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Aspartic Acid

Q: What are the different types or variations of Aspartic Acid?

Aspartic acid, also known as aspartate, exists in both L-aspartic acid and D-aspartic acid forms. The L-form is the naturally occurring and more common variant, while the D-form is less prevalent but also plays important biological roles. Both forms have unique properties and applications in areas like neuroscience, cell signaling, and metabolic processes.

Aspartic acid is a non-essential amino acid that plays a crucial role in various biological processes.
It serves as a building block for proteins and is involved in the citric acid cycle, a key metabolic pathway.
Aspartic acid can be synthesized in the body and is also obtained through dietary sources, such as dairy products, legumes, and certain meats.
This versatile amino acid has been the subject of extensive research, with studies exploring its potential applications in fields like neuroscience, immunology, and cell signaling.
PubCompare.ai's AI-driven platform can help researchers identify the most accurate and reproducbile protocols for working with aspartic acid, enabling efficient and reliable investigations.

Most cited protocols related to «Aspartic Acid»

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.

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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

Local Distance Difference Test (lDDT) for Protein Structure Evaluation

Cited 69 times

lDDT measures how well the environment in a reference structure is reproduced in a protein model. It is computed over all pairs of atoms in the reference structure at a distance closer than a predefined threshold R_o (called inclusion radius), and not belonging to the same residue. These atom pairs define a set of local distances L. A distance is considered preserved in the model M if it is, within a certain tolerance threshold, the same as the corresponding distance in . If one or both the atoms defining a distance in the set are not present in M, the distance is considered non-preserved. For a given threshold, the fraction of preserved distances is calculated. The final lDDT score is the average of four fractions computed using the thresholds 0.5 Å, 1 Å, 2 Å and 4 Å, the same ones used to compute the GDT-HA score (Battey et al., 2007 (link)). For partially symmetric residues, where the naming of chemically equivalent atoms can be ambiguous (glutamic acid, aspartic acid, valine, tyrosine, leucine, phenylalaine and arginine), two lDDTs, one for each of the two possible naming schemes, are computed using all non-ambiguous atoms in M in the reference. The naming convention giving the higher score in each case is used for the calculation of the final structure-wide lDDT score.
The lDDT score can be computed using all atoms in the prediction (the default choice), but also using only distances between Cα atoms, or between backbone atoms. Interactions between adjacent residues can be excluded by specifying a minimum sequence separation parameter. Unless explicitly specified, the calculation of the lDDT scores for all experiments described in this article has been performed using default parameters, i.e. R_o = 15 Å, using all atoms at zero sequence separation.

Mariani V., Biasini M., Barbato A, & Schwede T. (2013). lDDT: a local superposition-free score for comparing protein structures and models using distance difference tests. Bioinformatics, 29(21), 2722-2728.

Publication 2013

Arginine Aspartic Acid Conferences Glutamic Acid Immune Tolerance Leucine Radius Staphylococcal Protein A Tyrosine Valine Vertebral Column

Zinc Finger Protein Binding Sites

Cited 38 times

Single ZFP-binding sites—Individual zinc finger modules can be linked together to form multi-finger arrays that recognize specific sequences in double-stranded genomic DNA (Figure 2a). These multi-finger arrays can be fused to other protein domains, such as transcriptional activation or repression domains, in order to target them to specific locations within large genomes (1–4 ). Because a single ZF recognition helix typically binds three contiguous nucleotides in DNA, most binding sites for single ZF proteins (which we designate'single ZF array binding sites’) have lengths that are multiples of three base pairs. However, certain ZF modules containing aspartic acid in the +2 position of the DNA recognition helix appear to recognize four nucleotides. This can result in ‘target site overlap’ between adjacent ZF modules or, if the Asp-containing module occurs in the amino-terminal position of an array, the requirement for an additional 3' nucleotide in the ZF array binding site (19 (link)).
Dimeric zinc finger nuclease sites—Zinc finger nucleases (ZFNs) consist of a zinc finger array fused to a non-specific dsDNA nuclease (e.g. the nuclease domain of the Type IIS restriction enzyme FokI) (5 (link),6 (link),8 (link),10 (link)). ZFNs made with FokI nuclease are catalytically active only as dimers (20 (link)). Thus, a full ZFN target site consists of two ZF ‘half-sites’ on complementary DNA strands, separated by a ‘spacer’ of five or six base pairs, as shown in Figure 2b (6 (link),21 (link)). In this article, we designate the two ‘half-sites’ together with the spacer as a ‘dimeric ZF nuclease site.’

Sander J.D., Zaback P., Joung J.K., Voytas D.F, & Dobbs D. (2007). Zinc Finger Targeter (ZiFiT): an engineered zinc finger/target site design tool. Nucleic Acids Research, 35(Web Server issue), W599-W605.

Publication 2007

Aspartic Acid Binding Proteins Binding Sites DNA, Complementary DNA, Double-Stranded DNA Restriction Enzymes Fingers Genome Helix (Snails) Nucleotides Protein Domain Repression, Psychology Transcriptional Activation Zinc Fingers

Construction and Purification of XRCC1 Mutants

Cited 35 times

pCDEX vector encompassing the cDNA encoding human XRCC1 was kindly given by K. Caldecott (Sussex, UK). Truncated forms of XRCC1 were subcloned in-frame with GST in the eukaryotic pBC vector (26 (link)). Construction of the Flag-tagged XRCC1 encoding plasmid was described elsewhere (18 (link)). The S371L and S371D mutations of XRCC1 were generated by PCR by changing the AGC codon encoding a serine by a CTG or a GAT codon encoding a leucine or an aspartic acid, respectively. The mutated cDNA was cloned in the pCDEX vector. Wild-type and mutant sequences of human XRCC1 were cloned into the EcoRI site of pEGFP-C3 vector (Clontech). P53 oligonucleotides sense: 5′-AATTAGAACCTCCACTTTCTCAAGAAGCTTTCGCTGATCTTTGGAAGAAAC-3′ antisense: 5′-TCGAGTTTCTTCCAAAGATCAGCGAAAGCTTCTTGAGAAAGTGGAGGTTCT-3′ corresponding to amino acids 11–25 were annealed and cloned in the EcoRI and XhoI sites of the prokaryotic vector pGEX (Amersham Biosciences). XRCC1 (282–428) including BRCT1 domain, XRCC1 (282–428) S371L, XRCC1 (282–428) S371D and XRCC1 (527–633) including BRCT2 domain cDNAs were amplified by PCR and cloned in pGEX vector. GST fusion proteins were produced in Escherichia coli (BL21) and soluble proteins were purified using glutathione–Sepharose beads as indicated by the manufacturer.

Lévy N., Martz A., Bresson A., Spenlehauer C., de Murcia G, & Ménissier-de Murcia J. (2006). XRCC1 is phosphorylated by DNA-dependent protein kinase in response to DNA damage. Nucleic Acids Research, 34(1), 32-41.

Publication 2006

Amino Acids Aspartic Acid Cloning Vectors Codon Deoxyribonuclease EcoRI DNA, Complementary Escherichia coli Eukaryota Glutathione Homo sapiens Leucine Mutation Oligonucleotides Plasmids Prokaryotic Cells Proteins Reading Frames Sepharose Serine XRCC1 protein, human

En-Bloc Tissue Staining Protocol

Cited 24 times

Large-volume en-bloc staining was performed as follows (also see Supplementary Table 1 for details). Tissue was first immersed in 2% OsO₄ aqueous solution (Serva) buffered with cacodylate (0.15 M, pH 7.4) at room temperature for 90 min. The staining buffer was then replaced by 2.5% ferrocyanide (Sigma-Aldrich) in 0.15 M cacodylate buffer (pH 7.4) and incubated at room temperature for another 90 min. Sequentially, the tissue was incubated in filtered thiocarbohydrazide (saturated aqueous solution at room temperature, Sigma-Aldrich) at 40 °C for 45 min, 2% unbuffered OsO₄ aqueous solution at room temperature for 90 min and 1% UA (Serva) aqueous solution at 4 °C overnight. Double rinses in nanopure filtered water for 30 min each were performed between the ferrocyanide and thiocarbohydrazide step, the thiocarbohydrazide and OsO₄ step, and the OsO₄ and UA step. On the next day, the tissue (still in UA solution) was warmed up to 50 °C (oven) for 120 min. After being washed twice in nanopure filtered water at room temperature for 30 min, the tissue was incubated in a lead aspartate solution at 50 °C for 120 min. The lead aspartate solution was prepared by dissolving 0.066 g lead nitrate (Sigma-Aldrich) in 10 ml 0.03 M aspartic acid (Serva) and pH adjusted to 5 with 1 N KOH. The tissue was then washed twice in nanopure filtered water for 30 min. The image in Supplementary Fig. 2b was taken from a tissue block stained with the same procedure described above except that the 120 min 50 °C incubation in UA was omitted.

Hua Y., Laserstein P, & Helmstaedter M. (2015). Large-volume en-bloc staining for electron microscopy-based connectomics. Nature Communications, 6, 7923.

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Publication 2015

Aspartate Aspartic Acid Buffers Cacodylate hexacyanoferrate II lead nitrate Strains thiocarbohydrazide Tissues

Most recents protocols related to «Aspartic Acid»

Microbial Seed Treatments for Enhanced Crop Performance

Not available on PMC !

Example 2

A. Seed Treatment with Isolated Microbe

In this example, an isolated microbe from Tables 1-3 will be applied as a seed coating to seeds of corn (Zea mays). Upon applying the isolated microbe as a seed coating, the corn will be planted and cultivated in the standard manner.

A control plot of corn seeds, which did not have the isolated microbe applied as a seed coating, will also be planted.

It is expected that the corn plants grown from the seeds treated with the seed coating will exhibit a quantifiably higher biomass than the control corn plants.

The biomass from the treated plants may be about 1-10% higher, 10-20% higher, 20-30% higher, 30-40% higher, 40-50% higher, 50-60% higher, 60-70% higher, 70-80% higher, 80-90% higher, or more.

The biomass from the treated plants may equate to about a 1 bushel per acre increase over the controls, or a 2 bushel per acre increase, or a 3 bushel per acre increase, or a 4 bushel per acre increase, or a 5 bushel per acre increase, or more.

In some aspects, the biomass increase is statistically significant. In other aspects, the biomass increase is not statistically significant, but is still quantifiable.

B. Seed Treatment with Microbial Consortia

In this example, a microbial consortium, comprising at least two microbes from Tables 1-3 will be applied as a seed coating to seeds of corn (Zea mays). Upon applying the microbial consortium as a seed coating, the corn will be planted and cultivated in the standard manner.

A control plot of corn seeds, which did not have the microbial consortium applied as a seed coating, will also be planted.

It is expected that the corn plants grown from the seeds treated with the seed coating will exhibit a quantifiably higher biomass than the control corn plants.

The biomass from the treated plants may be about 1-10% higher, 10-20% higher, 20-30% higher, 30-40% higher, 40-50% higher, 50-60% higher, 60-70% higher, 70-80% higher, 80-90% higher, or more.

In some aspects, the biomass increase is statistically significant. In other aspects, the biomass increase is not statistically significant, but is still quantifiable.

C. Treatment with Agricultural Composition Comprising Isolated Microbe

In this example, an isolated microbe from Tables 1-3 will be applied as an agricultural composition, administered to the corn seed at the time of sowing.

For example, it is anticipated that a farmer will apply the agricultural composition to the corn seeds simultaneously upon planting the seeds into the field. This can be accomplished, for example, by applying the agricultural composition to a hopper/bulk tank on a standard 16 row planter, which contains the corn seeds and which is configured to plant the same into rows. Alternatively, the agricultural composition can be contained in a separate bulk tank on the planter and sprayed into the rows upon planting the corn seed.

A control plot of corn seeds, which are not administered the agricultural composition, will also be planted.

It is expected that the corn plants grown from the seeds treated with the agricultural composition will exhibit a quantifiably higher biomass than the control corn plants.

The biomass from the treated plants may be about 1-10% higher, 10-20% higher, 20-30% higher, 30-40% higher, 40-50% higher, 50-60% higher, 60-70% higher, 70-80% higher, 80-90% higher, or more.

In some aspects, the biomass increase is statistically significant. In other aspects, the biomass increase is not statistically significant, but is still quantifiable.

D. Treatment with Agricultural Composition Comprising Microbial Consortia

In this example, a microbial consortium, comprising at least two microbes from Tables 1-3 will be applied as an agricultural composition, administered to the corn seed at the time of sowing.

A control plot of corn seeds, which are not administered the agricultural composition, will also be planted.

It is expected that the corn plants grown from the seeds treated with the agricultural composition will exhibit a quantifiably higher biomass than the control corn plants.

The biomass from the treated plants may be about 1-10% higher, 10-20% higher, 20-30% higher, 30-40% higher, 40-50% higher, 50-60% higher, 60-70% higher, 70-80% higher, 80-90% higher, or more.

In some aspects, the biomass increase is statistically significant. In other aspects, the biomass increase is not statistically significant, but is still quantifiable.

A. Seed Treatment with Isolated Microbe

A control plot of corn seeds, which did not have the isolated microbe applied as a seed coating, will also be planted.

It is expected that the corn plants grown from the seeds treated with the seed coating will exhibit a quantifiable and superior ability to tolerate drought conditions and/or exhibit superior water use efficiency, as compared to the control corn plants.

The drought tolerance and/or water use efficiency can be based on any number of standard tests from the art, e.g leaf water retention, turgor loss point, rate of photosynthesis, leaf color and other phenotypic indications of drought stress, yield performance, and various root morphological and growth patterns.

B. Seed Treatment with Microbial Consortia

A control plot of corn seeds, which did not have the microbial consortium applied as a seed coating, will also be planted.

C. Treatment with Agricultural Composition Comprising Isolated Microbe

In this example, an isolated microbe from Tables 1-3 will be applied as an agricultural composition, administered to the corn seed at the time of sowing.

A control plot of corn seeds, which are not administered the agricultural composition, will also be planted.

It is expected that the corn plants grown from the seeds treated with the with the agricultural composition will exhibit a quantifiable and superior ability to tolerate drought conditions and/or exhibit superior water use efficiency, as compared to the control corn plants.

D. Treatment with Agricultural Composition Comprising Microbial Consortia

In this example, a microbial consortium, comprising at least two microbes from Tables 1-3 will be applied as an agricultural composition, administered to the corn seed at the time of sowing.

A control plot of corn seeds, which are not administered the agricultural composition, will also be planted.

A. Seed Treatment with Isolated Microbe

A control plot of corn seeds, which did not have the isolated microbe applied as a seed coating, will also be planted.

It is expected that the corn plants grown from the seeds treated with the seed coating will exhibit a quantifiable and superior ability to utilize nitrogen, as compared to the control corn plants.

The nitrogen use efficiency can be quantified by recording a measurable change in any of the main nitrogen metabolic pool sizes in the assimilation pathways (e.g., a measurable change in one or more of the following: nitrate, nitrite, ammonia, glutamic acid, aspartic acid, glutamine, asparagine, lysine, leucine, threonine, methionine, glycine, tryptophan, tyrosine, total protein content of a plant part, total nitrogen content of a plant part, and/or chlorophyll content), or where the treated plant is shown to provide the same or elevated biomass or harvestable yield at lower nitrogen fertilization levels compared to the control plant, or where the treated plant is shown to provide elevated biomass or harvestable yields at the same nitrogen fertilization levels compared to a control plant.

B. Seed Treatment with Microbial Consortia

A control plot of corn seeds, which did not have the microbial consortium applied as a seed coating, will also be planted.

It is expected that the corn plants grown from the seeds treated with the seed coating will exhibit a quantifiable and superior ability to utilize nitrogen, as compared to the control corn plants.

C. Treatment with Agricultural Composition Comprising Isolated Microbe

In this example, an isolated microbe from Tables 1-3 will be applied as an agricultural composition, administered to the corn seed at the time of sowing.

A control plot of corn seeds, which are not administered the agricultural composition, will also be planted.

It is expected that the corn plants grown from the seeds treated with the agricultural composition will exhibit a quantifiable and superior ability to utilize nitrogen, as compared to the control corn plants.

D. Treatment with Agricultural Composition Comprising Microbial Consortia

In this example, a microbial consortium, comprising at least two microbes from Tables 1-3 will be applied as an agricultural composition, administered to the corn seed at the time of sowing.

A control plot of corn seeds, which are not administered the agricultural composition, will also be planted.

The inoculants were prepared from isolates grown as spread plates on R2A incubated at 25° C. for 48 to 72 hours. Colonies were harvested by blending with sterile distilled water (SDW) which was then transferred into sterile containers. Serial dilutions of the harvested cells were plated and incubated at 25° C. for 24 hours to estimate the number of colony forming units (CFU) in each suspension. Dilutions were prepared using individual isolates or blends of isolates (consortia) to deliver 1×10⁵cfu/microbe/seed and seeds inoculated by either imbibition in the liquid suspension or by overtreatment with 5% vegetable gum and oil.

Seeds corresponding to the plants of table 15 were planted within 24 to 48 hours of treatment in agricultural soil, potting media or inert growing media. Plants were grown in small pots (28 mL to 200 mL) in either a controlled environment or in a greenhouse. Chamber photoperiod was set to 16 hours for all experiments on all species. Air temperature was typically maintained between 22-24° C.

Unless otherwise stated, all plants were watered with tap water 2 to 3 times weekly. Growth conditions were varied according to the trait of interest and included manipulation of applied fertilizer, watering regime and salt stress as follows:

- Low N—seeds planted in soil potting media or inert growing media with no applied N fertilizer
- Moderate N—seeds planted in soil or growing media supplemented with commercial N fertilizer to equivalent of 135 kg/ha applied N
- Insol P—seeds planted in potting media or inert growth substrate and watered with quarter strength Pikovskaya's liquid medium containing tri-calcium phosphate as the only form phosphate fertilizer.
- Cold Stress—seeds planted in soil, potting media or inert growing media and incubated at 10° C. for one week before being transferred to the plant growth room.
- Salt stress—seeds planted in soil, potting media or inert growing media and watered with a solution containing between 100 to 200 mg/L NaCl.

Untreated (no applied microbe) controls were prepared for each experiment. Plants were randomized on trays throughout the growth environment. Between 10 and 30 replicate plants were prepared for each treatment in each experiment. Phenotypes were measured during early vegetative growth, typically before the V3 developmental stage and between 3 and 6 weeks after sowing. Foliage was cut and weighed. Roots were washed, blotted dry and weighed. Results indicate performance of treatments against the untreated control.

TABLE 15

StrainShootRoot

Microbe sp.IDCropAssayIOC (%)IOC (%)

Bosea thiooxidans123EfficacyEfficacy

overall100%100%

Bosea thiooxidans54522WheatEarly vigor - insol P30-40 —

Bosea thiooxidans54522RyegrassEarly vigor50-60 50-60

Bosea thiooxidans54522RyegrassEarly vigor - moderate P0-100-10

Duganella violaceinigra111EfficacyEfficacy

overall100%100%

Duganella violaceinigra66361TomatoEarly vigor0-100-10

Duganella violaceinigra66361TomatoEarly vigor30-40 40-50

Duganella violaceinigra66361TomatoEarly vigor20-30 20-30

Herbaspirillum huttiense222Efficacy—

overall100%

Herbaspirillum huttiense54487WheatEarly vigor - insol P30-40 —

Herbaspirillum huttiense60507MaizeEarly vigor - salt stress0-100-10

Janthinobacterium sp.222Efficacy—

Overall100%

Janthinobacterium sp.54456WheatEarly vigor - insol P30-40 —

Janthinobacterium sp.54456WheatEarly vigor - insol P0-10—

Janthinobacterium sp.63491RyegrassEarly vigor - drought0-100-10

stress

Massilia niastensis112EfficacyEfficacy

overall80%80%

Massilia niastensis55184WheatEarly vigor - salt stress0-1020-30

Massilia niastensis55184WinterEarly vigor - cold stress0-1010-20

wheat

Massilia niastensis55184WinterEarly vigor - cold stress20-30 20-30

wheat

Massilia niastensis55184WinterEarly vigor - cold stress10-20 10-20

wheat

Massilia niastensis55184WinterEarly vigor - cold stress<0<0

wheat

Novosphingobium rosa211EfficacyEfficacy

overall100%100%

Novosphingobium rosa65589MaizeEarly vigor - cold stress0-100-10

Novosphingobium rosa65619MaizeEarly vigor - cold stress0-100-10

Paenibacillus amylolyticus111EfficacyEfficacy

overall100%100%

Paenibacillus amylolyticus66316TomatoEarly vigor0-100-10

Paenibacillus amylolyticus66316TomatoEarly vigor10-20 10-20

Paenibacillus amylolyticus66316TomatoEarly vigor0-100-10

Pantoea agglomerans323EfficacyEfficacy

33%50%

Pantoea agglomerans54499WheatEarly vigor - insol P40-50 —

Pantoea agglomerans57547MaizeEarly vigor - low N<00-10

Pantoea vagans55529MaizeEarly vigor<0<0

(formerly P. agglomerans)

Polaromonas ginsengisoli111EfficacyEfficacy

66%100%

Polaromonas ginsengisoli66373TomatoEarly vigor0-100-10

Polaromonas ginsengisoli66373TomatoEarly vigor20-30 30-40

Polaromonas ginsengisoli66373TomatoEarly vigor<010-20

Pseudomonas fluorescens122Efficacy—

100%

Pseudomonas fluorescens54480WheatEarly vigor - insol P>100 —

Pseudomonas fluorescens56530MaizeEarly vigor - moderate N0-10—

Rahnella aquatilis334EfficacyEfficacy

80%63%

Rahnella aquatilis56532MaizeEarly vigor - moderate N10-20 —

Rahnella aquatilis56532MaizeEarly vigor - moderate N0-100-10

Rahnella aquatilis56532WheatEarly vigor - cold stress0-1010-20

Rahnella aquatilis56532WheatEarly vigor - cold stress<00-10

Rahnella aquatilis56532WheatEarly vigor - cold stress10-20 <0

Rahnella aquatilis57157RyegrassEarly vigor<0—

Rahnella aquatilis57157MaizeEarly vigor - low N0-100-10

Rahnella aquatilis57157MaizeEarly vigor - low N0-10<0

Rahnella aquatilis58013MaizeEarly vigor0-1010-20

Rahnella aquatilis58013MaizeEarly vigor - low N0-10<0

Rhodococcus erythropolis313Efficacy—

66%

Rhodococcus erythropolis54093MaizeEarly vigor - low N40-50 —

Rhodococcus erythropolis54299MaizeEarly vigor - insol P>100 —

Rhodococcus erythropolis54299MaizeEarly vigor<0<0

Stenotrophomonas chelatiphaga611EfficacyEfficacy

60%60%

Stenotrophomonas chelatiphaga54952MaizeEarly vigor0-100-10

Stenotrophomonas chelatiphaga47207MaizeEarly vigor<0 0

Stenotrophomonas chelatiphaga64212MaizeEarly vigor0-1010-20

Stenotrophomonas chelatiphaga64208MaizeEarly vigor0-100-10

Stenotrophomonas chelatiphaga58264MaizeEarly vigor<0<0

Stenotrophomonas maltophilia612EfficacyEfficacy

43%66%

Stenotrophomonas maltophilia54073MaizeEarly vigor - low N50-60 —

Stenotrophomonas maltophilia54073MaizeEarly vigor<00-10

Stenotrophomonas maltophilia56181MaizeEarly vigor0-10<0

Stenotrophomonas maltophilia54999MaizeEarly vigor0-100-10

Stenotrophomonas maltophilia54850MaizeEarly vigor 00-10

Stenotrophomonas maltophilia54841MaizeEarly vigor<00-10

Stenotrophomonas maltophilia46856MaizeEarly vigor<0<0

Stenotrophomonas rhizophila811EfficacyEfficacy

12.5%37.5%

Stenotrophomonas rhizophila50839MaizeEarly vigor<0<0

Stenotrophomonas rhizophila48183MaizeEarly vigor<0<0

Stenotrophomonas rhizophila45125MaizeEarly vigor<0<0

Stenotrophomonas rhizophila46120MaizeEarly vigor<00-10

Stenotrophomonas rhizophila46012MaizeEarly vigor<0<0

Stenotrophomonas rhizophila51718MaizeEarly vigor0-100-10

Stenotrophomonas rhizophila66478MaizeEarly vigor<0<0

Stenotrophomonas rhizophila65303MaizeEarly vigor<00-10

Stenotrophomonas terrae221EfficacyEfficacy

50%50%

Stenotrophomonas terrae68741MaizeEarly vigor<0<0

Stenotrophomonas terrae68599MaizeEarly vigor<00-10

Stenotrophomonas terrae68599Capsicum *Early vigor20-30 20-30

Stenotrophomonas terrae68741Capsicum *Early vigor10-20 20-30

The data presented in table 15 describes the efficacy with which a microbial species or strain can change a phenotype of interest relative to a control run in the same experiment. Phenotypes measured were shoot fresh weight and root fresh weight for plants growing either in the absence of presence of a stress (assay). For each microbe species, an overall efficacy score indicates the percentage of times a strain of that species increased a both shoot and root fresh weight in independent evaluations. For each species, the specifics of each independent assay is given, providing a strain ID (strain) and the crop species the assay was performed on (crop). For each independent assay the percentage increase in shoot and root fresh weight over the controls is given.

US11871752B2. Agriculturally beneficial microbes, microbial compositions, and consortia (2024-01-16). BIOCONSORTIA, INC. [US]. Inventors: Peter Wigley [NZ], Susan Turner [US], Caroline George [NZ], Thomas Williams [US], Kelly Roberts [US], Graham Hymus [US], Kelvin Lau [NZ].

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Patent 2024

Ammonia Asparagine Aspartic Acid Biological Assay Bosea thiooxidans Calcium Phosphates Capsicum Cells Chlorophyll Cold Shock Stress Cold Temperature Crop, Avian Dietary Fiber DNA Replication Droughts Drought Tolerance Embryophyta Environment, Controlled Farmers Fertilization Glutamic Acid Glutamine Glycine Growth Disorders Herbaspirillum Herbaspirillum huttiense Leucine Lolium Lycopersicon esculentum Lysine Maize Massilia niastensis Methionine Microbial Consortia Nitrates Nitrites Nitrogen Novosphingobium rosa Paenibacillus Paenibacillus amylolyticus Pantoea agglomerans Pantoea vagans Phenotype Phosphates Photosynthesis Plant Development Plant Embryos Plant Leaves Plant Proteins Plant Roots Plants Polaromonas ginsengisoli Pseudoduganella violaceinigra Pseudomonas Pseudomonas fluorescens Rahnella Rahnella aquatilis Retention (Psychology) Rhodococcus erythropolis Rosa Salt Stress Sodium Chloride Sodium Chloride, Dietary Stenotrophomonas chelatiphaga Stenotrophomonas maltophilia Stenotrophomonas rhizophila Stenotrophomonas terrae Sterility, Reproductive Strains Technique, Dilution Threonine Triticum aestivum Tryptophan Tyrosine Vegetables Zea mays

Directed Engineering of TpH2 Enzyme

Not available on PMC !

Example 2

Directed TpH Engineering

It was found that Homo sapiens TpH2, i.e., the fragment set forth as SEQ ID NO:13; hsTpH2, was sensitive to p-chlorophenylalanine. However, mutations at residues N97 and/or P99 were found to confer resistance to p-chlorophenylalanine and to exhibit improved 5HTP biosynthesis after growing cells in the presence of 100 mg/l of tryptophan overnight at 3TC. A further, saturated mutagenesis, study found that isoleucine (I) was a beneficial amino acid change at residue N97, while cysteine (C), aspartic acid (D), leucine (L) and glutamine (Q) were shown to be beneficial at residue P99. In particular, the combined changes 1\197I/P99D in hsTpH2 showed a >15% increase in 5HTP production in the presence of 100 mg/l tryptophan and the combined changes N97I/P99C in hsTpH2 showed a >25% increase in 5HTP biosynthesis, over the parent TPH2 sequence (SEQ ID NO:13) after acquiring the E2K mutation.

US11866749B2. Optimized microbial cells for production of melatonin and other compounds (2024-01-09). Danmarks Tekniske Universitet [DK]. Inventors: Hao Luo [DK], Jochen Förster [DK].

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Patent 2024

5-Hydroxytryptophan Amino Acids Anabolism Aspartic Acid Cells Cysteine Fenclonine Glutamine Homo sapiens Isoleucine Leucine Melatonin Mutagenesis Mutation Parent Tryptophan

Enzyme Activity Assays in Fabry Mice

GLA activities were determined in Fabry mouse tissues using previously described methods (Desnick et al., 1973 (link)). In brief, tissue samples were homogenized in chilled reporter lysis buffer (Promega) and protease inhibitor (Pierce) was added to the lysates. Protein concentrations were determined using the Bio-Rad Colorimetric Protein Assay Kit. 10 μL of tissue lysate was added to an equal volume of 10 mM 4-methylumbelliferyl-α-D-galactopyranoside (Sigma-Aldrich), dissolved in assay buffer (0.2 M citrate, 0.4 M phosphate buffer, pH 4.4), and 0.1 M N-acetylgalactosamine (Sigma Aldrich), the latter to inhibit α-galactosidase B activity (Mayes et al., 1981 (link)). Following a 30 min incubation at 37°C, reactions were terminated by the addition of 480 μL of 0.1 M ethylenediamine, pH 10.3. The amount of 4-methylumbelliferone (4-MU) produced was determined by measuring fluorescence using a Synergy H1 fluorometer (BioTek). Tissue α-Gal A activities were expressed as nmol of 4-MU produced per h per mg of total protein (nmol/h/mg). Measurement of plasma GLA activities in wildtype mice for PK studies was performed as described above with the following modifications: lysates were incubated with 5 mM 4-methylumbelliferyl α-D-galactopyranoside in assay buffer [20 mM citrate, 30 mM sodium phosphate (pH 4.4), 0.1 M N-acetylgalactosamine, and 4 mg/mL BSA], and the reaction was stopped by addition of stop buffer (0.1 M Glycine, 0.1 N NaOH], as previously described (Shen et al., 2016 (link)).
AGA activity was measured with 1 mM L-aspartic acid β-(7- amido-4-methylcoumarin) in 10% SuperBlock and 90% 50 mM Tris-HC (pH 7.5) for 60 min at 37°C, and then adding 100 µL of stop buffer [0.2 M glycine, 0.175 M NaOH (pH 10.6)], as previously described (Mononen et al., 1993 (link)). GUSB enzyme assay was performed using 10 mM 4-methylumbelliferyl-β-D-glucuronide (Merck) in 0.1 M sodium acetate (pH 4.6) at 37°C for 30 min, and reactions were stopped by 0.1 M sodium carbonate (Grubb et al., 2008 (link)). GAA activity assay was performed with 3 mM 4-methylumbelliferyl-a-D-glucopyranoside (Merck) in assay buffer (30 mM sodium citrate, 40 mM sodium phosphate dibasic, pH 4.0) at 37°C for 3 h (Flanagan et al., 2009 (link)). Reactions were stopped by the addition of an equal volume of 0.4 M glycine, pH 10.8. IDS activity assay was performed with 2.5 mM 4-Methylumbelliferyl sulfate potassium salt (Merck) in 50 mM sodium acetate, at 37°C for 4 h (Dean et al., 2006 (link)). Reactions were stopped with glycine carbonate buffer (pH 10.7). Fluorescence was measured by microplate reader with 360/40 nm excitation and 440/30 nm emission filters.

Chen Y.H., Tian W., Yasuda M., Ye Z., Song M., Mandel U., Kristensen C., Povolo L., Marques A.R., Čaval T., Heck A.J., Sampaio J.L., Johannes L., Tsukimura T., Desnick R., Vakhrushev S.Y., Yang Z, & Clausen H. (2023). A universal GlycoDesign for lysosomal replacement enzymes to improve circulation time and biodistribution. Frontiers in Bioengineering and Biotechnology, 11, 1128371.

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Publication 2023

4-benzaldehydesulfonic acid 4-methylumbelliferyl sulfate, potassium salt 7-methylcoumarin Acetylgalactosamine Aspartic Acid Biological Assay Buffers Carbonates Cardiac Arrest Citrates Colorimetry Enzyme Assays Ethylenediamines Exhaling Fluorescence Galactose Galactosidase Glucuronides Glycine Hymecromone Mice, House Phosphates Plasma Promega Protease Inhibitors Proteins RRAD protein, human Sodium Acetate sodium carbonate Sodium Citrate sodium phosphate Tissues Tromethamine

Artificial Saliva Preparation and Matrix Interactions

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Publication 2023

Alanine Albumins Ammonia Amylase Ascorbic Acid Aspartic Acid Biological Assay Buffers Calcium chloride Cysteine Glutamic Acid Glycine Histidine Homo sapiens Isoleucine Leucine Lysine Magnesium Chloride Methionine Phenylalanine Potassium Chloride potassium phosphate, monobasic Proline Rivers Saliva, Artificial Serine Serum Sodium Chloride sodium phosphate, monobasic Technique, Dilution tecogalan sodium Threonine Tryptophan Tyrosine Urea Valine

SARS-CoV-2 Spike Protein Detection

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Publication 2023

Alanine Albumins Ammonia Amylase Ascorbic Acid Aspartic Acid Biopharmaceuticals Blood Calcium chloride Carbon Black Chlorides Cystamine Dihydrochloride Electric Conductivity Glucans Glutamic Acid Glutaral Glycine Gold Graphite Histidine Homo sapiens Hydrochloric acid Immunoglobulins Isoleucine isononanoyl oxybenzene sulfonate Leucine Lysine Magnesium Chloride Males Men Methionine Nails Phenylalanine Polyethylene Terephthalates Polymers Potassium Chloride potassium ferricyanide potassium ferrocyanide potassium phosphate, dibasic potassium phosphate, monobasic Powder Proline Recombinant Proteins Saliva SARS-CoV-2 Serine Serum Serum Albumin, Bovine Silver sodium borohydride Sodium Chloride Sodium Citrate Dihydrate sodium phosphate, monobasic Soft Drinks Strains Sulfuric Acids Threonine Tryptophan Tyrosine Urea Valine

Top products related to «Aspartic Acid»

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L-aspartic acid is a naturally occurring amino acid used in various laboratory applications. It serves as a building block for proteins and plays a role in cellular processes. This product is suitable for use in biochemical research and analysis.

Aspartic acid by Merck Group

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Aspartic acid is a non-essential amino acid commonly used as a laboratory reagent. It serves as a building block for proteins and is involved in various metabolic processes. The product is intended for research and analytical applications.

Glycine by Merck Group

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Glycine is a colorless, crystalline amino acid that is used as a raw material in the production of various pharmaceutical and chemical products. It serves as a key component in buffer solutions and is commonly employed in the preparation of cell culture media and various biological assays.

L glutamic acid by Merck Group

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L-glutamic acid is a naturally occurring amino acid that serves as a key ingredient in various laboratory applications. It is a white, crystalline powder with a molecular formula of C₅H₉NO₄. L-glutamic acid plays a crucial role in numerous biochemical processes and is commonly used in chemical analysis, buffer preparation, and as a building block for other compounds.

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Glutamic acid is a laboratory chemical compound used as a buffer and pH adjuster in various experimental procedures. It serves to maintain the desired pH levels in solutions and biological samples.

Phenylalanine by Merck Group

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Phenylalanine is an amino acid that is used as a laboratory reagent. It is a colorless and odorless crystalline solid. Phenylalanine is a naturally occurring essential amino acid that is required for protein synthesis.

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Arginine is an amino acid used in the production of various laboratory equipment. It is a key component in the manufacture of buffers, reagents, and other solutions essential for scientific research and analysis.

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Alanine is a laboratory equipment product manufactured by Merck Group. It is an amino acid commonly used in biochemical and analytical applications.

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L-phenylalanine is an essential amino acid that serves as a fundamental building block for proteins. It is a commonly used laboratory reagent in various applications, including biochemical research and analysis.

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L-valine is an amino acid that serves as a building block for proteins. It is a colorless, crystalline solid that is soluble in water and alcohol. L-valine is commonly used in the production of pharmaceutical and laboratory products.

What are the different types or variations of Aspartic Acid?

How can Aspartic Acid be used in research and applications?

Aspartic acid is a versatile amino acid with a wide range of research and application potentials. It is commonly used as a precursor for the synthesis of other important biomolecules, such as asparagine and various neurotransmitters. Aspartic acid also plays a crucial role in the citric acid cycle, making it essential for energy production and metabolism. Additionally, it has been studied for its potential applications in fields like immunology, where it may influence immune cell function and signaling.

What are some common usage challenges with Aspartic Acid?

One of the key challenges with working with Aspartic Acid is ensuring accurate and reproducible results. Due to its central role in various biological processes, minor variations in experimental protocols can significantly impact the outcomes. Researchers may struggle to identify the most effective methods for isolating, purifying, and quantifying Aspartic Acid from samples. Proper handling and storage conditions are also critical to maintain the integrity of Aspartic Acid.

How can PubCompare.ai help with Aspartic Acid research?

PubCompare.ai's AI-driven platform can be invaluable for researchers working with Aspartic Acid. The platform allows you to efficiently screen a vast database of literature, pre-prints, and patents to identify the most accurate and reproducible protocols. By leveraging AI to pinpiont critical insights, PubCompare.ai can help you compare multiple protocols side-by-side and choose the optimal approach for your specific research goals. This can save time, improve the reliability of your results, and enhance your overall productivity in Aspartic Acid-related studies.

More about "Aspartic Acid"

Aspartic acid, also known as L-aspartic acid or Asp, is a non-essential amino acid that plays a crucial role in various biological processes.
This versatile compound serves as a building block for proteins and is involved in the citric acid cycle, a key metabolic pathway.
Aspartic acid can be synthesized within the body and is also obtained through dietary sources, such as dairy products, legumes, and certain meats.
Aspartate and its related compounds, including L-glutamic acid (Glu), glycine (Gly), phenylalanine (Phe), arginine (Arg), and alanine (Ala), have been extensively researched for their potential applications in fields like neuroscience, immunology, and cell signaling.
Studies have explored the use of L-aspartic acid, L-phenylalanine, and L-valine in nutritional supplements and therapeutic interventions.
PubCompare.ai's AI-driven platform can help researchers identify the most accurate and reproducible protocols for working with aspartic acid and its related compounds, enabling efficient and reliable investigations.
By comparing multiple protocols side-by-side, researchers can pinpoint the optimal approach to address their specific research needs and deliver reliable results.