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Dimethylamine

Dimethylamine is a chemical compound with the formula (CH3)2NH.
It is a colorless, flammable gas with a strong, fishy odor.
Dimethylamine is used in the production of various pharmaceuticals, pesticides, and other industrial chemicals.
It is also a naturally occurring substance found in some foods and is a byproduct of the decomposition of organic matter.
Researchers may use dimethylamine in a variety of applications, such as in the synthesis of other chemicals or as a precursor for the production of more complex molecules.
When studying dimethylamine, it is important to consider its phsycial and chemical properties, potential hazards, and appropriate safety measures.
PubCompare.ai can help streamline dimethylamine research by providing access to relevant protocols and enabling comparisons to identify the best approaches for your needs.

Most cited protocols related to «Dimethylamine»

All NMR experiments were performed
at 298 K on a Bruker Avance III 800 MHz spectrometer equipped with
a cryogenically cooled probe and Z-gradients suitable for inverse
detection. A few spiking experiments were performed on a Bruker 700
MHz spectrometer equipped with a room temperature probe and Z-gradients
suitable for inverse detection. The one-pulse or NOESY pulse sequence
along with the CPMG (Carr–Purcell–Meiboom–Gill)
pulse sequence, all with water suppression using presaturation, were
used for 1H 1D NMR experiments. To confirm unknown metabolite
identification, spectra were obtained after each addition of 5–10
μL of stock solution (1 mM) of the authentic compounds to the
methanol-precipitated (2:1 v/v) serum samples (see SI Table S1); in the case of volatile compounds, such as acetone,
ethanol, 2-butanol, dimethylamine, and urea, spiking experiments were
performed using ultrafiltered serum samples. To enable comparison
of metabolite concentrations from various protein precipitation methods
(SI Table S2), the CPMG experiments were
performed with 128 transients and a sufficiently long recycle delay
(D1 = 15 s). To aid unknown metabolite identification, homonuclear
two-dimensional (2D) experiments, such as 1H–1H double quantum filtered correlation spectroscopy (DQF-COSY)
and 1H–1H total correlation spectroscopy
(TOCSY) experiments, were performed on serum samples after protein
precipitation using methanol (2:1 v/v). The 2D experiments were performed
with suppression of the residual water signal by presaturation during
the relaxation delay. For DQF-COSY and TOCSY experiments, sweep widths
of 9600 Hz were used in both dimensions; 512 or 400 FIDs were obtained
with t1 increments for DQF-COSY or TOCSY,
respectively, each with 2048 complex data points. The number of transients
used was 16, and the relaxation delay was 2.0 s for DQF-COSY and 1.5
s for TOCSY. The resulting 2D data were zero-filled to 1024 points
in the t1 dimension. A 90° shifted
squared sine-bell window function was applied to both dimensions before
Fourier transformation. Chemical shifts were referenced to the internal
TSP signal for 1H 1D or 2D spectra. Bruker Topspin versions
3.0 or 3.1 software packages were used for NMR data acquisition, processing,
and analyses.
Publication 2014
1H NMR 2-butanol Acetone dimethylamine Ethanol Gills Methanol Proteins Pulse Rate Recycling Serum Short Interspersed Nucleotide Elements Spectrum Analysis Transients Urea
Calibration standards and serum samples were prepared in the same manner. The following concentrations of calibrators, in water, were used: 5, 12.5, 25, 50, 100, 150, 200, 250 µM for l-arginine, 0.05, 0.13, 0.25, 0.5, 1.0, 1.5, 2, and 2.5 µM for ADMA and SDMA, and 1, 2.5, 5, 10, 20, 30, 40, and 50 µM for l-citrulline, and 0.14, 0.35, 0.7, 1.4, 2.8, 4.2, 5.6, 7.0 µM for DMA. The following procedure was conducted: 100 µL aliquots of calibration standards or serum, 10 µL of internal standard solution (50 µM D6-DMA, 20 µM D7-ADMA, and 100 µM D7-arginine, respectively) and 50 µL of borate buffer (0.025 M Na2B4O7·10H2O, 1.77 mM NaOH, pH 9.2) were placed into 2.0 mL polypropylene tubes and vortexed (1 min, 25 °C). Derivatization was conducted using 400 µL of acetonitrile (ACN) and 10 µL of 10% BCl in ACN. The solutions were incubated and vortexed (5 min, 25 °C), centrifuged (7 min, 10,000 RPM, 4 °C), and 100 µL of the clear supernatant was transferred into glass vials containing 400 µL of water.
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Publication 2018
acetonitrile Arginine BCL10 protein, human Borates Buffers Citrulline Polypropylenes Serum
Benzoyl chloride (BCl), hydrochloride salts of unlabeled dimethylamine (D0-DMA), hexadeutero-dimethylamine (D6-DMA, declared as 99 at.% 2H), l-arginine, SDMA, ADMA, l-citrulline, and sodium tetraborate were procured from Sigma-Aldrich (Poznan, Poland). Isotope-labeled l-arginine:HCl (D7-arginine, 98%) and asymmetric dimethylarginine (2,3,3,4,4,5,5-D7-ADMA, 98%) were obtained from Cambridge Isotope Laboratories (Tewksbury, MA, USA). Methanol, acetonitrile, water, and formic acid were acquired from Merck Millipore (Warsaw, Poland), and leucine–enkephalin was obtained from Waters (Milford, MA, USA).
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Publication 2018
acetonitrile Arginine benzoyl chloride Citrulline dimethylamine dimethylamine hydrochloride Enkephalin, Leucine formic acid Isotopes Methanol N,N-dimethylarginine Salts sodium borate
Sialic acid linkage-specific derivatization by ethyl esterification was performed as described previously12 (link). Briefly, 1 µL of released plasma N-glycans (containing the released glycans from 0.2 µL of plasma) was added to 20 µL ethyl esterification reagent (250 mM EDC and 250 mM HOBt in EtOH) and incubated for 1 h at 37 °C. Subsequently, 20 µL MeCN was added and N-glycans were purified by cotton HILIC SPE as described before12 (link),29 (link). Samples were eluted in 10 µL MQ. In addition, an amidation step was introduced in the protocol, for the robust stabilization of the α2,3-linked sialic acids, by adding 4, 6 or 8 µL of 28% NH4OH to the reaction mixture after 1 h incubation. The addition of the ammonia was followed by an incubation step of 2 h at 37 °C. After incubation, 24, 26 or 28 µL MeCN was added to the mixture and the N-glycans were purified by cotton HILIC SPE, with an elution in 10 µL MQ. The optimized ethyl esterification protocol with amidation step (EEA) used 4 µL of 28% NH4OH solution. Furthermore, another option for the linkage-specific derivatization of the sialic acids was investigated, in which the sialic acids were differentially modified by double amidation (DA), as described previously11 (link). Briefly, 1 µL of released plasma N-glycans was added to 20 µL dimethylamidation reagent (250 mM dimethylamine, 250 mM EDC and 500 mM HOBt and in DMSO) and incubated for 1 h at 60 °C. An additional incubation followed of 2 h at 60 °C after the addition of 8 µL 28% NH4OH. Eighty microlitres of MeCN was added to the samples and the derivatized N-glycans were purified by cotton HILIC SPE, with elution in 10 µL MQ.
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Publication 2019
1-hydroxybenzotriazole Ammonia dimethylamine Esterification Ethanol Gossypium N-Acetylneuraminic Acid Plasma Polysaccharides Sialic Acids Sulfoxide, Dimethyl
M.HpaII-His6 was expressed and purified as previously described (Duxin et al., 2014 (link)). Briefly, pHpaII-Avitag-His6 was transformed in T7 Express Competent E.coli cells (NEB), cells cultured in the presence of 100 μg/mL ampicillin until the OD600 reached 0.7. The culture was supplemented with 0.5 mM IPTG for 3 hours, collected by centrifugation and resuspended in 15 mL Lysis Buffer (20 mM Tris pH 8.5, 500 mM KCl, 10% glycerol, 10 mM imidazole and protease inhibitors (Roche)). Cells were lysed by sonication and cleared by centrifugation at 20, 000 x g for 30 min. Cleared lysate was applied onto Ni-NTA resin (QAGEN). The resin was washed with 25 mL of Lysis Buffer containing 30 mM imidazole and the protein eluted with Elution Buffer (20 mM Tris pH 8.5, 100 mM KCl, 10% glycerol and 250 mM imidazole). Eluate was dialyzed overnight in Storage Buffer (20 mM Tris pH 8.5, 100 mM KCl, 1 mM DTT, 30% glycerol) and protein aliquots snap frozen and kept at −80°C. To generate lysine-methylated M.HpaII, purified M.HpaII-His6 was first denatured by dialyzing against 20 mM HEPES pH 7.5, 100 mM KCl, 6M Guanidine HCl, 10% glycerol. Denatured M.HpaII protein was then methylated using Reductive Alkylation Kit (Hampton Research) via the addition of dimethylamine borane and formaldehyde according to the manufacturer’s protocols. The methylation reaction was stopped by addition of 100 mM Tris pH 7.5 and 5 mM DTT (final concentrations). Methylated M.HpaII was then renatured by sequentially dialyzing against Renaturing Buffer (20 mM Tris pH 8.5, 100mM KCl, 1mM DTT, 10% glycerol) supplemented with 4, 2, and 0 M Guanidine HCl for 1 hr each at 4°C. The renatured protein was then dialyzed against storage buffer (20 mM Tris pH 8.5, 100 mM KCl, 1 mM DTT, 30% glycerol) and stored at −80°C.
LacI-biotin protein was purified from T7 Express Competent cells (NEP) (Duxin et al., 2014 (link)). Briefly, pET11a-LacI and pBirAcm (Avidity) were co-transformed and cells cultured in the presence of 100 μg/mL ampicillin and 34 μg/mL chloramphenicol at 37°C until OD600 reached 0.6. The culture was supplemented with 1 mM IPTG and 50 μM biotin for 2 hours. Cells were collected by centrifugation and resuspended in Buffer 1 (50 mM Tris pH 7.5, 5 mM EDTA, 100 mM NaCl, 10% sucrose, 1 mM DTT, protease inhibitors (Roche), 0.2 mg/mL lysozyme (Sigma), 0.1% Brij 58) and rotated for 30 min at room temperature. The cell lysate was pelleted by centrifugation for 60 min at 20, 000 x g and the insoluble pellet was resuspended in 10 mL of Extraction Buffer (50 mM Tris pH 7.5, 5 mM EDTA, 1M NaCl, 30 mM IPTG, 1 mM DTT and protease inhibitors). The resuspended pellet was homogenized by sonication and pelleted again for 60 min at 20, 000 x g. The supernatant was collected and 1% polymin P was added to 0.045%. Lysate was rotated for 30 min at 4°C and pelleted at 20, 000 x g for 20 min. The supernatant was transferred to a new tube and ammonium sulfate was added to a final saturation of 37% followed by rotation for 30 min at 4°C. The pellet was recovered and resuspended in 2 mL of Wash Buffer (50 mM Tris pH 7.5, 1 mM EDTA, 100 mM NaCl, 1 mM DTT and protease inhibitors). The resuspension was applied to a column containin 1 mL of softlink avidin resin and inbutated for 1 hour at 4°C. The column was washed with 15 mL of Wash Buffer, and the protein eluted with Elution buffer (50 mM Tris pH 7.5, 1 mM EDTA, 100 mM NaCl, 1 mM DTT and 5 mM biotin). Protein was dialyzed overnight with Dialysis Buffer (50 mM Tris pH 7.5, 1 mM EDTA, 150 mM NaCl, 1 mM DTT and 30% glycerol) and stored at −80°C.
Xenopus SPRTN with an N-terminal FLAG tag was cloned into pFastBac1 (Thermo Fisher Scientific) using primers A and B. SPRTN mutations were introduced via Quikchange mutagenesis and confirmed by Sanger sequencing. SPRTN Baculoviruses were prepared using the Bac-to-Bac system (Thermo Fisher Scientific) according to the manufacturer’s protocols. SPRTN was expressed in 250 mL suspension cultures of Sf9 insect cells (Thermo Fisher Scientific) by infection with SPRTN baculovirus for 48 hr. Sf9 cells were subsequently collected via centrifugation and resuspended in Lysis Buffer (50 mM Tris pH 7.5, 500 mM NaCl, 10% Glycerol, 1X Roche EDTA-free Complete protease inhibitor cocktail, 0.5 mM PMSF, 0.2% Triton X-100). To lyse cells, the suspension was subjected to three freeze/thaw cycles, passed through a 21 g needle, and then sonicated. The cell lysate was spun at 25000 rpm in a Beckman SW41 rotor for 1hr. The soluble fraction was collected and then incubated with 200 μL anti-FLAG M2 affinity resin (Sigma) for 90 min at 4°C. The resin was then washed once with 10 mL Lysis Buffer, twice with Wash Buffer (50 mM Tris pH 7.5, 500 mM NaCl, 10% Glycerol, 0.2% Triton X-100), and three times with Buffer A (50 mM Tris pH 7.5, 500 mM NaCl, 10% Glycerol). FLAG-SPRTN was eluted with Buffer A supplemented with 100 μg/mL 3xFLAG peptide (Sigma). Elution fractions containing FLAG-SPRTN protein were pooled and dialyzed against 20 mM Tris pH 7.5, 300 mM NaCl, 10% Glycerol, 1mM DTT at 4°C for 12 hr and then dialyzed against Storage Buffer (20 mM Tris pH 7.5, 150 mM NaCl, 10% Glycerol, 1mM DTT) at 4°C for 3 hr. Aliquots of FLAG-SPRTN were then stored at −80°C.
Xenopus recombinant TRAIP wild-type (WT) and TRAIP R18C were expressed and purified with a 6xHis-SUMO tag in bacteria. Briefly, Rosetta 2 (DE3) pLysS competent cells (Novagen) were transformed with pH6-SUMO-TRAIP WT or pH6-SUMO TRAIP R18C and cells grown in the presence of 100 μg/mL ampicillin and 27 μg/mL chloramphenicol at 37°C until OD600 reached 0.6. Cells were then transferred to 16°C for 30 min and supplemented with 0.1 mM IPTG and 50 μM ZnSO4 overnight. The culture was collected by centrifugation and resuspended in Lysis Buffer (20 mM HEPES pH 7.5, 400 mM sodium acetate, 10% glycerol, 20 mM imidazole, 10 μM ZnSO4, 0.1% NP-40, 1 mM DTT and protease inhibitors). The lysate was sonicated, and ammonium sulfate and polyethyleneimine were added to final concentrations of 300 mM and 0.45%, respectively, and incubated for 15 min at 4°C. The lysate was centrifuged at 40, 000 x g for 45 min and the soluble fraction recovered and precipitated with ammonium sulfate. The precipitated fraction was collected by centrifugation at 40,000 x g for 45 min and resuspended in Lysis Buffer and rotated for 30 min with NiNTA resin at room temperature. The resin was washed three times with Wash Buffer (20 mM HEPES pH 7.5, 400 mM sodium acetate, 10% glycerol, 20 mM imidazole, 10 μM ZnSO4, 0.01% NP-40, 1 mM DTT and protease inhibitors) and the protein was eluted from resin with Elution Buffer (20 mM HEPES pH 7.5, 400 mM sodium acetate, 10% glycerol, 120 mM imidazole, 10 uM ZnSO4, 0.01% NP-40, 1 mM DTT). The eluate was then dialized with Dialysis Buffer (20 mM HEPES pH 7.5, 400 mM sodium acetate, 120 mM imidazole, 10% glycerol) overnight at 4°C in the presence of 0.03 mg/mL Ulp1. Aliquots were flash frozen and stored at −80°C.
Xenopus recombinant 6xHis-Geminin was expressed and purified as previously described (McGarry and Kirschner, 1998 (link)). Briefly, BL21 cells were transformed with pET28a-His-Geminin and cultured until the OD600 reached 0.6. The culture was supplemented with 0.5 mM IPTG for 3 hours, collected by centrifugation and resuspended in 10 mL Buffer S (50 mM NaPi pH 7.6, 5 mM BME, 1 mM PMSF and 2 mM benzamidine) containing 10 mg lysozyme and 1% Triton X-100. Cells were incubated for 10 min at room temperature and supplemented with 1 mL of 5M NaCl. Cells were then sonicated and pelleted at at 20, 000 x g for 30 min. Cleared lysate was supplemented with 20 mM imidazole and applied onto Ni-NTA resin (QAGEN) for 1 hour at 4C. The resin was washed with Buffer W (50 mM NaPi pH 7.6, 0.5 M NaCl, 0.1% Triton X-100, 5 mM BME, 20 mM imidazole), and the protein eluted with Elution Buffer (50 mM NaPi pH 7.6, 0.5M NaCl, 5 mM BME). The protein was dialyzed overnight with (10 mM Tris pH 8, 0.5M NaCl and 5% glycerol). Aliquots were flash frozen and stored at −80°C.
Primer A: 5′ – GAT CGG ATC CAT GGA CTA CAA AGA CGA TGA CGA CAA GGG TGA TAT GCA GAT GTC GGT AG – 3′
Primer B: 5′- GAT CCT CGA GTT ATT ATG TAT TGC AGT TTT GTA AGC AGG TGT CTA AAT G −3′
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Publication 2019

Most recents protocols related to «Dimethylamine»

N, N, N’-trimethyl-1,3-propanediamine (10.0 g; 0.0861 mol) was dissolved in a 200 mL tetrahydrofuran–triethylamine (v:v, 1:1) mixture, after which the appropriate alkanoyl (decanoyl, dodecanoyl, tetradecanoyl, or hexadecanoyl) chloride (0.0861 mol) was added dropwise during intensive stirring. After that, the reaction mixture was stirred for 6 h at room temperature, followed by the filtration of triethylamine hydrochloride, the by-product. The filtrate was then evaporated and cautiously dried under reduced pressure to obtain N-[3-(dimethylamine)propyl]-N-methyoalkylamides as viscous liquids. The yield we obtained was 98–99.5%.
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Publication 2024
A mixture of disubstituted triazine 10 (3 mmol) and dimethylamine (3 mmol) in dioxane (15 mL) was stirred at room temperature for 1 h. The mixture was poured onto crushed ice, filtered, and washed with water.
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Publication 2024
The chemicals used in the experiments were of analytical grade and HPLC grade. Trimethylamine hydrochloride (TMA.HCl), Dimethylamine hydrochloride (DMA.HCl), Methylamine hydrochloride (MMA.HCl) were purchased from Himedia and Trimethylamine n-oxide dihydrate from Sigma Aldrich. The syringe-driven lters (MCE hydrophilic, 0.22µm pore size, 13mm diameter) were purchased from Himedia and Eppendorf tubes from Tarsons.
Publication 2024
1,3-Dichloro-2-propanol, propanol, sodium carbonate, 1-dodecene, 1-octene, 1-tetradecene, 1-hexadecene, hydrogen peroxide, phosphotungstic acid, phosphoric acid ethyl alcohol, and methyl alcohol were purchased from Aladdin. Diethyl ether, dodecyl-tetradecyl-dimethylamine, and sodium tungstate were purchased from Wilmar. The above reagents were analytically pure samples. The standard samples used for gas chromatography (1-dodecene, 1-octene, dodecane epoxide and epoxyoctane) were chromatographically pure and purchased from Aladdin.
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Publication 2024
1-bromohexane (98%), 1-bromooctane (99%), 1-bromodecane (98%) and 1-bromododecane (95%) were obtained from Sigma-Aldrich Co. (St. Louis, MO, USA). Dimethylamine hydrochloride (99%) was purchased from Acros Organics company (Geel, Belgium). Diethyl ether (99.5%), ethanol (99.8%), acetone (99.5%), sodium hydroxide (99%) and ethyl chloroacetate (99%) were purchased from POCH S.A. (Gliwice, Poland). Deionized water used for synthesis had a specific conductivity not higher than 0.4 μS∙cm−1 at 20 °C.
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Publication 2024

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Dimethylamine is a colorless, flammable gas with a fishy odor. It is commonly used as a chemical intermediate in the production of various pharmaceuticals, pesticides, and other industrial chemicals.
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Methanol is a clear, colorless, and flammable liquid that is widely used in various industrial and laboratory applications. It serves as a solvent, fuel, and chemical intermediate. Methanol has a simple chemical formula of CH3OH and a boiling point of 64.7°C. It is a versatile compound that is widely used in the production of other chemicals, as well as in the fuel industry.
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Formic acid is a colorless, pungent-smelling liquid chemical compound. It is the simplest carboxylic acid, with the chemical formula HCOOH. Formic acid is widely used in various industrial and laboratory applications.
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Trimethylamine is a colorless, flammable gas with a fishy odor. It is commonly used as a reagent in organic synthesis and as a precursor for other chemical compounds.
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Acetonitrile is a colorless, volatile, flammable liquid. It is a commonly used solvent in various analytical and chemical applications, including liquid chromatography, gas chromatography, and other laboratory procedures. Acetonitrile is known for its high polarity and ability to dissolve a wide range of organic compounds.
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Ethanol is a clear, colorless liquid chemical compound commonly used in laboratory settings. It is a key component in various scientific applications, serving as a solvent, disinfectant, and fuel source. Ethanol has a molecular formula of C2H6O and a range of industrial and research uses.
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L-arginine is an amino acid that plays a crucial role in various physiological processes. It serves as a substrate for the production of nitric oxide, which is essential for maintaining healthy blood flow and cardiovascular function. This lab equipment product can be utilized for research and scientific applications related to the study of L-arginine and its associated biological functions.
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DMSO is a versatile organic solvent commonly used in laboratory settings. It has a high boiling point, low viscosity, and the ability to dissolve a wide range of polar and non-polar compounds. DMSO's core function is as a solvent, allowing for the effective dissolution and handling of various chemical substances during research and experimentation.
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The Agilent 6410 Series Triple Quadrupole mass spectrometer is a sensitive and selective analytical instrument designed for quantitative and qualitative analysis of chemical compounds. It utilizes triple quadrupole technology to provide accurate mass measurements and fragmentation data for the identification and quantification of target analytes.
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Sodium borohydride is a reducing agent commonly used in organic synthesis and analytical chemistry. It is a white, crystalline solid that reacts with water to produce hydrogen gas. Sodium borohydride is frequently employed in the reduction of carbonyl compounds, such as aldehydes and ketones, to alcohols. Its primary function is to facilitate chemical transformations in a laboratory setting.

More about "Dimethylamine"

Dimethylamine (DMA) is a colorless, flammable gas with a strong, fishy odor.
It is a chemical compound with the formula (CH3)2NH and is used in the production of various pharmaceuticals, pesticides, and other industrial chemicals.
DMA is also a naturally occurring substance found in some foods and is a byproduct of the decomposition of organic matter.
Researchers may use dimethylamine in a variety of applications, such as in the synthesis of other chemicals or as a precursor for the production of more complex molecules.
When studying dimethylamine, it is important to consider its physical and chemical properties, potential hazards, and appropriate safety measures.
Related compounds and terms include methanol, formic acid, trimethylamine, acetonitrile, ethanol, L-arginine, and DMSO.
These substances may be used in conjunction with or as alternatives to dimethylamine in various research and industrial applications.
For example, the Agilent 6410 Series Triple Quadrupole mass spectrometer can be used to analyze and detect dimethylamine and other related compounds.
Sodium borohydride is another chemical that may be used in reactions involving dimethylamine.
PubCompare.ai, the leading AI platform for reproducible protocols, can help streamline dimethylamine research by providing access to relevant protocols and enabling comparisons to identify the best approaches for your needs.
Easily locate protocols from literature, pre-prints, and patents, and leverage AI-driven comparisons to optimize your dimethylamine research.