Search results for: MOUSE ANTI BOVINE ALBUMIN-MONOCLONAL ANTIBODY
#28965804 2017/10/02 Save this To Up
Neutralization of placental growth factor as a novel treatment option in diabetic retinopathy.The current standard of care in clinical practice for diabetic retinopathy (DR), anti-vascular endothelial growth factor (VEGF) therapy, has shown a significant improvement in visual acuity. However, treatment response can be variable and might be associated with potential side effects. This study was designed to investigate inhibition of placental growth factor (PlGF) as a possible alternative therapy for DR. The effect of the anti-PlGF antibody (PL5D11D4) was preclinically evaluated in various animal models by investigating different DR hallmarks, including inflammation, neurodegeneration, vascular leakage and fibrosis. The in vivo efficacy was tested in diabetic streptozotocin (STZ) and Akimba models and in the laser induced choroidal neovascularization (CNV) mouse model. Intravitreal (IVT) administration of the anti-PlGF antibody was compared to anti-VEGFR-2 antibody (DC101), anti-VEGF antibody (B20), VEGF-Trap (aflibercept) and triamcinolone acetonide (TAAC). Vascular leakage was investigated in the mouse STZ model by fluorescein isothiocyanate labeled bovine serum albumin (FITC-BSA) perfusion and in the Akimba model by fluorescein angiography (FA). Repeated IVT administration of the anti-PlGF antibody reduced vascular leakage, which was comparable to a single administration of VEGFR-2 inhibition in the mouse STZ model. PL5D11D4 treatment did not alter retinal ganglion cell (RGC) density, as demonstrated by Brn3a staining, whereas DC101 significantly reduced RGC number with 20%. Immunohistological stainings were performed to investigate inflammation (CD45, F4/80) and fibrosis (collagen type 1a). In the CNV model, IVT injection(s) of PL5D11D4 dose-dependently reduced inflammation and fibrosis, as compared to PBS treatment. Equimolar single administration of the anti-PlGF antibody and aflibercept (21 nM) and TAAC decreased leukocyte and macrophage infiltration with 50%, whereas DC101 and B20 (21 nM) had no effect on the inflammatory response. Similar results were observed in the mouse STZ model on the number of microglia and macrophages in the retina. Repeated administration of PL5D11D4 (21 nM) and TAAC similarly reduced fibrosis, while no effect was observed after equimolar DC101, B20 nor aflibercept administration (21 nM). In summary, the anti-PlGF antibody showed comparable efficacy as well-characterized VEGF-inhibitor on the process of vascular leakage, but differentiates itself by also reducing inflammation and fibrosis, without triggering a neurodegenerative response.
1329 related Products with: Neutralization of placental growth factor as a novel treatment option in diabetic retinopathy.Mouse Anti-Insulin-Like G IGF-1R Signaling Phospho- Growth Factor (Human) Ant Goat Anti-Human Fibroblas Rat monoclonal anti mouse Rat monoclonal anti mouse Rat monoclonal anti mouse Rat monoclonal anti mouse Rat monoclonal anti mouse Hamster anti mouse Insuli Epidermal Growth Factor ( Epidermal Growth Factor (
#28813459 2017/08/16 Save this To Up
β2-microglobulin gene duplication in cetartiodactyla remains intact only in pigs and possibly confers selective advantage to the species.Several β2-microglobulin (B2M) -bound protein complexes undertake key roles in various immune system pathways, including the neonatal Fc receptor (FcRn), cluster of differentiation 1 (CD1) protein, non-classical major histocompatibility complex (MHC), and well-known MHC class I molecules. Therefore, the duplication of B2M may lead to an increase in the biological competence of organisms to the environment. Based on the pig genome assembly SSC10.2, a segmental duplication of ~45.5 kb, encoding the entire B2M protein, was identified in pig chromosome 1. Through experimental validation, we confirmed the functional duplication of the B2M gene with a completely identical coding sequence between two copies in pigs. Considering the importance of B2M in the immune system, we performed the phylogenetic analysis of B2M duplication in ten mammalian species, confirming the presence of B2M duplication in cetartioldactyls, like cattle, sheep, goats, pigs and whales, but non-cetartiodactyl species, like mice, cats, dogs, horses, and humans. The density of long interspersed nuclear element (LINE) at the edges of duplicated blocks (39 to 66%) was found to be 2 to 3-fold higher than the average (20.12%) of the pig genome, suggesting its role in the duplication event. The B2M mRNA expression level in pigs was 12.71 and 7.57 times (2-ΔΔCt values) higher than humans and mice, respectively. However, we were unable to experimentally demonstrate the difference in the level of B2M protein because species specific anti-B2M antibodies are not available. We reported, for the first time, the functional duplication of the B2M gene in animals. The identification of partially remaining duplicated B2M sequences in the genomes of only cetartiodactyls indicates that the event was lineage specific. B2M duplication could be beneficial to the immune system of pigs by increasing the availability of MHC class I light chain protein, B2M, to complex with the proteins encoded by the relatively large number of MHC class I heavy chain genes in pigs. Further studies are necessary to address the biological meaning of increased expression of B2M.
1943 related Products with: β2-microglobulin gene duplication in cetartiodactyla remains intact only in pigs and possibly confers selective advantage to the species.FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu DNA (cytosine 5) methyltr Human Epstein-Barr Virus Integrin â3 (Phospho Tyr Integrin â3 (Phospho Tyr Interferon-a Receptor Typ Akt Inhibitor, Isozyme Se Mouse Epstein-Barr Virus Rat TGF-beta-inducible ea
#28751177 2017/07/28 Save this To Up
In vitro screening of the open source Pathogen Box identifies novel compounds with profound activities against Neospora caninum.Neospora caninum is a major cause of abortion in cattle and represents an important veterinary health problem of great economic significance. The Medicines for Malaria Venture (MMV) Pathogen Box, an open-source collection of 400 compounds with proven anti-infective properties against a wide range of pathogens, was screened against a N. caninum beta-galactosidase reporter strain grown in human foreskin fibroblasts. A primary screening carried out at 1µM yielded 40 compounds that were effective against N. caninum tachyzoites. However, 30 of these compounds also affected the viability of the host cells. The 10 remaining compounds exhibited IC50 values between 4 and 43nM. Three compounds with IC50 values below 10nM, namely MMV676602, MMV688762 and MMV671636, were further characterized in vitro in more detail with respect to inhibition of invasion versus intracellular proliferation, and only MMV671636 had an impact on intracellular proliferation of tachyzoites. This was confirmed by transmission electron microscopy, showing that the primary target of MMV671636 was the mitochondrion. MMV671636 treatment of experimentally infected mice significantly reduced the number of animals with lung and brain infection, and these mice also exhibited a significantly reduced titer of antibodies directed against N. caninum antigens. Thus, MMV671636 is a promising starting point for the development of a future neosporosis therapy.
1289 related Products with: In vitro screening of the open source Pathogen Box identifies novel compounds with profound activities against Neospora caninum.Integrin β1 (CD29) Antib LPAM-1(Integrin α4, CD49 α-Internexin Antibody So INPP5F antibody Source Ra Interferon alpha-8 antibo Interferon alpha-6 antibo interleukin 17 receptor C TCP-1 theta antibody Sour TGF beta induced factor 2 F-box only protein 2 anti INPP1 antibody Source Rab ING5 antibody Source Rabb
#28743470 2017/07/26 Save this To Up
Molecular identification and antigenic characterization of Babesia divergens Erythrocyte Binding Protein (BdEBP) as a potential vaccine candidate.Host cell invasion is the only step where Babesia parasites are extracellular, and their survival is menaced during this step. Therefore, interfering with this critical stage is a target for an anti-Babesia intervention strategy. In this regard, recombinant protein encoding Babesia divergens Erythrocyte Binding Protein (BdEBP) was produced in Escherichia coli in the current study, and its antiserum was prepared in mice for further molecular characterization. Western blotting and indirect fluorescent antibody test (IFAT) revealed the specific reaction of the anti-rBdEBP serum with a corresponding authentic protein of B. divergens. Next, bovine RBCs were incubated with a B. divergens lysate, and anti-rBdEBP serum was produced in mice to detect the ability of BdEBP to bind with host cells. Bands corresponding to 29.6-kDa proteins in the protein-bound erythrocyte lysate were detected by specific immune rBdEBP using Western blotting. These results suggest that BdEBP is functional in the merozoite stage and may be involved in attachment to bovine RBCs. A significant inhibition of the in vitro growth of B. divergens culture treated with anti-rBdEBP serum was observed. Moreover, the efficacy of pre-incubated free merozoites to invade bovine erythrocytes was inhibited by 60% after incubation with 2mg/ml of anti-rBdEBP serum for 6h. The obtained data suggest the possible use of rBdEBP as a vaccine candidate against bovine babesiosis.
1886 related Products with: Molecular identification and antigenic characterization of Babesia divergens Erythrocyte Binding Protein (BdEBP) as a potential vaccine candidate.Rabbit Anti-Rat Androgen Carboxyfluorescein diacet EpiQuik General Protein D EpiQuik General Protein Acyl CoA binding Protein Mouse Anti-Human Retinol S100 alpha - Rabbit polyc Cell Meter™ Live Cell C Cell Meter™ Live Cell C Cell Meter™ Live Cell C Cell Meter™ Live Cell C Cell Meter™ Live Cell C
#28737447 2017/07/24 Save this To Up
PMab-52: Specific and Sensitive Monoclonal Antibody Against Cat Podoplanin for Immunohistochemistry.Podoplanin (PDPN) is expressed in several normal tissues, such as lymphatic endothelial cells, podocytes of renal glomerulus, and type I alveolar cells of lung. PDPN activates platelet aggregation by binding to C-type lectin-like receptor-2 (CLEC-2) on platelet. Although monoclonal antibodies (mAbs) against human PDPN, mouse PDPN, rat PDPN, rabbit PDPN, dog PDPN, and bovine PDPN have been established, anticat PDPN (cPDPN) mAbs have not been developed. In this study, we immunized mice with Chinese hamster ovary (CHO)-K1 cell lines expressing cPDPN, and developed anti-cPDPN mAbs. One of the clones, PMab-52 (IgM, kappa), detected cPDPN specifically in flow cytometry and Western blot analysis. PMab-52 is also useful for detecting feline squamous cell carcinoma cells in immunohistochemical analysis. PMab-52 is expected to be useful for investigating the function of cPDPN in feline carcinomas.
1317 related Products with: PMab-52: Specific and Sensitive Monoclonal Antibody Against Cat Podoplanin for Immunohistochemistry.MOUSE ANTI BOVINE ROTAVIR MOUSE ANTI BORRELIA BURGD MOUSE ANTI CANINE DISTEMP MOUSE ANTI HUMAN CD15, Pr MOUSE ANTI HUMAN CD19 RPE MOUSE ANTI HUMAN CD15, Pr MOUSE ANTI APAAP COMPLEX, RABBIT ANTI GSK3 BETA (pS Mouse Monoclonal Antibody Abeta (1-40 42) | 4D8 | o Anti C Reactive Protein A Anti AGO2 Human, Monoclon
#28668608 2017/07/02 Save this To Up
Babesia bovis BOV57, a Theileria parva P67 homolog, is an invasion-related, neutralization-sensitive antigen.Babesia bovis BOV57, which is a homolog of the Theileria parva vaccine candidate antigen P67, is expressed in both the tick and blood stages of the life cycle of this parasite. However, the vaccine potential of BOV57 remained to be investigated. In the present study, we generated recombinant BOV57 (rBOV57) and prepared polyclonal antibodies against rBOV57 in mice and rabbits. Indirect immunofluorescence assays conducted with the mouse anti-rBOV57 antibody demonstrated that BOV57 localized at the apical end of paired merozoites in infected bovine red blood cells, whereas the antigen was found in the parasite membrane around the apical end of intraerythrocytic single and extracellular merozoites. In an invasion-inhibition assay, the rabbit anti-rBOV57 antibody potentially inhibited RBC invasion of B. bovis merozoites in vitro. In addition, the invasion inhibition mediated by rabbit anti-rBOV57 antibody resulted in a reduced growth rate of B. bovis in the in vitro culture. These findings indicated that B. bovis BOV57 plays a critical role in the invasion of merozoites into red blood cells, suggesting its potential as a subunit vaccine candidate against B. bovis infection in cattle. Furthermore, we analyzed the genetic diversity of bov57 gene sequences isolated from Sri Lanka, Mongolia, the Philippines, and Vietnam. The bov57 gene sequences derived from Mongolia, the Philippines, and Vietnam were conserved, whereas insertion and/or deletion mutations resulted in sequence diversity among the Sri Lankan samples. In summary, BOV57 is an invasion-related, neutralization-sensitive antigen encoded by the bov57 gene, which displays higher sequence diversity than previously reported.
1145 related Products with: Babesia bovis BOV57, a Theileria parva P67 homolog, is an invasion-related, neutralization-sensitive antigen.Mouse Anti hPTH PTH rP Ta Factor VIII Related Anti Factor VIII Related Anti Factor VIII Related Anti Rabbit Polyclonal to Myco MOUSE ANTI BORRELIA BURGD Fos-related antigen 2 - N CD44 antigen isoform 4 an serologically defined col Primary antibody low den Rabbit Anti-Parvalbumin P Rabbit Anti-Parvalbumin P
#28626461 2017/06/19 Save this To Up
Neoglycoconjugate of Tetrasaccharide Representing One Repeating Unit of the Streptococcus pneumoniae Type 14 Capsular Polysaccharide Induces the Production of Opsonizing IgG1 Antibodies and Possesses the Highest Protective Activity As Compared to Hexa- and Octasaccharide Conjugates.Identifying protective synthetic oligosaccharide (OS) epitopes of Streptococcus pneumoniae capsular polysaccharides (CPs) is an indispensable step in the development of third-generation carbohydrate pneumococcal vaccines. Synthetic tetra-, hexa-, and octasaccharide structurally related to CP of S. pneumoniae type 14 were coupled to bovine serum albumin (BSA), adjuvanted with aluminum hydroxide, and tested for their immunogenicity in mice upon intraperitoneal prime-boost immunizations. Injections of the conjugates induced production of opsonizing anti-OS IgG1 antibodies (Abs). Immunization with the tetra- and octasaccharide conjugates stimulated the highest titers of the specific Abs. Further, the tetrasaccharide ligand demonstrated the highest ability to bind OS and CP Abs. Murine immune sera developed against tetra- and octasaccharide conjugates promoted pathogen opsonization to a higher degree than antisera against conjugated hexasaccharide. For the first time, the protective activities of these glycoconjugates were demonstrated in mouse model of generalized pneumococcal infections. The tetrasaccharide conjugate possessed the highest protective activities. Conversely, the octasaccharide conjugate had lower protective activities and the lowest one showed the hexasaccharide conjugate. Sera against all of the glycoconjugates passively protected naive mice from pneumococcal infections. Given that the BSA-tetrasaccharide induced the most abundant yield of specific Abs and the best protective activity, this OS may be regarded as the most promising candidate for the development of conjugated vaccines against S. pneumoniae type 14 infections.
2933 related Products with: Neoglycoconjugate of Tetrasaccharide Representing One Repeating Unit of the Streptococcus pneumoniae Type 14 Capsular Polysaccharide Induces the Production of Opsonizing IgG1 Antibodies and Possesses the Highest Protective Activity As Compared to Hexa- and Octasaccharide Conjugates.Single Strand DNA Ligase, Single Strand DNA Ligase, Thermostable TDG Enzyme & Thermostable TDG Kit Thermostable TDG Kit (DIS Thermostable TDG Kit *DIS Bovine Androstenedione,AS Rat Anti-CCT theta Antibo Rabbit Anti-Theophylline Sheep Anti-Theophylline 3 FDA Standard Frozen Tissu FDA Standard Frozen Tissu
#28625520 2017/06/19 Save this To Up
Immunogenicity of pulsatile-release PLGA microspheres for single-injection vaccination.The World Health Organization's Expanded Programme on Immunization has led to a dramatic rise in worldwide vaccination rates over the past 40years, yet 19.4 million infants remain underimmunized each year. Many of these infants have received at least one vaccine dose but may remain unprotected because they did not receive subsequent booster doses due to logistical challenges. This study aimed to develop injectable controlled release microparticles with kinetics that mimic common vaccine dosing regimens consisting of large antigen doses administered periodically over the course of months in order to eliminate the need for boosters. Sixteen poly(lactic-co-glycolic acid) (PLGA) microsphere formulations containing bovine serum albumin (BSA) as a model vaccine antigen were screened in vitro to determine their respective release kinetics. Three formulations that exhibited desirable pulsatile release profiles were then selected for studying immunogenicity in mice. Two low-dose microsphere formulations induced peak anti-BSA IgG antibody titers of 13.9±1.3 and 13.7±2.2 log2 compared to 15.5±1.5 log2 for a series of three bolus injections delivered at 0, 4, and 8weeks with an equivalent cumulative dose. Similarly, high-dose formulations induced peak antibody titers that were 16.1±2.1 log2 compared to 17.7±2.2 log2 for controls. All three microparticle formulations studied in vivo induced peak antibody titers that were statistically similar to bolus controls. These results suggest that pulsatile antigen release from polymeric microparticles is a promising approach for single-injection vaccination, which could potentially reduce the logistical burden associated with immunization in the developing world.
1960 related Products with: Immunogenicity of pulsatile-release PLGA microspheres for single-injection vaccination.Cellufine Formyl , 50 ml Cellufine Formyl Media Cellufine Formyl , 500 ml Cellufine Formyl Media Cellufine Formyl Media Formalin Solution (20%) Formalin Solution (20%) Formalin Solution (20%) Formalin (10% Neutral Bu Formalin (10% Neutral Bu Zinc Formalin Solution Zinc Formalin Solution
#28599705 2017/06/10 Save this To Up
Novel electrochemical immunoassay for human IgG1 using metal sulfide quantum dot-doped bovine serum albumin microspheres on antibody-functionalized magnetic beads.A new magneto-controlled electrochemical immunosensing system was developed for the sensitive detection of low-abundance protein (IgG1 used in this case) with a sandwich-type assay format on monoclonal mouse anti-human Fab-specific IgG1-functionalized magnetic bead. Metal sulfide (CdS) quantum dot-doped bovine serum albumin (QD-BSA) was synthesized and functionalized with monoclonal Fc-specific anti-human antibody. In the presence of IgG1, the immobilized antibody on magnetic bead was selective to capture the Fab region of the analyte, followed to be sandwiched by the conjugated antibody onto QD-BSA. The subsequent anodic stripping voltammetric analysis of cadmium ion, released by acid from quantum dot, was conducted at an in situ prepared mercury film electrode. Under optimal conditions, the voltammetric current increased with the increasing of target IgG1 within a dynamic working range from 10 pg mL(-1) to 100 ng mL(-1). The limit of detection of this immunosensor was evaluated to 3.4 pg mL(-1) at 3sblank criterion. The precision, selectivity and method accuracy were acceptable. Analysis of human serum samples revealed good accordance with the results obtained by commercial enzyme-linked immunosorbent assay method. Importantly, this concept offers promise for cost-effective analysis of low-abundance cancer biomarkers without the need of natural enzymes.
1169 related Products with: Novel electrochemical immunoassay for human IgG1 using metal sulfide quantum dot-doped bovine serum albumin microspheres on antibody-functionalized magnetic beads.Human Serum Albumin antib Human Serum Albumin antib Leptin ELISA Kit, Human A anti-Human Serum Albumin MOUSE ANTI HUMAN CD19 RPE Bovine serum albumin Anti Anti-Bovine Serum Albumin Anti-Bovine Serum Albumin Monoclonal Anti-Bovine Se BSA | bovine serum albumi BSA | bovine serum albumi BSA | bovine serum albumi
#28593185 2017/06/08 Save this To Up
Induction of Colonic Regulatory T Cells by Mesalamine by Activating the Aryl Hydrocarbon Receptor.Mesalamine is a first-line drug for treatment of inflammatory bowel diseases (IBD). However, its mechanisms are not fully understood. CD4(+) Foxp3(+) regulatory T cells (Tregs) play a potential role in suppressing IBD. This study determined whether the anti-inflammatory activity of mesalamine is related to Treg induction in the colon.
1240 related Products with: Induction of Colonic Regulatory T Cells by Mesalamine by Activating the Aryl Hydrocarbon Receptor.anti Transferrin receptor Rat monoclonal anti mouse Rat monoclonal anti mouse BACTERIOLOGY BACTEROIDES Human Tumor Necrosis Fact Interferon-a Receptor Typ Mouse Anti-Human Thyroid Mouse Anti-Human Thyroid TGR5 Receptor Agonist TNFRSF1B - Goat polyclona RANK Ligand Soluble, Huma Rat Toll Like Receptor 2(
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