANTI HUMAN CD15, Pr MOUSE ANTI HUMAN CD19 RPE MOUSE ANTI HUMAN CD15, Pr MOUSE ANTI APAAP COMPLEX, TMB Soluble Reagent (Hig TMB Soluble Reagent (Hig TMB Soluble Reagent (Hig
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Cytosolic Recognition of RNA Drives the Immune Response to Heterologous Erythrocytes.The archetypal T cell-dependent antigen is sheep red blood cells (SRBCs), which have defined much of what we know about humoral immunity. Early studies using solubilized or sonicated SRBCs argued that the intact structure of SRBCs was important for optimal antibody responses. However, the reason for the requirement of intact SRBCs for the response to polyvalent protein antigen remained unknown. Here, we report that the immune response to SRBCs is driven by cytosolic recognition of SRBC RNA through the RIG-I-like receptor (RLR)-mitochondrial anti-viral signaling adaptor (MAVS) pathway. Following the uptake of SRBCs by antigen-presenting cells, the MAVS signaling complex governs the differentiation of both T follicular cells and antibody-producing B cells. Importantly, the involvement of the RLR-MAVS pathway precedes that of endosomal Toll-like receptor pathways, yet both are required for optimal effect.
2739 related Products with: Cytosolic Recognition of RNA Drives the Immune Response to Heterologous Erythrocytes.FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu Human Ovary Total RNA AccuzolTM Total RNA Extra AccuzolTM Total RNA Extra Total RNA Extraction Kit Total RNA Human Adult Nor Total RNA - Human Tumor T Topoisomerase II; Clone Topoisomerase II; Clone
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Identification of B-cell linear epitopes in domains 1-3 of pyolysin of Trueperella pyogenes using polyclonal antibodies.Trueperella pyogenes is an important opportunistic pathogen. Pyolysin (PLO) makes important contributions to the pathogenicity of T. pyogenes. However, the structure and function of PLO has not been well documented. In the current study, epitopes in domain 1-3 of PLO have been mapped using rabbit anti-recombinant PLO (rPLO) polyclonal antibodies, and then the results were re-checked by using mouse and chicken anti-rPLO polyclonal antibodies, respectively. The results indicated that the region of aa 281-393 in PLO could not elicit antibodies against linear epitopes. A total of six B cell linear epitopes have been found in domain 1 of PLO. Two of the six epitopes (EP1 and EP2) were used to immunize mice and chicken. Chicken anti-EP1 and anti-EP2 serum and mouse anti-EP2 serum could react with rPLO and corresponding epitope polypeptide in western blot assay; however, only mouse anti-EP2 serum shows weak anti-hemolysis effect in the rPLO and sheep red blood system. Our results provide some new information to the research field of PLO structure and function.
1857 related Products with: Identification of B-cell linear epitopes in domains 1-3 of pyolysin of Trueperella pyogenes using polyclonal antibodies.Rabbit Anti-Cell death in Ofloxacin CAS Number [824 Cultrex96 Well 3D BME Cel Cell cycle antibody array Cell Cycle Control Phosph Cell Cycle Phospho-Specif T-Cell Receptor Signaling Cytokine (Mouse) Antibody Cytokine (Mouse) Antibody Cytokine (Rat) Antibody A Th1 Th2 Th17 (Human) Anti Chemokine (Human) Antibod
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