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Glutamate

Glutamate is a key neurotransmitter in the central nervous system, playing crucial roles in neuronal function, synaptic plasticity, and brain development.
It is the most abundant excitatory neurotransmitter, involved in a wide range of physiological and pathological processes.
Glutamte is synthesized from glutamine and is responsible for mediating fast excitatory synaptic transmission.
Dysregulation of glutamate signaling has been implicated in various neurological and psychiatric disorders, making it an important target for research and drug development.
Understanding the complex biology of glutamate is essential for advancing our knowledge of brain function and developing effective therapies.

Most cited protocols related to «Glutamate»

Improved Salt Bridge Interactions in CHARMM36

Cited 119 times

Another refinement in the C36m FF concerns improved description of salt bridge interactions involving guanidinium and carboxylate functional groups with a pair-specific non-bonded LJ parameter (NBFIX term in CHARMM) between the guanidinium nitrogen in arginine and the carboxylate oxygen in glutamate, aspartate as well as the C terminus. This salt bridge interaction was found to be too favorable in the CHARMM protein force fields as indicated by the overestimation of the equilibrium association constant of a guanidinium-acetate solution ,^{33 , 34} as well as the underestimation of its osmotic pressure (personal communication, Benoit Roux). The added NBFIX term increases the R_min from the 3.55 Å based on the Lorentz-Berthelot rule to a larger value of 3.637 Å (Shen and Roux, personal communication), which we subsequently showed to improve the agreement with the experimental osmotic pressure of guanidinium acetate solutions (Supplementary Figure 19). We noted that the NBFIX approach employed here differs from Piana et al’s work²⁷ where the CHARMM22 charges of the Arg, Asp and Glu side chains were reduced in magnitude, with both approaches leading to weaker and more realistic salt-bridge interactions. The NBFIX term makes sure only the specific interaction between Arg and Asp/Glu is modified, while the interaction of these residues with other amino acids, water, or ions are kept the same as in the C36 FF. Again, our aim is to improve the C36 FF with minimal changes in the model.

Huang J., Rauscher S., Nawrocki G., Ran T., Feig M., de Groot B.L., Grubmüller H, & MacKerell AD J.r. (2016). CHARMM36m: An Improved Force Field for Folded and Intrinsically Disordered Proteins. Nature methods, 14(1), 71-73.

Publication 2016

Acetate Amino Acids Arginine Aspartate aspartylglutamate Glutamate Guanidine Ions Nitrogen Osmotic Pressure Oxygen Proteins Sodium Chloride

Structural Insights into GluCl Receptor

Cited 58 times

GluCl_cryst was expressed from baculovirus-infected Sf9 cells and purified by metal ion affinity chromatography. The Fab complex was isolated by size-exclusion chromatography. The GluCl_cryst-Fab complex was concentrated to 1-2 mg/mL and supplemented with synthetic lipids and ivermectin. Crystallization was performed by hanging drop vapor diffusion at 4°C with a precipitating solution containing 21-23% PEG 400, 50 mM sodium citrate pH 4.5 and 70 mM sodium chloride. Cryoprotection was achieved by soaking crystals in precipitant solution supplemented with 30% PEG 400. Additional complexes were obtained by soaking crystals in cryoprotectant containing L-glutamate, picrotoxin or sodium iodide. Diffraction data were indexed, integrated and scaled and the structure solved by molecular replacement using a GLIC-derived homology model of GluCl_cryst and a Fab homology model as search probes. The molecular replacement phases were used to initiate autobuilding and the resulting model was iteratively improved by cycles of manual adjustment and crystallographic refinement. Function of GluCl was examined by two-electrode voltage clamp experiments and by [³H]-L-glutamate saturation and competition binding assays.

Hibbs R.E, & Gouaux E. (2011). Principles of activation and permeation in an anion-selective Cys-loop receptor. Nature, 474(7349), 54-60.

Publication 2011

Baculoviridae Biological Assay Chromatography, Affinity Cryoprotective Agents Crystallization Crystallography Diffusion Gel Chromatography Glutamate Ivermectin Lipids Metals Picrotoxin polyethylene glycol 400 Sf9 Cells Sodium Chloride Sodium Citrate Sodium Iodide

Computational Metabolomics: Correlations and Identification

Cited 43 times

An important advantage of computational metabolomics lies in the use of correlations among ion signals to aid in determination of chemical identity. Metabolites are interconnected by a series of biochemical reactions, and this network of metabolites is organized in a hierarchical manner such that many small modules combine to form larger modules.^{56 (link),57} Correlation-based network and modularity analysis is one approach to elucidate the association structure of metabolites. Although there are several mechanisms that could lead to correlations between metabolites, the association structure can be used to identify ions derived from the same metabolite,^{58 (link)–60 (link)} identify biotransformations,^{61 (link)} and detect associations between environmental exposures and endogenous metabolites.^{15 (link)}For high abundance unidentified chemicals, multiple spectral features arising from a single chemical provide valuable structural information to characterize a chemical. A network of ions where a pair of ions is linked if their correlation exceeds the significance threshold, e.g., |r| > 0.8, can be generated to identify isotopes, adducts, and in-source fragments associated with a chemical (Figure 4). A similar approach can be used to identify biotransformations and other related metabolites.^{60 (link)} Metabolome-wide association studies (MWAS) allow identification of associations between a specific target variable, e.g., cotinine levels in individuals, and metabolic profiles.^{8 (link),62 (link)–64 (link)} In an MWAS, statistical tests are performed for association of a parameter (e.g., disease biomarker, chemical, or other measured parameter) with each m/z feature to test for significance of association. Application of targeted MWAS using correlation-based criteria identified choline-related metabolites and demonstrated similarity between correlation patterns of choline in different species (Figure 5).^{64 (link)}Correlation-based network analysis can also facilitate identification of in-source fragments. Gas-chromatography–mass spectrometry with electron ionization sources results in a large number of characteristic spectra indicative of chemical functional groups and structure.^{61 (link),65} Electrospray ionization can produce in-source fragmentation (e.g., loss of NH₃, H₂O, CHOOH, etc.) from electrical potentials or heat applied in the ion source.^{66 (link),67 (link)} Because in-source fragments can mimic accurate masses of other common metabolites, computational methods that identify adducts, isotopes, and in-source fragments (based on clustering of highly correlated coeluting ions) increases the ability to correctly assign chemical identities. An example is the in-source formation of pyroglutamate from glutamine or glutamate.^{68 (link)} The identification of in-source fragments requires consideration of chromatographic conditions to separate possible coeluting chemicals, as well as ion source conditions. When using soft ionization techniques, in-source fragmentation is only commonly observed for highly abundant metabolites, many low abundance chemicals will generate only a single detectable signal.^{3 (link),18 (link)} To ensure detected, unannotated ions are unique chemicals, it is important to perform targeted MWAS to exclude the possibility of a signal originating from source fragments, adducts, and/or isotopes. To increase confidence of chemical identification, alternative detection methods with increased sensitivity for unknown chemicals and methods for defining unknown ions will be needed.
In addition to characterizing ions arising from known chemicals, MWAS using univariate and multivariate approaches can be used to generate hypotheses about biochemical roles of features with no database matches. This process uses targeted MWAS with validated metabolites or xMWAS, where “x” corresponds to other–omes (transcriptome, microbiome, genome, etc.). Krumsiek et al. used a systems-level approach where they combined genome-wide association analysis, knowledge-based pathway information, and metabolic networks to predict the identity of unknown metabolites.^{69 (link)} Other studies have used integrative methods based on partial least-squares regression (PLS) to determine correlations between the metabolome and the transcriptome,⁷⁰ proteome,^{71 (link)} and microbiome.^{72 (link)} These methods combined with pathway and literature based information can provide alternative approaches for generating hypotheses about chemical identity, particularly for low abundance chemicals.

Uppal K., Walker D.I., Liu K., Li S., Go Y.M, & Jones D.P. (2016). Computational Metabolomics: A Framework for the Million Metabolome. Chemical research in toxicology, 29(12), 1956-1975.

Publication 2016

Biological Markers Biotransformation Choline Chromatography Cotinine Electricity Electrons Environmental Exposure Gas Chromatography-Mass Spectrometry Genome Genome-Wide Association Study Glutamate Glutamine Hypersensitivity Ions Isotopes Metabolic Networks Metabolic Profile Metabolome Microbiome Proteome Pyroglutamate Transcriptome

Advancing White Matter Imaging Techniques

Cited 41 times

Though the vast majority of recent MRI studies of white matter have focused on diffusion, MT or relaxometry, there are other techniques that may provide complementary information. One of the oldest methods is MR spectroscopy, which may be used to characterize specific metabolites in the tissue including NAA (N-acetylaspartate), creatine, choline and neurotransmitters like GABA and glutamine/glutamate. Each of these metabolites reflects different physiological processes and have unique spectral signatures. Of significant interest in white matter is NAA, which is a marker of the presence, density and health of neurons including the axonal processes. In fact, NAA may be one of the most specific markers of healthy axons and, as such, it is surprising that it is not used more widely for the investigation of white matter in the brain. This may be due in part to the fact that MR spectroscopy is extremely sensitive to the homogeneity of the magnetic field, which makes it challenging to apply in areas near air or bone interfaces. The concentrations of the metabolites are also in the micromolar range (compare with multiple molar for water), thus, large voxels must be used and the acquisition speed is slow. Therefore, MR spectroscopy studies are often limited by poor coverage, poor resolution, and long scan times.
The recent push towards ever higher magnetic fields makes quantitative MRI methods more challenging. Imaging distortions in DTI studies increase proportional to the field strength. The RF power deposition (SAR – specific absorption rate) increases quadratically with the magnetic field strength, which limits the application of MT pulses and can also limit the flip angles used in steady state imaging. However, susceptibility weighted imaging is one method that greatly benefits from higher magnetic field strengths. Recent studies have observed interesting contrast in white matter tracts as a function of orientation and degree of myelination (Liu et al., 2011 ). Stunning images of white matter tracts have recently been obtained in ex vivo brain specimens (Sati et al., 2011 ). Techniques for characterizing white matter in the human brain are only beginning to be developed.
Other white matter cellular components are the glia, which include oligodendrocytes, astrocytes, and microglia. In general, there are no specific markers of changes in either oligodendrocytes or astrocytes. Recent evidence suggests that hypointense white matter lesions on T1w imaging may indicate reactive astrocytes (Sibson et al., 2008 (link)). Increases in microglia often accompany inflammation, which can be detected using contrast agents, either gadolinium or superparamagnetic iron oxide (SPIO) particles. Recent studies have suggested that SPIO particles are preferentially taken up by macrophages in inflammatory regions. The impact of these contrast agents on other quantitative MRI measures have not (Oweida et al., 2004 (link)) been widely studied, thus multimodal imaging studies must be designed carefully.

Alexander A.L., Hurley S.A., Samsonov A.A., Adluru N., Hosseinbor A.P., Mossahebi P., Tromp D.P., Zakszewski E, & Field A.S. (2011). Characterization of Cerebral White Matter Properties Using Quantitative Magnetic Resonance Imaging Stains. Brain Connectivity, 1(6), 423-446.

Publication 2011

Astrocytes Axon Bones Brain Cellular Structures Choline Contrast Media Creatine Diffusion ferric oxide Gadolinium gamma Aminobutyric Acid Glutamate Glutamine Homo sapiens Inflammation Macrophage Magnetic Fields Magnetic Resonance Spectroscopy Microglia Molar Myelin Sheath N-acetylaspartate Neuroglia Neurons Neurotransmitters Oligodendroglia Physiological Processes Pulses Radionuclide Imaging Susceptibility, Disease Tissues White Matter

Cell Culture Maintenance Protocols

Cited 32 times

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Publication 2011

antibiotic G 418 Antibiotics Cells Culture Media Glutamate Growth Factor hygromycin A Penicillins Puromycin Streptomycin

Most recents protocols related to «Glutamate»

Characterization of Plasmodium falciparum Glutamine Synthetase

Not available on PMC !

Example 2

Prokaryotic GS-I proteins found in some eukaryotes frequently display no GS catalytic activity and may have different functions. In humans, for example, most tissues/organs express only catalytically-active GS-II. In contrast, human GS-I does not exhibit GS activity. It is expressed only in the lens of the eye and has designated lengsin (lens GS-like protein), probably with a structural role.

To examine the catalytic activity of PfGS-I, PfGS-I gene was cloned and expressed in E. coli and then GS activity of the purified protein was assayed. PfGS-I produced glutamine from glutamate in the presence of ATP, Mg²⁺ and ammonia (FIG. 2A) demonstrates that PfGS-I is a functional GS.

US11877996B1. Arsinothricin as a multi-stage antimalarial (2024-01-23). None [US], None [US], None [US], None [US]. Inventors: Masafumi Yoshinaga [US], Barry P. Rosen [US], Jun Li [US], Guodong Niu [US].

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Patent 2024

Ammonia enzyme activity Escherichia coli Eukaryota Genes Glutamate Glutamine Homo sapiens Lens, Crystalline Prokaryotic Cells Proteins Synapsin I Tissues

Enhancing Klotho Expression and Neuroprotection

Not available on PMC !

Example 5

To determine whether the ZFP3 constructs increase Klotho expression in mice, the ZFP3 constructs were transfected into a N2a knock-in line which comprises NLuc inserted into 3′-UTR of the Klotho gene (Chen et al., 2018. J. Mol. Neurosci. 64(2): 175-184). Referring to FIG. 5, both ZFP3_Egr1_site3 and ZFP3 VPR increased Klotho gene expression.

Next, a glutamate toxicity assay was performed using a HT-22 hippocampal cell line as a model for neuronal death by oxidative damage. Cytotoxicity was assayed as described by Zeldich et al. (2014. J. Biol. Chem. 289: 24700-15). Transfection of HT-22 cells with ZFP3_VPR significantly increased cell viability in the presence of either 3 mM or 4 mM glutamate as measured by CellTiter-Glo (FIG. 6). Over-expression of the extracellular domain of Klotho (KL980 construct) also increased cell viability, but the effects were not as substantial (FIG. 6).

US11866469B2. DNA binding proteins and uses thereof (2024-01-09). Klogenix LLC [US]. Inventors: Ci-Di Chen [US].

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Patent 2024

Cell Lines Cells Cell Survival Cytotoxin DNA-Binding Proteins EGR1 protein, human Gene Expression Genes Glutamate KL protein, human Mus Neurons Oxidative Damage Transfection

Tyrode and Extracellular Solutions for Voltage-Clamp Experiments

Tyrode solution contained (in mM) 140 NaCl, 5 KCl, 2.5 CaCl₂, 2 MgCl₂, and 10 HEPES. The standard extracellular solution for voltage-clamp experiments contained (in mM) 140 TEA-methane-sulfonate, 2.5 CaCl₂, 2 MgCl₂, 1 4-aminopyridine, 10 HEPES, and 0.002 tetrodotoxin. For the experiments described in Figs. 1 and 2, the extracellular solution also contained 0.33% DMSO. The standard pipette solution contained (in mM) 120 K-glutamate, 5 Na₂-ATP, 5 Na₂-phosphocreatine, 5.5 MgCl₂, 5 glucose, and 5 HEPES. For measurements of rhod-2 Ca²⁺ transients, it also contained 15 EGTA, 6 CaCl₂, and 0.1 rhod-2. For measurements with fluo-4, isolated muscle fibers were incubated for 30 min in the presence of Tyrode solution containing 10 μM fluo-4 AM. All solutions were adjusted to pH 7.20. The Ringer solution used for muscle force measurements contained (in mM) 140 NaCl, 6 KCl, 3 CaCl₂, 2 MgCl₂, and 10 HEPES, adjusted to pH 7.40.
Probenecid was prepared as a 0.3 M aliquoted stock solution in DMSO and used in the extracellular solution at 0.5, 1, or 2 mM. Carbenoxolone was prepared as a 10 mM stock solution in the extracellular solution and used at 0.1 mM. These concentrations were chosen on the basis of their effectiveness and wide use to block Panx1 channels throughout the literature (e.g., Dahl et al., 2013 (link)). When testing the effect of either probenecid or carbenoxolone using the preincubation protocol (Figs. 1 and 2), fibers were bathed in the drug-containing extracellular solution from the beginning of the intracellular dialysis with the rhod-2-containing solution (i.e., 30 min before taking measurements). The ¹⁰panx1 peptide and the scrambled control peptide (¹⁰panx1SCr) were tested under the same conditions at 200 µM while the P2Y2 antagonist AR-C 118925XX was tested at 10 µM. All chemicals and drugs were purchased from Sigma-Aldrich, except for tetrodotoxin (Alomone Labs), rhod-2 and fluo-4 (Thermo Fisher Scientific), and AR-C 118925XX (TOCRIS—Bio-Techne).
In vitro fluorescence measurements using droplets of a solution containing (in mM) 120 K-glutamate, 10 HEPES, 15 EGTA, 6 CaCl₂, and 0.1 rhod-2, with or without probenecid, showed that fluorescence intensity in the presence of 1 mM probenecid corresponded to 1.09 ± 0.12% (n = 6) the intensity in the absence of probenecid, excluding an interaction of the drug with the dye to explain the effect on resting fluorescence in muscle fibers.

Jaque-Fernandez F., Allard B., Monteiro L., Lafoux A., Huchet C., Jaimovich E., Berthier C, & Jacquemond V. (2023). Probenecid affects muscle Ca2+ homeostasis and contraction independently from pannexin channel block. The Journal of General Physiology, 155(4), e202213203.

Publication 2023

Aminopyridines Carbenoxolone Cardiac Arrest Dialysis Solutions Drug Interactions Egtazic Acid Figs Fluo 4 Fluorescence Glucose Glutamate HEPES Magnesium Chloride methanesulfonate Muscle Tissue P2RY2 protein, human Peptides Pharmaceutical Preparations Phosphocreatine Probenecid Protoplasm rhod-2 Ringer's Solution Sodium Chloride Sulfoxide, Dimethyl Tetrodotoxin Transients Tyrode's solution

Culturing HEK293T and Primary Murine T Cells

HEK293T cells (ATCC), used for retroviral packaging, were passaged in DMEM supplemented with 10% FBS and penicillin/streptomycin. Primary murine T cells were cultured in RPMI-1640 supplemented with 10% FBS, penicillin/streptomycin, L-glutamate, and 2-mercaptoethanol (T cell media). All cells were maintained in a humidified incubator with 5% CO₂ at 37°C.

Seth A., Yokokura Y., Choi J.Y., Shyer J.A., Vidyarthi A, & Craft J. (2023). AP-1–independent NFAT signaling maintains follicular T cell function in infection and autoimmunity. The Journal of Experimental Medicine, 220(5), e20211110.

Publication 2023

2-Mercaptoethanol Cells Glutamate Mus Penicillins Retroviridae Streptomycin T-Lymphocyte

Isolation and Treatment of Striatal Neurons

Primary striatal neurons were isolated from ICR mice at embryonic day 17 as previously described (Fitting et al., 2014 (link); Zou et al., 2011 (link)). Briefly, striatal tissues were dissected, minced, and incubated for 30 min at 37^oC in neurobasal medium (NBM) containing 0.015 mg/mL DNase and 2.5 mg/ml trypsin. NBM was supplemented with 25 mM glutamate, 0.5 mM glutamine, B27 (Invitrogen), and an antibiotic-antimycotic solution (Sigma). Cells were then triturated, filtered (2×) through a 70 μm-diameter pore membrane, and seeded into six-well plates (15 × 10⁵ neurons/well) pre-coated with poly-L-lysine. Cells were maintained in NBM supplemented at decreasing concentrations of glutamate (days 1–4, 25 mM; days 5–6, 12.5 mM; days 7–11, 0 mM) at 37^oC in a 5% CO₂ environment until they matured (at 11 days). Based on our findings that TDP-43 phosphorylation was greatest following co-exposure to morphine and Tat in murine brain tissues, and to optimize detecting alterations in TDP-43 phosphorylation, we co-exposed cells to Tat and morphine to verify the involvement of CK2 in the pathologic TDP-43 phosphorylation. Cells were either treated with vehicle (DNase/RNase-free non-pyrogenic Ultrapure water), co-treated with Tat (100 nM) and morphine (500 nM), or a combination of Tat, morphine, and 0.5, 1, or 2 µM concentrations of the highly selective CK2 antagonist CX-4945 (#A11060, AdooQ Bioscience, Irvine, CA). CX-4945 (Silmitasertib) was granted Orphan Drug Designation by the US FDA in December 2021 for the treatment of medulloblastoma and potentially other rare diseases targeting CK2. Vehicle-treated cells served as controls. The selected concentrations of Tat and morphine do not affect cell viability within 24 h (Zou et al., 2011 (link)). The doses of CX-4945 selected for testing are those previously determined to reduce pro-inflammatory mediators to baseline levels in immune cells (Jang et al., 2017 (link)). Treated neurons were incubated at 37^oC in a 5% CO₂ environment for 24 h. Afterward, the cells were harvested, and the cytoplasmic and nuclear fractions were extracted using a NE-PER nuclear and cytoplasmic extraction kit (Thermo Fisher). BCA was used to determine protein concentrations and samples were stored in aliquots at −80^oC until use.

Ohene-Nyako M., Nass S.R., Richard H.T., Lukande R., Nicol M.R., McRae M., Knapp P.E, & Hauser K.F. (2023). Casein Kinase 2 Mediates HIV- and Opioid-Induced Pathologic Phosphorylation of TAR DNA Binding Protein 43 in the Basal Ganglia. ASN NEURO, 15, 17590914231158218.

Publication 2023

Antibiotics Brain Cells Cell Survival CX 4945 Cytoplasm Deoxyribonucleases Drugs, Orphan Embryo Glutamate Glutamine Inflammation Mediators Lysine Medulloblastoma Mice, Inbred ICR Morphine Mus Neurons Phosphorylation Poly A Proteins protein TDP-43, human Rare Diseases Ribonucleases silmitasertib Striatum, Corpus Tissue, Membrane Tissues Trypsin

Top products related to «Glutamate»

Glutamate by Merck Group

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Glutamate is a laboratory instrument used to measure the concentration of the amino acid glutamate in various samples. It functions by utilizing enzymatic reactions and spectrophotometric detection to quantify the amount of glutamate present.

Fetal bovine serum (fbs) by Thermo Fisher Scientific

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Fetal Bovine Serum (FBS) is a cell culture supplement derived from the blood of bovine fetuses. FBS provides a source of proteins, growth factors, and other components that support the growth and maintenance of various cell types in in vitro cell culture applications.

Penicillin streptomycin by Thermo Fisher Scientific

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Penicillin/streptomycin is a commonly used antibiotic solution for cell culture applications. It contains a combination of penicillin and streptomycin, which are broad-spectrum antibiotics that inhibit the growth of both Gram-positive and Gram-negative bacteria.

L glutamate by Merck Group

Sourced in United States, Germany, United Kingdom, Japan, France, Sao Tome and Principe

L-glutamate is a laboratory reagent used as a buffer component in various biochemical and cell culture applications. It serves to maintain the appropriate pH and ionic balance in experimental systems. L-glutamate is a naturally occurring amino acid that plays a role in cellular metabolism and signaling processes.

L glutamate by Thermo Fisher Scientific

Sourced in United States, United Kingdom, Germany, Spain

L-glutamate is a laboratory-grade amino acid that is commonly used as a reagent in various scientific applications. It serves as a core component in cell culture media, enzymatic assays, and biochemical analyses. The product provides a reliable and consistent source of this essential amino acid for researchers and laboratory professionals.

Neurobasal medium by Thermo Fisher Scientific

Sourced in United States, Germany, United Kingdom, Japan, Italy, Canada, Spain, France, Switzerland, China, Australia, Israel, Denmark, Ireland, Sweden, Austria

Neurobasal medium is a cell culture medium designed for the maintenance and growth of primary neuronal cells. It provides a defined, serum-free environment that supports the survival and differentiation of neurons. The medium is optimized to maintain the phenotypic characteristics of neurons and minimizes the growth of non-neuronal cells.

Dulbecco modified eagle medium (dmem) by Thermo Fisher Scientific

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DMEM (Dulbecco's Modified Eagle's Medium) is a cell culture medium formulated to support the growth and maintenance of a variety of cell types, including mammalian cells. It provides essential nutrients, amino acids, vitamins, and other components necessary for cell proliferation and survival in an in vitro environment.

Glutamate by Thermo Fisher Scientific

Sourced in United States, United Kingdom, Germany

Glutamate is a laboratory reagent used in various biochemical applications. It serves as a basic amino acid that is involved in several metabolic pathways. Glutamate can be used in a range of analytical techniques to study cellular processes and molecular interactions.

Penicillin by Thermo Fisher Scientific

Sourced in United States, United Kingdom, Germany, China, France, Canada, Japan, Australia, Switzerland, Italy, Israel, Belgium, Austria, Spain, Brazil, Netherlands, Gabon, Denmark, Poland, Ireland, New Zealand, Sweden, Argentina, India, Macao, Uruguay, Portugal, Holy See (Vatican City State), Czechia, Singapore, Panama, Thailand, Moldova, Republic of, Finland, Morocco

Penicillin is a type of antibiotic used in laboratory settings. It is a broad-spectrum antimicrobial agent effective against a variety of bacteria. Penicillin functions by disrupting the bacterial cell wall, leading to cell death.

B27 supplement by Thermo Fisher Scientific

Sourced in United States, United Kingdom, Germany, Japan, Canada, China, Italy, France, Switzerland, Spain, Israel, Australia, Austria, Poland, Denmark, Palestine, State of

B27 supplement is a serum-free and animal component-free cell culture supplement developed by Thermo Fisher Scientific. It is designed to promote the growth and survival of diverse cell types, including neurons, embryonic stem cells, and other sensitive cell lines. The core function of B27 supplement is to provide a defined, optimized combination of vitamins, antioxidants, and other essential components to support cell culture applications.

What is Glutamate and what are its key functions?

Glutamate is a critical neurotransmitter in the central nervous system, playing pivotal roles in neuronal function, synaptic plasticity, and brain development. It is the most abundant excitatory neurotransmitter, involved in a wide range of physiological and pathological processes. Glutamate is synthesized from glutamine and is responsible for mediating fast excitatory synaptic transmission. Understanding the complex biology of glutamate is essential for advancing our knowledge of brain function and developing effective therapies.

How can Glutamate signaling go awry, and what are the implications?

Dysregulation of glutamate signaling has been implicated in various neurological and psychiatric disorders. Imbalances in glutamate levels or receptor function can contribute to conditions like excitotoxicity, neurodegeneration, epilepsy, and mental health disorders. Studying the mechanisms underlying glutamate dysregulation is crucial for developing targeted treatments and interventions for these complex neurological and psychiatric conditions.

Are there different types or variations of Glutamate?

Yes, there are several variations of glutamate that play distinct roles. These include N-methyl-D-aspartate (NMDA) receptors, alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors, and metabotropic glutamate receptors (mGluRs). Each type of glutamate receptor has unique properties and functions, contributing to the diverse effects of glutamate signaling in the brain. Understanding the specific roles of these glutamate receptor subtypes is crucial for targeted drug development and therapeutic interventions.

How can PubCompare.ai help with Glutamate research?

PubCmopare.ai allows you to screen protocol literature more efficiently and leverage AI to pinpoint critical insights. The platform can help researchers identify the most effective protocols related to Glutamate for their specific research goals. PubCompare.ai's AI-driven analysis can highlight key differences in protocol effectiveness, enabling you to choose the best option for reproducibility and accuracy in your Glutamte studies.

What are some common challenges in working with Glutamate?

One common challenge in Glutamate research is ensuring accurate and reproducible measurements. Glutamate levels can be influenced by various factors, such as sample preparation, analytical methods, and experimental conditions. Researchers must carefully optimize their protocols to accurately quantify Glutamate and minimize variability. PubCompare.ai can assist in this process by helping identify the most robust and reliable protocols from the literature, enabling researchers to enhance the quality and consistency of their Glutamate-related experiments.

More about "Glutamate"

Glutamate, a pivotal neurotransmitter in the central nervous system, plays a vital role in neuronal functioning, synaptic plasticity, and brain development.
As the most abundant excitatory neurotransmitter, glutamate is responsible for mediating fast excitatory synaptic transmission and is involved in a wide range of physiological and pathological processes.
Glutamine, the precursor to glutamate, is essential for the synthesis of this key neurotransmitter.
L-glutamate, a form of glutamate, is commonly used in cell culture media such as Neurobasal medium and DMEM, often supplemented with fetal bovine serum (FBS) and penicillin/streptomycin antibiotics to support cell growth and survival.
Dysregulation of glutamate signaling has been implicated in various neurological and psychiatric disorders, including Alzheimer's disease, Parkinson's disease, schizophrenia, and depression.
As such, understanding the complex biology of glutamate is crucial for advancing our knowledge of brain function and developing effective therapies targeting this important neurotransmitter system.
PubCompare.ai, an AI-driven platform, can optimize your glutamte research by helping you locate the best protocols from literature, pre-prints, and patents using its AI-powered comparisons.
This cutting-edge tool can enhance the reproducibility and accuracy of your glutamate studies, providing valuable insights and accelerating your research endeavors.