Matrix-Assisted Laser Desorption Ionization-Mass Spectrometry (MALDI-MS) spectra were obtained either on an UltraflXtreme apparatus (BrukerDaltonics, Bremen, Germany) operating in positive linear mode with delayed extraction or on a MicroflexII apparatus (BrukerDaltonics, Bremen DE) in positive reflectron mode. The samples were co-crystallized with a 10 mg/mL solution of hydroxy α-cyano-4-cinnamic acid (HCCA) on the MALDI-MS target by the dry droplet method. MALDI-MS spectra were acquired with an accelerating potential of 20 KV and a laser power set to the minimum level necessary to obtain an efficient signal. Spectrum mass calibration was based on external calibration using an appropriate peptide standard mixture (Peptide Calibration Standard, BrükerDaltonics).
Microflex 2
Manufactured by Bruker
Sourced in Germany
The Microflex II is a matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometer designed for the rapid identification and characterization of microorganisms. It utilizes a high-performance laser and advanced detection technology to generate accurate mass spectra for microbial samples.
Automatically generated - may contain errors
Lab products found in correlation
3 protocols using microflex 2
1
MALDI-MS Spectral Acquisition Protocol
2
MALDI-ToF Analysis of Unlabeled and MTSL-Labeled UreG
Check if the same lab product or an alternative is used in the 5 most similar protocols
Determination of Global Mass of unlabeled and labeled UreG. Mass analysis (MALDI-ToF) was performed to confirm the labeling (theoretical mass increment resulting for one MTSL grafted on the protein is of 184.2 Da).
Samples of ~70 pmol of UreG (unlabeled) and UreGMTSL (labeled) were prepared by dilution in 10 µL of 0,1% of trifluoro-acetic acid (TFA) in water (v/v) before being spotted onto a MALDI target plate (1 µL). A saturated solution of sinapinic acid matrix (1 µL) in 40% acetonitrile/water, 0,1% TFA (v/v) was added. The global mass was measured on a MALDI-ToF mass spectrometer Microflex II from Bruker Daltonics in the range of 2000 to 55000 Da in a positive linear mode. External mass calibration was performed using the signals of trypsinogen and protein A from the Protein standard II (Bruker Daltonics). The error on the measurement is of + /− 5 Da.
+ Expand
Determination of Global Mass of unlabeled and labeled UreG. Mass analysis (MALDI-ToF) was performed to confirm the labeling (theoretical mass increment resulting for one MTSL grafted on the protein is of 184.2 Da).
Samples of ~70 pmol of UreG (unlabeled) and UreGMTSL (labeled) were prepared by dilution in 10 µL of 0,1% of trifluoro-acetic acid (TFA) in water (v/v) before being spotted onto a MALDI target plate (1 µL). A saturated solution of sinapinic acid matrix (1 µL) in 40% acetonitrile/water, 0,1% TFA (v/v) was added. The global mass was measured on a MALDI-ToF mass spectrometer Microflex II from Bruker Daltonics in the range of 2000 to 55000 Da in a positive linear mode. External mass calibration was performed using the signals of trypsinogen and protein A from the Protein standard II (Bruker Daltonics). The error on the measurement is of + /− 5 Da.
3
MALDI-TOF mass spectrometry of proteins
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
Global molecular mass of Sm-PLVG, rPLA 2 (-5), rPLA 2 (+5) and Long chain was determined by by matrix-assisted laser desorption ionization time-of-flight (MALDI ToF) mass spectrometry using a Microflex II instrument (Bruker Daltonics,Bremen, Germany) in a positive linear mode. Range was set from 3600 to 40,000 Da and pulse ion extraction was set to 160 ns. External mass calibration was done just before the acquisition of samples using protein calibration standard I (Bruker Daltonics, Germany). A saturated solution of α-Cyano-4-hydroxycinnamic acid (HCCA) in 70% acetonitrile/30% water 0.1% TFA was used as matrix. Deposits were made onto a MALDI Target plate according to a dried droplet method and each dried spot was then desalted three times by adding, and removing immediately after, 1.5 µl of 0.1% TFA/water followed by a supplementary addition of matrix.
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
Revolutionizing how scientists
search and build protocols!