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Triethanolamine

Manufactured by Merck Group
469 citations
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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.

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Triethanolamine is a commercially available product from Merck Group and its authorized distributors. The pricing typically ranges from $25 to $100 per liter, depending on the purity and packaging. As this is an active product, there is no official replacement model.

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469 protocols using «triethanolamine»

1

Synthesis of Zinc Oxide Nanoparticles

2025
Triethanolamine (C6H15NO3, ≥ 99%), zinc acetate
dihydrate (Zn(CH3COO)2.2H2O, >99.5%),
zinc chloride (ZnCl2, > 98%), methanol (CH3OH,
≥ 99.9%), ethanol (C2H5OH, ≥ 99.9%),
potassium hydroxide (KOH, ≥ 99.9%), ethylene glycol (C2H6O2, ≥ 99%), thiourea (CH4N2S, ≥ 99%) were purchased from Merck, Germany.
Tetramethylammonium hydroxide (TMAH) (C4H13NO,
≥ 97%) was obtained from Sigma-Aldrich, Germany. Carbon dioxide
gas (CO2, ≥ 99%), and nitrogen gas (N2, ≥ 99%) were acquired from CV Sangkuriang.
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2

Doxorubicin and Ferulic Acid Lipid Nanoparticles

2025
Hydrogenated soya phosphatidylcholine (HSPC) and distearylphospatidyl-ethanolamine-methoxy-(polyethylene-glycol) (DSPE-mPEG2000, the mean molecular weight of PEG is 2000 g/mol) were purchased from NOF Co. Ltd. (Tokyo, Japan). Cholesterol was obtained from Wako Pure Chemical Industries Inc. (Osaka, Japan). Triethanolamine was obtained from Sigma Aldrich, Co. Ltd. (Darmstadt, Germany). Doxorubicin hydrochloride (DOX) was secured from LC Laboratories (Woburn, Massachusetts), and Ferulic Acid (FA) was purchased from Tokyo Chemical Industry (Tokyo, Japan). Phosphate-buffered saline (pH 7.4) comprised 8 g sodium chloride, 0.2 g potassium chloride, 1.15 g disodium hydrogen phosphate, and 0.2 g potassium dihydrogen phosphate per liter (Oxoid Ltd., Hampshire, UK). All other chemicals used in this study were of the highest grade available.
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3

Topical Antimicrobial Formulation Development

2025
Materials used in this experiment are as follows: Tween 80 and Span 20 (Merck NJ, United States of America), distilled water (Central Research Lab, CMUL, Idi-Araba, Lagos), chlorhexidine (Elaeis guineensis oil [Maubold Essensce, Lagos, Nigeria]), curcumin and phosphatidylcholine (Sigma-Aldrich Co., St. Louis, Missouri, United States of America), methanol (Merck, Darmstadt, Germany), phosphate buffer (Loba Chemie, Colaba, Mumbai, India), 1% cremophor (RH40) (Macklin Biochemical, Shanghai, China), Carbopol Ultrez (Surfachem, United Kingdom), distilled water, chlorhexidine (Sigma-Aldrich Co., St. Louis, Missouri, United States of America), triethanolamine (Merck, New Jersey, USA), Dettol (Reckitt Benckiser), normal saline (Unidex, Lagos, Nigeria), Mueller–Hinton agar (HiMedia Laboratories), and methylparaben and propylparaben (Sigma-Aldrich Co., St. Louis, Missouri, United States of America).
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4

Synthesis and Characterization of Ti3AlC2 Powder

2025
Ti3AlC2 powder (400 mesh) was purchased from Nanochemazone (Leduc, Alberta, Canada). Hydrofluoric acid (HF, 48–51%) and dimethyl sulfoxide (DMSO, ACS reagent, 99.9%) were supplied by Thermo Scientific (Fair Lawn, NJ, USA). Methanol (≥99.9%), ammonium persulfate (APS, ACS reagent, ≥98.0%), isopropyl alcohol (IPA), triethanolamine (TEA, reagent grade, 98%), thiophene (≥99%), methylene blue (MB), orange G (OG), and rhodamine B (RhB) were all obtained from Sigma-Aldrich Korea (Seoul, Republic of Korea). Cetyltrimethylammonium bromide (CTAB, 99%) was purchased from Daejung Chem (Siheung, Republic of Korea).
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5

Culturing and Infecting Leishmania infantum

2025
Leishmania infantum (MHOM/ES/92/LLM-320; isoenzyme typed MON-1) was cultured in M199 medium supplemented with 20% fetal bovine serum (Gemini Bio-Products), 100 μ/mL penicillin and 100 μg/mL streptomycin (Gibco), 2 mM L-glutamine (Gibco), 40 mM HEPEs (Gibco), 0,1 mM adenine (Sigma) in 50 mM HEPEs, 5 mg/mL hemin (Sigma) in 50% triethanolamine (Sigma), and 1 mg/mL 6-biotin (Sigma). Cultures were maintained at 26 °C. For mouse infections, metacyclic promastigotes were purified from stationary-phase cultures by Ficoll (Sigma) density gradient (8% and 20%), as adapted from Spath and Beverley65 (link), and centrifuged at 500 × g for 10 min, at 25 °C. Mice were intravenously inoculated with 3 × 106 metacyclic promastigotes in 100 μl of 1 × PBS.
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Top 5 most cited protocols using «triethanolamine»

1

Microfluidic Hydrogel Encapsulation

Flow-focusing microfluidic geometry was utilized to form polymer droplets. Both shielding and crosslinker phases consisted of light mineral oil (Sigma) with 2% SPAN80 (Sigma). The crosslinker phase also contained an emulsion, at a ratio of 1:15, of 20 mg/mL dithiothreitol (DTT) (Sigma) in PBS. A co-flowing shielding phase protected the macromer solution – a 5% PEG-4MAL (10 kDa or 20 kDa, Laysan Bio) solution containing molecules or cells to be encapsulated – from the crosslinker phase until droplets of the macromer solution were formed. DTT rapidly diffused into macromer droplets, forming crosslinked microgels. To functionalize hydrogel with GRGDSPC (‘RGD’, AAPPTec), macromer was reacted for 20 minutes before encapsulation with 2.0 mM RGD in buffer solution containing 4 mM triethanolamine (Sigma). After formation, microgels were washed 5 times by centrifugation to remove mineral oil and excess DTT.
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Corresponding organizations : Woodruff Health Sciences Center

2

Tau Protein Isolation and Tryptic Digestion

Aliquots (4 µg) of Tau 12 (binding region aa 9–18, Nordic Biosite), HT7 (aa 159–163, Thermo Scientific), and BT2 (aa 194–198, Thermo Scientific) were added to 50 µL/each magnetic Dynabeads M-280 and incubated 2 h on a rocking platform at room temperature. The beads were washed three times with double volume of PBS (10 mM Na-phosphate, 0.15 M NaCl, and pH 7.4). The antibody was cross-linked using 20 mM dimethyl pimelimidate dihydrochloride (DMP; Sigma-Aldrich) and 0.2 M triethanolamine (pH 8.2, Sigma-Aldrich) according to the manufacturer’s product description. The cross-linked beads were washed twice in PBS and blocked with Roti-Block (Carl Roth) for 1 h on a rocking platform at room temperature. Antibody-conjugated beads and Tween 20 (final concentration in the sample: 0.025%) were added to 3 mL CSF or 7 µL of a TBS-soluble fraction of brain homogenate diluted in 270 µL PBS. For some of the samples intended for tryptic digestion, 100 fmol of a 13C15N lysine- and arginine-labeled tau 1N4R protein standard (provided by Dr. Thomas McAvoy, Merck Research Laboratories) were added. Samples were incubated overnight on a rocking platform at + 4 °C. The magnetic beads/sample solution was transferred to a magnetic particle processor (KingFisher, Thermo Fisher Scientific) (tube 1). The following three wash steps (tubes 2–4) were conducted for 10 s in 1 mL of each washing buffer: 0.025% Tween 20 in PBS (tube 2), PBS (tube3), and 50 mM ammonium hydrogen carbonate (tube 4, pH 8.0). Tau was eluted from the beads by adding 100 µL 0.5% formic acid (tube 5) for 4 min. The eluted fractions were transferred to 0.65 mL prelubricated microcentrifuge tubes (Costar, Cat. 3206) and dried in a vacuum centrifuge. After drying, 10 µL of a solution of 1 µg trypsin in 390 µL 50 mM ammonium hydrogen carbonate was added to half of the samples and incubated overnight at + 37 °C. The reaction was stopped by adding 2 µL of 10% formic acid in ultra-pure water. The other half was analyzed intact for endogenous peptides. Samples were dried in a vacuum centrifuge and stored at − 80 °C pending analysis. Following the same protocol described above, we immunoprecipitated tau from CSF and brain lysate with the neo-epitope-specific antibodies to verify their specificity.
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Corresponding organizations : University of Gothenburg, University of Pennsylvania, Lund University, University of Perugia, Banner Sun Health Research Institute, National Hospital for Neurology and Neurosurgery, University College London, Sahlgrenska University Hospital

3

Photodegradable Microparticle Synthesis and Characterization

Poly (ethylene glycol) di-photodegradable-acrylate (PEGdiPDA; Mn ∼ 4,070 Da) was synthesized as previously described.11 (link),12 (link) Poly (ethylene glycol) tetrathiol (PEG4SH; Mn ∼ 5,000 Da) was synthesized as previously described.20 (link) Photodegradable microparticles were prepared via inverse suspension polymerization, in which PEGdiPDA was copolymerized with PEG4SH via base-catalyzed Michael addition in an aqueous phase that was suspended in an organic phase. Briefly, the organic phase was comprised of 5 ml of hexane containing 150 mg of a 3:1 ratio by weight of sorbitan monooleate (Span 80, Sigma-Aldrich) and poly (ethylene glycol)-sorbitan monooleate (Tween 80, Sigma-Aldrich).21 The volume of the aqueous phase was 0.25 mL comprised of 300 mM triethanolamine (Sigma-Aldrich) at pH 8.0 with 6.2 wt % of PEGdiPDA, 3.8 wt % PEG4SH, and protein. Bovine serum albumin labeled with Alexa Fluor 488 or Alexa Fluor 594 (BSA-488 or BSA-594; Invitrogen) were entrapped at 0.8 mg/ml, TGF-β1 (Peprotech) was entrapped at 0.4 μg/ml, and the fluorescently labeled Annexin-V (Invitrogen) was entrapped at 20 v/v % Annexin-V conjugate solution. All of the components of the aqueous phase except for the PEG4SH solution were combined in a 1.7 ml microcentrifuge tube while the organic phase was added to a 20 ml scintillation vial with a stir bar. To initiate polymerization, the PEG4SH was added to the aqueous phase, which was subsequently vortexed for 10 s and quickly added to the organic phase. Mixing on a stir plate formed and maintained the inverse suspension between the two phases and the polymerization was allowed to proceed overnight.
Upon completion of the polymerization, the suspension was centrifuged (Eppendorf Centrifuge Model 5702) at 1000 rcf for 10 minutes and the supernatant was decanted. The microparticles were washed twice with hexanes and recovered with the same centrifugation conditions and once in 2-propanol and centrifuged at 2000 rcf for 10 minutes. The particles were then suspended in 1× PBS and washed three times by centrifuging (Eppendorf Centrifuge Model 5418) at 16,873 rcf for 15 minutes. The recovered particles were stored in PBS at 4°C and a portion was imaged on a low vacuum scanning electron microscope (LVSEM, JSM-6480LV).
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Corresponding organizations : University of Colorado Boulder, Howard Hughes Medical Institute

4

Immunoprecipitation of SNAP-25 from Brain and CSF

The immunoprecipitation method for brain tissue extracts and CSF samples was performed according to Öhrfelt et al. with minor modifications
[39 (link)]. Briefly, an aliquot (1 μg) of the mouse monoclonal antibody SP12 (1 g/L) or the mouse monoclonal antibody SMI81 (1 g/L) or IgG from murine serum (1 g/L, Sigma-Aldrich) (a negative control), was separately added to 100 μL magnetic Dynabeads M-280 Sheep anti-mouse IgG (Invitrogen Corporation) and incubated 1 h on a rocking platform at room temperature. The beads were washed three times with 1 mL of PBS (10 mM Na-phosphate, 0.15 M NaCl, pH 7.4). The antibodies were cross-linked using 20 mM dimethyl pimelimidate dihydrochloride (Sigma-Aldrich) and 0.2 M triethanolamine (pH 8.2 Sigma-Aldrich) according to the manufacturer’s product description. The cross-linked beads were washed two times in PBS and were blocked with Roti-Block (Carl Roth) for 1 h on a rocking platform at room temperature. Each brain tissue extract (soluble, membrane-bound, and membrane-raft associated proteins) (26 μg of total protein) and CSF samples (German cohort, 890 μL; Swedish cohort I, 700 μL; Swedish cohort II, 600 μL) were adjusted with 20% Triton and PBS to a final concentration of 0.2% Triton and a final volume of 1 mL). Samples and magnetic beads were incubated overnight on a rocking platform at +4°C. The magnetic beads/sample solution was transferred to the KingFisher magnetic particle processor (Thermo Fisher Scientific), tube 1. The following three wash steps (tubes 2-4) were conducted for 10 s in 1 mL of each washing buffer: (tube 2) 0.025% Tween 20 in PBS, (tube 3) PBS and (tube 4) 50 mM ammonium hydrogen carbonate (NH4HCO3, pH 8.0). SNAP-25 was then eluted from the beads by adding 100 μL 0.5% formic acid (FA) (tube 5) for 4 min. The eluted fractions were transferred to 0.5 mL Protein LoBind Tube (Eppendorf AG) and dried in a vacuum centrifuge.
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Corresponding organizations : University of Gothenburg, University of British Columbia, Central Institute of Mental Health, Lund University, University College London, National Hospital for Neurology and Neurosurgery

5

Immunoblotting of Tissue Samples

Tissue samples for immunoblotting were placed in 10 ml ice-cold isolation solution, containing 250 mM sucrose, 10 mM triethanolamine (Sigma-Aldrich, St. Louis, MO, USA), 1 mg/ml leupeptin (Sigma-Aldrich) and 0.1 mg/ml phenylmethylsulfonyl fluoride (Sigma-Aldrich) titrated to pH 7.6, and the mixture was homogenized at 13,600 × g with three strokes for 15 sec using a tissue homogenizer (PowerGun 125; Thermo Fisher Scientific, Pittsburgh, PA, USA). Following homogenization, the total protein concentration was measured using a bicinchoninic acid protein assay reagent kit (Thermo Fisher Scientific, Rockford, IL, USA), which was adjusted to 2 mg/ml with isolation solution. Equal amounts of protein and sample buffer were separated using 12% gradient SDS-PAGE, stained with Coomassie Brilliant Blue and transferred to a polyvinylidene fluoride membrane. The blotted membrane was blocked with Tris-buffered saline containing 5% milk, and incubated with HIF-1α, VEGF or CD34 rabbit polyclonal antibodies (1:500; Santa Cruz Biotechnology, Inc., Santa Cruz, CA, USA), followed by incubation with a HRP-coupled secondary antibody (1:1000; Cell Signaling Technology, Inc., Danvers, MA, USA). The proteins were detected using enhanced chemiluminescence (Thermo Fisher Scientific). All immunoblots were representative of at least three independent experiments.
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Corresponding organizations : Chongqing Medical University, Inner Mongolia Medical University, First Affiliated Hospital of Chongqing Medical University, Fourth Hospital of Inner Mongolia

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