> Chemicals & Drugs > Amino Acid > Aspartate

Aspartate

Aspartate is a nonessential amino acid that plays a crucial role in various metabolic processes within the body.
It is involved in the citric acid cycle, where it serves as an intermediate in the conversion of carbohydrates, fats, and proteins into energy.
Aspartate also contributes to the synthesis of nucleic acids and certain neurotransmitters, making it an important component in neurological function.
Reserach into the role of aspartate in health and disease is ongoing, with studies exploring its potential applications in areas such as energy metabolism, neurodegeneration, and cell signalling.
PubCompare.ai offers powerful tools to optimize aspartate research, helping scientists locate the best protocols and enhance reproducibility and accuracy in their studies.

Most cited protocols related to «Aspartate»

Whole-cell Patch-clamp Electrophysiology

Cited 160 times

Data were obtained using conventional whole cell patch-clamp techniques.
Micropipette fabrication and data acquisition were as described previously for
undiseased donor heart[85] (link). Axopatch 200 amplifiers, Digidata 1200 converters,
and pClamp software were used (Axon Instruments/Molecular Devices). Experiments
were performed at 37°C.
The standard bath solution contained, in mM: NaCl 144,
NaH₂PO₄ 0.33, KCl 4.0, CaCl₂ 1.8,
MgCl₂ 0.53, Glucose 5.5, and HEPES 5.0 at pH of 7.4, and pipette
solutions contained K-aspartate 100, KCl 25, K₂ATP 5,
MgCl₂ 1, EGTA 10 and HEPES 5. The pH was adjusted to 7.2 by KOH
(+15−20 mM K⁺).
For L-type Ca²⁺ current measurement, the bath solution contained
in mM: tetraethylammonium chloride (TEA-Cl) 157, MgCl₂ 0.5, HEPES 10,
and 1 mM CaCl₂, or BaCl₂, or SrCl₂ (pH 7.4 with
CsOH). The pipette solution contained (in mM) CsCl 125, TEA-Cl 20, MgATP 5,
creatine phosphate 3.6, EGTA 10, and HEPES 10 (pH 7.2 with CsOH).
For Na⁺/Ca²⁺ exchange current measurement, the
bath solution contained, (in mM): NaCl 135, CsCl 10, CaCl2 1, MgCl₂1, BaCl₂ 0.2, NaH₂PO₄ 0.33, TEACl 10, HEPES 10,
glucose 10 and (in µM) ouabain 20, nisoldipine 1, lidocaine 50, pH 7.4.
The pipette solution contained (in mM): CsOH 140, aspartic acid 75, TEACl 20,
MgATP 5, HEPES 10, NaCl 20, EGTA 20, CaCl2 10 (pH 7.2 with CsOH).

O'Hara T., Virág L., Varró A, & Rudy Y. (2011). Simulation of the Undiseased Human Cardiac Ventricular Action Potential: Model Formulation and Experimental Validation. PLoS Computational Biology, 7(5), e1002061.

Full text: Click here

Publication 2011

Adenosine Triphosphate, Magnesium Salt Aspartate Aspartic Acid Axon barium chloride Bath Cells cesium chloride Egtazic Acid Glucose Heart HEPES Lidocaine Magnesium Chloride Medical Devices Nisoldipine Ouabain Phosphocreatine Sodium Chloride Tetraethylammonium Chloride Tissue Donors

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

PASTEC: Modular TE Consensus Classifier

Cited 92 times

PASTEC was developed in the REPET package [7] . In this context, we used PASTEC to classify the consensus TE sequences found de novo in a genome. PASTEC uses several features of TEs to classify TE consensus sequences. It searches for structural evidence and sequence similarities stored in a MySQL database obtained during a preprocessing step. The structural features considered are TE length, presence of a LTR (long terminal repeat) or TIR (terminal inverted repeat) detected with a custom-built tool (with a minimum length of 10 bp, a minimum identity of 80%, the taking into account of reciprocal orientations of terminal repeats and a maximal length of 7000 bp), the presence of SSRs (simple sequence repeats detected with the tandem repeat finder (TRF) tool [8] (link)), the polyA tail and an ORF (open reading frame). The blastx and tblastx routines are used to search for similarities to known TEs in Repbase Update, and the hmmer3 package [9] to search against a HMM profile databases (TE-specific or not), after translation in all six frames. Sequence similarities are also identified by blastn searches against known rDNA sequences, known host genes and known helitron ends. The databanks used are preprocessed and formatted. The Repbase Update for PASTEC can be downloaded from http://www.girinst.org/repbase/index.html, whereas the HMM profile databank formatted for PASTEC is available from the REPET download directory (http://urgi.versailles.inra.fr/download/repet/).
PASTEC classifies TEs by testing all classifications from Wicker's hierarchical TE classification system. Each possible classification is weighted according to the available evidence, with respect to the classification considered. TEs are currently classified to class and order level. PASTEC can also determine whether a TE is complete on the basis of four criteria: sequence coverage for known TEs, profile coverage, presence of terminal repeats for certain classes, presence of a polyA or SSR tail for LINEs and SINEs, and the length of the TEs with respect to expectations for the class concerned.
We designed PASTEC as a modular multi-agent classifier. The system is composed of four types of agents: retrievers, classifiers, filter agents, and a super-agent (Figure 1). The retriever agents retrieve the pre-computed analysis results stored in the MySQL database. They act on the requests of the classifier or filter agents, filtering, formatting and supplying the results. The classifier and filter agents are specialized to recognize a particular category. For example, the LTR agent can determine only whether the TE is a LTR or not. The classifier and filter agents act on the request of the super-agent, deciding whether they can classify the TE or not. For example, the LTR agent decides whether the consensus TE is a LTR on the basis of the following evidence: presence of the ENV (envelope protein) profile (a condition sufficient for classification), the presence of INT (integrase), RT (reverse transcriptase), GAG (capsid protein), AP (aspartate proteinase) and RH (RNase H) profiles together with the detection of a LTR (long terminal repeat), a blast match with the sequence of a known LTR retrotransposon. The super-agent resolves classification conflicts and formats the output file. It resolves conflicts by using a confidence index normalized to 100. For example, the LTR agent calculates a confidence index with the following rules: presence of ENV profiles (+2 because this condition is sufficient for classification), presence of a long terminal repeat and an INT, GAG, RT, RH or AP profile (+1 for each profile combined with the long terminal repeat), +1 for each profile (ENV, AP, RT, RH and GAG) found in the same frame in the same ORF. If the consensus matches at least one known LTR retrotransposon, the LTR agent adds +2 for each type of blast (blastx or tblastx) at the confidence index. Finally, the length of the TE is taken into account because we add +1 if the TE without the long terminal repeat is between 4000 and 15000 bp in length, and we decrease the confidence index by 1 if the TE without the long terminal repeat is less than 1000 bp or more than 15000 bp long. The super-agent uses the maximum confidence index defined for each classifier agent to normalize the confidence index for each classification to 100 and then compare the different classifications. Advanced users can edit all decisions rules and maximum confidence indices in the Decision_rules.yaml file.
The output can be read by humans and is biologist-friendly. A single line specifies the name of the TE, its length, status, class, order, completeness, confidence index and all the features characterizing it. A status of “potential chimeric” or “OK” is assigned to the TE. If the TE is not considered to be “OK” then users must apply their own expertise. A TE is declared “potential chimeric” when at least two classifications are possible. In this case, PASTEC chooses the best status based on the available evidence, or does not classify the TE if no decision is possible. In this last case, all possible classifications are given (separated by a pipe symbol “|”). We present an example of PASTEC output in table S1. PASTEC output is a tabular file, with the columns from left to right indicating the name of the TE, its length, the orientation of the sequence, chimeric/non-chimeric status (OK indicating that the element is not potentially chimeric), class (class I in this case), order. In the first line of the example provided, the TE is a LTR. We presume that the element is complete because we have no evidence to suggest that it is incomplete, and the confidence index is 71/100. The last column summarizes all the evidence found: coding sequence evidence, such as the results of tblastX queries against the Repbase database (TE_BLRtx evidence), blastX queries against the Repbase database (TE_BLRx evidence) and profiles. A blast match is taken account if coverage exceeds 5%, and a profile is taken into account if its coverage exceeds 20% (these parameters can be edited in the configuration file). For each item of coding sequence evidence, the coverage of the subject is specified. The structural evidence is also detailed: >4000 bp indicates that TE length without terminal repeats is between 4000 and 15000 bp, the next item of information presented in the comments columns is the presence of terminal repeats: we have a LTR in this case, with an LTR length of 433 bp; two long ORFs have been identified, the last of which contains four profiles in the same frame and is up to 3000 bp long. Other evidence provided for this example includes the partial match with a Drosophila melanogaster gene (coverage 16.55% and the TE contains 18% SSRs). The super-agent determines whether a TE is complete based on whether it is sufficiently long, whether the expected terminal repeats or polyA tail are present, whether blast match coverage exceeds 30% and profile coverage exceeds 75%. The second line of the example corresponds to a potentially chimeric TE, for which human expertise is required.

Hoede C., Arnoux S., Moisset M., Chaumier T., Inizan O., Jamilloux V, & Quesneville H. (2014). PASTEC: An Automatic Transposable Element Classification Tool. PLoS ONE, 9(5), e91929.

Full text: Click here

Publication 2014

Aspartate Capsid Proteins Chimera Consensus Sequence DNA, Ribosomal Drosophila melanogaster FCER2 protein, human Gene Products, env Genes Genome Homo sapiens Integrase Open Reading Frames Peptide Hydrolases Poly(A) Tail Poly A Reading Frames Retrotransposons Ribonuclease H RNA-Directed DNA Polymerase Short Interspersed Nucleotide Elements Short Tandem Repeat Tail Tandem Repeat Sequences Terminal Repeat Sequences

Generation of Diverse Amino Acid Conformations

Cited 74 times

To maximize transferability of the parameters, multidimensional structure scans were employed to generate conformational diversity. For smaller side chains, grid scans in dihedral space were used to generate side chain variety, including both α and β backbone conformations for each side chain rotamer. Grid scans were generated for Val in one dimension, as it only has χ1, at an interval of 10°. Grids were generated for Asp⁻, Asn, Cys, Phe, His (δ-, ɛ-, and doubly-protonated), Ile, Leu, Ser, Thr, and Trp in two dimensions, as they have χ1 and χ2, at intervals of 20°, yielding 324 structures per amino acid.
We were unable to exhaustively explore side chain conformational space side chains with more than two rotatable bonds. Tyrosine has 3 rotatable χ bonds, but dihedral space is reduced as 180° rotation of either the phenol (χ2) or of the hydroxyl produce the same effect when accounting for symmetry of the ring. We therefore fully scanned each tyrosine dihedral when the other two were at a stable rotamer defined as any instance of that value in the rotamer library for this amino acid, rounded to the nearest 10° and limiting χ2 to (−90°, 90°] to account for symmetry. Stable rotamers for the hydroxyl, not in the rotamer library, were inferred from the QM energy profiles discussed above. Stable rotamers were 180° or ±60° for χ1, ±30° or 90° for χ2, and 0° or 180° for the hydroxyl. Conformations were generated using a full scan for each dihedral (at 20° increments), repeated for every combination of stable rotamer values for the other two dihedrals. As protonated aspartate has nearly the same dihedrals as Tyr (χ1, χ2 and hydroxyl), it was scanned in the same manner, but without χ2 restriction because aspartate does not have the same symmetry properties.
Cysteine presents a special case, as it can form disulfide bonds that bridge two amino acids. In addition to developing parameters for reduced Cys (no disulfide), a pair of Cys dipeptides with a disulfide bond was employed to scan the S-S energy profile. However, a disulfide between Cys_A and Cys_B has a total of five dihedrals: χ1_A, χ2_A, χ_SS, χ2_B, and χ1_B. As full sampling across five dihedrals is clearly intractable, conformation space was reduced by applying the same χ1 / χ2 values to both dipeptides. Using this symmetry, a two-dimensional scan was performed for all χ1 / χ2 combinations using 20° spacing; this scan was repeated with χ_SS restrained to 180°, ±60°, or ±90° (five 2D scans). Separately, the χ_SS profile was scanned with 20° spacing using χ1 of 180° or ±60° and χ2 of 180° or ±60° (nine 1D scans total). As with the other amino acids, the entire procedure was repeated with the backbone in α and β conformations; here, both dipeptides adopted the same backbone conformation.
The remaining side chains, Arg⁺, Gln, Glu (protonated), Glu⁻,Lys⁺, and Met, have at least three side chain dihedrals (Table S1). Rather than performing a grid search, MD simulations were used to generate diverse conformations of these side chains. Each dipeptide was simulated twice, with α or β backbone restraints, for 100 ns each. To overcome kinetic traps, these simulations were performed at 500 K and the dielectric was set to 4r. Next, a diverse subset was generated by mapping each conformation to a multidimensional grid spaced 10° in each χ. The five lowest energy conformations at each grid point were saved. From each simulation grid, five hundred structures were randomly selected (comparable to the number generated by the grid procedure described above for Tyr). Because the longer, more flexible side chains of these amino acids can adopt conformations with strong interactions between backbone and side chain, conformations where we suspected the in vacuo MM description may produce fitting artifacts were excluded, using electrostatic and distance cutoffs defined in the Supporting Information.

Maier J.A., Martinez C., Kasavajhala K., Wickstrom L., Hauser K.E, & Simmerling C. (2015). ff14SB: Improving the accuracy of protein side chain and backbone parameters from ff99SB. Journal of chemical theory and computation, 11(8), 3696-3713.

Publication 2015

Amino Acids Aspartate Dipeptides Disulfides DNA Library Electrostatics Hydroxyl Radical Kinetics Phenol Radionuclide Imaging Tyrosine Vertebral Column

Evaluating Frequency and Phase Drift Correction Methods for Brain MRS

Cited 38 times

Simulated brain proton MRS data were generated with known frequency and phase drift errors to evaluate the performance of the proposed method and compare it with previously described methods. First, simulated point resolved spectroscopy pulse sequence (PRESS) model spectra (echo time [TE] = 80 ms; 2048 points; spectral width = 2000 Hz; B₀ = 3T) were generated for 22 metabolites, six macromolecule resonances, and a water resonance using an in-house MATLAB-based implementation of the density matrix formalism as described previously (10 (link)). The model spectra were then exponentially line-broadened to a linewidth of 6 Hz and combined in approximately physiological concentrations to produce a simulated, noise-free MR spectrum. The amplitude of the simulated residual water resonance was chosen to be approximately twice the height of the N-acetyl aspartate (NAA) resonance. The spectrum was then replicated 128 times to simulate 128 acquired averages, and frequency and phase drifts were applied to each average. The frequency error, f, of each average, N, was chosen as a linear slope superposed with noise, ε_f, according to:f (N) = (5/128)N + ε_f Hz, and the phase error, φ, of each average was chosen as a flat slope superposed with noise, ε_φ, according to: φ(N) − (0)N + εφ degrees. The added noise terms, ε_f and ε_φ, involved the addition of a random value at each point N with mean values of zero and standard deviations of 0.2 Hz and 2 degrees, respectively. These terms were used to roughly approximate the effects of physiological and bulk noise. Finally, a normally distributed random noise seed was added to the each of the simulated averages to achieve the desired SNR. To approximate a range of SNR conditions, spectra were generated using per-average SNR values (measured as the peak NAA amplitude divided by the standard deviation of the added noise) of 20, 10, 5, and 2.5. For each SNR value, 10 simulated datasets (each with 128 averages) were generated as described above, and a frequency and phase drift correction was performed on each dataset using the spectral registration method, as well as two existing correction methods; the creatine fitting method (7 (link)), and the residual water method (2 (link)), as described below. To evaluate the various correction methods, the frequency estimation error and phase estimation error were quantified for each of the correction methods. Specifically, the estimation error was obtained by taking the difference between the measured drift and the actual drift and calculating the standard deviation of this residual difference across all 128 averages.

Near J., Edden R., Evans C.J., Paquin R., Harris A, & Jezzard P. (2014). Frequency and Phase Drift Correction of Magnetic Resonance Spectroscopy Data by Spectral Registration in the Time Domain. Magnetic resonance in medicine, 73(1), 44-50.

Publication 2014

Aspartate Brain Creatine Dietary Fiber ECHO protocol physiology Protons Pulse Rate Spectrum Analysis Vibration

Most recents protocols related to «Aspartate»

PCV2b ORF2 BDH Mutant Expression

Not available on PMC !

Example 3

Several other substitutions at amino acid site 63 were produced to compare to the PCV2b ORF BDH native strain. The results from the evaluation of the PCV2b ORF2 BDH mutant constructs are shown in FIGS. 7A and 7B. The results demonstrate that in addition to the amino acid mutation from arginine (R) to threonine (T) at position 63, arginine (R) 63 to glycine (G), arginine (R) 63 to glutamine (Q), and arginine (R) 63 to aspartate (D) increased the expression of PCV2b ORF2 BDH in Sf+ cells at least Four-fold as compared to the wild type. In particular the single mutations R63G and R63Q increased PCV2b ORF2 BDH expression in Sf+ cells to levels similar to PCV2a ORF2.

US11858963B2. PCV2 ORF2 protein variant and virus like particles composed thereof (2024-01-02). Boehringer Ingelheim Animal Health USA Inc. [US]. Inventors: Luis Alejandro Hernandez [US], Christine Margaret Muehlenthaler [US], Eric Martin Vaughn [US], Gregory Haiwick [US].

Full text: Click here

Patent 2024

Amino Acids Amino Acid Substitution Arginine Aspartate Cells Figs Glutamine Glycine Mutant Proteins Mutation Strains Threonine Virion

Engineered Selenium Biosensor Protein

The binding constant (K_d) was calculated using GraphPad Prism software by fitting the ligand-titration
curve in the binding isotherm equation: S = (r–r_apo)/(r_sat–r_apo) = [L]/(K_d + [L]), where S is the saturation, [L] is the ligand concentration, r is the ratio, r_apo is a ratio in the absence of ligand, and r_sat is the ratio at saturation.
Point
mutations were added to the SelFS gene to produce mutants that would
increase the sensor’s physiological detection array. The structure
of SeBP was acquired from the PDB to determine the amino acid residues
present in the protein’s binding pocket that facilitate selenium
binding.^{22 (link)} Using the QuikChange site-directed
mutagenesis kit from Agilent USA, three mutants were produced by replacing
the amino acid residues at positions 29 (isoleucine), 42 (lysine),
and 61 (aspartate) with arginine, tryptophan, and cysteine, respectively.
All these mutants of the SelFS protein were expressed and purified
as described above for further analysis. SelFS was also utilized for in vivo selenium flux measurement investigations.

Bano R., Mohsin M., Zeyaullah M, & Khan M.S. (2023). Real-Time Monitoring of Selenium in Living Cells by Fluorescence Resonance Energy Transfer-Based Genetically Encoded Ratiometric Nanosensors. ACS Omega, 8(9), 8625-8633.

Publication 2023

Amino Acids Arginine Aspartate Cysteine Genes Isoleucine Ligands Lysine physiology prisma Protein S Proteins Selenium Tryptophan

Liver Fibrosis Assessment via Serum Biomarkers

Protocol full text hidden due to copyright restrictions

Open the protocol to access the free full text link

Publication 2023

Albumins Aspartate Blood Platelets Comprehensive Metabolic Panel D-Alanine Transaminase Diabetes Mellitus Diagnosis Fibrosis Fibrosis, Liver Hypersensitivity Injuries Lavandula angustifolia Liver Liver Cirrhosis Serum Transferase

Isolation of Atrial Myocytes from Mice

Atrial Myocytes were dissociated as previously described (Jansen and Rose, 2019 (link)). Briefly, mice were anesthetized by inhalation of isoflurane (2% in air) then heparinized by intraperitoneal injection of Heparin (200 UI). Mice anesthesia was checked by absence of the paw withdrawal reflex. Mice were subsequently killed by cervical dislocation and atrial appendages were rapidly excised. After the excision, all digestion steps were realized at 37°C. Atria were quickly washed and minced in modified Tyrode solution (in mmol/L: 140 NaCl, 5.4 KCl, 1.2 KH₂PO₄, 5 HEPES, 5.55 Glucose, 1 MgCl₂, 1.8 CaCl₂, 5 U/mL Heparin; pH 7.4 with NaOH) and transferred in a pre-digestion buffer solution (in mmol/L: 140 NaCl, 5.4 KCl, 1.2 KH₂PO₄, 5 HEPES, 18.5 Glucose, 50 Taurine, 0.066 CaCl₂, 1 mg/mL Bovine Serum Albumin; pH 6.9 with NaOH). After 5 min of pre-digestion, tissues were transferred in a digestion solution corresponding to the pre-digestion buffer supplemented by 0.11 mg/mL (equivalent to 0.34 Wünsch unit/mL and 36.7 units/mL Dispase) of Liberase (Medium Thermolysine, Roche, France). The digestion step lasted 20–23 min. After digestion was completed, atrial stripes were washed in a modified Kraft-Brühe solution (in mmol/L: 100 K-Glutamate, 10 K-Aspartate, 25 KCl, 10 KH₂PO₄, 2 MgSO4, 20 Taurine, 5 Creatine, 0.5 EGTA, 20 Glucose, 5 HEPES, 0,1% Bovine Serum Albumin; pH 7.2 with KOH), and mechanically triturated in this solution to allow cell isolation. Once the dissociation ended, cells were gradually reintroduced to 1 mmol/L calcium concentration by addition of calcium in the Kraft-Brühe solution (in mmol/L of free calcium: 0.125, 0.25, 0.375, 0.5, 0.625, 0.75, 0.875, and 1). Cells were used for patch clamp experiments during the 8 h following the dissociation. Only rod shaped and striated cells were used for experiments.

Guillot B., Boileve A., Walton R., Harfoush A., Conte C., Sainte-Marie Y., Charron S., Bernus O., Recalde A., Sallé L., Brette F, & Lezoualc’h F. (2023). Inhibition of EPAC1 signaling pathway alters atrial electrophysiology and prevents atrial fibrillation. Frontiers in Physiology, 14, 1120336.

Full text: Click here

Publication 2023

Anesthesia Aspartate Auricular Appendage Buffers Calcium Cells Cell Separation Creatine Digestion dispase Egtazic Acid Glucose Glutamate Heart Atrium Heparin HEPES Inhalation Injections, Intraperitoneal Isoflurane Joint Dislocations Liberase Magnesium Chloride Mus Muscle Cells Neck Reflex Serum Albumin, Bovine Sodium Chloride Sulfate, Magnesium Taurine Tissues Tyrode's solution

Electrophysiological Recording Solutions

The standard 20 mM Ca²⁺ extracellular Ringer’s solution used for electrophysiological experiments contained 135 mM NaCl, 4.5 mM KCl, 20 mM CaCl₂, 1 mM MgCl₂, 10 mM D-glucose, and 5 mM HEPES (pH 7.4 with NaOH). 110 mM Ca²⁺ solution contained 110 mM CaCl₂, 10 mM D-glucose, and 5 mM HEPES (pH 7.4 with NaOH). The divalent-free (DVF) solution contained 150 mM NaCl, 10 mM HEDTA, 1 mM EDTA, and 10 mM HEPES (pH 7.4 with NaOH). 10 mM TEA-Cl was added to prevent contamination from voltage-gated K⁺ channels. All internal solutions contained 8 mM MgCl₂ and 10 mM HEPES (pH 7.2 with CsOH). The standard 8 mM BAPTA internal solution (which was used in the experiments shown in all Figures unless otherwise indicated) contained 135 mM Cs aspartate and 8 mM BAPTA. The 20 mM BAPTA solution contained 95 Cs asparatate and the 0.8 mM BAPTA solution contained 145 mM Cs aspartate (all pH 7.2). The 10 mM EGTA solution contained 130 mM Cs aspartate, and the 20 mM EGTA solution contained 110 mM Cs aspartate (pH 7.2).

Yeung P.S., Yamashita M, & Prakriya M. (2023). A pathogenic human Orai1 mutation unmasks STIM1-independent rapid inactivation of Orai1 channels. eLife, 12, e82281.

Full text: Click here

Publication 2023

1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid Aspartate Edetic Acid Egtazic Acid Glucose HEPES Magnesium Chloride N-(hydroxyethyl)ethylenediaminetriacetic acid Ringer's Solution Sodium Chloride Voltage-Gated Potassium Channel

Top products related to «Aspartate»

Axopatch 200b amplifier by Molecular Devices

Sourced in United States, France, Japan, Germany, United Kingdom

The Axopatch 200B is a high-performance patch-clamp amplifier designed for electrophysiology research. It is capable of amplifying and filtering electrical signals from single-cell preparations, providing researchers with a tool to study ion channel and membrane properties.

Aspartate by Merck Group

Sourced in United States

Aspartate is a laboratory reagent used in various biochemical and analytical applications. It is a key component in the measurement of aspartic acid levels in biological samples. Aspartate serves as a substrate in enzymatic reactions and can be used to monitor enzyme activity or metabolite concentrations.

Pclamp 10 by Molecular Devices

Sourced in United States, Germany, Canada, United Kingdom, China, Australia

PClamp 10 software is a data acquisition and analysis platform for electrophysiology research. It provides tools for recording, analyzing, and visualizing electrical signals from cells and tissues.

N methyl d aspartate nmda by Merck Group

Sourced in United States, Germany

N-methyl-D-aspartate (NMDA) is a synthetic compound that acts as an agonist at the NMDA receptor, a type of glutamate receptor found in the central nervous system. It is commonly used in laboratory research settings to study neurological processes and functions.

L aspartate by Merck Group

Sourced in United States

L-aspartate is a laboratory reagent used in various biochemical and analytical applications. It is a naturally occurring amino acid that serves as a key compound in several metabolic pathways. The primary function of L-aspartate is to provide a source of nitrogen and carbon for the synthesis of other biomolecules.

Glutamate by Merck Group

Sourced in United States, Germany, Japan, United Kingdom, France, Macao, Brazil, Canada, China

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.

Axopatch 200b by Molecular Devices

Sourced in United States, United Kingdom, France

The Axopatch 200B is a high-performance patch-clamp amplifier designed for electrophysiological research. It is capable of recording and amplifying small electrical signals from cells and tissues with high precision and low noise.

N methyl d aspartate by Merck Group

Sourced in United States

N-methyl-D-aspartate is a synthetic compound used as a chemical tool in laboratory research. It functions as an agonist, specifically activating the N-methyl-D-aspartate (NMDA) receptor, which is an important glutamate receptor in the central nervous system. This compound is primarily utilized for experimental purposes to study the biological and pharmacological properties of the NMDA receptor.

Pclamp 9 by Molecular Devices

Sourced in United States, France, Canada

PClamp 9 software is a comprehensive data acquisition and analysis software designed for electrophysiology research. It provides a suite of tools for recording, visualizing, and analyzing electrical signals from cells and tissues.

Aspartate assay kit by Abcam

Sourced in United Kingdom, United States

The Aspartate Assay Kit is a laboratory tool designed to quantify the levels of aspartate, an important amino acid, in various biological samples. This kit provides a simple, rapid, and sensitive method to measure aspartate concentrations.

More about "Aspartate"

Aspartate, also known as L-aspartate or aspartic acid, is a nonessential amino acid that plays a crucial role in various metabolic processes within the body.
It is a key intermediate in the citric acid cycle, where it helps convert carbohydrates, fats, and proteins into energy.
Aspartate is also involved in the synthesis of nucleic acids and certain neurotransmitters, making it an important component in neurological function.
Research into the role of aspartate in health and disease is ongoing, with studies exploring its potential applications in areas such as energy metabolism, neurodegeneration, and cell signaling.
The Axopatch 200B amplifier and PClamp 10 software are powerful tools used by researchers to study the electrophysiological properties of neurons and the role of aspartate and related compounds like N-methyl-D-aspartate (NMDA) and glutamate in neuronal function.
The Aspartate Assay Kit is another valuable resource for researchers, allowing them to accurately measure aspartate levels in biological samples.
By utilizing these tools and resources, scientists can optimize their aspartate research, enhance reproducibility and accuracy, and uncover new insights into the imetabolic and neurological functions of this essential amino acid.
PubCompare.ai, the leading AI-driven platform, offers powerful tools to help researchers in this field.
The platform's advanced AI comparisons can assist scientists in locating the best protocols from literature, preprints, and patents, empowering them to conduct more effective and efficient aspartate research.
With PubCompare.ai, researchers can experience the future of research optimization and take their aspartate studies to new heights.