Search results for: Rabbit Anti-PBEF1(CT) Polyclonal Antibody
#33977321 2021/05/11 To Up
Production of polyclonal antibody against the recombinant PirB protein of Vibrio parahaemolyticus.Acute hepatopancreatic necrosis disease (AHPND) is caused by toxin-producing strains of Vibrio parahaemolyticus which contain deadly binary toxins PirA and PirB encoded in pVA1 plasmid. The polyclonal antibodies against PirB protein could be used to develop immunochromatographic test strip for in-field diagnosis of AHPND.
Ngoc-Diem Duong, Khai-Hoan Nguyen-Phuoc, Kim-Yen Thi Do, Nguyet-Thu Thi Nguyen, Thuoc Linh Tran, Hieu Tran-Van
1789 related Products with: Production of polyclonal antibody against the recombinant PirB protein of Vibrio parahaemolyticus.100ug Lyophilized100ug100ug Lyophilized100ug100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized
#33974477 2021/05/11 To Up
Motilin Receptor Expression Found in the Human Main and Accessory Lacrimal Glands.: In this study, we investigated the presence of motilin receptors (MR) in adnexal tissue including the human main lacrimal gland.: 17 adnexal human specimens comprising of 11 isolated human main lacrimal gland specimens, four full-thickness human eyelid excisions and two exenterations containing full-thickness eyelid and portions of the main lacrimal gland were immunolabelled with a rabbit polyclonal human MR antibody.: Our results demonstrated that all main lacrimal gland specimens (13/13, 100%) were positive for MR expression with a predominance (10/13 (77%) of grade 1+ punctate distribution. Motilin receptors were not found in eccrine glands, cutaneous sebaceous glands, glands of Zeis or glands of Moll (0/6, 0%). We also confirmed MR expression in the accessory lacrimal gland tissue.: In summary, we discovered the MR receptor in the lacrimal and accessory lacrimal gland - the significance of which, in the lacrimal gland, remains unclear - but motilin may play a role in the muscarinic control of aqueous tear secretion.
Richard R Sadig, Alexandra Allende, Geoffrey Hall, Dinh Tran, Michele C Madigan, Stephanie L Watson, Kenneth G-J Ooi
1710 related Products with: Motilin Receptor Expression Found in the Human Main and Accessory Lacrimal Glands.100 μg100 μg100 μg0.1 mg100 μg50 ul96 wells (1 kit) 100ul96T1000 100ul100 μg
#33968077 2021/04/23 To Up
A Double-Antibody Sandwich ELISA for Sensitive and Specific Detection of Swine Fibrinogen-Like Protein 1.F
Xin Zhang, Haipeng Zhu, Xu Zheng, Yunjie Jiao, Lulu Ning, En-Min Zhou, Yang Mu
2845 related Products with: A Double-Antibody Sandwich ELISA for Sensitive and Specific Detection of Swine Fibrinogen-Like Protein 1.1 kit0.1 mg25 µg100ug Lyophilized100 ml100 TESTS100ug100μg100ug Lyophilized0.1 ml0.1 mg96 tests
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#33960377 2021/05/07 To Up
Detection of four quinolone antibiotic by chemiluminescence based on a novel Nor-Biotin bifunctional ligand and SA-ALP technology.A simple and effective direct competitive chemiluminescence immunoassay for detection of four kind of quinolone antibiotics in milk was established using Nor-Biotin(biotin-modified Norfloxacin) bifunctional ligand and SA-ALP signal amplification technology. The polyclonal antibody was obtained after immunization of New Zealand White rabbits using Norfloxacin-derived antigen. "Click chemistry" was used for the rapid and facile synthesis of the Nor-Biotin bifunctional ligand. After the optimization of the incubation time and reaction buffer, the direct competitive ChemiLuminescence assay (dcCLIA) method was developed and used for sensitive detection of four kinds of quinolone drugs (norfloxacin (NOR), pefloxacin (PFLX), ciprofloxacin (CIP), and danofloxacin (DFLX)). The IC50 of the four kinds of quinolone drugs ranged from 7.35 ng/mL to 24.27 ng/mL, and the lowest detection limits (LOD) ranged from 0.05 ng/mL to 0.16 ng/mL, which were below their maximum residue levels (MRLs), approved by the EU for treatment of food-producing animals. To demonstrate the applicability of the assay, artificially contaminated milk samples with the four-quinolone drugs were analyzed. The mean recovery rates of the drugs ranged from 86.31% to 112.11%.
Zhenyu Han, Tieqiang Sun, Zehua Xu, Longxing Fan, Hanxuan Yun, Xuejiao Ge, Xiao Liu, Ying Liu, Bao'an Ning
2099 related Products with: Detection of four quinolone antibiotic by chemiluminescence based on a novel Nor-Biotin bifunctional ligand and SA-ALP technology.0.2 mg50 50 100ug0.25 mg100ug100ug50 100ug0.5 mg25 100 TESTS
#33944773 2021/05/03 To Up
Molecular characterization and protective efficacy of a new conserved hypothetical protein of Eimeria tenella.Eimeria tenella is an obligate intracellular parasite that actively invades cecal epithelial cells of chickens. This parasite encodes a genome of more than 8000 genes. However, more than 70% of the gene models for this species are currently annotated as hypothetical proteins. In this study, a conserved hypothetical protein gene of E. tenella, designated EtCHP18905, was cloned and identified, and its immune protective effects were evaluated. The open reading frame of EtCHP18905 was 1053bp and encoded a protein of 350 amino acids with a molecular weight of 38.7kDa. The recombinant EtCHP18905 protein (rEtCHP18905) was expressed in E. coli. Using western blot, the recombinant protein was successfully recognized by anti GST-Tag monoclonal antibody and anti-sporozoites protein rabbit serum. Real-time quantitative PCR analysis revealed that the EtCHP18905 mRNA levels were higher in sporozoites than in unsporulated oocysts, sporulated oocysts and second-generation merozoites. Western blot analysis showed that EtCHP18905 protein expression levels were lower in sporozoites than in other stages. Immunofluorescence analysis indicated that the EtCHP18905 protein was located on the surface of sporozoites and second-generation merozoites. Inhibition experiments showed that the ability of sporozoites to invade host cells was significantly decreased after treatment with the anti-rEtCHP18905 polyclonal antibody. Vaccination with rEtCHP18905 protein was able to significantly decrease mean lesion scores and oocyst outputs as compared to non-vaccinated controls. The results suggest that the rEtCHP18905 protein can induce partial immune protection against infection with E. tenella and could be an effective candidate for the development of new vaccines.
Huanzhi Zhao, Shunhai Zhu, Qiping Zhao, Bing Huang, Guiling Liu, Zhihang Li, Lu Wang, Hui Dong, Hongyu Han
1217 related Products with: Molecular characterization and protective efficacy of a new conserved hypothetical protein of Eimeria tenella.100ul 100ul 100ul1000 TESTS/0.65ml 100ul100ul 100ul1 Set20 100ug1 mg100ug Lyophilized
#33938398 2021/05/01 To Up
Development of a group-specific antibody-based immunoassay method for simultaneously detecting sildenafil-like adulterants in herbal spirit drinks.Phosphodiesterase type 5 (PDE-5) inhibitors are commonly used to treat erectile dysfunction. There is a problem with synthesis and illegal use of a wide range of analogues of the licenced drugs and a simple class-wide analytical method is required. In this work, based on structural modelling, we developed an immunological method using norneovardenafil as a hapten as it contains only the general sub-structure and the common features of sildenafil-like adulterants, such as hydrophobic centres, hydrogen-bond donor atoms and hydrogen-bond acceptor atoms. Thus theoretically it could induce production of antibody which could recognise multiple sildenafil-like adulterants. By immunising rabbits, a group-specific polyclonal antibody was obtained with the desired broad-spectrum molecular recognition performance against sildenafil-like adulterants. Then, an indirect competitive enzyme-linked immunosorbent assay (icELISA) was developed for the detection of sildenafil-like adulterants in herbal spirit drinks. Under the optimised conditions, the icELISA method showed broad linear ranges for acetildenafil, sildenafil and vardenafil respectively of 0.7 to 27.7 μg/kg, 1.0 to 70.7 μg/kg and 1.5 to 22.7 μg/kg, with half-maximal inhibition concentration (IC) values of 4.5 μg/kg, 8.3 μg/kg and 5.7 μg/kg, respectively. For eleven herbal spirit drinks, there was good agreement between total levels of sildenafil-like adulterants measured by icELISA and levels of each of four individual adulterants determined by LC-MS/MS. In short, the developed icELISA can be employed for rapid and simple screening for adulteration of herbal spirit drinks with sildenafil-like compounds.
Haoyu Chen, Yongyi Zhang, Yantao Hua, Yuanxin Tian, Hong Wang, Zhenlin Xu, Xuecai Tan, Yudong Shen, Jinyi Yang
2768 related Products with: Development of a group-specific antibody-based immunoassay method for simultaneously detecting sildenafil-like adulterants in herbal spirit drinks.4 Membranes/Box4 Membranes/Box4 Arrays/Slide4 Arrays/Slide4 Membranes/Box4 Membranes/Box4 Arrays/Slide4 Membranes/Box4 Membranes/Box4 Arrays/Slide4 Membranes/Box4 Membranes/Box
#33902633 2021/04/26 To Up
Monoclonal antibodies specific for the hemagglutinin-neuraminidase protein define neutralizing epitopes specific for Newcastle disease virus genotype 2.VII from Egypt.Newcastle disease is a devastating disease in poultry caused by virulent Newcastle disease virus (NDV), a paramyxovirus endemic in many regions of the world despite intensive vaccination. Phylogenetic analyses reveal ongoing evolution of the predominant circulating genotype 2.VII, and the relevance of potential antigenic drift is under discussion. To investigate variation within neutralization-sensitive epitopes within the protein responsible for receptor binding, i.e. the Hemagglutinin-Neuraminidase (HN) spike protein, we were interested in establishing genotype-specific monoclonal antibodies (MAbs).
Ibrahim Moharam, Olayinka Asala, Sven Reiche, Hafez Hafez, Martin Beer, Timm Harder, Christian Grund
1513 related Products with: Monoclonal antibodies specific for the hemagglutinin-neuraminidase protein define neutralizing epitopes specific for Newcastle disease virus genotype 2.VII from Egypt.0.25 mg25 µg0.2 mg0.2 mg100 TESTS0.1 mg100.00 ug0.1 mg1 ml25 µg250 ml1 LITRE
#33895264 2021/04/23 To Up
Preparation of a polyclonal antibody against the non-structural protein, NSs of SFTSV.Severe fever with thrombocytopenia syndrome virus (SFTSV) is newly discovered virus which is the member of the order Bunyavirales, family phenuiviridae, phlebovirus genus. Its genome is composed of 3 segments of negative-sense RNA L, M and S. NSs is a non structure protein encoded by S segment which is important for viral replication and virulence. NSs protein of SFTSV is only involved in the regulation of host innate immune responses and suppression of IFN-promoter activities. So, the exact functions of this protein need to be studied deeply. To understand the exact role of NSs from SFTSV in viral replication and host immune response, a qualified antibody against this protein is required. In this study, NSs gene of SFTSV, was cloned into a bacterial expression vector (pGEX-6P-1) and the recombinant plasmid was transformed into Escherichia coli BL21 (DE3) cells. The SFTSV NSs fusion protein was purified using Glutathione Sepharose 4B and utilized as an antigen to immunize rabbits and obtain an anti-SFTSV NSs polyclonal antibody. Proper expression of the fusion protein and polyclonal antibody specificity were confirmed by western blotting and immunofluorescence analyses. The polyclonal antibody recognized NSs from SFTSV specifically. This is the first report that NSs can form viroplasm-like structures not only in infected cells but also in transfected cells with NSs plasmids. This polyclonal antibody will be useful for future studies of NSs functions.
Xiaoli Tao, Xiaofang Wang, Ye Yuan, Wei Zhao, Kai Yu, Nian Liu, Ying Lu, Yibo Zhang, Xupeng Jin, Yanfei Shen, Hongyan Zhao, Yonggang Li, Wei Tong
1339 related Products with: Preparation of a polyclonal antibody against the non-structural protein, NSs of SFTSV.100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100 100ug Lyophilized200ul100ug Lyophilized100ug100ug Lyophilized100ug Lyophilized100ug Lyophilized
#33894246 2021/04/21 To Up
Neutralization of crotamine by polyclonal antibodies generated against two whole rattlesnake venoms and a novel recombinant fusion protein.Crotamine is a paralyzing toxin (MW: ~5 kDa) found in different proportions in some rattlesnake venoms (up to 62%). Mexican pit viper antivenoms have shown low immunoreactivity against crotamine, which is an urgent quality to be improved. The objective of this work was to evaluate the ability of a novel recombinant fusion protein composed of sphingomyelinase D and crotamine, and two whole venoms from Crotalus molossus nigrescens and C. oreganus helleri to produce neutralizing antibodies against crotamine. These immunogens were separately used for immunization procedures in rabbits. Then, we generated three experimental antivenoms to test their cross-reactivity via western-blot against crotamine from 7 species (C. m. nigrescens, C. o. helleri, C. durissus terrificus, C. scutulatus salvini, C. basiliscus, C. culminatus and C. tzabcan). We also performed pre-incubation neutralization experiments in mice to measure the neutralizing potency of each antivenom against crotamine induced hind limb paralysis. Our antivenoms showed broad recognition across crotamine from most of the tested species. Also, neutralization against crotamine paralysis symptom was successfully achieved by our three antivenoms, albeit with different efficiencies. Our results highlight the use of crotamine enriched venoms and our novel recombinant fusion protein as promising immunogens to improve the neutralizing potency against crotamine for the improvement of Mexican antivenoms.
Roberto Ponce-López, Edgar Neri-Castro, Felipe Olvera-Rodríguez, Elda E Sánchez, Alejandro Alagón, Alejandro Olvera-Rodríguez
1505 related Products with: Neutralization of crotamine by polyclonal antibodies generated against two whole rattlesnake venoms and a novel recombinant fusion protein.100 250 ul1000 TESTS/0.65ml0.2 mg1 mg200ul0.1 mg100 100 1 mg0.1 mg1 mg
#33861252 2021/03/19 To Up
Simultaneous immunodetection of ionophore antibiotics, salinomycin and narasin, in poultry products and milk.Rabbit polyclonal antibodies were generated against the ionophore antibiotic salinomycin (SAL) as a determinant of the BSA-SAL conjugate. The homologous ELISA format was found to be preferred for similar recognition of SAL and narasin (NAR) with IC values of 0.55 and 0.57 ng mL, respectively. Both analytes could be determined in the range of 0.1-2.7 ng mL (IC-IC) with a detection limit of 0.03 ng mL. To analyze matrices, individual pretreatment of samples was required. For chicken muscles, simple buffer extraction was sufficient to recover 87-110% of ionophores. Extraction with acetonitrile followed by evaporation of the solvent was best for recovering 67-108% SAL and NAR from egg homogenate. A feature of the extraction of ionophores from milk was the elimination of fat-mediated interference by organic solvation. It was found that the absence of Na and K ions during reconstitution of sample extracts was a key factor contributing to the increase in the average recovery of ionophores from 32% to 93%. Thanks to this special pretreatment and improved recovery, the developed immunoassay method was suitable for the analysis of ionophore antibiotics SAL and NAR in a milk matrix, which has not been previously reported.
Maksim A Burkin, Inna A Galvidis
1774 related Products with: Simultaneous immunodetection of ionophore antibiotics, salinomycin and narasin, in poultry products and milk.1000 tests100ug1 ml100 mg10 mg100ug500 MG25 mg96T100ul50 ug 50 mg
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