The largest database of trusted experimental protocols

Expressionl cms mass spectrometer

Manufactured by Advion
Sourced in United Kingdom

The ExpressionL CMS mass spectrometer is a laboratory instrument that uses mass spectrometry technology to analyze and identify chemical compounds. It is designed to provide accurate and reliable mass measurements of various molecules.

Automatically generated - may contain errors

9 protocols using expressionl cms mass spectrometer

1

Synthesis and Characterization of Copper(II) Complex

Check if the same lab product or an alternative is used in the 5 most similar protocols
[Cu(tmpa)(MeCN)](OTf)2 was afforded
as reported.28 (link) 4-((tButyldimethylsilyl)oxy)butan-1-ol was obtained from Santa
Cruz Biotechnology and used as received. All other chemicals and solvents
were purchased from Merck or VWR and were used as received as well.
Deoxygenated and anhydrous solvents were obtained from a PureSolv
PS-MD-5 solvent dispenser (Innovative Technology). Column chromatography
was performed on alumina (Al2O3, activated,
basic, Brockmann I, 58 Å pore size, pH 9.5 ± 0.5) . Thin
layer chromatography (TLC) was performed using TLC plates from  Machery-Nagel
(Alugram Aloz, Al2O3, with F254 indicator
on aluminum backing, pH 9). Compounds were visualized on TLC plates
by UV detection at 254 nm. 1H, COSY, 13C APT,
HSQC, and HMBC NMR spectra were recorded on a Bruker 400 MHz (100.6
MHz for 13C) NMR spectrometer using the residual solvent
as internal standard. Mass spectra were obtained by high resolution
mass spectrometry (HRMS) using a TOF Synapt G2-Si mass spectrometer
equipped with an electrospray ionization source in positive ion mode
with leu-enkephalin (m/z = 556.2771)
as an internal lock mass. TLC/mass spectrometry (TLC/MS) analysis
was performed on an Advion Plate Express TLC Plate Reader connected
to an Advion expressionL CMS mass spectrometer.
+ Open protocol
+ Expand
2

Characterization of CCK-2R Compounds

Check if the same lab product or an alternative is used in the 5 most similar protocols
Characterisation of all CCK-2R-targeted compounds is provided in the Supplementary Materials (Figures S1–S4). Electrospray ionisation-mass spectra for characterisation of the substances were acquired on an expressionL CMS mass spectrometer (Advion Ltd., Harlow, UK).
+ Open protocol
+ Expand
3

Peptide Identity and Integrity Analysis

Check if the same lab product or an alternative is used in the 5 most similar protocols
Evaluation of peptide identity and integrity is provided in the Additional file 1 (Fig. S1–S12). An expressionL CMS mass spectrometer (Advion Ltd., Harlow, UK) was used for characterization of the substances.
+ Open protocol
+ Expand
4

Characterization of CCK-2R Compounds

Check if the same lab product or an alternative is used in the 5 most similar protocols
Characterization of all CCK-2R-targeted compounds is provided in the Supplementary Materials (Figures S1–S17). Electrospray ionization mass spectrometry for characterization of the substances were acquired on an expressionL CMS mass spectrometer (Advion Ltd., Harlow, UK).
+ Open protocol
+ Expand
5

CCK-2R Compound Characterization

Check if the same lab product or an alternative is used in the 5 most similar protocols
Characterization of all CCK-2R-targeted compounds is provided in the Additional file 1: (Fig. S1–S17). Electrospray ionization-mass spectra for characterization of the substances were acquired on an expressionL CMS mass spectrometer (Advion Ltd., Harlow, UK).
+ Open protocol
+ Expand
6

Structural and Electrochemical Characterization

Check if the same lab product or an alternative is used in the 5 most similar protocols
31P NMR spectra were recorded at ambient temperature using a Bruker Avance DPX-400 MHz instrument. All the 1H NMR spectra were recorded at ambient temperature using either Bruker Avance DPX-400 or Bruker Avance DPX-500 MHz instruments. Mass analyses were performed with an Advion ExpressionL CMS mass spectrometer using APCI+ mode. Elemental analyses were performed by the Midwest Microlab, LLC, in Indianapolis, IN. X-ray crystallography data of complexes 3 and 5 were collected at the X-ray Structural Laboratory at Marquette University (Milwaukee, WI) using a SuperNova, Dual, Cu at home/near, Atlas diffractometer [Cu Kα (λ = 1.54184)] at 100.15 K. The structure was solved with the Olex2 structure solution program using Charge Flipping and refined with the ShelXL refinement package using Least Squares minimization. Electrochemical data of both 3 and 5 (approximately 1 mmol in THF) were collected in a classic three-electrode system: a Pt working electrode, a Pt counter electrode, and a Ag/Ag+ reference electrode, using a WaveNow USB Potentiostat from Pine Research Instrumentation.
+ Open protocol
+ Expand
7

Synthesis and Characterization of Air-Sensitive Compounds

Check if the same lab product or an alternative is used in the 5 most similar protocols
All operations were conducted under a dry argon atmosphere by using standard Schlenk and glovebox techniques. Solvents were dried rigorously and degassed before use. Me3P=CH2,24iBu2BCl,25 and LiP(tBu)226 were synthesized according to procedures reported in the literature. The chemical shifts are expressed in ppm and 1H and 13C signals are given relative to tetramethylsilane (TMS). Coupling constants (J) are given in Hertz as positive values, regardless of their real individual signs. The multiplicity of the signals is indicated as s, d, q, sept, or m for singlet, doublet, quartet, septet, or multiplet, respectively. The assignments were confirmed, as necessary, with the use of 2D NMR correlation experiments. MS measurements were performed on an Advion expressionL CMS mass spectrometer under atomic pressure chemical ionization (APCI). IR spectra were measured with a Bruker Alpha spectrometer by using the attenuated total reflection (ATR) technique on powdered samples, and the data are quoted in wavenumbers (cm−1). The intensity of the absorption band is indicated as vw (very weak), w (weak), m (medium), s (strong), vs (very strong), and br (broad). Melting points were measured with a Thermo Fischer melting point apparatus and are not corrected. Elemental analyses were carried out in the institutional technical laboratories of the Karlsruhe Institute of Technology (KIT).
+ Open protocol
+ Expand
8

HPLC Purification and Analysis of Proteins

Check if the same lab product or an alternative is used in the 5 most similar protocols
Reversed-phase HPLC purifications and analyses were performed on a Dionex Ultimate 3000 HPLC system. Specific columns, mobile phases, and gradient details are described in the appropriate sections below or in Supporting Information. For LC-ESI-MS analyses, the Dionex Ultimate 3000 HPLC was interfaced with an Advion CMS expressionL mass spectrometer. LC-ESI-MS data were analyzed using Advion Data Express software, and protein charge ladders were deconvoluted using a maximum-entropy algorithm provided by Analyst 1.4.2 software.
Desalting of protein solutions and immobilized metal affinity chromatography (IMAC) utilizing an imidazole gradient were carried out on an NGC Quest™ 10 Plus FPLC system (Bio-Rad) equipped with a 10 mL Bio-Scale™ Mini Bio-Gel® P-6 Desalting Cartridge or a 5 mL Bio-Scale™ Mini Nuvia™ IMAC Ni-Charged column. Additional details on mobile phase conditions, flow rates, and gradients are provided in the appropriate sections below.
UV-Vis measurements for estimating the concentration of protein and peptide solutions were obtained using either a Nanodrop ND-1000 spectrophotometer (ThermoFisher) or a Biotek® Epoch™ Microplate Spectrophotometer.
Imaging of SDS-PAGE gels stained with Coomassie Brilliant Blue R-250 was performed using a Gel Doc™ EZ imager (Bio-Rad).
Water used in all experimental procedures was purified using a Milli-Q Advantage A10 system (Millipore).
+ Open protocol
+ Expand
9

Sortase-Mediated Peptide Conjugation Assay

Check if the same lab product or an alternative is used in the 5 most similar protocols
LPATS/LPATA/LPAT-LII peptide substrates (50 μM), alanine amide nucleophile (5 mM), and wildtype spySrtA enzyme (5 μM in the reaction with LPATS, otherwise 1 μM) were combined at room temperature and incubated for the times indicated. All reactions contained 10% (v/v) sortase reaction buffer (500 mM Tris [pH 7.5] and 1500 mM NaCl) as well as ≤1.1% (v/v) residual dimethyl sulfoxide from the peptide substrate stock solutions. Reactions were analyzed using a Dionex Ultimate 3000 HPLC system interfaced with an Advion CMS expressionL mass spectrometer. Separations were achieved with a Phenomenex Kinetix 2.6 μM C18 100 Å column (100 × 2.1 mm) (aqueous [95% H2O, 5% MeCN, 0.1% formic acid]/MeCN [0.1% formic acid] mobile phase at 0.3 ml/min, gradients adjusted for each substrate to achieve separation between relevant reaction components).
+ Open protocol
+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Sign up for free.
Registration takes 20 seconds.
Available from any computer
No download required

Sign up now

Revolutionizing how scientists
search and build protocols!