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Triethanolamine

Triethanolamine is a versatile organic compound with a wide range of applications in research and industry.
It is a colorless, viscous liquid with a mild odor, and is commonly used as a surfactant, pH adjuster, and emulsifier.
Triethanolamine plays a key role in a variety of research areas, including cosmetics, pharmaceuticals, and materials science.
Optimizing research protocols for triethanolamine can be a time-consuming and challenging task, but PubCompare.ai's AI-driven platform can help streamline the process.
The platform allows researchers to easily locate relevant protocols from literature, pre-prints, and patents, and leverages AI-powered comparisons to identify the best protocols and products.
This can improve reproducibility and enhance the overall efficiency of the research workflow.
Whether you're studying the chemical properties of triethanolamine or exploring its applications, PubCompare.ai's innovative solution can be a valuable tool in your research arsenal.

Most cited protocols related to «Triethanolamine»

1
Urine Exosome Isolation and Analysis
Cited 22 times
Urine (96 ml) was used for centrifugation. Urine samples were placed in a centrifuge (Beckman L8-70M ultracentrifuge; Beckman Coulter, Fullerton, CA) and centrifuged at 17,000 × g for 10 min at 37 °C (13,600 r.p.m.). The supernatant was saved and the 17,000 × g pellets were resuspended in an isolation solution (250 mM sucrose, 10 mM triethanolamine (pH 7.6)) followed by incubation with either DTT (final concentration of 200 mg/ml; MP Biomedicals, Solon, OH) or vehicle at 37 °C for 5–10 min. During the DTT or vehicle incubation, samples were vortexed every 2 min. The temperature, incubation time, and DTT concentration were chosen on the basis of preliminary experiments (see Supplementary Figures). The incubated suspensions were then transferred to clean centrifuge tubes (Beckman polycarbonate catalog no. 355630) and more isolation solution was added to a final volume of 8 ml. The samples were centrifuged again at 17,000 × g for 10 min at 37 °C. The two supernatants from the 17,000 × g spins were pooled and ultracentrifuged at 200,000 × g for 1 h at 37 °C. Pellets were solubilized in 1.5% SDS and 50 mM Tris-HCl (pH 6.8). These samples were used for immunoblotting as described below. For the electron microcopy of urinary exosomes, pellets obtained from the 200,000 × g spin from each subject were resuspended in 1 × phosphate-buffered saline.
Fernández-Llama P., Khositseth S., Gonzales P.A., Star R.A., Pisitkun T, & Knepper M.A. (2010). Tamm-Horsfall protein and urinary exosome isolation. Kidney International, 77(8), 736-742.
Publication 2010
Centrifugation Electrons Exosomes isolation Pellets, Drug Phosphates polycarbonate Saline Solution Solon Sucrose triethanolamine Tromethamine Urine
2
Mitochondrial Respiration in Type 2 Diabetes
Cited 15 times
Subjects Informed consent was obtained from all subjects. The study was conducted in accordance with the principles of the Declaration of Helsinki, and was approved by the local ethics committee for Frederiksberg and Copenhagen County. Mitochondrial respiration was measured in permeabilised skeletal muscle fibres obtained from needle biopsies of the vastus lateralis in men with (n = 11) or without (control; n = 8) type 2 diabetes. The characteristics of the subjects are provided in Table 1 and Fig. 1. All subjects were in good health but classified as living a typical Westernised sedentary lifestyle, participating only in routine activities of daily living (walking, gardening, etc.) and not engaged in regular structured or individualised aerobic or strength training programmes or athletics. None of the control subjects had a family history of diabetes and none was receiving treatment for a disease. The diabetic patients were treated for their diabetes with diet or oral glucose-lowering medicine. All medications were withheld 24 h prior to the experiment. The patients with type 2 diabetes had no clinical signs of long-term diabetic complications and were representative of patients treated in the primary care sector.

Characteristics of the subjects

 Type 2 diabetic subjects (n = 11)Control subjects (n = 8)
Age (years)62 ± 258 ± 1
Height (cm)177 ± 3179 ± 1
BMI (kg/m2)32 ± 2*28 ± 1
Time since diagnosis (years)5 ± 2–
Fasting insulin (pmol/l)61 ± 9*34 ± 6
Fasting glucose (mmol/l)9.0 ± 0.5*5.4 ± 0.1
Complex I activity (nmol min−1 mg protein−1)50.8 ± 6.058.3 ± 4.7
Citrate synthase activity (pmol mg−1 s−1)1.6 ± 0.12.0 ± 0.2
mtDNA (copies/μg tissue) ×103119 ± 7*147 ± 12
mtDNA/genomic DNA2,773 ± 2523,030 ± 185

Data are means±SEM. *p < 0.05 vs control subjects

Glucose (a) and insulin (b) concentrations in venous plasma before (t = 0 min) and during an OGTT. The patients with type 2 diabetes had higher fasting glucose levels and were severely insulin resistant compared with healthy control subjects (*p < 0.05). Black and white symbols represent healthy control subjects and patients with type 2 diabetes, respectively

Subjects were fasted overnight prior to the experiment. A catheter was inserted into an antecubital vein for blood sampling. After local anaesthesia of the skin and the subcutis, a muscle biopsy was taken (Tru-Core; PBN-Medicals, Stenløse, Denmark) and then a 120-min OGTT (75 g glucose dissolved in 300 ml of water) was performed. At t = 30 min, a second muscle biopsy was taken.A portion of the obtained muscle tissue was frozen immediately in liquid nitrogen and stored at −80°C for later analysis (see below), and a smaller piece (2–6 mg) was placed onto a Petri dish on ice with 1 ml of relaxing solution containing Ca2+/EGTA buffer (10 mmol/l), free calcium (0.1 μmol/l), imidazole (20 mmol/l), K+/4-morpholinoethanesulfonic acid (MES) (50 mmol/l), dithiothreitol (DTT; 0.5 mmol/l), MgCl2 (6.56 mmol/l), ATP (5.77 mmol/l), phosphocreatine (15 mmol/l), pH 7.1, and individual fibre bundles were separated with two pairs of sharp forceps, achieving a high degree of fibre separation. The fibre bundles were permeabilised for 30 min in 3 ml of ice-cold relaxing solution containing saponin (50 μg/ml) [10 (link)]. After rinsing in respiration medium (MiR05; Oroboros, Innsbruck, Austria) containing sucrose (110 mmol/l), potassium lactobionate (60 mmol/l), EGTA (0.5 mmol/l), MgCl2.6H2O (3 mmol/l), taurine (20 mmol/l), KH2PO4 (10 mmol/l), HEPES (20 mmol/l), sucrose (110 mmol/l), BSA (1 g/l), pH 7.1, the muscle bundles were blotted and measured for wet weight in a balance controlled for constant relative humidity, so that all biopsy samples were hydrated to the same degree. The muscle bundles were then immediately transferred into a respirometer (Oxygraph-2k; Oroboros) containing air-saturated respiration medium at 37°C.The Oxygraph-2k is a two-chamber titration-injection respirometer with a limit of oxygen flux detection of 1 pmol s−1 ml−1. The instrumentation allows for O2 flux measurements with only 0.04 mg of mitochondrial protein or 1.5 mg of muscle fibres (wet weight). Standardised instrumental and chemical calibrations were performed to correct for back-diffusion of O2 into the chamber from the various components, leak from the exterior, O2 consumption by the chemical medium, and sensor O2 consumption [11 (link)]. O2 flux was resolved by software capable of converting nonlinear changes in the negative time derivative of the oxygen concentration signal.
Analysis of muscle tissue Citrate synthase activity and complex I activity were measured spectrophotometrically at 37°C. Citrate synthase activity was determined as described previously [12 (link)], and complex I activity was assessed by measuring the oxidation of NADH (300 μmol/l) using ubiquinone 1 (100 μmol/l) as the acceptor. The complex I rotenone-sensitive activity was measured by the addition of rotenone (1 μmol/l). The protein content, needed to calculate the specific activity, was measured using a commercially available assay (BCA, Sigma Chemicals, St Louis, MO, USA). For measurement of mitochondrial DNA (mtDNA) content, DNA was isolated from muscle biopsy samples (∼10 mg) by proteinase K digestion at 55°C for 3 days. The 100-μl digestion mix contained 50 mU proteinase K (PCR grade, Roche, Basel, Switzerland), 20 mmol/l Tris-HCl (pH 8.4) and 50 mmol/l KCl. After incubation at 80°C for 45 min, the remains were spun down and the supernatant fraction diluted ×200 in triethanolamine titanate (TE) plus 1 ng/μl salmon sperm DNA (Sigma). 5 μl of this dilution was amplified in a 25 μl PCR reaction containing 1×Quantitect SYBR Green Master Mix (Qiagen, Hilden, Germany) and 100 nmol/l of each primer. The amplification was monitored real-time using the MX3000P Real-time PCR machine (Stratagene, La Jolla, CA, USA). The primers were designed to target genomic DNA (Forward: AGG TGC TGT CAG GAA GCA AGG A, Reverse: TAG GGG GAG GAG GGA ACA AGG A) or mtDNA (Forward: CCC CTG CCA TAA CCC AAT ACC A, Reverse: CCA GCA GCT AGG ACT GGG AGA GA). The threshold cycle (Ct) values were related to a standard curve made with the cloned PCR products.
Respirometry protocol All measurements of respiration were made in duplicate, simultaneously. Resting, routine respiration (state 2, absence of adenylates) was assessed by the addition of malate (1.5 mmol/l) and glutamate (19 mmol/l) as the complex I substrate supply, and then state 3 respiration was assessed by the addition of ADP (4.8 mmol/l). The addition of succinate (9.5 mmol/l) provided state 3 respiration with parallel electron input to complexes I and II. The integrity of the outer mitochondrial membrane was established by the addition of cytochrome c (19 μmol/l); no stimulation of respiration was observed. We examined ADP control of coupled respiration and uncoupling control through addition of the protonophore carbonylcyanide-4-(trifluoromethoxy)-phenylhydrazone (FCCP) (0.7 μmol/l). The addition of rotenone (0.1 μmol/l) resulted in inhibition of complex I for examination of O2 flux with complex II substrate alone, while antimycin A (12 μmol/l) was added to inhibit complex III to observe non-mitochondrial respiration with small contributions from electron leak in the uncoupled state. The concentrations of substrates and inhibitors used were based on prior experiments conducted for optimisation of the titration protocols.
Data analysis All values are given as means±SEM for all experiments, run in duplicate or triplicate. For all statistical evaluations, a p value of less than 0.05 was considered significant. Statistical analysis of differences in oxygen flux between healthy control subjects and patients with type 2 diabetes was carried out with a two-way ANOVA for repeated measures. In the case of a significant main effect and interaction between the variables, the Holm-Sidak method was used for post hoc analysis. All other comparisons between the two groups were performed using the unpaired Student’s t test. SigmaStat version 3.11 (Systat software, Richmond, CA, USA) was used in all analyses.
Boushel R., Gnaiger E., Schjerling P., Skovbro M., Kraunsøe R, & Dela F. (2007). Patients with type 2 diabetes have normal mitochondrial function in skeletal muscle. Diabetologia, 50(4), 790-796.
Publication 2007
3
Purification of Human Lipoxygenases
Cited 11 times
Human reticulocyte 15-lipoxygenase-1 (15-hLO-1) and human platelet 12-lipoxygenase (12-hLO) were expressed as N-terminally, His6-tagged proteins and purified to greater than 90% purity, as evaluated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis.9 (link), 35 (link) Human 5-lipoxygenase (5-hLO) in a pET21 expression vector was received from the Tatulian Lab (University of Central Florida).36 (link) It was transformed into E. coli BL21-DE3 and grown overnight in LB medium (50 mL) with 0.1 mg/mL Ampicillin at 25 °C. Next, the 50 mL growth mixture was separated into 7 × 2 L flasks of media and grown at 30 °C until the OD600 reached 0.6. The cells were then induced with 0.25 mM IPTG, followed by lowering the temperature to 18 °C. The cells were harvested 16 – 20 hours post-induction by pelleting at 5,000 g (10 min) and stored at −80 °C until purification.
The frozen cell pellet was resuspended in buffer A (10 mM β-mercaptoethanol, 0.1 mM EDTA, and 50 mM triethanolamine (pH 7.3)) and placed on ice. Cells were lysed using a Power Laboratory Press and cleared by spinning at 40,000 g (25 min). Proteins in the supernatant were precipitated at 50% saturated ammonium sulfate and spun at 40,000 g (25 min). Proteins in the salt pellet can be stored under liquid nitrogen with negligible loss of 5-hLO activity for over 6 months. The salt pellets were resuspended in buffer A for use in activity assays.
Robinson S.J., Hoobler E.K., Riener M., Loveridge S.T., Tenney K., Valeriote F.A., Holman T.R, & Crews P. (2009). Using Enzyme Assays to Evaluate the Structure and Bioactivity of Sponge-Derived Meroterpenes. Journal of natural products, 72(10), 1857-1863.
Publication 2009
4
Quantifying Tissue Glutathione Levels
Cited 11 times
Frozen tissue was weighed on ice and rapidly homogenized in ice cold 3% sulfosalicylic acid (SSA) containing 0.1mM EDTA with a PowerGen Model 125 blade-type homogenizer to yield a 10% (w/v) homogenate. 200 μL of this homogenate was immediately transferred to 1 mL of a 10 mM NEM solution prepared in 100 mM potassium phosphate buffer on ice. Another aliquot of the homogenate was diluted 1:50 in 0.01 N HCl in H2O for use in determination of total glutathione. Tubes were then centrifuged at 4°C, 14,000 × g, for 4 minutes and the deproteinized supernatants were transferred to fresh tubes. All samples were kept on ice. Removal of excess NEM was accomplished by chromatographic separation using a small C18 column (Sep-Pak; Waters Associates, Millipore Corporation, Milford, PA). 700 μL of sample was passed through the column (~1 drop/sec) by injection and into a fresh tube, followed by 1 mL of 100 mM potassium phosphate buffer. Regeneration of the column for use with subsequent samples was accomplished with a 6 mL methanol rinse using a fresh syringe. To prevent interference due to methanol in the enzymatic assay, the column was air dried using the same syringe, rinsed with H2O, and air dried again, before applying the next sample. In all, the process required < 5 minutes per sample. Between experiments, the C18 cartridges were stored in methanol. Determination of GSSG using 2VP as the GSH masking agent was done as described (Griffith, 1980 (link)), in parallel with the above experiments. Briefly, 200 μL of the deproteinized supernatant was mixed with 4 μL 2VP and 12 μL triethanolamine (to pH 7.0–7.5) and incubated at room temperature for 1 h. Following the 1 h incubation, 2VP treated samples were diluted 1:30 in 100 mM potassium phosphate buffer. GSH sample supernatants in HCl were further diluted 1:26 in 100 mM potassium phosphate before measurement. NEM treated samples were used without further dilution.
McGill M.R, & Jaeschke H. (2015). A direct comparison of methods used to measure oxidized glutathione in biological samples: 2-vinylpyridine and N-ethylmaleimide. Toxicology mechanisms and methods, 25(8), 589-595.
Publication 2015
Buffers Chromatography Cold Temperature Edetic Acid Enzyme Assays Freezing Glutathione Disulfide Methanol potassium phosphate Regeneration sulfosalicylic acid Syringes Technique, Dilution Tissues triethanolamine
5
In-Situ Hybridization of Adult Sycon Sponge
Cited 9 times
Adult Sycon specimens were collected from fjords located near Bergen, Norway (+60° 27' 33", +4° 56' 1") during the reproductive season from May to September (2008 to 2011). For in-situ hybridization, samples were immediately fixed in 100 mM MOPS, pH 7.5; 0.5 M sodium chloride; 2 mM MgSO4; 4% paraformaldehyde; 0.05% glutaraldehyde over night at 4°C, stepped into and extensively washed in 70% EtOH and stored at −20°C until processing. Macro sections of sponges in 24 well plates (Nunc) were rehydrated and washed in PBS/0.1% Tween (PTw). Samples were pretreated with 7.5 μg/mL proteinase K for 10 minutes at 37°C, followed by quenching with glycine (2 mg/mL PTw). Acetylation was performed by serial treatment with 0.1 M triethanolamine containing 0, 1.5, and 3 μl/mL acetic anhydride. Re-fixation was done in 4% paraformaldehyde/0.05% glutaraldehyde in PBS for 1 h at room temperature, followed by extensive washing in PTw. Tissue was prehybridized as previously described
[33 (link)] in 2 mL-tubes for 90 to 180 min at 51°C. Probe hybridization was done with denatured RNA probe (0.1-0.3 ng/μL, approximately 1 kb) for 12 to 18 h at 51°C. Stringent washes were carried out at 55°C as following: 1 × 10 min in hybridization buffer; 2 × 10 min 50% formamide/4 × SSC/0.1%; 2 × 10 min 50% formamide/2 × SSC/0.1% Tween; 2 × 10 min 25% formamide/2 × SSC/0.1% Tween, followed by 3 × 15 min 2 × SSC/0.1% Tween at room temperature. Samples were transferred to maleic acid buffer and incubated in 2% (w/v) Blocking Reagent (Roche) for 60 min at room temperature. After overnight incubation with AP-coupled anti-Digoxigenin-Fab fragments (Sigma, 1:5,000) at 4°C, samples were washed in maleic acid buffer at least 6 × 30 min. Probe was detected using NBT/BCIP as substrate (Roche) with tissue equilibrated in alkaline phosphatase buffer (100 mM sodium chloride, 50 mM MgCl2, 100 mM Tris pH 9.5, 0.1% Tween, 1 mM Levamisole). The staining reaction (0.5 to 3 days) was stopped with PBS/0.5% Tween, samples were transferred to 100% glycerol for microscopy or ethanol-dehydrated and embedded in epoxy resin (Sigma) for sectioning. Pictures of whole mount samples and sections were taken using a Nikon DS-U3 microscope and processed in Photoshop.
Fortunato S., Adamski M., Bergum B., Guder C., Jordal S., Leininger S., Zwafink C., Rapp H.T, & Adamska M. (2012). Genome-wide analysis of the sox family in the calcareous sponge Sycon ciliatum: multiple genes with unique expression patterns. EvoDevo, 3, 14.
Full text: Click here
Publication 2012
acetic anhydride Acetylation Acid Hybridizations, Nucleic Adult Alkaline Phosphatase Buffers Digoxigenin Endopeptidase K Epoxy Resins Ethanol Fjord formamide Glutaral Glycerin Glycine Immunoglobulins, Fab In Situ Hybridization Levamisole Magnesium Chloride maleic acid Microscopy morpholinopropane sulfonic acid paraform Porifera Reproduction RNA Probes Sodium Chloride Sulfate, Magnesium Tissues triethanolamine Tromethamine Tweens

Most recents protocols related to «Triethanolamine»

1
Triethanolamine: Versatile Surfactant Synthesis
Not available on PMC !
Description: The main application of triethanolamine is the synthesis of surfactants, like emulsifiers. It is frequently included in formulas for both consumer and commercial goods. Triethanolamine stabilizes and buffers pH levels, neutralizes fatty acids, and solubilizes oils and other substances that aren't entirely soluble in water. In certain instances, triethanol ammonium salts are more soluble than other possible alkali metal salts, and they produce fewer alkaline products than when the salt is made from alkali metal hydroxides. Sunscreen lotions, liquid laundry detergents, dishwashing liquids, general cleaners, hand sanitizers, polishes, metalworking fluids, paints, shaving cream, and printing inks are a few common products that contain triethanolamine.
Rokade R.S., Vidhate S.R., Kale D.S., & Somani S.J. (2024). Formulation and development of herbal facewash using Beal leaves: Aegle marmelos. World Journal of Biology Pharmacy and Health Sciences, 17(1), 061-074.
Publication 2024
2
Synthesis of Triethanolamine Esters
Triethanolamine (0.01 mol) was reacted with myristic acid (0.02 mol) and (0.03 mol) to obtain the triethanolamine diester (2a) and triester (2b), respectively. The mixture was refluxed at 110 °C in the presence of toluene as solvent and 0.001 wt % P-toluene sulfonic acid. The reaction was completed when the theoretical amount of water was removed. The mixture was cooled and toluene was vacuum evaporated to obtain the diethyl ethanolamine tridecantrioate (2a) and triethyl amine tridecantrioate (2b).
El Nagy H.A, & Mohamed M.A. (2024). Stable diesel microemulsion using diammonium ionic liquids and their effects on fuel properties, particle size characteristics and combustion calculations. Scientific Reports, 14, 7728.
Full text: Click here
Publication 2024
3
Carbomer-based Lavender-SLN Gel Formulation
Carbomer 940 (0.5% w/v) was used as a gelling agent to formulate Lav-SLN-G after optimizing the selected variables. 0.5% of Carbopol was dispersed in water for 24 h to prevent the formation of lumps. After 24 h, Lav- SLN dispersion equal to 3% in gel’s final volume was added and completely uniformed using a mechanical stirrer. Next, 20% propylene glycol and 3–4 drops of triethanolamine were added to the product, respectively. As soon as triethanolamine was added, an enhanced viscous solution turning to gel was observed [41 (link)].
Fahimnia F., Nemattalab M, & Hesari Z. (2024). Development and characterization of a topical gel, containing lavender (Lavandula angustifolia) oil loaded solid lipid nanoparticles. BMC Complementary Medicine and Therapies, 24, 155.
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Publication 2024
4
Microemulgel Formulation Development
Not available on PMC !
Several batches of microemulgel were created, each containing different gelling agents and varying concentrations. The emulsion was prepared with 2% C. deodara extract. Gelling agents were hydrated in water, and triethanolamine was used to regulate the pH. Then, the emulsion was blended into the gel with vigorous stirring to produce the microemulgel formation. The USP was generously provided by Martin Dow Pharm. Ltd. Lahore, while Tween 80, isopropyl myristate (IPM), n-butanol, Carbopol 940, and triethanolamine were procured from Sigma-Aldrich Pakistan. All solvents and materials used were of analytical grade, with distilled water being utilized throughout the formulation processes (Shripathy Dharmasthala et al., 2019) .
Machewar K., Kakde R., & Sabale P. (2024). A novel method: Developing and accessing a herbal microemulgel containing Cedrus deodara (Roxb.) G. Don extract for its in vitro anti-inflammatory effects. Annals of Phytomedicine An International Journal, 13(1).
Publication 2024
5
Enzymatic Glucose Determination Assay
Not available on PMC !
The d-glucose released was determined enzymatically with the hexokinase/glucose-6-phosphate dehydrogenase assay by photometric measurement (340 nm) in microtiter plates. For the determination, 235 µL of triethanolamine buffer (triethanolamine hydrochloride 181.1 mM, NADP + 1.65 mM, ATP 3.66 mM, and MgSO 4 x 7 H 2 O 3.65 mM) and 15 µL of sample were added to a microplate. Mixing was then performed in the microplate reader, and the absorbance A1 value was read after 3 min. Subsequently, 5 µL of hexokinase/glucose-6 phosphate dehydrogenase (Megazyme International, Wicklow, Ireland) was added and mixed again. The absorbance A2 value was measured after 25 min. The glucose concentration was determined using a calibration curve (range: 0.05-2 g/L glucose monohydrate).
Lutz-Wahl S., Mozer H., Kussler A., Schulz A., Seitl I, & Fischer L. (2024). A new β-galactosidase from Paenibacillus wynnii with potential for industrial applications. Journal of dairy science, 107(6).
Publication 2024

Top products related to «Triethanolamine»

1
Triethanolamine by Merck Group
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Triethanolamine is a clear, viscous liquid chemical compound. It is a primary function is to serve as a pH adjuster and emulsifier in various laboratory applications.
2
Ethanol by Merck Group
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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.
3
Sodium hydroxide (naoh) by Merck Group
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Sodium hydroxide is a chemical compound with the formula NaOH. It is a white, odorless, crystalline solid that is highly soluble in water and is a strong base. It is commonly used in various laboratory applications as a reagent.
4
Methanol by Merck Group
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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.
5
Dimethyl sulfoxide (dmso) by Merck Group
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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.
6
Fetal bovine serum (fbs) by Thermo Fisher Scientific
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Fetal Bovine Serum (FBS) is a cell culture supplement derived from the blood of bovine fetuses. FBS provides a source of proteins, growth factors, and other components that support the growth and maintenance of various cell types in in vitro cell culture applications.
7
Bovine serum albumin (bsa) by Merck Group
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Bovine serum albumin (BSA) is a common laboratory reagent derived from bovine blood plasma. It is a protein that serves as a stabilizer and blocking agent in various biochemical and immunological applications. BSA is widely used to maintain the activity and solubility of enzymes, proteins, and other biomolecules in experimental settings.
8
Hydrochloric acid (hcl) by Merck Group
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Hydrochloric acid is a commonly used laboratory reagent. It is a clear, colorless, and highly corrosive liquid with a pungent odor. Hydrochloric acid is an aqueous solution of hydrogen chloride gas.
9
Acetonitrile by Merck Group
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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.
10
Triethanolamine tea by Merck Group
Sourced in United States, Germany
Triethanolamine (TEA) is a clear, viscous, and colorless chemical compound that serves as a versatile laboratory reagent. It functions as a pH buffer, emulsifier, and chelating agent in various scientific applications.

More about "Triethanolamine"

Triethanolamine (TEA) is a versatile organic compound with a wide range of applications in research and industry.
It is a colorless, viscous liquid with a mild odor, and is commonly used as a surfactant, pH adjuster, and emulsifier.
This versatile chemical plays a key role in a variety of research areas, including cosmetics, pharmaceuticals, and materials science.
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The platform can help you discover the most effective methods for working with triethanolamine, as well as related compounds like ethalolamine, ethanol, sodium hydroxide, methanol, DMSO, FBS, bovine serum albumin, hydrochloric acid, and acetonitrile.
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