Search results for: Anti-Armadillo Drosophila protein Monoclonal Antibody
#35177602 2022/02/17 To Up
Heterotypic interactions drive antibody synergy against a malaria vaccine candidate.Understanding mechanisms of antibody synergy is important for vaccine design and antibody cocktail development. Examples of synergy between antibodies are well-documented, but the mechanisms underlying these relationships often remain poorly understood. The leading blood-stage malaria vaccine candidate, CyRPA, is essential for invasion of Plasmodium falciparum into human erythrocytes. Here we present a panel of anti-CyRPA monoclonal antibodies that strongly inhibit parasite growth in in vitro assays. Structural studies show that growth-inhibitory antibodies bind epitopes on a single face of CyRPA. We also show that pairs of non-competing inhibitory antibodies have strongly synergistic growth-inhibitory activity. These antibodies bind to neighbouring epitopes on CyRPA and form lateral, heterotypic interactions which slow antibody dissociation. We predict that such heterotypic interactions will be a feature of many immune responses. Immunogens which elicit such synergistic antibody mixtures could increase the potency of vaccine-elicited responses to provide robust and long-lived immunity against challenging disease targets.
Robert J Ragotte, David Pulido, Amelia M Lias, Doris Quinkert, Daniel G W Alanine, Abhishek Jamwal, Hannah Davies, AdÃ©la Nacer, Edward D Lowe, Geoffrey W Grime, Joseph J Illingworth, Robert F Donat, Elspeth F Garman, Paul W Bowyer, Matthew K Higgins, Simon J Draper
1056 related Products with: Heterotypic interactions drive antibody synergy against a malaria vaccine candidate.100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug50 µg 2.0 ml 100ug Lyophilized1mg100ug Lyophilized100ug Lyophilized100μl 100ul
#35124238 2022/02/04 To Up
Mutually exclusive expression of sex-specific and non-sex-specific fruitless gene products in the Drosophila central nervous system.The fruitless gene of Drosophila produces multiple protein isoforms, which are classified into two major classes, sex-specific Fru proteins (FruM) and non-sex specific proteins (FruCOM). Whereas FruM proteins are expressed in â¼2000 neurons to masculinize their structure and function, little is known about FruCOM's roles. As an attempt to obtain clues to the roles of FruCOM, we compared expression patterns of FruCOM and FruM in the central nervous system at the late larval stage. We found that nearly all neuroblasts express FruCOM but not FruM, whereas a subset of ganglion mother cells and differentiated neurons express FruM but not FruCOM. It is inferred that FruCOM proteins support fundamental stem cell functions, contrasting to FruM proteins, which play major roles in sex-specific differentiation of neurons.
Kosei Sato, Daisuke Yamamoto
1055 related Products with: Mutually exclusive expression of sex-specific and non-sex-specific fruitless gene products in the Drosophila central nervous system.2 Pieces/Box4 Membranes/Box2 Pieces/Box4 Arrays/Slide4 Membranes/Box4 Membranes/Box2 Pieces/Box4 Membranes/Box2 Pieces/Box5mg4 Arrays/Slide
#34852239 2021/11/30 To Up
The epitope arrangement on flavivirus particles contributes to Mab C10's extraordinary neutralization breadth across Zika and dengue viruses.The human monoclonal antibody C10 exhibits extraordinary cross-reactivity, potently neutralizing Zika virus (ZIKV) and the four serotypes of dengue virus (DENV1-DENV4). Here we describe a comparative structure-function analysis of C10 bound to the envelope (E) protein dimers of the five viruses it neutralizes. We demonstrate that the C10 Fab has high affinity for ZIKV and DENV1 but not for DENV2, DENV3, and DENV4. We further show that the C10 interaction with the latter viruses requires an E protein conformational landscape that limits binding to only one of the three independent epitopes per virion. This limited affinity is nevertheless counterbalanced by the particle's icosahedral organization, which allows two different dimers to be reached by both Fab arms of a C10 immunoglobulin. The epitopes' geometric distribution thus confers C10 its exceptional neutralization breadth. Our results highlight the importance not only of paratope/epitope complementarity but also the topological distribution for epitope-focused vaccine design.
Arvind Sharma, Xiaokang Zhang, Wanwisa Dejnirattisai, Xinghong Dai, Danyang Gong, Wiyada Wongwiwat, StÃ©phane Duquerroy, Alexander Rouvinski, Marie-Christine Vaney, Pablo Guardado-Calvo, Ahmed Haouz, Patrick England, Ren Sun, Z Hong Zhou, Juthathip Mongkolsapaya, Gavin R Screaton, Felix A Rey
2827 related Products with: The epitope arrangement on flavivirus particles contributes to Mab C10's extraordinary neutralization breadth across Zika and dengue viruses.One 96-Well Strip Microplmin 2 cartons1 g1 mg5 mg1
#34585149 2021/09/13 To Up
Live and fixed imaging of translation sites at single mRNA resolution in the embryo.Significant regulation of gene expression is mediated at the translation level. Here, we describe protocols for imaging and analysis of translation at single mRNA resolution in both fixed and living embryos. These protocols use the SunTag system, in which the protein of interest is visualized by inserting a peptide array that is recognized by a single chain antibody. Simultaneous detection of individual mRNAs using the MS2/MCP system or by smFISH allows translation sites to be identified and quantified. For complete information on the generation and use of this protocol, please refer to Vinter etÂ al. (2021).
Daisy J Vinter, Caroline Hoppe, Hilary L Ashe
2616 related Products with: Live and fixed imaging of translation sites at single mRNA resolution in the embryo.1ml1 Set900 tests
#34196449 2021/07/01 To Up
Immunohistochemical detection of hepatocyte nuclear factor-4Î± in vertebrates.Hepatocyte nuclear factor-4Î± (HNF4Î±) presents in multiple isoforms generated using alternative promoter (P1 and P2) and splicing. Neither conservation of tissue distribution of HNF4Î± isoforms, nor presence of alternative promoter usage is known. In this study, to detect the expression of HNF4Î± in some species of animals, we have applied monoclonal antibodies against P1 (K9218) and P2 (H6939) promoter-driven and P1/P2 promoter-driven H1415 HNF4Î± for immunohistochemistry and western blot analysis. Antibody K9218 was observed in the hepatocytes, proximal tubules of the kidney, and epithelial cells in the mucosa of the small intestine and colon of rats, chicken, and tortoise, whereas antibody H6939 signal were detected in the stomach, pancreas, bile duct, and pancreatic duct of human and rats. The signal for antibody K9218 was recognized in tissues of a wide range of mammals, bird, reptile, amphibian, and fish as well. Antibody H1415 displayed a positive reaction in hepatocytes and intestinal epithelial cells in chicken and tortoise, whereas the bile duct, mucosal epithelial cells in the stomach, or pancreas in these animals were negative. Western blotting showed the binding of the antibody with HNF4Î± protein from each animal. The sequence of human HNF4Î± was 100% identical to murine and rat HNF4Î±, 88.9% to chicken, 77.8% to Xenopus HNF4Î±, and 81.5% to medaka. However, the specific part of human and invertebrate Drosophila HNF4 shares only 14.8% sequence identity. This antibody is useful for detecting HNF4Î± isoforms in a wide range of vertebrates, and suggests many insights into animal evolution.
Shuying Jiang, Toshiya Tanaka, Ren Yagami, Go Hasegawa, Hajime Umezu, Yukio Fujiyoshi, Tatsuhiko Kodama, Makoto Naito, Yoichi Ajioka
1153 related Products with: Immunohistochemical detection of hepatocyte nuclear factor-4Î± in vertebrates.100.00 ugProtein2 0.1 mg100 μg1 mg100.00 ug0.1ml (1mg/ml)0.5mg100.00 ug
#33459708 // To Up
A Single-Chain Variable Fragment Antibody Inhibits Aggregation of Phosphorylated Tau and Ameliorates Tau Toxicity in vitro and in vivo.Alzheimer's disease (AD) is a common cause of dementia among elderly people. Hyperphosphorylation and aggregation of tau correlates with the clinical progression of AD; therefore, therapies targeting the aggregation of tau may have potential applications for anti-AD drug development. Several inhibitors of tau aggregation, including small molecules and antibodies, have been found to decrease the aggregation of tau and the corresponding pathology.
Sen Li, Yushan Yi, Ke Cui, Yanqiu Zhang, Yange Chen, Dou Han, Ling Sun, Xiaohui Zhang, Fei Chen, Yixin Zhang, Yufeng Yang
2069 related Products with: A Single-Chain Variable Fragment Antibody Inhibits Aggregation of Phosphorylated Tau and Ameliorates Tau Toxicity in vitro and in vivo.4 Membranes/Box1 Set1 Set1 Set1 Set100ug Lyophilized2 Pieces/Box1 Set1 Set1 Set1 Set100μg
#33252040 2020/11/30 To Up
Cryo-EM structure of the calcium release-activated calcium channel Orai in an open conformation.The calcium release-activated calcium channel Orai regulates Ca entry into non-excitable cells and is required for proper immune function. While the channel typically opens following Ca release from the endoplasmic reticulum, certain pathologic mutations render the channel constitutively open. Previously, using one such mutation (H206A), we obtained low (6.7 Ã ) resolution X-ray structural information on Orai in an open conformation (Hou et al., 2018). Here we present a structure of this open conformation at 3.3 Ã resolution using fiducial-assisted cryo-electron microscopy. The improved structure reveals the conformations of amino acids in the open pore, which dilates by outward movements of subunits. A ring of phenylalanine residues repositions to expose previously shielded glycine residues to the pore without significant rotational movement of the associated helices. Together with other hydrophobic amino acids, the phenylalanines act as the channel's gate. Structured M1-M2 turrets, not evident previously, form the channel's extracellular entrance.
Xiaowei Hou, Ian R Outhwaite, Leanne Pedi, Stephen Barstow Long
2648 related Products with: Cryo-EM structure of the calcium release-activated calcium channel Orai in an open conformation.100ug100ug 100ul100 μg 100ul
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#32601208 2020/06/29 To Up
Pharmacological disruption of the Notch transcription factor complex.Notch pathway signaling is implicated in several human cancers. Aberrant activation and mutations of Notch signaling components are linked to tumor initiation, maintenance, and resistance to cancer therapy. Several strategies, such as monoclonal antibodies against Notch ligands and receptors, as well as small-molecule Î³-secretase inhibitors (GSIs), have been developed to interfere with Notch receptor activation at proximal points in the pathway. However, the use of drug-like small molecules to target the downstream mediators of Notch signaling, the Notch transcription activation complex, remains largely unexplored. Here, we report the discovery of an orally active small-molecule inhibitor (termed CB-103) of the Notch transcription activation complex. We show that CB-103 inhibits Notch signaling in primary human T cell acute lymphoblastic leukemia and other Notch-dependent human tumor cell lines, and concomitantly induces cell cycle arrest and apoptosis, thereby impairing proliferation, including in GSI-resistant human tumor cell lines with chromosomal translocations and rearrangements in Notch genes. CB-103 produces Notch loss-of-function phenotypes in flies and mice and inhibits the growth of human breast cancer and leukemia xenografts, notably without causing the dose-limiting intestinal toxicity associated with other Notch inhibitors. Thus, we describe a pharmacological strategy that interferes with Notch signaling by disrupting the Notch transcription complex and shows therapeutic potential for treating Notch-driven cancers.
Rajwinder Lehal, Jelena Zaric, Michele Vigolo, Charlotte Urech, Viktoras Frismantas, Nadine Zangger, Linlin Cao, Adeline Berger, Irene Chicote, Sylvain LoubÃ©ry, Sung Hee Choi, Ute Koch, Stephen C Blacklow, Hector G Palmer, Beat Bornhauser, Marcos GonzÃ¡lez-GaitÃ¡n, Yvan Arsenijevic, Vincent Zoete, Jon C Aster, Jean-Pierre Bourquin, Freddy Radtke 100ul30 Reactions96200ug6Kit96200ug96200ug 25UG200ug
#32522980 2020/06/10 To Up
Spt6 is a maintenance factor for centromeric CENP-A.Replication and transcription of genomic DNA requires partial disassembly of nucleosomes to allow progression of polymerases. This presents both an opportunity to remodel the underlying chromatin and a danger of losing epigenetic information. Centromeric transcription is required for stable incorporation of the centromere-specific histone dCENP-A in M/G1 phase, which depends on the eviction of previously deposited H3/H3.3-placeholder nucleosomes. Here we demonstrate that the histone chaperone and transcription elongation factor Spt6 spatially and temporarily coincides with centromeric transcription and prevents the loss of old CENP-A nucleosomes in both Drosophila and human cells. Spt6 binds directly to dCENP-A and dCENP-A mutants carrying phosphomimetic residues alleviate this association. Retention of phosphomimetic dCENP-A mutants is reduced relative to wildtype, while non-phosphorylatable dCENP-A retention is increased and accumulates at the centromere. We conclude that Spt6 acts as a conserved CENP-A maintenance factor that ensures long-term stability of epigenetic centromere identity during transcription-mediated chromatin remodeling.
Georg O M Bobkov, Anming Huang, Sebastiaan J W van den Berg, Sreyoshi Mitra, Eduard Anselm, Vasiliki Lazou, Sarah Schunter, Regina Feederle, Axel Imhof, Alexandra Lusser, Lars E T Jansen, Patrick Heun0.2 mg100ug Lyophilized100ug Lyophilized100 ml0.1 mg100ug Lyophilized100 ul1 mg100ug Lyophilized0.1ml (1mg/ml)100ug Lyophilized20 ug
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