Euonymus europaeus lectin. 4Storage: -20°CApplication note .



Euonymus europaeus lectin. EEL also has applications as a endothelial/epithelial marker in canine tissues and has been studied in Kashin-Beck disease. The history of lectins started with the discovery of ricin about 130 years ago but since then our understanding of lectins has dramatically changed. They are drawn in yellow when only part of the sequences contains a signal peptide and/or a transmembrane region Nov 23, 2009 · Results Comprehensive in silico analyses indicate that the recently identified Euonymus europaeus lectin domain represents a conserved structural unit of a novel family of putative carbohydrate-binding proteins, which will further be referred to as the Euonymus lectin (EUL) family. Although the lectin reacts with several blood groups it does not react with A 1 blood group substance and it is not inhibited by any simple sugars. Technical Specifications:Ligand Source:Euonymus europaeusMolecular Weight: 140 kDaCarbohydrate Specificity:Galα1,3Galβ4GlcNAc, Fucα1,2 (Galα1,3)Galβ1,4GlcNAcInhibiting/Eluting Sugar:LactoseCarbohydrate for Elution: 0. Abstract Lectins are proteins with diverse molecular structures that share the ability to recognize and bind specifically and reversibly to carbohydrate structures without changing the carbohydrate moiety. 4Storage: -20°CApplication note Jul 1, 2017 · Domain architectures of class V chitinase-related agglutinin (CRA), Euonymus europaeus lectin (EUL), and Galanthus nivalis agglutinin (GNA) homologs. Sep 10, 2014 · Euonymus europaeus lectin (EEL) is a carbohydrate-binding protein derived from the fruit of the European spindle tree. Analysis of the deduced sequence indicated that EEA is synthesized Oct 14, 2011 · The Euonymus lectin (EUL) domain was recognized as the structural motif for a novel class of putative carbohydrate binding proteins. Molecular cloning of the “old” but still unclassified Euonymus europaeus agglutinin (EEA) demonstrated that the lectin is a homodimeric protein composed of 152 residue subunits. Nov 1, 2021 · In this review, we provide a historical introduction to lectins, their classification, and summarize the current knowledge about the roles plant lectins play in modulating the availability of photosynthates, and in cell signaling associated with various biological processes. Over the years the research focus was . The EUL domain is widespread among plants. Signal peptides and transmembrane regions are drawn in black when they are present in all sequences with this domain architecture. Euonymus europaeus lectin (EEL) is a carbohydrate-binding protein derived from the fruit of the European spindle tree. This lectin binds to endothelial cells from human and non-human sources and recognizes carbohydrate structures on the surface of stimulated murine peritoneal lymphoid cells. EEL was first identified for its erythrocyte agglutinating properties and specificity for B and H blood groups. Nov 23, 2009 · Comprehensive in silico analyses indicate that the recently identified Euonymus europaeus lectin domain represents a conserved structural unit of a novel family of putative carbohydrate-binding proteins, which will further be referred to as the Euonymus lectin (EUL) family. A lectin with complex blood group and carbohydrate specificity has been isolated from the seeds of the spindle tree. Confocal microscopy demonstrated that the lectin from Euonymus europaeus (EEA) as well as the EUL protein from Arabidopsis thaliana (ArathEULS3) are located in the nucleocytoplasmic compartment of the plant cell. The lectin of Euonymus europaeus at concentrations of 5-21 micrograms/ml causes activation of the classical complement (C) pathway (C1, C4, C2) when added to normal human serum at 37 degrees C. Comprehensive in silico analyses indicate that the recently identified Euonymus europaeus lectin domain represents a conserved structural unit of a novel family of putative carbohydrate-binding proteins, which will further be referred to as the Euonymus lectin (EUL) family. 2MLactoseBlood Group Specificity: O (-SA), BConjugate: FITCForm: LiquidIsoelectric (pI): 4. zzv uv mpeowl rfbb6 dada omb4 dfw k5ok 2q 2zd