Tricine

Manufactured by Thermo Fisher Scientific

Tricine is a laboratory buffer solution used in electrophoresis and other biochemical applications. It serves as a buffer agent to maintain a specific pH range. The product provides a stable and consistent pH environment for various experimental procedures.

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Tricine sample buffer (7 citations) Novex 16% tricine gels (6 citations) Novex Tricine SDS sample buffer (5 citations) Novex 10–20% Tricine Gels (5 citations) Novex 10–20% Tris‐Tricine gels (4 citations) Novex Tricine SDS Sample Buffer (2X) (3 citations) Tricine SDS Running Buffer (3 citations) Tricine–SDS-PAGE gel (3 citations) Novex Tricine gels (3 citations) Tris-Tricine gradient gel (3 citations)

9 protocols using tricine

Purification and Characterization of Enzymes

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Aprotinin, pepstatin, leupeptin, phenylmethylsulfonyl fluoride (PMSF), tricine, ampicillin, DEAE-Sephacel, Ultrogel Aca-44, β-mercaptoethanol, pyridoxal 5’-phosphate, succinyl-CoA, α-ketoglutarate dehydrogenase, HEPES-free acid, MOPS, thiamine pyrophosphate and NAD⁺ were obtained from Sigma-Aldrich Chemical Company. Glucose, glycerol, acetic acid, methanol, glycine, disodium ethylenediamine tetraacetic acid dihydrate, tricine, ammonium sulfate and potassium hydroxide were purchased from Fisher Scientific. Centricon concentrators were from Millipore. SDS-PAGE reagents and Phusion DNA Polymerase were acquired from Thermo Scientific. 5-Aminolevulinic acid (ALA) hydrochloride was purchased from Acros Organics. Bmtl, Sall, BlpI, and BamHI restriction enzymes were obtained from New England BioLabs, Inc. Oligonucleotides were synthesized by Integrated DNA Technologies. T4 DNA ligase and ligase buffer were obtained from Thermo Scientific Fermentas and bicinchoninic acid protein determination kits were purchased from Thermo Scientific Pierce.

Fratz E.J., Clayton J., Hunter G.A., Ducamp S., Breydo L., Uversky V.N., Deybach J.C., Gouya L., Puy H, & Ferreira G.C. (2015). Human Erythroid 5-Aminolevulinate Synthase Mutations Associated with X-Linked Protoporphyria Disrupt Conformational Equilibrium and Enhance Product Release. Biochemistry, 54(36), 5617-5631.

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Preparation of Neurotransmitter Standard Solutions

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Sodium hydroxide (NaOH) was purchased from EMD Millipore (San Diego, CA). Dextrose and tricine were from Fisher Scientific (Pittsburgh, PA). LC grade acetonitrile (ACN) was from VWR (Radnor, PA). d4-Acetylcholine (d4-ACh) was from CDN Isotopes Inc. (Pointe-Claire, QC). All solutions were made with HPLC grade submicron filtered water (Fisher Chemical, Fair Lawn, NJ). Stock solutions of serine (Ser), threonine (Thr), asparagine (Asn), glutamine (Gln), alanine (Ala), histidine (His), aspartate (Asp), tyrosine (Tyr), γ-aminobutyric acid (GABA), valine (Val), methionine (Met), leucine (Leu), phenylalanine (Phe), tryptophan (Trp), arginine (Arg), taurine (Tau), glycine (Gly), glutamate (Glu), dopamine (DA), serotonin (5-HT), proline (Pro), trans-4-hydroxy proline (Hyp), cysteine (Cys), lysine (Lys), isoleucine (Ile), α-aminobutyric acid (α-ABA), β-aminobutyric acid (β-ABA), β-homoserine (β-HSer), tyramine (TryA), citrulline (Cit), kynurenine (Kyn), 2-aminoadipic acid (Aad), ornithine (Orn), histamine (Hist), 5-hydroxytryptophan (5-HTP), N-acetylcysteine (NAC), epinephrine (Epi), and acetylcholine (ACh) were made in LC water and diluted to working concentrations using a balanced salt solution (BSS) containing 25 mM tricine, 125 mM NaCl, 5.9 mM KCl, 1.2 mM MgCl₂, 2.4 mM CaCl₂, and various glucose concentrations as described in the text, and the pH was adjusted to 7.4 with NaOH.

Ogunkunle E.O., Donohue M.J., Steyer D.J., Adeoye D.I., Eaton W.J, & Roper M.G. (2022). Small molecules released from islets of Langerhans determined by liquid chromatography – mass spectrometry. Analytical Methods, 14(21), 2100-2107.

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Heterologous Protein Expression and Purification

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Yeast extract and curcumin were obtained from Acros Organics (Geel, Belgium). Tryptic soy agar and gold(III) chloride trihydrate were acquired from MP Biomedicals (Santa Ana, CA). Ampicillin, isopropyl β-D-1-thiogalactopyranoside (IPTG), imidazole, sodium monobasic phosphate, sodium dibasic phosphate, sodium dodecyl sulfate, sodium hydroxide, sodium chloride, sucrose, tris-hydrochloride, tryptone, PFU high fidelity, DpnI, ACS grade methanol and urea were obtained from Fisher Scientific (Pittsburgh, PA). 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid (HEPES), magnesium sulfate, nickel chloride, sodium borohydride were purchased from Sigma Aldrich (St. Louis, MO). Tricine was purchased from Alfa Aesar (Ward Hill, MA). Glacial acetic acid and Factor Xa cleavage kit were purchased from EMD Millipore (Rockland, MA). Ethyl acetate was purchased from Pharmco-AAPER (Brookfield, CT). Ethylenediaminetetraacetic acid (EDTA) and hydrochloric acid were acquired from VWR (Radnor, PA). HPLC grade methanol was obtained from Ricca Chemical Company (Arlington, TX). Sephadex™ G-25 medium beads were purchased from Amersham Pharmacia Biotech AB (Piscataway, NJ). Columns were purchased from Bio-Rad (Hercules, CA).

Dai M., Frezzo J., Sharma E., Chen R., Singh N., Yuvienco C., Caglar E., Xiao S., Saxena A, & Montclare J. (2016). Engineered Protein Polymer-Gold Nanoparticle Hybrid Materials for Small Molecule Delivery. Journal of nanomedicine & nanotechnology, 7(1), 356.

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Heterologous Protein Expression and Purification

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Characterizing Peptide-Loaded Hydrogels

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Hydrogels were swollen in buffer (50 mM Tricine (Acros Organics), 50 mM NaCl, 10 mM CaCl₂, 50 μM ZnCl₂ (Alfa Aesar), and 0.05 wt% Brij35 (Alfa Aesar) in ddH₂O, pH 7.4) at 37 °C for 24 hours to achieve equilibrium swelling before characterization. Hydrogel images were collected using a Canon E05 Rebel T2i digital camera. Mass swelling ratio was determined by measuring equilibrium swelling and dry gel mass after lyophilization. The efficiency of peptide incorporation into the hydrogels was measured by collecting the buffer solution and quantifying the amount of peptide released into buffer via absorbance at 205 nm, as previously described (section 2.1). The amount of peptide incorporated into the gel but not fully crosslinked was quantified by incubating gels in 1 mL of 0.35 mg/mL Ellman’s reagent in PBS for 30 minutes, then measuring absorbance at 405 nm on a Tecan infiniteM200 microplate reader, and comparing to a standard curve generated using peptide alone [47 (link)].

Van Hove A.H., Beltejar M.J, & Benoit D.S. (2014). Development and in vitro assessment of enzymatically-responsive poly(ethylene glycol) hydrogels for the delivery of therapeutic peptides. Biomaterials, 35(36), 9719-9730.

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Hydrogel Degradation Kinetics Assay

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After formation, hydrogels were incubated in 1 mL buffer (10 mM CaCl₂, 50 mM NaCl, 50 μM ZnCl₂ (Alfa Aesar), 50 mM Tricine (Acros Organics), and 0.05 wt% Brij35 (Alfa Aesar) in ddH₂O, pH 7.4) at 37 °C. After 24 hours, buffer solutions were exchanged with either fresh buffer or buffer containing 10 nM recombinant human MMP2 (MMP2, PeproTech). As MMP2 inactivates over time, solutions were collected and replaced at a minimum every 48 hours [24 (link)]. At various time points, solutions were collected and stored at −80 °C until quantification, and hydrogel wet and dry (post-lyophilization) masses were obtained (swelling ratio Q=M_wet/M_dry). Hydrogel degradation kinetics were fit to a pseudo-first-order degradation equation [25 (link)] to determine the degradation kinetic time constant, k_deg (eqn. 1):

\frac{M_{t}}{M_{0}} \propto e^{- k_{\deg} * t}

Van Hove A.H., Burke K., Antonienko E., Brown E I.I.I, & Benoit D.S. (2015). Enzymatically-responsive pro-angiogenic peptide-releasing poly(ethylene glycol) hydrogels promote vascularization in vivo. Journal of controlled release : official journal of the Controlled Release Society, 217, 191-201.

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99mTc-Radiolabeled M2-Targeting Peptide Synthesis

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Hydrazine nicotinamide (HYNIC)-conjugated M2-targeting precision peptide
was custom synthesized by a commercial vendor (GeneScript, Piscataway, NJ) using
standard peptide synthesis. Then, 250 μg of HYNIC-M2-targeting conjugated
peptide was radio labeled with 99m-Tc-pertechnetate in the presence of a
solution containing tricine (14.4 mg mL⁻¹: Acros Organics) and
stannous chloride (0.5 mg mL⁻¹: Acros Organics) in oxygen free
condition (air was purged by N₂). Following this step, the mixture
was centrifuged to remove the unconjugated peptide using 1K centrifugal filter
at 3200 × g for 15 min. The amount of radiolabeled
peptide was detected using a dose calibrator (CRC-25R: Capintec, Inc.). A dose
of approximately 300 μCi of radiolabeled peptide was injected per
animal.

Rashid M.H., Borin T.F., Ara R., Alptekin A., Liu Y, & Arbab A.S. (2020). Generation of Novel Diagnostic and Therapeutic Exosomes to Detect and Deplete Protumorigenic M2 Macrophages. Advanced therapeutics, 3(7), 1900209.

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Quantitative Immunoblot Analysis of AβPP

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Pulverized brain aliquots extracted with TBS containing 1% Triton X-100 was used for immunoblot. Equal amount of total protein was separated on SDS-PAGE or 16% Tricine (Invitrogen) for AβPP C-terminal fragments (CTF). Gel was transferred onto nitrocellulose membrane (Amersham Hybond-ECL). Membrane was blocked with 5% non-fat milk and incubated overnight at 4°C with anti-human AβPP antibody (mouse mAb, P2-1, 1:1000), anti-AβPP CTF (rabbit pAb, 1:1000), anti-MBP (rabbit pAb, 61B 1:1000), anti-neurospecific β-tubulin (Abcam ab18207, 1:2000). Horse-radish peroxidase conjugated secondary antibodies (Amersham) were used for detection at 1:5000 dilution. Membrane was developed using ECL (Pierce) and chemiluminescence signals were quantitated with VersaDoc (BioRad Model 3000). Chemiluminescence signals were normalized to that of the internal control and presented as percentage to the level of Tg-5xFAD.

Ou-Yang M.H., Xu F., Liao M.C., Davis J., Robinson J.K, & Van Nostrand W.E. (2014). The N-terminal region of myelin basic protein reduces fibrillar amyloid-β deposition in Tg-5xFAD mice. Neurobiology of aging, 36(2), 801-811.

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Protein Separation and Identification

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Proteins from the CM prepared in the absence of serum were separated using a combination of anion exchange chromatography and SDS-PAGE resulting in a two dimensional separation of the proteins. A gravity fed DEAE-650M anion exchange column 1.6 cm×1.5 cm was equilibrated in PBS buffer diluted three fold with water (1/3 PBS). A 20 mL volume of each supernatant was diluted with 40 mL of water resulting in the same salt concentration as the equilibrating buffer and loaded onto the column. Then column was washed with 10 mL of 1/3PBS. Elution was done stepwise with 800 µL of 0.1 M, 0.2 M, and 0.5 M NaCl in water. Each fraction was precipitated using one volume of trichloroacetic acid (TCA) (1.42 g/mL) to four volumes of sample fraction, and allowed to precipitate overnight at −20°C. The samples were then centrifuged in table top Eppendorf centrifuge at 16000 g to pellet the proteins. The pellets were washed twice with cold acetone and the precipitated proteins were dissolved in 20 µL of 1x SDS-electrophoresis loading buffer and loaded equally on two gels (10% Tricine, Invitrogen). One gel was stained with Coommassie Brilliant Blue and the other was used for electroblotting of proteins to PVDF membrane, Coommasie staining and N-terminal sequence analysis.

Sayers K.T., Brooks A.D., Sayers T.J, & Chertov O. (2014). Increased Secretory Leukocyte Protease Inhibitor (SLPI) Production by Highly Metastatic Mouse Breast Cancer Cells. PLoS ONE, 9(8), e104223.

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