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M 106

M 106 is a spiral galaxy located in the constellation Ursa Major.
It is one of the largest and brightest galaxies in the night sky, visible to the naked eye under dark skies.
M 106 is classified as a Seyfert galaxy, meaning it has an active galactic nucleus powered by a supermassive black hole.
Astronomers have studied M 106 extensively to understand the role of active galactic nuclei in galaxy evolution and the growth of black holes.
The galaxy's distinctive spiral arms and bright core make it a fascinating object for amateur and professional astronomers alike to observe and explore.

Most cited protocols related to «M 106»

LC-MS instrumentation consisted of a breadboard Evosep One coupled to an LTQ Orbitrap for the more than 2000 HeLa injection experiment, and the Evosep One production version coupled to an Q Exactive HF-X Orbitrap (Thermo Fisher Scientific) for all other experiments. Purified peptides were separated on the HPLC columns with 3 μm Reprosil-Pur C18 beads (Dr. Maisch, Ammerbuch, Germany) and dimensions indicated below in Fig. 6B. On the LTQ Orbitrap MS, data were acquired with a Top6 data dependent shotgun method and with a Top12 method for the Q Exactive HF-X instrument. On the Q Exactive HF-X Orbitrap, the target value for the full scan MS spectra was 3 × 106 charges in the 300–1650 m/z range with a maximum injection time of 50 ms and a resolution of 60,000 at m/z 200. Fragmentation of precursor ions was performed by higher-energy C-trap dissociation (HCD) with a normalized collision energy of 27 eV (24 (link)). MS/MS scans were performed at a resolution of 15,000 at m/z 200 with an ion target value of 5 × 104 and a maximum injection time of 25 ms. Dynamic exclusion was set to 15 s to avoid repeated sequencing of identical peptides.
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Publication 2018
HeLa Cells High-Performance Liquid Chromatographies M-200 M 106 Peptides Radionuclide Imaging Reprosil Tandem Mass Spectrometry Z-200
Twenty 3-4-month-old wild boar piglets were bought in a commercial farm known to be free of mycobacterial lesions at slaughter and with a fully negative ELISA test [35] (link). The animals were housed in class III bio-containment facilities where they had ad libitum food and water. Wild boar piglets were randomly assigned to one of four treatment groups: Group 1, unvaccinated controls; Group 2, parenterally vaccinated with heat-inactivated M. bovis; Group 3, orally vaccinated with heat-inactivated M. bovis; Group 4, orally vaccinated with live BCG. Oral vaccines were delivered in baits designed for wild boar piglets [36] (link). For the challenge, 5 ml of a suspension containing 106 colony forming units (cfu) of an M. bovis field strain were administered by the oropharyngeal route as described in previous experiments [17] (link), [37] (link).
The animals were handled nine times during the experiment, including the vaccination (T1, day 1), the challenge two months after vaccination (T2, day 60), and the necropsy four months after challenge and six months after vaccination (T3, day 189). In addition to T1, T2 and T3, blood samples were taken at days 8, 21, and 49 post-vaccination (p.v), and after challenge at days 74, 83, 104 and 133 p.v.
Handling procedures and sampling frequency were designed to reduce stress and health risks for subjects, according to European (86/609) and Spanish laws (R.D. 223/1988, R.D. 1021/2005). The protocol was approved by the Committee on the Ethics of Animal Experiments of the Regional Agriculture Authority (Diputación Foral de Vizcaya, Permit Number: 2731-2009).
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Publication 2011
Animals Autopsy BLOOD Enzyme-Linked Immunosorbent Assay Europeans Food Hispanic or Latino M 106 Mycobacterium Oropharynxs Strains Sus scrofa Vaccination Vaccines
IgG1 or λ1 antibody specific for the NP hapten was detected by ELISA using two different coupling ratios of NP–BSA as the coating antigens. In brief, 96-well flat bottom plates (Falcon; Becton Dickinson, Oxnard, CA) were coated with 50 μg/ml NP5–BSA or NP26– BSA in 0.1 M carbonate buffer (pH 9.0) at 4°C overnight, and blocked with 0.5% BSA in carbonate buffer. Serially diluted sera were then added to each well and incubated at 4°C overnight. On each plate, serially diluted H33Lγ1/λ1, a monoclonal antibody recognizing the NP hapten (Ka = 2.0 × 107 M−1)2 was also included as a control. After washing with PBS containing 0.1% Tween 20, HRP-conjugated goat anti–mouse IgG1 or biotinylated Ls136 was added and incubated at room temperature for 2 h. HRP-conjugated streptavidin was added to detect biotinylated Ls136; HRP activity was visualized using a TMB peroxidase substrate kit (Bio-Rad Laboratories, Hercules, CA) and optical densities were determined at 450 nm. The concentrations of anti-NP IgG1 or λ1 antibodies were estimated by comparison to standard curves created from the H33Lγ1/λ1 control on each plate. To estimate the affinity of NP-binding antibody in the sera, the ratio of NP5-binding antibody to NP26-binding antibody was calculated (43 (link)).
The affinity threshold of antibody binding to each NP–BSA conjugate was determined by using several monoclonal antibodies with different affinities for NP. H33Lγ1/λ1 bound equally well to both NP–BSA conjugates, whereas a monoclonal antibody with a Ka = 106 M−1 showed a 20-fold lower binding to NP5–BSA than to NP26–BSA. A monoclonal antibody with a Ka = 2.3 × 105 M−1 had a 10-fold lower binding to NP26–BSA than one with a Ka = 1.0 × 106 M−1. Thus, antibody with a Ka ⩾2.0 × 107 M−1 can be detected with NP5–BSA, and one with a Ka ⩾106 M−1 can be detected with NP26–BSA.
Publication 1998
4-hydroxy-5-nitrophenyl acetic acid Antibodies Antibody Affinity Antibody Specificity Antigens Buffers Carbonates Enzyme-Linked Immunosorbent Assay Goat IgG1 Immunoglobulins KA-107 M 106 Mice, House Monoclonal Antibodies Peroxidase Serum Streptavidin Tween 20 Vision

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Publication 2011
Actins Anti-Antibodies Antibodies Antibodies, Anti-Idiotypic Biological Assay CD29 Antigen Collagen Type I CTTN protein, human Esters Flow Cytometry GAPDH protein, human Gifts Goat Homo sapiens IgG1 Immunoglobulin Isotypes Integrins lysosomal-associated membrane protein 1, human LysoTracker M 106 Molecular Probes Monoclonal Antibodies Mus Plasma Protoplasm RAB8A protein, human Rabbits sulfosuccinimidyl 6-(biotinamido)hexanoate Synaptotagmin VII Western Blot
Immunoprecipitated STAT3 from total liver lysates or BMMs was subjected to SDS-PAGE. The bands corresponding to STAT3 were excised, and the proteins were reduced, alkylated, and in-gel digested with trypsin. The peptides were extracted, lyophilized, resuspended in 2%ACN/0.1% formic acid, and analyzed by LC-MS/MS using a nanoAcquity (Waters Corp.) coupled to an LTQ Orbitrap Velos (Thermo Fisher Scientific). Samples were injected onto an in-house packed C18AQ (Michrom Biosciences) trap column (100 µm internal diameter × 2 cm, 5 µm particle size) and were washed with 1% ACN/0.1% formic acid for 20 min at 2 µl/min, then loaded onto an analytical column (C18AQ, 100 µm internal diameter × 22 cm, 5 µm particle size). The linear gradient for separation consisted of 5–36% mobile phase B over 120 min at a 250-nl/min flow rate, where mobile phase A was 0.1% formic acid in water and mobile phase B was 0.1% formic acid in ACN. The LTQ Orbitrap Velos was operated in data-dependent mode: the 10 most intense precursors were selected for subsequent collision-induced dissociation (CID) fragmentation. Resolution for the precursor scan (m/z 300–2,000) was set to 60,000 at m/z 400 with a target value of 106 ions. The MS/MS scans were acquired in the linear ion trap with a target value of 1,000. The normalized collision energy was set to 35% for CID. Precursors with unknown charge or a charge state of 1 and 4 or higher were excluded. Raw data files were processed using Proteome Discoverer version 2.0 (Thermo Fisher Scientific). Peak lists were searched against a Homo sapiens Uniprot database using Sequest. The following parameters were used to identify tryptic peptides for protein identification: 10 ppm precursor ion mass tolerance; 0.6 D product ion mass tolerance; up to two missed trypsin cleavage sites; carbamidomethylation of Cys set as a fixed modification; and hexNAc (+203.0794 D) of N/S/T, oxidation of M, and phosphorylation of S/T/Y set as variable modifications. The Percolator node was used to determine false discovery rates (FDRs), and a peptide FDR of 5% were used to filter all results.
Publication 2017
Cytokinesis formic acid Homo sapiens Immune Tolerance Liver M 106 Peptides Phosphorylation Proteins Proteome Radionuclide Imaging SDS-PAGE STAT3 protein, human Tandem Mass Spectrometry Trypsin Z 300

Most recents protocols related to «M 106»

The experiments were conducted as the methods described in our prior studies5 (link),16 (link),17 (link). The period when the distant primary tumor grew was deemed the pre-metastatic phase. The metastatic phase was defined as the period after the intravenous (i.v.) injection of tumor cells into tumor-bearing mice. Synergistic tumor grafts were generated through subcutaneous (s.c.) or mammary fat pad (m.f.p.) implantation of 5 × 106 tumor cells into 8 to 10-week-old mice. We injected tumor cells into mice with growing primary tumors of the same size (size-matched). For the tumor cell homing assays, 1–2 × 104 fluorescent dye (PKH26, Sigma-Aldrich, St. Louis, MO, USA)-labeled metastatic cells were i.v. infused into the mice. At 24–48 h after tumor cell infusion, the lungs were perfused with phosphate-buffered saline (PBS) under physiological pressure to remove circulating tumor cells and then excised. Four to five randomly selected lung tissue fragments (3 mm in diameter) were chosen, and three 10 μm sections per fragment were evaluated using a confocal microscope (SP8 Leica, LSM-710, Carl Zeiss MicroImaging GmbH, Germany) or a fluorescence microscope (BZ-9000, Keyence, Osaka, Japan). The labeled tumor cell counts were normalized to the total tissue surface area. Age- and sex-matched mice were used for the experiments.
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Publication 2023
Biological Assay Breast Cells Circulating Neoplastic Cells Fluorescent Dyes Grafts Lung M 106 Microscopy, Confocal Microscopy, Fluorescence Mus Neoplasms Ovum Implantation Pad, Fat Phosphates physiology PKH 26 Pressure Saline Solution Tissues
We provide an analytical model to show that disassembling an assembly pair using a large external magnet is very unlikely. We first consider a simple case, and then we generalize the case for more complex configurations.
In the simple case, we fix one NdFeB assembly magnet (1.2 × 1 × 0.5 mm) where its center position is at the origin of the Cartesian coordinate system (x = y = z = 0). Its dipole position points toward the positive x direction ( x1=[0, 0, 0]T with magnetic dipole moment m1=[m1,0, 0]T ). Now, we consider placing a dipole magnet on the left in the x coordinate (position: x2=[L,0, 0]T , with magnetic dipole moment m2=[m2,0, 0]T ), as shown in Supplementary Fig. 7a.
The magnetic force between the two dipole magnets is: Fm1m2=3μ04πr4r^×m1×m2+r^×m2×m12r^m1m2+5r^[(r^×m1)(r^×m2)] where μ0 is the magnetic permeability in a vacuum and r is the relative position vector between the centers of the two dipole moments m1 and m2 . r=x1x2=[L,0,0]T
After plugging in all the relevant values, the force between two magnets can be expressed as Fm1m2=3μ04πr4m1m2100
Now let us consider that there are two magnets with opposite dipole directions, as shown in Supplementary Fig. 7b. In this case, two magnets ( m2 and m3 ) generate opposite force directions on magnet m1 . We would like to use this case to find the scaling effect of magnet m3 that can destabilize the assembly pair m1 and m2 .
If we consider both m1 and m2 to be NdFeB assembly magnets (1.2 × 1 × 0.5 mm), then we consider the third magnet with an opposite dipole direction with magnetic moment m3=[m3,0, 0]T , which provides a repulsion force. If we consider that m3 is sufficiently large that the force can balance the attraction force for m2 , it needs to be balanced; as a result: Fm1m2+Fm1m3=0 3μ04πL4m1m23μ04πD4m1m3=0
The required m3 needs to be large as m3=D4L4m2 at position x3=[D,0, 0]T to balance the magnetic force generated by m2 . Now, if we assume that m3 is a cube magnet with an edge size of a, we can rewrite the equation as MNdFeBa3=D4L4m2 where MNdFeB is the magnetization of the NdFeB magnet, which is equal to 1.08×106  A m^(-1). If we now consider D as a variable and consider how a needs to scale with D, we will find a=m2MNdFeBL43D43
It shows that with an increasing distance D, the third magnet needs to increase rapidly in size ( ~D43 ) to match the force. This means that the magnet needs to be larger than a to destabilize the assembly pair between m1 and m2 . If the m2 magnet is touching m1 , as in the assembly pair, the required size of m3 can be so large that it is physically impossible to fit on the left side. If one changes the m3 direction, it will only decrease the magnetic repulsion force. The above scaling law provides an important insight that the magnetic gradient generated by a nearby permanent magnet is very unlikely to destabilize the magnetic assembly pair. The analysis results also resonate with our experimental observations. Therefore, we can conclude that the assembly will be stable in our envisioned applications regardless of the neighboring NdFeB magnet configurations.
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Publication 2023
Cloning Vectors Disgust Genitalia M 106 Permeability Vacuum
All peptide samples were measured in a single-shot manner in a Q-Exactive HF-X hybrid quadrupole-orbitrap mass spectrometer (Thermo Fisher Scientific) after peptide separation by high-performance liquid chromatography (nanoLC 1200, Thermo Fisher Scientific) using a 50 cm reversed-phase column (made in house, packed with 1.9 µm C18 ReproSil particles). Peptides were eluted over a 90-minute-gradient from 0% to 95% buffer B (0.1% formic acid and 80% ACN) with a flow rate of 300 nL/minute.
Full scans were obtained from 300 to 1650 m/z with a target value of 3 × 106 ions at a resolution of 60,000 at 200 m/z. The fifteen most intense ions (Top15) of each full scan were fragmented with higher-energy collisional dissociation (HCD) (target value 1 × 105 ions, maximum injection time 120 ms, isolation window 1.4 m/z, underfill ratio 1%), and fragments were detected in the Orbitrap mass analyzer at a resolution of 15,000 at 200 m/z.
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Publication 2023
Buffers formic acid High-Performance Liquid Chromatographies Hybrids Ions isolation M 106 Peptides Radionuclide Imaging Reprosil
Protein quantification was done using an A280 extinction coefficient of 106,660 M−1cm−1 for BAP1/ASXL1 complex on a Nanodrop spectrophotometer (Thermo-Fisher).
Publication Preprint 2023
Extinction, Psychological M 106 Proteins
The resonance method, also known as the Impact-Echo method, is an acoustic nondestructive method based on the principle of introducing a mechanical shock to the test body and recording the response of the test body to this excitation pulse. It is a common nondestructive method used in defectoscopy in various technical fields. Its particular variant, IE, is adapted for testing building materials, elements, and structures. Mechanical waves can propagate in three forms:

longitudinal waves (P-wave),

item transverse (shear) waves (S-wave), and

surface waves Raigley waves (R-wave).

These waves move through the material at a speed depending on the acoustic impedance Z of the material being measured. If the wave hits the interface of materials with different acoustic impedance, the mechanical energy of the wave is reflected, refracted, or absorbed. For an example, air has an acoustic impedance of 1.275 kg · m 2· s 1 , whereas concrete has an acoustic impedance equal to 10.35×106 kg · m 2· s 1 . This phenomenon is described by Snell’s law [25 (link)]. Due to this phenomenon, mechanical waves are reflected at the interface between the cement composite and the air cavity or surrounding environment. At the same time, mechanical waves interfacing with cracks, steel, and other materials that may be embedded in the concrete mass are affected. As a result, the incidental mechanical wave on the piezoceramic sensor has complex characteristics. The procedure of testing by IE method is illustrated in Figure 3.
The standard process for evaluating this waveform consists of applying a fast Fourier transform (FFT) and converting the measured signal from the time domain to the frequency domain. Then the dominant frequencies that can be assigned to the expected shape frequency are evaluated. In addition to these parameters, however, many other parameters can be assessed on the frequency spectrum that are no longer covered by the standard NDT approach within the IE method. Therefore, the aim of this paper is to verify whether the use of even nonstandard parameters obtained from measured acoustic signals can improve the accuracy in the classification of thermally degraded plain concrete test bodies.
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Publication 2023
Acoustics Dental Caries Dental Cements ECHO protocol Human Body M 106 Pulse Rate Shock Steel Vibration

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More about "M 106"

M 106, also known as the Canes Venatici Galaxy, is a prominent spiral galaxy located within the Ursa Major constellation.
It is one of the largest and most luminous galaxies visible to the naked eye, particularly under dark skies.
This Seyfert galaxy, characterized by an active galactic nucleus powered by a supermassive black hole, has been extensively studied by astronomers to further understand the role of these central engines in the evolution of galaxies and the growth of black holes.
The distinctive spiral arms and bright core of M 106 make it a fascinating object of interest for both amateur and professional astronomers alike.
Researchers have utilized advanced scientific instrumentation, such as the NanoAcquity UPLC system, LTQ Orbitrap XL, Guava easyCyte, and COMSOL Multiphysics Simulation Software, Version 5.1, to conduct in-depth analyses and gain a deeper understanding of this celestial object.
In addition to its visual appeal, M 106 has also been the subject of interdisciplinary research, with scientists employing techniques like mass spectrometry using the EASY-nLC 1200 system and Orbitrap Fusion Lumos mass spectrometer, as well as spectrophotometry with the NanoDrop 2000 spectrophotometer and the UltiMate 3000 RSLCnano system, to study the galaxy's composition, structure, and dynamics.
The insights gained from these studies have contributed to our overall knowledge of galaxy formation, evolution, and the role of supermassive black holes in shaping the Universe.
Whether you're an amateur stargazer, a professional astronomer, or simply fascinated by the mysteries of the cosmos, M 106 remains a captivating and well-studied object that continues to reveal the complexities and wonders of our galactic neighborhood.
With the help of advanced analytical tools and software, such as Analyst version 1.4.2, researchers can delve deeper into the secrets of this spiral galaxy and unravel the broader implications for our understanding of the universe.