Search results for: Asialoganglioside GM1
#29317695 // Save this To Up
Alterations in the properties of the cell membrane due to glycosphingolipid accumulation in a model of Gaucher disease.Gaucher disease is a lysosomal storage disease characterized by the malfunction of glucocerebrosidase resulting in the accumulation of glucosylceramide and other sphingolipids in certain cells. Although the disease symptoms are usually attributed to the storage of undigested substrate in lysosomes, here we show that glycosphingolipids accumulating in the plasma membrane cause profound changes in the properties of the membrane. The fluidity of the sphingolipid-enriched membrane decreased accompanied by the enlargement of raft-like ordered membrane domains. The mobility of non-raft proteins and lipids was severely restricted, while raft-resident components were only mildly affected. The rate of endocytosis of transferrin receptor, a non-raft protein, was significantly retarded in Gaucher cells, while the endocytosis of the raft-associated GM1 ganglioside was unaffected. Interferon-γ-induced STAT1 phosphorylation was also significantly inhibited in Gaucher cells. Atomic force microscopy revealed that sphingolipid accumulation was associated with a more compliant membrane capable of producing an increased number of nanotubes. The results imply that glycosphingolipid accumulation in the plasma membrane has significant effects on membrane properties, which may be important in the pathogenesis of Gaucher disease.
2962 related Products with: Alterations in the properties of the cell membrane due to glycosphingolipid accumulation in a model of Gaucher disease.FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu Cell Meter™ Fluorimetri Cell Meter™ Fluorimetri Thermal Shaker with cooli FDA Standard Frozen Tissu FDA Standard Frozen Tissu Multiple organ tumor tiss Oral squamous cell cancer Toxoplasma gondii GRA8, r
#28955740 // Save this To Up
Characterization of lipid rafts in human platelets using nuclear magnetic resonance: A pilot study.Lipid microdomains ('lipid rafts') are plasma membrane subregions, enriched in cholesterol and glycosphingolipids, which participate dynamically in cell signaling and molecular trafficking operations. One strategy for the study of the physicochemical properties of lipid rafts in model membrane systems has been the use of nuclear magnetic resonance (NMR), but until now this spectroscopic method has not been considered a clinically relevant tool. We performed a proof-of-concept study to test the feasibility of using NMR to study lipid rafts in human tissues. Platelets were selected as a cost-effective and minimally invasive model system in which lipid rafts have previously been studied using other approaches. Platelets were isolated from plasma of medication-free adult research participants (n=13) and lysed with homogenization and sonication. Lipid-enriched fractions were obtained using a discontinuous sucrose gradient. Association of lipid fractions with GM1 ganglioside was tested using HRP-conjugated cholera toxin B subunit dot blot assays. 1H high resolution magic-angle spinning nuclear magnetic resonance (HRMAS NMR) spectra obtained with single-pulse Bloch decay experiments yielded spectral linewidths and intensities as a function of temperature. Rates of lipid lateral diffusion that reported on raft size were measured with a two-dimensional stimulated echo longitudinal encode-decode NMR experiment. We found that lipid fractions at 10-35% sucrose density associated with GM1 ganglioside, a marker for lipid rafts. NMR spectra of the membrane phospholipids featured a prominent 'centerband' peak associated with the hydrocarbon chain methylene resonance at 1.3 ppm; the linewidth (full width at half-maximum intensity) of this 'centerband' peak, together with the ratio of intensities between the centerband and 'spinning sideband' peaks, agreed well with values reported previously for lipid rafts in model membranes. Decreasing temperature produced decreases in the 1.3 ppm peak intensity and a discontinuity at ~18 °C, for which the simplest explanation is a phase transition from Ld to Lo phases indicative of raft formation. Rates of lateral diffusion of the acyl chain lipid signal at 1.3 ppm, a quantitative measure of microdomain size, were consistent with lipid molecules organized in rafts. These results show that HRMAS NMR can characterize lipid microdomains in human platelets, a methodological advance that could be extended to other tissues in which membrane biochemistry may have physiological and pathophysiological relevance.
2269 related Products with: Characterization of lipid rafts in human platelets using nuclear magnetic resonance: A pilot study.Anti AGO2 Human, Monoclon Anti AGO2 Human, Monoclon Human Macrophage Inflamma Human Macrophage Inflamma Human Interleukin-32 alph Human Interleukin-1-alpha Interferon-a Receptor Typ Goat Anti-Human Synaptota Goat Anti-Human STK39 SPA Goat Anti-Human SPHK1, (i Goat Anti-Human SODD, (in Goat Anti-Human SIGLEC8,
#28935104 // Save this To Up
Syntheses of Fluorescent Gangliosides for the Studies of Raft Domains.Gangliosides, glycosphingolipids containing one or more sialic acids in the glycan chain, are involved in various important biological processes in cell plasma membranes (PMs). However, the behaviors and functions of gangliosides are poorly understood, primarily because of the lack of fluorescent analogs that are equivalent to native gangliosides that can be used as chemical and physical probes. In this study, we developed entirely chemical methods to synthesize fluorescent gangliosides (GM3, GM2, GM1, and GD1b) in which the glycan components are site-specifically labeled with various fluorescent dyes. The functional evaluations of the synthesized fluorescent gangliosides demonstrated the great influence of fluorescent dye on the physical properties of gangliosides in PMs and revealed the fluorescent ganglioside analogs which show similar behaviors to the native gangliosides.
N,N,N Trimethyl 4 (6 phen MarkerGeneTM Fluorescent Ofloxacin CAS Number [824 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
#28894900 // Save this To Up
Interaction Between Luteinizing Hormone-Releasing Hormone and GM1-Doped Cholesterol/Sphingomyelin Vesicles: A Spectroscopic Study.Understanding the role of neural membrane in translocation and action of neurohormone is of great importance. Luteinizing hormone-releasing hormone (LHRH) is a neuropeptide hormone and it acts as a final signaling molecule by stimulating the synthesis of LH and FSH to maintain reproduction in all vertebrates. The receptors of LHRH are found in breast tumors and pituitary gland in the brain. Moreover, neural plasma membrane is also found to contain specific binding site for LHRH. The mechanism by which LHRH binds to membrane before it binds to the receptors is a very critical step and can have a profound impact upon the translation of peptide across the membrane. A complex form of glycosphingolipids known as Ganglioside is an important component of plasma membrane of nerve cells and breast tumor tissues. They play an important role in various physiological membrane processes. Therefore, the interaction of ganglioside-containing membrane with LHRH might be crucial in aiding the LHRH to translate through the neural membrane and reach its receptor for binding and activation. Using CD, UV-Absorbance, and fluorescence spectroscopy, the effect of Ganglioside Monosialo 1(GM1)-induced conformational changes of LHRH in the presence of Cholesterol (CHOL)/Sphingomyelin (SM) and GM1/CHOL/SM vesicles was studied. The aforesaid spectroscopic studies show that LHRH is able to bind with both the vesicles, but GM1-containing vesicles interact more effectively than vesicles without GM1. CHOL/SM vesicles partially disturb the conformation of the peptide. Moreover, binding of LHRH to GM1/CHOL/SM vesicles induces loss of conformational rigidity and attainment of a random coil.
2271 related Products with: Interaction Between Luteinizing Hormone-Releasing Hormone and GM1-Doped Cholesterol/Sphingomyelin Vesicles: A Spectroscopic Study.MOUSE ANTI HUMAN LUTEINIZ Luteinizing Hormone Relea Luteinizing Hormone Relea Epidermal Growth Factor ( Epidermal Growth Factor ( Human Growth Hormone anti Human Growth Hormone anti Human Growth Hormone anti Mouse Anti-Human Thyroid Mouse Anti-Human Thyroid Rat adrencocorticotropic Rat growth hormone releas
#28796418 // Save this To Up
Role of the GM1 ganglioside oligosaccharide portion in the TrkA-dependent neurite sprouting in neuroblastoma cells.GM1 ganglioside (II3 NeuAc-Gg4 Cer) is known to promote neurite formation in neuroblastoma cells by activating TrkA-MAPK pathway. The molecular mechanism by which GM1 is involved in the neurodifferentiation process is still unknown, however, in vitro and in vivo evidences have suggested that the oligosaccharide portion of this ganglioside could be involved. Here, we report that, similarly to the entire GM1 molecule, its oligosaccharide II3 NeuAc-Gg4, rather than its ceramide (Cer) portion is responsible for the neurodifferentiation process by augmenting neurite elongation and increasing the neurofilament protein expression in murine neuroblastoma cells, Neuro2a. Conversely, asialo-GM1, GM2 and GM3 oligosaccharides are not effective in neurite elongation on Neuro2a cells, whereas the effect exerted by the Fuc-GM1 oligosaccharide (IV2 αFucII3 Neu5Ac-Gg4 ) is similar to that exerted by GM1 oligosaccharide. The neurotrophic properties of GM1 oligosaccharide are exerted by activating the TrkA receptor and the following phosphorylation cascade. By photolabeling experiments performed with a nitrophenylazide containing GM1 oligosaccharide, labeled with tritium, we showed a direct interaction between the GM1 oligosaccharide and the extracellular domain of TrkA receptor. Moreover, molecular docking analyses confirmed that GM1 oligosaccharide binds the TrkA-nerve growth factor complex leading to a binding free energy of approx. -11.5 kcal/mol, acting as a bridge able to increase and stabilize the TrkA-nerve growth factor molecular interactions.
1523 related Products with: Role of the GM1 ganglioside oligosaccharide portion in the TrkA-dependent neurite sprouting in neuroblastoma cells.Thermal Shaker with cooli FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu Multiple organ tumor tiss MultiGene Gradient therm anti HSV (II) gB IgG1 (mo anti HCMV IE pp65 IgG1 (m anti HCMV gB IgG1 (monocl
#28778444 // Save this To Up
Tumor necrosis factor-alpha -863C/A polymorphism is associated with Guillain-Barré syndrome in Bangladesh.Guillain-Barré syndrome (GBS) is a post-infectious autoimmune polyneuropathy regulated by pro- and anti-inflammatory cytokines; TNFA polymorphisms may exert immune pathogenic roles in GBS. We assessed TNFA promoter region polymorphisms (-238G/A, -308G/A, -857C/T, -863C/A) in Bangladeshi patients with GBS (n=300) and healthy controls (n=300) by PCR-RFLP and ASO-PCR. TNFA -863CA was significantly associated with GBS disease susceptibility (P=0.0154) and disease severity (P=0.0492). TNFA -238A allele was more frequent among anti-ganglioside (GM1) antibody-positive patients (P=0.0092) and -863AA associated with AMAN subtype of GBS (P=0.0398). TNFA -863C/A may contribute to GBS severity and pathogenesis in Bangladeshi patients.
1667 related Products with: Tumor necrosis factor-alpha -863C/A polymorphism is associated with Guillain-Barré syndrome in Bangladesh.ELISA Kit for Tumor Necr Human Tumor Necrosis Fact TNFRSF1B - Goat polyclona Mouse Tumor Necrosis Fact Rat Tumor Necrosis Factor ELISA Kit for Tumor Necro Mouse Tumor Necrosis Fact Human Tumor Necrosis Fact Tumor necrosis factor (TN RANK Ligand Soluble, Huma Rabbit Anti-Insulin Recep Rabbit Anti-Insulin Recep
#28734966 // Save this To Up
Development of new ganglioside probes and unraveling of raft domain structure by single-molecule imaging.Gangliosides are involved in a variety of biological roles and are a component of lipid rafts found in cell plasma membranes (PMs). Gangliosides are especially abundant in neuronal PMs and are essential to their physiological functions. However, the dynamic behaviors of gangliosides have not been investigated in living cells due to a lack of fluorescent probes that behave like their parental molecules. We have recently developed, using an entirely chemical method, four new ganglioside probes (GM1, GM2, GM3, and GD1b) that act similarly to their parental molecules in terms of raft partitioning and binding affinity. Using single fluorescent-molecule imaging, we have found that ganglioside probes dynamically enter and leave rafts featuring CD59, a GPI-anchored protein. This occurs both before and after stimulation. The residency time of our ganglioside probes in rafts with CD59 oligomers was 48ms, after stimulation. The residency times in CD59 homodimer and monomer rafts were 40ms and 12ms, respectively. In this review, we introduce an entirely chemical-based ganglioside analog synthesis method and describe its application in single-molecule imaging and for the study of the dynamic behavior of gangliosides in cell PMs. Finally, we discuss how raft domains are formed, both before and after receptor engagement. This article is part of a Special Issue entitled Neuro-glycoscience, edited by Kenji Kadomatsu and Hiroshi Kitagawa.
1589 related Products with: Development of new ganglioside probes and unraveling of raft domain structure by single-molecule imaging.Ofloxacin CAS Number [824 PolyTek HRP Anti-Rabbit PolyTek HRP Anti-Mouse P Diaph1 FH3 domain (75 440 Diaph1 FH2 domain (752 11 E. coli SSB (Single Stran E. coli SSB (Single Stran E. coli SSB (Single Stran E. coli SSB (Single Stran Taq SSB (Single Stranded Taq SSB (Single Stranded COOH Modified Single Wall
#28673733 // Save this To Up
Enhanced soluble production of cholera toxin B subunit in Escherichia coli by co-expression of SKP chaperones.The cholera toxin B subunit (CTB) is a nontoxic portion of the cholera toxin that retains mucosal adjuvant properties. Expression of CTB in Escherichia coli is difficult as CTB aggregates and accumulates as insoluble inclusion bodies. To remedy this problem, the periplasmic chaperone, SKP, was investigated as possible co-expression partner to increase the solubility of recombinant CTB (rCTB) in E. coli. The result showed co-expression of SKP enhanced the soluble expression of rCTB in E. coli. Moreover, soluble rCTB was successfully expressed and secreted into the periplasmic space through the direction of the LTB leader signal. rCTB in periplasm was purified using an immobilized d-galactose resin; GM1-ELISA experiments showed that rCTB retains strong GM1 ganglioside-binding activity. Intranasal administration of ovalbumin (OVA) with rCTB significantly induced both mucosal and humoral immune responses specific to OVA. These data indicate that co-expression of the molecular chaperone SKP with CTB increased the solubility of rCTB while maintaining its function.
2582 related Products with: Enhanced soluble production of cholera toxin B subunit in Escherichia coli by co-expression of SKP chaperones.Rabbit Anti-Cholera Toxin RANK Ligand Soluble, Huma RANK Ligand Soluble, Huma BYL-719 Mechanisms: PI3K- Mouse Anti-Cholera Toxin Octyl â D 1 thioglucopyr pCMVLuxA Mammalian LuxA E pCMVLuxB Mammalian LuxB E pCAMBIA0105.1R Vector, (G Mouse Anti-Cholera Toxin BCIP INT Solution BCIP INT Solution
#28628327 // Save this To Up
Impact of the Niemann-Pick c1 Gene Mutation on the Total Cellular Glycomics of CHO Cells.Niemann-Pick disease type C (NPC) is an autosomal recessive lipid storage disorder, and the majority of cases are caused by mutations in the NPC1 gene. In this study, we clarified how a single gene mutation in the NPC1 gene impacts the cellular glycome by analyzing the total glycomic expression profile of Chinese hamster ovary cell mutants defective in the Npc1 gene (Npc1 KO CHO cells). A number of glycomic alterations were identified, including increased expression of lactosylceramide, GM1, GM2, GD1, various neolacto-series glycosphingolipids, and sialyl-T (O-glycan), which was found to be the major sialylated protein-bound glycan, as well as various N-glycans, which were commonly both fucosylated and sialylated. We also observed significant increases in the total amounts of free oligosaccharides (fOSs), especially in the unique complex- and hybrid-type fOSs. Treatment of Npc1 KO CHO cells with 2-hydroxypropyl-β-cyclodextrin (HPBCD), which can reduce cholesterol and glycosphingolipid (GSL) storage, did not affect the glycomic alterations observed in the GSL-, N-, and O-glycans of Npc1 KO CHO cells. However, HPBCD treatment corrected the glycomic alterations observed in fOSs to levels observed in wild-type cells.
1672 related Products with: Impact of the Niemann-Pick c1 Gene Mutation on the Total Cellular Glycomics of CHO Cells.FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu BACTERIOLOGY BACTEROIDES TCP-1 theta antibody Sour Recombinant Thermostable Recombinant Thermostable Recombinant Thermostable Recombinant HBsAg adr [fr Recombinant HBsAg adr [fr Recombinant HBsAg adr [fr
#28499815 // Save this To Up
New insight into the interaction of TRAF2 C-terminal domain with lipid raft microdomains.In this study we provide the first evidence of the interaction of a truncated-TRAF2 with lipid raft microdomains. We have analyzed this interaction by measuring the diffusion coefficient of the protein in large and giant unilamellar vesicles (LUVs and GUVs, respectively) obtained both from synthetic lipid mixtures and from natural extracts. Steady-state fluorescence measurements performed with synthetic vesicles indicate that this truncated form of TRAF2 displays a tighter binding to raft-like LUVs with respect to the control (POPC-containing LUVs), and that this process depends on the protein oligomeric state. Generalized Polarization measurements and spectral phasor analysis revealed that truncated-TRAF2 affects the membrane fluidity, especially when vesicles are heated up at physiological temperature. The addition of nanomolar concentration of TRAF2 in GUVs also seems to exert a mechanical action, as demonstrated by the formation of intraluminal vesicles, a process in which ganglioside GM1 plays a crucial role.
1263 related Products with: New insight into the interaction of TRAF2 C-terminal domain with lipid raft microdomains.TRAF2 & ACTG1 Protein Pro TRAF2 & CHUK Protein Prot TRAF2 & ERN1 Protein Prot TRAF2 & FLNA Protein Prot TRAF2 & CDKN1B Protein Pr TRAF2 & MAPK9 Protein Pro IKBKB & TRAF2 Protein Pro TRAF2 & TRAF1 Protein Pro TRAF2 & FRAP1 Protein Pro TRAF2 & ZBTB16 Protein Pr APPL1 & TRAF2 Protein Pro GSTP1 & TRAF2 Protein Pro
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45 Fax 0032 16 50 90 45
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50 Fax 01 43 25 01 60
52062 Aachen Deutschland
Tel 0241 40 08 90 86 Fax 0241 55 91 05 36
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
Schweiz Züri +41435006251
Česká republika Praha +420246019719
Ireland Dublin +35316526556
Norge Oslo +4721031366
Finland Helsset +358942419041
Sverige Stockholm +46852503438
Ελλάς Αθήνα +302111768494
Magyarország Budapest +3619980547
GENTAUR Poland Sp. z o.o.
ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
Tel 058 710 33 44
Fax 058 710 33 48
GENTAUR Nederland BV
5521 DG Eersel Nederland
Tel 0208-080893 Fax 0497-517897
Piazza Giacomo Matteotti, 6, 24122 Bergamo
Tel 02 36 00 65 93 Fax 02 36 00 65 94
53 Iskar Str. 1191 Kokalyane, Sofia