C1345

Manufactured by Merck Group

Sourced in Macao

The C1345 is a laboratory equipment product manufactured by Merck Group. It is designed for performing various scientific experiments and analyses in a controlled laboratory environment. The core function of the C1345 is to provide a reliable and consistent platform for conducting research and experiments.

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8 protocols using c1345

Local DRG Drug Delivery and Verification

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Local application of drugs onto DRGs was done as previously described [21 (link)] with slight modifications. Briefly, after rats were anesthetized by isoflurane (1.5–2.5%), a midline incision was made at the L4–L6 spinal level, muscles were gently pulled aside to visualize the caudal edge of L4–L6 vertebra. A small, partial laminectomy by rongeur (501269, WPI, Florida USA) was used to expose the left L4–L6 DRGs. Drugs were dissolved in 2 μl normal saline by gelatin sponge. The incision was closed with sutures, and rats with hind limb paralysis or paresis after surgery were excluded. The drugs used were NOX2-specific blocking peptide gp91-tat (AS-63818, Anaspec, Fremont, CA), PKCε-specific blocking peptide εV1-2 (AS-62187, Anaspec), PKCε-specific activator peptide ψεRACK (AS-63818, Anaspec), H₂O₂ (323381, Sigma, St. Louis, MO), ROS scavenger PBN (B7263, Sigma), and catalase (C1345, Sigma).
To verify if the treatment of drug was limited to the specific DRG, CFSE (21888, Sigma; 100 μM in 2 μl each DRG), a fluorescent dye, was applied onto L5 DRG by gelatin sponge. One hour after application, the animal was sacrificed, and L5 DRG and proximal spinal cord segment were excised. The DRG sections (16 μm) and spinal cord sections (25 μm) were cut in a cryostat (CM1950, Leica, Nussloch, Germany). Fluorescent images were obtained with a laser confocal microscope (LSM700, Zeiss, Germany).

Xu J., Wu S., Wang J., Wang J., Yan Y., Zhu M., Zhang D., Jiang C, & Liu T. (2021). Oxidative stress induced by NOX2 contributes to neuropathic pain via plasma membrane translocation of PKCε in rat dorsal root ganglion neurons. Journal of Neuroinflammation, 18, 106.

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Antioxidants Modulate LPS-Induced Response

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C2C12 cells were co-treated with either 50pg/mL of LPS with or without the cell-permeable antioxidants, N-acetyl-L-cysteine (NAC) or Catalase [30 (link)–33 (link)]. Cells were treated with either 20 mM of NAC (A7250; Sigma-Aldrich, St. Louis MO) or 25 U/mL of Catalase (C1345; Sigma-Aldrich, St. Louis MO) for 2 hours. Cells were pretreated with Catalase for 30 minutes before the addition of LPS.

Frisard M.I., Wu Y., McMillan R.P., Voelker K.A., Wahlberg K.A., Anderson A.S., Boutagy N., Resendes K., Ravussin E, & Hulver M.W. (2014). Low levels of lipopolysaccharide modulate mitochondrial oxygen consumption in skeletal muscle. Metabolism: clinical and experimental, 64(3), 416-427.

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Enzymatic Activity Assessment of Detached Biofilms

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Detached biofilms (10 mg) was taken and suspended in 100 ml of isotonic solution. An assessment of enzymatic activities was determined by Iwase et al. (2013 (link)) by plotting a standard curve with the known concentration (or unit of enzyme activity). Standard Catalase was prepared separately in distilled water for each concentration (Catalase from bovine liver 2,950 units/mg solid; 65% protein; 4,540 units/mg protein, the product number C1345, Sigma-Aldrich). Furthermore, bacterial suspension (100 μl) was taken to Pyrex tube (13 mm diameter, 100 mm height, borosilicate glass; Corning, USA). Afterwards, 100 μl of 1% Triton X-100 and 100 μl of undiluted hydrogen peroxide (30%) was taken to the solution and mixed thoroughly and incubated at room temperature. Then the height of the O₂-forming foam was measured using a ruler. We measured the O₂-foam which was constant for 15 min. All these steps performed under ice condition (sample was kept in an ice bucket) to prevent the loss of active enzyme.

Karn S.K., Fang G, & Duan J. (2017). Bacillus sp. Acting as Dual Role for Corrosion Induction and Corrosion Inhibition with Carbon Steel (CS). Frontiers in Microbiology, 8, 2038.

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Single-molecule Imaging Buffer Preparation

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The samples were imaged in a water-based buffer that contained 200 U/ml glucose oxidase, 1000 U/ml catalase, 10% w/v glucose, 200 mM Tris-HCl pH 8.0, 10 mM NaCl, 50 mM MEA with addition of 2 mM COT. The mixture of 4 kU/ml glucose oxidase (G2133, Sigma) and 20 kU/ml catalase (C1345, Sigma) was stored at −20 °C in an aqueous buffer containing 25 mM KCl, 4 mM TCEP, 50% v/v glycerol and 22 mM Tris-HCl pH 7.0. MEA-HCl (30080, Sigma) was stored at a concentration of 1 M in H₂O at −20 °C. COT (138924, Sigma) was stored at 200 mM in dimethyl sulfoxide at −20 °C.
The samples were mounted immediately prior imaging using ~200 µl of the imaging buffer and placing a clean coverslip on top of it while avoiding bubbles. The interface between the plastic bottom of the petri dish and the clean coverslip in a well with imaging buffer is sufficiently airtight thanks to the surface tension and allows for long imaging runs (≥8 h) without pH shift. After imaging, the samples were rinsed once with PBS and kept in PBS at +4 °C.

Andronov L., Genthial R., Hentsch D, & Klaholz B.P. (2022). splitSMLM, a spectral demixing method for high-precision multi-color localization microscopy applied to nuclear pore complexes. Communications Biology, 5, 1100.

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Active Cross-linked Filament Bundles

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MTs were mixed with the molecular motor clusters that act as active cross-linkers and with ATP (A2383, Sigma) that drives the activity of the gel. The aqueous dispersion contains a nonadsorbing polymer [polyethylene glycol (PEG), 20 kDa; 95172, Sigma] that promotes the formation of filament bundles via depletion interaction. To maintain a constant concentration of ATP during the experiments, we added an enzymatic ATP-regenerator system based on phosphoenolpyruvate (P7127, Sigma) and pyruvate kinase (434301, Invitrogen), which converted adenosine 5′-diphosphate back into ATP. Several antioxidant components were also included in the solution to prevent protein residues from forming disulfide bonds and to minimize fluorophore damage by oxygen species. The antioxidants were as follows: Trolox (238813, Sigma), DTT (43815, Sigma), and an oxygen-scavenging enzymatic mixture that includes glucose (G8270, Sigma), glucose oxidase (G2133, Sigma), and catalase (C1345, Sigma).

Guillamat P., Kos Ž., Hardoüin J., Ignés-Mullol J., Ravnik M, & Sagués F. (2018). Active nematic emulsions. Science Advances, 4(4), eaao1470.

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NSCLC Cell Lines Treated with Chemotherapy Agents

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Human non-small cell lung cancer (NSCLC)-derived cell lines A549, H460 and H520 were purchased from American Type Culture Collection (Manassas, VA, USA) and China Center for Type Culture Collection (Wuhan, China). All these cells were grown in DMEM (Gibco/Invitrogen, C11995500CP, Carlsbad, CA, USA) supplemented with 10% fetal bovine serum (Gibco/Invitrogen, 10099-141) and antibiotics (penicillin/streptomycin, 100 U/ml, Gibco/Invitrogen, 15140-122) at 37 °C in 5% CO₂. Cells were plated in cell culture plates and allowed to adhere overnight, subsequently treated by DMSO, TMZ, POH, TMZ + POH and TMZ − POH (all 100 μM) for 48 hours, respectively. In some experiments, ROS scavengers, catalase (CAT, Sigma-Aldrich, C1345) and N-acetyl-L-cysteine (NAC, Sigma-Aldrich, A7250) were employed 2 hours before the above treatments.

Song X., Xie L., Wang X., Zeng Q., Chen T.C., Wang W, & Song X. (2016). Temozolomide-perillyl alcohol conjugate induced reactive oxygen species accumulation contributes to its cytotoxicity against non-small cell lung cancer. Scientific Reports, 6, 22762.

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Catalase Activity Quantification in Cells

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Catalase activity was determined by measuring the decrease in H₂O₂. Cells were homogenized with 0.1% Triton in PBS and centrifuged at 17,000×g for 30 min at 4 °C. Supernatants were incubated with 5 mM H₂O₂ in PBS. The decrease of H₂O₂ was measured at 240 nm for 3 min at 30 s intervals, using a microplate reader (PowerWave HT, Biotek). Catalase activity in the samples was determined using a standard catalase calibration curve (Sigma, C1345; 0–150 u/ml). Catalase activity was expressed as units per milligram protein^{71 (link)}.

Albert-Garay J.S., Riesgo-Escovar J.R, & Salceda R. (2022). High glucose concentrations induce oxidative stress by inhibiting Nrf2 expression in rat Müller retinal cells in vitro. Scientific Reports, 12, 1261.

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Native PAGE Analysis of Parasite Protein Complexes

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Proteins from parasites were solubilised in Native PAGE Sample Buffer (Thermo Fisher Scientific) containing 2 mM EDTA, 1 × cOmplete protease inhibitors (Sigma) and 1% (v/v) TX-100 (Sigma) at 2.5 × 10⁵ parasites per μL. Samples were separated by Clear Native PAGE on a NativePAGE 4–16% Bis-Tris protein gel (Thermo Fisher Scientific) using BN-PAGE buffers prepared without cathode buffer additive, but with sodium deoxycholate (0.05% w/v, Sigma, D6750) and n-dodecyl β-D-maltoside (0.01% w/v, Sigma, D4641). After separation, the lane containing the NativeMark protein ladder (Thermo Fisher Scientific) was removed and stained with Coomassie. An in-gel Complex IV activity assay was performed on the remaining lanes as described in [27 (link)]. Briefly, the gel was equilibrated in 50 mM KH₂PO₄ buffer (pH 7.2) for 15 minutes before incubating in freshly made Complex IV activity buffer (KH₂PO₄ (50 mM, pH 7.2), cytochrome c (0.1% w/v from horse heart, Sigma, C2506), catalase (0.1% w/v from bovine liver, Sigma, C1345), sucrose (7.5% w/v, Sigma, S9378) and 3,3′-diaminobenzidine tetrahydrochloride (DAB, 0.1% w/v, Sigma, D8001) until staining of the no ATc sample was visible. The gel was then fixed in methanol (50% v/v) and acetic acid (10% v/v), re-connected with the Coomassie-stained protein ladder and imaged using a ChemiDoc MP imaging system (BioRad).

Leonard R.A., Tian Y., Tan F., van Dooren G.G, & Hayward J.A. (2023). An essential role for an Fe-S cluster protein in the cytochrome c oxidase complex of Toxoplasma parasites. PLOS Pathogens, 19(6), e1011430.

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