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Potassium Cyanide

Potassium cyanide is an inorganic compound with the chemical formula KCN.
It is a highly toxic substance that can be lethal if ingested or inhaled.
Potassium cyanide is used in various industrial processes, such as electroplating, metal extraction, and organic synthesis.
Researchers working with potassium cyanide must exercise extreme caution and follow strict safety protocols to prevent accidental exposure or misuse.
PubCompare.ai's AI-powered research optimization can help you find the most accurate and reproducible protocols for working with potassium cyanide, ensuring your research is optimized for success.
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Most cited protocols related to «Potassium Cyanide»

1
Rodent Brain Tissue Preparation for Microscopy
Muscle tissue was prepared as described in Schwarz et al. (2000) (link). For the preparation of rodent brain tissue the animals were perfused transcardially first with 30 ml of phosphate-buffered saline and then with 40 ml of fixative solution (4% paraformaldehyde in 0.1M PBS [pH 7.4]). The brain tissue was then removed and kept in fixative over night at 4 °C. After being washed twice in PBS, tissue slices (0.2 to 1.5 mm thick) were cut on a vibratome (752 M Vibroslice, Campden Instruments, Leichester, United Kingdom) and kept for 24 h in PBS at 4 °C. Pieces about 1.5 mm in size were then excised and washed three times for 30 min each in cacodylate buffer at pH 7.4.The tissue was postfixed for 2 h in 2% osmium tetroxide/1.5% potassium ferric cyanide in aqueous solution at room temperature. Then the tissue was subjected to a contrast enhancement step by soaking it over night in a solution of 4% uranyl acetate in a 25% methanol/75% water mixture (Stempak and Ward 1964 (link)) at room temperature. After that the tissue was dehydrated in a methanol sequence (25%, 70%, 90%, and 100% for 30 min each) followed by infiltration of the epoxy (Spurr, Epon 812, or Araldite, all from Serva, Heidelberg, Germany) monomer (epoxy/methanol 1:1, for 3 h rotation at room temperature; epoxy/methanol 3:1, overnight at 4°C; pure epoxy, 3 h rotating at room temperature). Polymerization was 48 h at 60 °C for Epon and at 70 °C for Spurr and Araldite. The block face was trimmed to a width of several hundred microns and a length of about 500 μm using either a conventional microtome or a sharp knife. SEM images of the untrimmed block face can be used to select the desired field of view before the final trimming step producing the desired small cutting pyramid.
Denk W, & Horstmann H. (2004). Serial Block-Face Scanning Electron Microscopy to Reconstruct Three-Dimensional Tissue Nanostructure. PLoS Biology, 2(11), e329.
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Publication 2004
Animals araldite Brain Buffers Cacodylate EPON Epon 812 Epoxy Resins Face Fixatives Methanol Microtomy Muscle Tissue Osmium Tetroxide paraform Phosphates Polymerization Potassium Cyanide Rodent Saline Solution spurr resin Tissues uranyl acetate
2
Multimodal Imaging of Biological Structures
Experimental datasets used in this study:

Vesicles are giant unilamellar vesicles made of DOPC, supplemented with 0.1% DOPE-Atto647N (ref AD-647N, Atto-tec, Germany) and 0.03% DSPE-PEG(2000) Biotin (ref 880129, Avanti Polar Lipids, USA) electroformed during 1 h at 1V RMS [44 (link)] in a sucrose buffer at 250 milliosmoles. Vesicules were adhered on avidin coated glass coverslips, deflated with an hyperosomotic shock due to buffer evaporation and imaged with a Yokogawa spinning-disc CSU-X1 mounted on a Nikon Ti-Eclipse microscope stand using a 100x objective with NA 1.3 (z spacing 340 nm, xy pixel size 122 nm).

MRI dataset was acquired from a normal healthy person, using a FLAIR sequence.

FIB-SEM 80% confluent HeLa cells were rinsed once with PBS, fixed for 3h on ice using 2.5% glutaraldehyde/2% paraformaldehyde in buffer A (0.15M cacodylate, 2mM CaCl2). Then cells were extensively washed on ice in buffer A, pelleted and incubated 1h on ice in 2% osmium tetroxide and 1.5% potassium Ferro cyanide in buffer A and finally rinsed 5 times in distilled water at room temperature. Cells were then incubated 20min at room temperature in 0.1M thiocarbohydrazide, which had been passed through a 0.22 μm filter, and extensively washed with water. Samples were incubated overnight at 4° C protected from light in 1% uranyl-acetate, washed in water, further incubated in 20mM lead aspartame for 30min at 60°C and finally washed in water. Samples were dehydrated in a graded series ethanol, embedded in hard Epon and incubated for 60h at 45°C then for 60 h at 60°C. A small bloc was cut and mounted on a pin, coated with gold and inserted into the chamber the HELIOS 660 Nanolab DualBeam SEM/FIB microscope (FEI Company, Eindhoven, Netherlands). ROI were prepared using focused ion beam (FIB) and ROI set to be approximatively 20 microns wide. For imaging, electrons were detected using Elstar In-Column secondary electrons Detector (ICD). During acquisition process, the thickness of the FIB slice between each image acquisition was 5 nm.

The drosophila egg chamber is dissected from a drosophila ovary. Cell nuclei were stained with DAPI and cell membranes labeled with the fusion proteins Nrg::GFP and Bsg::GFP [45 (link)]. The egg chamber was embedded in Vectashield and spacers were used to prevent tissue deformation. Images were acquired using an inverted Olympus point scanning confocal microscope IX81 with a 60x objective NA 1.42(z spacing 750 nm, xy pixel size 265 nm).

Machado S., Mercier V, & Chiaruttini N. (2019). LimeSeg: a coarse-grained lipid membrane simulation for 3D image segmentation. BMC Bioinformatics, 20, 2.
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Publication 2019
1,2-distearoyl-sn-glycero-3-phosphoethanolamine-N-methoxy-poly(ethylene glycol 2000) 1,2-oleoylphosphatidylcholine Aspartame Avidin Biotin Buffers Cacodylate Cell Nucleus Cells DAPI Drosophila Electrons EPON Ethanol Focused Ion Beam Scanning Electron Microscopy Gigantism Glutaral Gold HeLa Cells Light Lipids Microscopy Microscopy, Confocal Neuregulins Osmium Tetroxide Ovary paraform Plasma Membrane Potassium Cyanide Shock Sucrose thiocarbohydrazide Tissues Unilamellar Vesicles uranyl acetate
3
Structure Determination of mTOR-mLST8 Complex
Initial phases were obtained from isomorphous and anomalous differences of two heavy atom derivatives, prepared by soaking crystals in stabilization buffer lacking DTT and supplemented with 1 mM uranyl acetate (1 hour), or with 0.4 mM potassium-gold cyanide (75 min.) at at 4° C. Initial phases, calculated with the program SHARP50 had a mean figure of merit of 0.35 (35.0 to 4.5 Å). The uranyl derivative had a dispersive phasing power (Pp) of 0.89 and anomalous Pp of 0.60, with a dispersive Rcullis of 0.79 and anomalous Rcullis of 0.95. The gold derivative had a dispersive Pp of 0.80 and anomalous Pp of 0.29, with a dispersive Rcullis of 0.66 and anomalous Rcullis of 0.98. The phases were improved using solvent flattening and two-fold ncs averaging with multiple masks with the program DM51 . The model was built using O52 (link) and refined first with REFMAC551 and then with PHENIX53 (link), using tight ncs restraints on atom positions. The final model contains residues 1385 to 2549 of human mTOR, and 8 to 324 of human mLST8. mTORΔN residues 1376-1384 at the N-terminus, residues 1815-1866 in the FAT domain, and residues 2437-2491 between kα9b and kα10 in the KD are disordered. mLST8 residues 1-7 and 325-326 from the N- and C-termini are disordered. The Ramachandran plot, calculated by PROCHECK, has 88.5, 11.0 and 0.5 % of the residues in the most favored, additionally allowed, and generously allowed regions, respectively. There are no residues in disallowed regions. The Rfree test set of the Native data contains 1699 reflections.
Yang H., Rudge D.G., Koos J.D., Vaidialingam B., Yang H.J, & Pavletich N.P. (2013). mTOR kinase structure, mechanism and regulation by the rapamycin-binding domain. Nature, 497(7448), 217-223.
Publication 2013
Buffers derivatives FRAP1 protein, human Gold gold cyanide Homo sapiens MLST8 protein, human Potassium Potassium Cyanide Reflex Solvents uranyl acetate
4
Measuring Mitochondrial SOD2 Activity

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Publication 2012
Biological Assay Cardiac Arrest cytochrome C(L) enzyme activity Potassium Cyanide Proteins RRAD protein, human SOD2 protein, human SOD3 protein, human Superoxides Xanthine Oxidase
5
Aortic Protein Expression and Enzyme Activity
Aortas were used as a surrogate large elastic artery to provide sufficient tissue for analysis of protein expression by western blot and enzyme activity as described previously (Cernadas et al. 1998 (link); Blackwell et al. 2004 (link); Ungvari et al. 2008 (link); Lesniewski et al. 2009 (link)). Aortas were excised, cleared of surrounding tissues and frozen in liquid nitrogen before storage at -80°C. For assay the tissue was pulverized over liquid nitrogen and homogenized in ice-cold RIPA lysis buffer containing protease and phosphatase inhibitors (Protease Inhibitor Cocktail Tablet (Roche) and 0.01% phoshatase inhibitor cocktail (Sigma)). Fifteen μg of protein was loaded on 12% polyacrylamide gels, separated by electrophoresis and transferred onto nitrocellulose membranes for western blot analysis. Antibodies for western analysis included anti-glyceraldehyde-3-phosphate dehydrogenase (GAPDH, Cell Signaling, Danvers, MA), anti-p67phox, anti-eNOS (BD Biosciences, San Jose, CA), anti-nitrotyrosine, anti-SIRT1, anti-catalase (Abcam, Cambridge, MA), anti-manganese superoxide dismutase (MnSOD) (Stressgen, Ann Arbor, MI). Enzyme activity of MnSOD was determined in aortic lysates (1 μg protein) using a superoxide dismutase (SOD) activity assay kit in the presence of 1 mmol/L potassium cyanide to block copper-zinc SOD (CuZnSOD) activities. Enzyme activity for catalase was measured using a kit (Cayman Chemical Ann Arbor, MI). NADPH oxidase activity (10 μg total protein) was measured using a Amplex red xanthine/xanthine oxidase assay kit (Invitrogen, Carlsbad, CA) according to manufacturer instructions with NADPH (200 μmol/L/reaction) as the reaction substrate. Pro-inflammatory cytokines interleukin-1 beta, interleukin-6, interferon gamma and tumor necrosis factors alpha were measured using a multiplex SearchLight Chemiluminescent Array Kit (Thermo Fisher Scientific Inc.) according to manufacturer's instructions.
Rippe C., Lesniewski L., Connell M., LaRocca T., Donato A, & Seals D. (2010). Short-term Calorie Restriction Reverses Vascular Endothelial Dysfunction in Old Mice by Increasing Nitric Oxide and Reducing Oxidative Stress. Aging cell, 9(3), 304-312.
Publication 2010
3-nitrotyrosine Antibodies Aorta Arteries Biological Assay Buffers Caimans Cardiac Arrest Caspase 1 Catalase Cold Temperature Copper Cytokine Electrophoresis enzyme activity Freezing GAPDH protein, human Glyceraldehyde-3-Phosphate Dehydrogenases Inflammation inhibitors Interferon Type II Interleukin-1 beta Interleukin-6 NADP NADPH Oxidase neutrophil cytosol factor 67K Nitrocellulose Nitrogen NOS3 protein, human Phosphoric Monoester Hydrolases polyacrylamide gels Potassium Cyanide Protease Inhibitors Proteins Radioimmunoprecipitation Assay Sirtuin 1 SOD2 protein, human Superoxide Dismutase Superoxide Dismutase-1 Tablet Tissue, Membrane Tissues Tumor Necrosis Factor-alpha Western Blot Western Blotting Xanthine Oxidase Zinc

Most recents protocols related to «Potassium Cyanide»

1
Synthesis and Evaluation of Auranofin Metabolites
Aurocyanide (Gold(I) potassium cyanide) was purchased from Alfa Aesar (Ward Hill, MA, USA). l-thio-3-D-glucopyranosato-(triethylphosphine) gold(I) (M1) was synthesized from chloro(triethylphosphine) gold(I) and the thiosugar. Other proposed metabolites of auranofin (M2-M6) were obtained from Sigma (St. Louis, MO, USA). Recombinant human transforming growth factor-β1 (TGF-β1) was supplied by PeproTech (Cranbury, NJ, USA). TAA, lipopolysaccharide (LPS), and adenosine triphosphate (ATP) were purchased from Sigma (St. Louis, MO, USA).
Kim H.Y., Otgontenger U., Kim J.W., Lee Y.J., Kim S.B., Lim S.C., Kim Y.M, & Kang K.W. (2023). Anti-fibrotic effect of aurocyanide, the active metabolite of auranofin. Archives of Pharmacal Research, 46(3), 149-159.
Publication 2023
Adenosine Triphosphate Auranofin Gold gold cyanide Homo sapiens Lipopolysaccharides Potassium Cyanide TGF-beta1 Thiosugars
2
Quantification of Aortic ALP Activity
ALP activity was measured by using an ALP assay kit (Nanjing Jiancheng Bioengineering, Nanjing, China). The proteins were extracted from the aortic tissues or A7r5 cells in 0.05% Triton X-100 in PBS and quantified using a bicinchoninic acid (BCA, ThermoFisher, Waltham, MA, USA) protein assay. The 5 μL supernatant of samples was mixed with reaction mixture including alkaline buffer solution 50 μL mainly containing disodium phenyl phosphate and substrate solution 50 μL mainly containing 4-aminoantipyrine and potassium cyanide. They were incubated at 37 °C for 15 min, then developer 150 μL was added into each well. The absorbance was detected at 520 nm wavelength and the results were normalized to the level of total protein.
Wang H.Y., Wang F.Z., Chang R., Wang Q., Liu S.Y., Cheng Z.X., Gao Q., Zhou H, & Zhou Y.B. (2023). Adrenomedullin Improves Hypertension and Vascular Remodeling partly through the Receptor-Mediated AMPK Pathway in Rats with Obesity-Related Hypertension. International Journal of Molecular Sciences, 24(4), 3943.
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Publication 2023
Ampyrone Aorta bicinchoninic acid Biological Assay Buffers Cells Potassium Cyanide Proteins sodium phosphate, dibasic Tissues Triton X-100
3
Measuring SOD1 and SOD2 Activities
Supernatants were collected from cell pellets lysed in SOD activity buffer (20 mM HEPES, pH 7.2, containing 1 mM EGTA, 210 mM mannitol, and 70 mM sucrose) using an ice sonication cooling cycle. The collected supernatants were diluted (with a buffer of 50 mM Tris-HCL, pH 8.0) or concentrated using a 10 kDa cutoff centrifuge concentrator (Amicon, Charlotte, NC, USA) to adjust enzymatic activity into a linear-curve range. Total SOD activity was measured using a superoxide dismutase assay kit (706002, Cayman, Ann Arbor, MI, USA). The SOD2 activity was measured by adding 10 μL of potassium cyanide solution (freshly prepared) into the sample to a final concentration of 3 mM in the assay to explicitly inhibit the SOD1 activity [72 (link)]. The actual SOD1 activity was calculated by subtracting the SOD2 activity from the total SOD activity. In the assay of effect of protein complex formation on SOD1 activity, 20 μg of His-tag-purified SOD1 and YWHAE or YWHAZ protein each were added into 100 μL of the mixture (with the SOD activity assay buffer). The mixture was incubated, at 4 °C, for 0, 1, 2, 4, and 15 h with SOD1 to YWHAE or YWHAZ at 1:1 ratio or for 15 h with SOD1 to YWHAE or YWHAZ at 1:3 ratio. At the end of the incubations, the mixture was used to assay for SOD1 activity.
Sun Z, & Lei X.G. (2023). Evidence and Metabolic Implications for a New Non-Canonical Role of Cu-Zn Superoxide Dismutase. International Journal of Molecular Sciences, 24(4), 3230.
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Publication 2023
Biological Assay Buffers Caimans Cardiac Arrest Cells Egtazic Acid enzyme activity HEPES Mannitol Pellets, Drug Potassium Cyanide Protein Biosynthesis Proteins SOD2 protein, human Sucrose Superoxide Dismutase Tromethamine YWHAE protein, human
4
Synthesis of N-Arylcyanothioformamides
All N-Arylcyanothioformamide 27a–x used herein were prepared according to our published procedure form various substituted isothiocyanates and potassium cyanide (Scheme 2a) [26 (link)]. These reactants were partially characterized by standard 1D NMR spectroscopy (1H and 13C) and the obtained spectral data matched those reported earlier [32 (link)].
Moussa Z., Paz A.P., Judeh Z.M., Alzamly A., Saadeh H.A., Asghar B.H., Alsaedi S., Masoud B., Almeqbaali S., Estwani S., Aljaberi A., Al-Rooqi M.M, & Ahmed S.A. (2023). First X-ray Crystal Structure Characterization, Computational Studies, and Improved Synthetic Route to the Bioactive 5-Arylimino-1,3,4-thiadiazole Derivatives. International Journal of Molecular Sciences, 24(4), 3759.
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Publication 2023
Isothiocyanates Potassium Cyanide Spectroscopy, Nuclear Magnetic Resonance
5
Cyanide-Binding and Oxy-Form Generation of BvPgb1.2
To prepare the cyanide form of BvPgb1.2, the purified protein was dialyzed in 10 mM potassium ferricyanide and 1 mM potassium cyanide dissolved in 50 mM MOPS for 8 h in 0.5 L solution; this process was performed twice. The cyanide-protein solution was passed through a PD10 column (Cytvia Life Science) to remove excess cyanide and the protein was concentrated using 10 kDa Vivaspin® 20 mL ultrafiltration units (Vivascience). The oxy form of BvPgb1.2 was generated by passing the purified Hb through a PD10 column (Cytvia Life Science) in order to equilibrate with the oxygenated buffer (50 mM MOPS).
Christensen S., Stenström O., Akke M, & Bülow L. (2023). Conformational Dynamics of Phytoglobin BvPgb1.2 from Beta vulgaris ssp. vulgaris. International Journal of Molecular Sciences, 24(4), 3973.
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Publication 2023
Buffers Cyanides morpholinopropane sulfonic acid Potassium Cyanide potassium ferricyanide Proteins Ultrafiltration

Top products related to «Potassium Cyanide»

1
Potassium cyanide by Merck Group
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Description not available
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Rotenone by Merck Group
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Rotenone is a naturally occurring insecticide and piscicide derived from the roots of certain tropical plants. It is commonly used as a research tool in laboratory settings to study cellular processes and mitochondrial function. Rotenone acts by inhibiting the electron transport chain in mitochondria, leading to the disruption of cellular respiration and energy production.
3
Potassium cyanide kcn by Merck Group
Sourced in United States, Germany
Potassium cyanide (KCN) is a chemical compound that is commonly used as a laboratory reagent. It is a white, crystalline solid that is highly soluble in water. Potassium cyanide is used in various analytical and synthetic procedures in research and development laboratories.
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Antimycin A is a chemical compound that acts as a potent inhibitor of mitochondrial respiration. It functions by blocking the electron transport chain, specifically by interfering with the activity of the cytochrome bc1 complex. This disruption in the respiratory process leads to the inhibition of cellular respiration and energy production within cells.
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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.
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Formic acid is a colorless, pungent-smelling liquid chemical compound. It is the simplest carboxylic acid, with the chemical formula HCOOH. Formic acid is widely used in various industrial and laboratory applications.
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Hydrochloric acid (hcl) 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.
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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.

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