Trizma

Manufactured by Merck Group

Sourced in United States, Italy

Trizma is a buffer compound that is used to maintain a specific pH in aqueous solutions. It is a tris-based buffer that is commonly used in various laboratory applications, including biochemical assays, protein purification, and molecular biology experiments. Trizma provides a consistent and stable pH environment for these processes.

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Lab products found in correlation

Icap q, by Thermo Fisher Scientific (5 mentions) Sodium chloride (nacl), by Thermo Fisher Scientific (5 mentions) Hepes, by Merck Group (4 mentions) Acrylamide, by Merck Group (4 mentions) Hydrochloric acid (hcl), by Merck Group (4 mentions) Sodium dodecyl sulfate (sds), by Merck Group (4 mentions) Sulforhodamine b salt, by Merck Group (3 mentions) Glycine, by Merck Group (3 mentions) Icp ms, by Thermo Fisher Scientific (3 mentions) Ammonium persulfate, by Merck Group (3 mentions) Glycerol, by Merck Group (3 mentions) Kanamycin, by Merck Group (3 mentions) Bovine serum albumin (bsa), by Merck Group (3 mentions) Sodium chloride (nacl), by Merck Group (3 mentions) Pierce bca protein assay kit, by Thermo Fisher Scientific (3 mentions) Monosodium glutamate, by Thermo Fisher Scientific (2 mentions) Sucrose, by Thermo Fisher Scientific (2 mentions) Sodium bicarbonate, by Thermo Fisher Scientific (2 mentions) Tris base, by Thermo Fisher Scientific (2 mentions) Hepes buffer, by Merck Group (2 mentions)

Close spelling variants of this product

Trizma base and acid Trizma base (TRIS) Tris(hydroxymethyl)-aminomethane (Trizma base 2-amino-2-(hydroxymethyl)-1,3-propanediol (TRIZMA base), Trizma pH 7.6 Trizma hydrochloride (Tris-HCl) Trizma preset crystals Trizma maleate Trizma pH 9.0 Trizma base solution

49 protocols using trizma

Proliferation of Lung Cancer Cells with Dox-Loaded Nanoparticles

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Cultured cells were detached with a trypsin–ethylenediami-netetraacetic acid (EDTA) solution (0.25%) and seeded into 24-well plates at a density of 15×10³ A549 cells/well and 2×10⁴ LL/2 cells/well. After incubation for 24 hours under culture conditions, the cells were treated with either free Dox (aqueous solution), blank (Dox-unloaded) PBCA NPs, or Dox-loaded PBCA NPs in increasing drug-equivalent concentrations from 0.01 to 10 μM. After an incubation time of 48 hours, a modified sulforhodamine B (SRB) protocol was followed.25 (link) The cells were washed three times with PBS, and 300 μL of 10% trichloroacetic acid was used to fix the cells (20 minutes at 4°C). Then, the cells were washed three times with distilled water and left to dry before 300 μL of SRB was added again. Incubation under mechanical stirring was continued for 20 minutes, and the excess SRB was removed by the addition of a 1% acetic acid solution. Then, the cells were left to dry. Finally, 200 μL of Trizma^® (10 mM, pH 10.5; Sigma-Aldrich) was used for dye resuspension. The optical density (OD) of SRB was measured at 492 nm (Titertek^® Multiskan colorimeter; Flow Laboratories Ltd, Oldham, UK) and analyzed with Ascent software version 2.6 (Thermo Labsystems, Helsinki, Finland).
The percentage of relative proliferation (RP, %) was calculated:

RP (%) = \frac{OD of treated cells}{OD of untreated cells} \times 100

Melguizo C., Cabeza L., Prados J., Ortiz R., Caba O., Rama A.R., Delgado Á.V, & Arias J.L. (2015). Enhanced antitumoral activity of doxorubicin against lung cancer cells using biodegradable poly(butylcyanoacrylate) nanoparticles. Drug Design, Development and Therapy, 9, 6433-6444.

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Quantifying Hepatic Myeloperoxidase Activity

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Freshly excised livers were snap-frozen and then crushed in liquid nitrogen. A MPO assay was performed on these samples. Briefly, pulverized liver tissue was added to a non-denaturing lysis buffer (TRIZMA, Sigma, 10% glycerol, and 0.2% Tween), and samples were exposed to three cycles of freeze-thawing, and then centrifuged to collect the lysate. The MPO reaction was carried out by first mixing 20 μl of liver lysate with 20 μl assay buffer (0.167 mg/ml o-dianisidine-HCL, 50 mM Na₂HPO₄, pH 5.4) in a 96-well plate, and then adding 200 μl of development solution (0.1% H₂O₂, 50 mM Na₂HPO₄, pH 5.4). Absorbance was measured at 450 nm every 15 s. MPO activity is expressed as the change in absorbance per minute per milligram of liver lysate protein (ΔmOD/min/mg protein). Immunohistochemical staining for MPO was also performed from excised liver tissue.

Patel S.J., Luther J., Bohr S., Iracheta-Vellve A., Li M., King K.R., Chung R.T, & Yarmush M.L. (2016). A Novel Resolvin-Based Strategy for Limiting Acetaminophen Hepatotoxicity. Clinical and Translational Gastroenterology, 7(3), e153-.

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Isolation and Purification of Bacterial Lipopolysaccharide

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LPS was prepared as described by Westphal and Jann [37 ]. Briefly, the bacteriawere inoculated in 250 mL of a Luria Bertani (LB) broth and incubated for 24 h at 30°C on a shaker at 250 rpm. The culture was then centrifuged at 10000 rpm for 10 min at 4°C, resuspended in 16.6 mL of TAE buffer (40 mM Tris-acetate, pH.8.5; 2 mM EDTA), and then mixed with 33.2 mL alkaline solution (containing 3 g of SDS, 0.6 g of Trizma (Sigma), and 160 mL of 2 N NaOH in 1000 mL of water). The suspension was heated at 55 to 60°C for 70 min and then mixed with phenol and chloroform in the ratio of 1 : 1 (V/V). The mixture was spun at 10 000 rpm for 10 min at 4°C and the supernatant obtained was mixed with 33.2 mL of water and 8.3 mL of 3 M sodium acetate buffer (pH 5.2). LPS was precipitated by adding twice the volume of ethanol. The precipitate was dissolved in 33.2 mL of 50 mM Tris-HCl, pH 8.0 (Sigma), and 100 mM sodium acetate, mixed well, and was then reprecipitated with twice the volume of ethanol. The combined water extract was dialyzed for 2–4 days against distilled water and then freeze-dried.

Abuelsaad A.S., Allam G, & Al-Solumani A.A. (2014). Hesperidin Inhibits Inflammatory Response Induced by Aeromonas hydrophila Infection and Alters CD4+/CD8+ T Cell Ratio. Mediators of Inflammation, 2014, 393217.

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Attenuated Bovine Rotavirus Strain 116E Formulation

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Example 1

The naturally attenuated asymptomatic human bovine reassortant rotavirus strain 116E (serotype G9P[11]) used in this development had ingredients like sodium chloride, monosodium glutamate, Tris base, sucrose, and sodium bicarbonate reagents obtained from Fisher Bioreagents. DMEM and MEM growth media was purchased from Corning Life Sciences (Tewksbury, Mass.). Trizma, Hepes buffer and L-Arginine were obtained from Sigma Aldrich Saint Louis, Mo. Sodium citrate anhydrous powder (ADM, Chicago, Ill.) and Sodium adipate was from TCI America (Portland, Oreg.). Although the examples refer to immunogenic compositions of attenuated Rotavirus, the formulations are applicable to other types of virus including, but not limited to the non-enveloped viruses such as norovirus, adenovirus, papilloma virus, and picornavirus, and the enveloped viruses, Hepatitis virus, Corona virus, Influenza virus, and rabies virus.

US11110163B2. Heat stable vaccines (2021-09-07). Inventprise, LLC [US]. Inventors: Subhash V. Kapre [US], Ivan A. Olave [US].

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Synthesis of Compound 1 using TRIZMA

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Example 3

This example demonstrates a synthesis of Compound 1 in an embodiment of the invention.

A solution of 2-hydroxy-4-[[2-[[(4-methylphenyl)sulfonyl]oxy]acetyl]amino] benzoic acid (10 mmol) was dissolved in THF/EtOH (1:1) (250 mL), and the resulting solution was cooled to 0° C. in an ice bath. Once the solution cooled, the 2-amino-2-(hydroxymethyl)-1,3-propanediol (TRIZMA™, Sigma-Aldrich, St. Louis, Mo.) (10 mmol) was added, and the mixture was stirred for 90 minutes at 0° C. Upon completion, the solvent was removed with care taken to keep the mixture at or below room temperature. The resulting residue was triturated with pentanes, and was placed under high vacuum at 0° C. for 2 hours and then backfilled with argon. The resulting white solid (quantitative yield) was stored in the freezer (−20° C.) until ready to use.

US10913709B2. STAT3 inhibitor formulation (2021-02-09). The United States of America, as represented by the Secretary, Department of Health and Human Services [US], GLG Pharma, LLC [US], MRIGLobal [US]. Inventors: Robert H. Shoemaker [US], Michael W. Lovell [US], Jonathan M. White [US], Shanker Gupta [US].

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Quantifying Reprimo Methylation by qMSP

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To quantify the methylation level of Reprimo, quantitative methylation-specific PCR (qMSP) was performed. Amplification reactions were carried out in triplicate in a volume of 20 μL that contained 1 μL of bisulfite-modified DNA; 300 nM of each primer; 50 nM probe (Table 1); 0.375 U platinum Taq polymerase (Invitrogen); 100 μM of dNTPs; 100 nM ROX dye reference (Invitrogen); 8.3 mM ammonium sulfate; 33.5 mM Trizma (Sigma, St. Louis, MO); 3.35 mM magnesium chloride; 5 mM mercaptoethanol; and 0.05 % DMSO [30 (link)]. Amplifications were carried out using the following profile: 95 °C for 10 min followed by 40 cycles at 95 °C for 30 s, 59 °C for 30 s and 72 °C for 30 s. Amplification reactions were carried out in 96-well plates in the Mx3000P QPCR System (Stratagene). Each plate included DNA samples, positive control (100 % methylated DNA, Zymo Research) and water blanks. The relative level of methylated DNA for RPRM was determined as a ratio of methylation-specific PCR-amplified gene to β-actin (reference gene) and then multiplied by 1000 for easier tabulation (average value of triplicates of the study gene divided by the average value of triplicates of β-actin × 1000) [30 (link), 31 (link)].

Buchegger K., Ili C., Riquelme I., Letelier P., Corvalán A.H., Brebi P., Huang T.H, & Roa J.C. (2016). Reprimo as a modulator of cell migration and invasion in the MDA-MB-231 breast cancer cell line. Biological Research, 49, 5.

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Allograft Adipose Matrix Characterization

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Antigen retrieval was performed on paraffin-embedded allograft adipose matrix with 10 mM sodium citrate buffer. Primary collagen I, III, IV, and VI antibodies (Abcam, Cambridge, Mass.) were used with hematoxylin counterstain (Sigma-Aldrich, St. Louis, Mo.). Growth factors were extracted using 4 M guanidine hydrochloride in 0.05 M Trizma (Sigma-Aldrich) or T-PER (Thermo Fisher, Waltham, Mass.) over 48 hours at 4°C. Growth factors were quantified using Luminex multiplexing (MilliporeSigma, St. Louis, Mo.) or by enzyme-linked immunosorbent assay (R&D Systems, Minneapolis, Minn.).

Kokai L.E., Schilling B.K., Chnari E., Huang Y.C., Imming E.A., Karunamurthy A., Khouri R.K., D’Amico R.A., Coleman S.R., Marra K.G, & Rubin J.P. (2019). Injectable Allograft Adipose Matrix Supports Adipogenic Tissue Remodeling in the Nude Mouse and Human. Plastic and Reconstructive Surgery, 143(2), 299-309.

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Acquisition and Preparation of Compounds for Cell and Animal Studies

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Authentic (−)-deguelin, rapamycin for in vitro studies and enzalutamide/MDV3100 were purchased from Cayman Chemical Company (Ann Arbor, MI, USA). rapamycin for animal studies was purchased from LC Laboratories (Woburn, MA, USA). R1881 was purchased from Perkin Elmer (Waltham, MA, USA). Sulforhodamine B salt, paclitaxel, 17-AAG, crystal violet, Trizma, Dulbecco’s phosphate-buffered saline (DPBS), HEPES, hydrocortisone, insulin, phenylmethanesulfonyl fluoride (PMSF), carboxymethyl cellulose, Tween-80, polyethylene glycol 400 and dimethyl sulfoxide (DMSO) were purchased from Sigma-Aldrich (St. Louis, MO, USA). Compounds for cell treatments were dissolved in DMSO and stored at −20°C. Compounds for in vivo studies were stored as stock solutions in DMSO (enzalutamide) or ethanol (rapamycin) at −20°C and diluted immediately before use.

Robles A.J., Cai S., Cichewicz R.H, & Mooberry S.L. (2016). Selective activity of deguelin identifies therapeutic targets for androgen receptor-positive breast cancer. Breast cancer research and treatment, 157(3), 475-488.

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Purification of Recombinant Proteins

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Sodium chloride, trizma, glycine, SDS, EDTA, ANS, Gdm-HCl, PMSF, and imidazole were obtained from Sigma Chemical Co. Nickel–nitrilotriacetate (Ni–NTA) agarose–based resin was brought from Qiagen. Mono-Q ion-exchange and superdex-75 (10/300 GL) gel filtration columns were purchased from GE Healthcare. LB agar, LB broth, glycerol, ammonium persulphate, IPTG, and kanamycin were purchased from Himedia Laboratories. Syringe filters (0.22 and 0.02 μm cutoff) were purchased from Millipore Corporation. All chemicals and reagents used were of analytical grade.

Badhwar P., Khan S.H, & Taneja B. (2022). Three-dimensional structure of a mycobacterial oligoribonuclease reveals a unique C-terminal tail that stabilizes the homodimer. The Journal of Biological Chemistry, 298(12), 102595.

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Analytical Characterization of Compounds

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Sulforhodamine B salt, Trizma, Dulbecco’s phosphate-buffered saline (DPBS), phenylmethanesulfonyl fluoride (PMSF), dimethyl sulfoxide (DMSO), crystal violet, and Kolliphor^® EL were purchased from Sigma-Aldrich (St. Louis, MO, USA). Acetic acid was purchased from Thermo Fisher Scientific (Waltham, MA, USA). Abemaciclib-mesylate was provided by Dr. Peter Houghton. The compounds used for in vitro cell treatments were dissolved in DMSO and stored at −20 °C. ATXII for in vivo studies was diluted in 50:50 DMSO:Kolliphor^® EL, stored at −20 °C, and diluted 1:10 in DPBS immediately prior to use. LCMS analyses were performed on a Shimadzu UFLC system with a quadrupole mass spectrometer using a Phenomenex Kinetex C18 column (3.0 mm × 75 mm, 2.6 μm) and a CH₃CN-H₂O (0.1% HCOOH) gradient solvent system. NMR spectra were obtained on a Varian a spectrometer (500 MHz for ¹H and 125 MHz for ¹³C) using acetone-d₆ (Aldrich) as the solvent. HPLC was performed on a Waters System equipped with a 1525 binary HPLC pump coupled to a 2998 PDA detector with a Phenomenex C18 column (21.2 × 250 mm or 10 × 250 mm, 5 μm).

Robles A.J., Dai W., Haldar S., Ma H., Anderson V.M., Overacker R.D., Risinger A.L., Loesgen S., Houghton P.J., Cichewicz R.H, & Mooberry S.L. (2021). Altertoxin II, a Highly Effective and Specific Compound against Ewing Sarcoma. Cancers, 13(24), 6176.

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