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Rhenium

Most cited protocols related to «Rhenium»

Probe library constructions, hybridization procedures and imaging conditions were previously described53 (link),54 (link). SmFISH probe libraries (Supplementary Data 8) were coupled to Cy5 or Alexa594. Endothelial cells were detected by Aqp1 staining. To detect cell borders alexa fluor 488 conjugated phalloidin (Rhenium A12379) was added to the GLOX buffer wash54 (link). Portal nodes were identified morphologically using the DAPI channel based on bile ductile, central vein was identified using smFISH for Glul in TMR, included in all hybridizations. For zonation validation profiles, images were taken as scans extending from the portal node to the central vein. Endothelial cells were classified into 7 layers as follows: cells that were in contact with Glul+ cells and that lined the central vein were classified as layer 1, cells that were in contact with Glul+ cells but resided in the sinusoidal channels were classified as layer 2, cells that surrounded the portal vessels at a distance of up to 1 hepatocyte were classified as layer 6, cells that lined the inside of the vessels in the portal node were classified as layer 7, sinusoidal cells in the mid-lobule area were assigned layers 3-5 using equal distances from layer 2 to layer 6. To validate the predicted zonation we selected 15 genes that were significantly zonated and had an average expression in the scRNAseq data of LECs of more than 10^-4 of the cellular UMIs - Rspo3, Cdh13, Thbd, Wnt2, Kit, Bmp2, Bmp4, Ccnd1, Lyve1, Stab1, Dll4, Zeb2, Efnb2, Ltbp4 and Klf4. smFISH did not yield a signal for Bmp4, Zeb2 and Klf4, whereas the remaining 12 genes are presented in Figure 4c. The results in Figure 4c were based on at least 30 cells from each layer and from 2 mice. Quantification of smFISH data was done using ImageM54 (link). Dots were counted in the first 5μm of the Z-stack, and divided by the segmented cell volume to obtain the mRNA concentration per cell.

Halpern K.B., Shenhav R., Massalha H., Toth B., Egozi A., Massasa E.E., Medgalia C., David E., Giladi A., Moor A.E., Porat Z., Amit I, & Itzkovitz S. (2018). Paired-cell sequencing enables spatial gene expression mapping of liver endothelial cells. Nature biotechnology, 36(10), 962-970.

Publication 2018

Acid Hybridizations, Nucleic Alexa594 alexa fluor 488 AQP1 protein, human Bile Blood Vessel BMP2 protein, human Bone Morphogenetic Protein 4 Buffers CCND1 protein, human CDH13 protein, human cDNA Library DAPI Endothelial Cells Genes Hepatocyte KLF4 protein, human Mus Phalloidine Radionuclide Imaging Rhenium RNA, Messenger Single-Cell RNA-Seq Sinusoidal Beds Veins WNT2 protein, human

Spatial Transcriptomics of Liver Zonation

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Publication 2015

Acid Hybridizations, Nucleic alexa fluor 488 Buffers cDNA Library Cells DAPI Duct, Bile Hepatocyte Phalloidine Polyploidy Rhenium Stem, Plant Tetraploidy Veins

Ribonucleotide Reductase Enzyme Assay

Wt-α₂ (2000 nmol/mg/min)
was expressed from pET28a-nrdA and purified as previously
described.^{35 (link)} Glycerol stocks of Y₇₃₁F-α₂ and C₄₃₉S-α₂ were
available from a previous study^{28 (link)} and were
expressed and purified as wt-α₂. All α₂ proteins were prereduced prior to use.^{21 (link)} [5-³H]-cytidine 5′-diphosphate sodium
salt hydrate ([5-³H]-CDP) was purchased from ViTrax (Placentia,
CA). 3′-Deuterated cytidine 5′-diphosphate ([3′-²H]-CDP) was available from a previous study,³⁶ in which it was synthesized as reported.^{22 (link),23 (link)} Tricarbonyl(1,10-phenanthroline)(4-bromomethyl-pyridine)rhenium(I)
hexafluorophosphate ([Re^I]-Br) was available
from a previous study.^{29 (link)}E. coli thioredoxin (TR, 40 μmol/min/mg) and thioredoxin reductase
(TRR, 1800 μmol/min/mg) were prepared as previously described.^{37 (link),38 (link)} 2,3,5-Trifluorotyrosine was synthesized enzymatically from pyruvate,
ammonia, and 2,3,6-trifluorophenol with tyrosine phenol lyase as the
catalyst.^{39 (link)} Assay buffer consists of 50
mM HEPES, 15 mM MgSO₄, and 1 mM EDTA adjusted to the specified
pH.

Olshansky L., Pizano A.A., Wei Y., Stubbe J, & Nocera D.G. (2014). Kinetics of Hydrogen Atom Abstraction from Substrate by an Active Site Thiyl Radical in Ribonucleotide Reductase. Journal of the American Chemical Society, 136(46), 16210-16216.

Publication 2014

Ammonia Biological Assay Buffers Cytidine Diphosphate Edetic Acid Escherichia coli Glycerin HEPES Phenanthrolines Proteins Pyridines Pyruvates Rhenium Sulfate, Magnesium Thioredoxin Reductase (NADPH) TXN protein, human Tyrosine Phenol-Lyase

Electrochemical Dissociation-Enhanced Mass Spectrometry

Mass spectrometry was performed using a modified Synapt G2-Si instrument with an electromagnetostatic ECD cell mounted between the exit of the ion mobility cell and the entrance of the transfer cell (see Figure 1). The instrument was operated in positive ion mode, and the capillary voltage was optimized between 1.75 and 2.50 kV. The cone voltage was optimized between 25 and 100 V for collision-induced unfolding experiments prior to ion mobility-ECD. The helium cell and ion mobility cell gas flows were optimized at 120 and 60 mL/min, respectively. The IM cell contained nitrogen pressurized to ∼2 mbar. The source temperature and desolvation temperature were set to 110 and 350 °C, respectively.
The ECD cell comprises seven cylindrical electrostatic lenses tuned to transmit cations and their fragments as they are generated through the interaction with a low-energy (1 eV) electron cloud. The electrons are generated from a hot rhenium loop filament coated with ytrrium oxide that the precursor ions pass through. Two of the electrostatic lens elements are samarium–cobalt alloy ring magnets and are designed to entrain the electrons to the central axis, thus enabling much greater overlap between the ions and electrons. The electrostatic voltages applied to the cell and filament current were optimized to obtain maximum transmission in non-ECD mode (normal operation) and maximum ECD fragment ion intensity in ECD mode. Different settings were required for ion mobility mode where the gas flow of N₂ from the IMS cell affected the optimum settings. The details of electrostatic potentials and filament current settings, both for ECD and the transmission of intact ions, are provided in Supporting Information S-1.
In order to physically fit the ECD cell, we replaced the standard transfer cell with a modified shorter version that was previously used to accommodate a surface-induced dissociation (SID) cell involved in a prior research project.^{32 (link)} The ECD cell was then secured onto the exit of the IMS cell. The higher-pressure region of the transfer cell was unaffected by the modification and could be used for additional collision induced dissociation if required, for example, to provide supplemental activation. Furthermore, this cell was still utilized to provide optimum collisional cooling and coupling to the orthogonal acceleration time-of-flight (TOF), thus maintaining transmission and TOF resolution.
Data analysis was performed using the recently published Masstodon software, which requires that multiple isotope peaks are observed with good mass accuracy for fragment identification.^{33 (link)} Peak assignments were then manually verified using MassLynx 4.1. Images showing the crystal structures were generated using YASARA View.^{34 (link)} Coordinate files were taken from the Protein Data Bank with accession codes 2DN2 (hemoglobin) and 4W6Z (ADH).

Williams J.P., Morrison L.J., Brown J.M., Beckman J.S., Voinov V.G, & Lermyte F. (2020). Top-Down Characterization of Denatured Proteins and Native Protein Complexes Using Electron Capture Dissociation Implemented within a Modified Ion Mobility-Mass Spectrometer. Analytical chemistry, 92(5), 3674-3681.

Publication 2020

Acceleration Alloys Capillaries Cations Cells Cytoskeletal Filaments Electrons Electrostatics Epistropheus Helium Hemoglobin Ions Isotopes Lens, Crystalline Mass Spectrometry Nitrogen Oxides Pressure Range of Motion, Articular Retinal Cone Rhenium samarium cobalt Transmission, Communicable Disease

Recombinant Expression of HIV-1 Vpu Protein

The Vpu gene (according to the sequence in [1] (link)) was cloned in the pMal-p2x commercial plasmid (New England BioLabs, Ipswich, MA) that carries a p-lac promotor and antibiotic resistance. The plasmid is designed to over express a fusion-taged maltose binding protein (MBP) on the N-terminus of the protein of interest, which in the current study is a codon optimized gene coding for Vpu of HIV-1 [43] (link). The chimera further carries a His-Tag at the C-terminus. This chimera construct was used throughout the study.
Two main strains of Escherichia coli K12 were used: DH10B and LB650. DH10B bacteria cells were purchased from Invitrogen (distributed by Rhenium, Modi'in Israel). LB650 bacteria were a kind gift of Prof. K. Jung (Ludwig-Maximilians Universität München) and Prof. G.A. Berkowitz (University of Connecticut). The bacteria carry deletions in genes connected to potassium uptake [39] .

Taube R., Alhadeff R., Assa D., Krugliak M, & Arkin I.T. (2014). Bacteria-Based Analysis of HIV-1 Vpu Channel Activity. PLoS ONE, 9(10), e105387.

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Publication 2014

Antibiotic Resistance, Microbial Bacteria Cells Chimera Codon Escherichia coli K12 Gene Deletion Genes, vpu HIV-1 Maltose-Binding Proteins Plasmids Potassium Rhenium Strains

Most recents protocols related to «Rhenium»

Quantification of LPS-specific B-Cell Response

Activation of PBMC and ELISPOT assay was performed for the measurement of IgG and IgA memory B-cell response to SF2a LPS^{62 (link),63 (link)}. PBMCs were isolated from whole blood using Ficoll-Paque PLUS (GE Healthcare) and incubated for 5 days with the activating reagents 10 ng/mL IL-2 (R&D Systems) and 1 µg/mL R848 (Invivogen) in RPMI-1640 supplemented with 10% Fetal Bovine Serum (BI inc, Rhenium). ELISPOT PVDF microtiter plates (Merck Millipore Corp.) were coated with 5 µg/mL of SF2a LPS or with Goat anti-human IgG-Fc antibody (EMD Millipore Corp.) or Goat anti-human IgA antibody (Bethyl Laborathories Inc.). Activated PBMCs were washed and added in duplicates in two concentrations (3 × 10⁵/100 µL/well and 1.5 × 10⁵/100 µL/well) to LPS coated wells. Activated PBMC at 3 × 10³/100 µL/well were serially 2-fold diluted and added to anti-IgG/IgA coated wells. Plates were incubated in a 37 °C CO₂ humidified incubator for 6 h and washed twice with PBS-Tween and twice with PBS. AP labeled anti-human IgG or anti-human IgA goat antibodies diluted 1:4000 (Bethyl Laborathories Inc.) were added to the wells and incubated ON at 4 °C. Plates were washed twice with PBS-Tween, twice with PBS, once with double distilled water (ddw) and the BCIP/NBT (Merck Millipore Corp.) substrate solution was added and incubated for 20 min. Reaction was stopped by washing twice with ddw and incubating with 200 µL/well ddw for 30 min in RT. The number of spots was counted using a stereoscope attached to a camera (SMZ800N, Nikon). Results are expressed as % LPS-specific antibody-secreting cells/total IgG or IgA secreting cells. An individual positive response after vaccination was defined as an increase in the percentage of SF2a LPS-specific-IgG and IgA secreting cells per total IgG or IgA secreting cells above a cut-off value represented by the mean of the same parameter and two Standard Deviations (SDs) calculated among all placebo recipients at each time point.

Meron-Sudai S., Asato V., Adler A., Bialik A., Goren S., Ariel-Cohen O., Reizis A., Mulard L.A., Phalipon A, & Cohen D. (2023). A Shigella flexneri 2a synthetic glycan-based vaccine induces a long-lasting immune response in adults. NPJ Vaccines, 8, 35.

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Publication 2023

anti-IgA anti-IgG Antibodies Biological Assay BLOOD Cells Enzyme-Linked Immunospot Assay Exanthema Fetal Bovine Serum Ficoll Goat Homo sapiens Immunoglobulin Fc Fragments Immunoglobulin G Immunoglobulins Memory B Cells Placebos polyvinylidene fluoride Rhenium Tweens Vaccination

Synthesis and Characterization of Rhenium Complexes

All chemicals were reagent grade and the solvents for HPLC were HPLC grade. Re₂(CO)₁₀ was converted to Re(CO)₅OTf as described in the literature [42 , 43 (link)]. Soybean lipoxygenase, sodium linoleate, DPPH, and 2,2-azobis-(2-amidinopropane) dihydrochloride (AAPH) were obtained from Sigma Chemical, Co. (St. Louis, MO, USA).
IR spectra were recorded as KBr pellets on a Spectrum BX spectrophotometer (Perkin Elmer, Waltham, MA, USA) in the region 4000–500 cm⁻¹. Elemental analysis was performed with ThermoFlash 2000 analyzer (Thermo Scientific, Waltham, MA, USA).¹H and ¹³C NMR spectra were obtained on a DD2 Agilent 500 MHz spectrometer. ESI-MS data were obtained on an MSQ Plus™ LC/ MS (Thermo Scientific, Waltham, MA, USA). Hitachi F2000 Fluorospectrometer was used for emission spectra. HPLC analyses were performed on an Agilent HP 1100 series pump (HP, Waldbronn, Germany), connected to an HP 1100 multiple wavelength photodiode array detector. RP-HPLC analyses of the rhenium complexes were performed on an Agilent Eclipse XDB C18 column (25 cm × 4.6 mm, 5 μm) by applying a binary gradient method of Solvent A: H₂O and Solvent B: methanol at a flow rate of 1 mL/min; System I: 100% of A initial composition that linearly converted to 25% A–75% B over 15 min, then to 5% A–95% B over 5 min. The composition was constant from 20 to 25 min at 95% B, before returning to initial conditions. Purification of the rhenium complexes was performed by semi-preparative HPLC on an Eclipse XDB C18 column (25 cm × 9.4 mm, 5 μm) by applying a binary gradient method of Solvent A: H₂O and Solvent B: methanol at a flow rate of 2 mL/min; System II: 50% of A initial composition that linearly converted to 25% A–75% B over 15 min, then to 5% A–95% B over 5 min. The composition was constant from 20 to 25 min at 95% B, before returning to initial conditions. System III: 60% of A initial composition that linearly converted to 25% A–75% B over 15 min, then to 5% A–95% B over 5 min. The composition was constant from 20 to 25 min at 95% B, before returning to initial conditions. The antioxidant properties of the compounds were measured on a PerkinElmer lambda 20 (PerkinElmer Inc., Waltham, MA, USA) or on a Shimadzu, UV-1700 Spectrophotometer (Shimadzu Corp, Kyoto, Japan).

Glykofridi P., Tziouri V.E., Xanthopoulos K., Vlachou M.E., Correia S., Fischer A.L., Thüne K., Hatzidimitriou A., Zerr I., Schmitz M., Sklaviadis T., Hadjipavlou-Litina D, & Papagiannopoulou D. (2023). Synthesis, structural characterization and study of antioxidant and anti-PrPSc properties of flavonoids and their rhenium(I)–tricarbonyl complexes. Journal of Biological Inorganic Chemistry, 28(2), 235-247.

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Publication 2023

2,2'-azobis(2-amidinopropane) Antioxidants Carbon-13 Magnetic Resonance Spectroscopy High-Performance Liquid Chromatographies Infrared Spectrophotometry Linoleate Lipoxygenase Methanol Pellets, Drug Rhenium Sodium Solvents Soybeans

Cytotoxicity Evaluation of Synthesized Ligands

The in vitro cytotoxicity of the synthesized ligands and their rhenium complexes was determined by the MTT method. The A431 cells were seeded in 96-well plates at a density of 4000 cells per 100 μL per well and incubated for 24 h so that they were attached to the wells. After 24 h, the studied derivatives were dissolved in DMSO (100 nM) and further diluted in D-MEM in various concentrations. The derivatives were added to the wells in final concentrations of 1 mM, 100 µM, 10 µM, 1 µM, 100 nM, and 10 nM, where the final concentration of DMSO did not exceed 1%. The six concentrations of each derivative and control existed quadrupled into the experiment. The derivatives and the cells were incubated for 72 h. After three days, the medium was removed, and the cells were incubated for 4 h in the presence of MTT (1 mg/mL 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide, Sigma, Saint Louis, MO, USA) in RPMI (PAA Laboratories GmbH, Pasching, Austria) without phenol red for 2 h at 37 °C. The MTT solution was removed, and 2-propanol was added to each well to stop the cleavage of the tetrazolium ring by dehydrogenase enzymes which convert MTT to an insoluble purple formazan in living cells. The plates were then agitated at room temperature for about 15–20 min, and the level of the colored formazan derivative was determined by measuring optical density (OD) on an ELISA reader (540/620 nm). The results, expressed as the mean of the OD of various replicates *100/OD of the control, were plotted against the corresponding compound concentration in a semi-log chart, and the IC₅₀ was determined from the dose-response curve. Cell proliferation assay was performed three times for each compound.

Makrypidi K., Kiritsis C., Roupa I., Triantopoulou S., Shegani A., Paravatou-Petsotas M., Chiotellis A., Pelecanou M., Papadopoulos M, & Pirmettis I. (2023). Evaluation of Rhenium and Technetium-99m Complexes Bearing Quinazoline Derivatives as Potential EGFR Agents. Molecules, 28(4), 1786.

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Publication 2023

Biological Assay Bromides Cell Proliferation Cells Cytokinesis Cytotoxin derivatives Enzyme-Linked Immunosorbent Assay Enzymes Formazans Isopropyl Alcohol Ligands MTT formazan Oxidoreductase Rhenium Sulfoxide, Dimethyl Tetrazolium Salts Vision

Radiolabeling of Quinazoline Derivatives

All solvents and laboratory chemicals were reagent grade and were used without further purification. The HPLC-grade solvents for high-performance liquid chromatography (HPLC) were degassed by a helium flux before and during use. IR spectra were recorded using the Brucker™ Alpha II™ FT-IR/ATR Spectrometer between 4000–400 cm⁻¹. NMR spectra were recorded on a Bruker 250 MHz or 500 MHz Avance DRX spectrometer using the residual solvent peak as a reference. HPLC analysis was performed on a Waters 600 chromatography system coupled to a Waters 2487 Dual l Absorbance detector and a Gabi gamma detector from Raytest. Separations were achieved on a Nucleosil C18 (10 mm, 250 mm × 4 mm) column eluted with a binary gradient system at a 1 mL/min flow rate. Mobile phase A was methanol containing 0.1% trifluoroacetic acid, while mobile phase B was water containing 0.1% trifluoroacetic acid. The elution gradient was 0–1 min 95% B (5% A), followed by a linear gradient to 85% A (15% B) in 8 min. This composition was held for 17 min. After a column wash with 95% A for 10 min, the column was re-equilibrated by applying the initial conditions (95% B) for 10 min prior to the next injection.
[^99mTc]NaTcO₄ was obtained in physiological saline as a commercial ⁹⁹Mo/^99mTc generator eluate (Ultra-Technekow™ V4 Generator, Curium Pharma, Petten, Netherlands). 6-Amino-4-[(3-bromophenyl)amino] quinazoline (1) [21 (link),22 (link)], N-(2-pyridylmethyl)aminoethyl acetate (PAMA) (3) [23 (link)] and the rhenium precursors ReBr(CO)₅ and fac-[Net₄]₂[ReBr₃(CO)₃] [24 (link)] as well as the radioactive precursor fac-[^99mTc][Tc(OH₂)₃(CO)₃]⁺ [25 (link)] have been synthesized according to the literature methods.

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Publication 2023

Acetate ARID1A protein, human Chromatography Curium farnesyl-protein transferase-alpha Gamma Rays Helium High-Performance Liquid Chromatographies Infrared Spectrophotometry Laboratory Chemicals Methanol physiology Quinazolines Radioactivity Rhenium Saline Solution Solvents Trifluoroacetic Acid

RNA Extraction and qRT-PCR Protocol

A half brain was placed in 1 mL Trizol reagent (15596026, Thermo Fisher, Waltham, MA, USA) and homogenized with a bullet blender homogenizer (Next Advance, Troy, NY, USA) at a maximum speed for 1 min. After solubilization, 200 µL chloroform was added to cause phase separation, where proteins are extracted to the organic phase, DNA resolves at the interface, and RNA remains in the aqueous phase. The consequent RNA phase cleaning was performed using Bio-Rad Aurum (732-6820, Bio-Rad Laboratories, Hercules, CA, USA). RNA samples purity, A₂₆₀/A₂₈₀ > 2.00, was considered acceptable for further analysis [57 (link)] (Supplementary Table S1). One microgram of total RNA was used for reverse transcription using a high-capacity cDNA reverse transcription kit (N8080119, Applied Biosystems, Rhenium, Israel). The quantitative real-time polymerase chain reaction was performed on the StepOne™ Real-Time PCR System (Applied Biosystems) using Fast SYBR Green Master (ROX) (4385612, Applied Biosystems). Hypoxanthine guanine phosphoribosyltransferase (HPRT) served as a reference gene in this analysis. A standard amplification program was used (1 cycle of 95 °C for 20 s, 40 cycles of 95 °C for 3 s, and 60 °C for 30 s). The primers used in this analysis are listed in Table 1. The results were normalized to reference gene expression within the same cDNA sample and calculated using the ΔCt method. Results are reported as fold changes relative to the control brains of sham animals and reported as mean ± SEM.

Golderman V., Goldberg Z., Gofrit S.G., Dori A., Maggio N., Chapman J., Sher I., Rotenstreich Y, & Shavit-Stein E. (2023). PARIN5, a Novel Thrombin Receptor Antagonist Modulates a Streptozotocin Mice Model for Diabetic Encephalopathy. International Journal of Molecular Sciences, 24(3), 2021.

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Publication 2023

Animals Brain Chloroform DNA, Complementary Fast Green Gene Expression Genes Hypoxanthine Phosphoribosyltransferase Oligonucleotide Primers Proteins Real-Time Polymerase Chain Reaction Reverse Transcription Rhenium trizol

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More about "Rhenium"

Rhenium (Re) is a rare, silvery-white, hard, dense, and corrosion-resistant transition metal with a high melting point.
It is commonly used in superalloys, catalysts, and electronic components due to its unique physical and chemical properties.
Rhenium research is critical for advancements in various industries, including aerospace, energy, and electronics.
PubCompare.ai is a powerful tool that helps optimize rhenium research by providing AI-driven comparisons of protocols from literature, pre-prints, and patents.
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The platform leverages advanced techniques like High-Capacity cDNA Reverse Transcription Kits, Penicillin/Streptomycin, FBS, Tissue-Tek medium, RNAlater solution, LysoTracker Green, and Silica gel 60 to enable seamless rhenium research.
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