Log In Sign up
The largest database of trusted experimental protocols

Flexanalysis

Manufactured by Bruker
Visit Supplier
Sourced in Germany, United States

FlexAnalysis is a software application developed by Bruker for the analysis of data from various analytical instruments. It provides a suite of tools for data processing, visualization, and interpretation, allowing users to efficiently analyze and interpret their experimental results.

Automatically generated - may contain errors

Lab products found in correlation

Flexcontrol, by Bruker (18 mentions) Biotools, by Bruker (7 mentions) Ultraflextreme, by Bruker (6 mentions) Flexcontrol software, by Bruker (4 mentions) Fleximaging, by Bruker (4 mentions) Autoflex speed, by Bruker (4 mentions) C18 ziptip, by Merck Group (4 mentions) Ultraflextreme mass spectrometer, by Bruker (3 mentions) Ultraflex 3, by Bruker (3 mentions) Fleximaging software, by Bruker (3 mentions) Microflex, by Bruker (3 mentions) Microflex lt mass spectrometer, by Bruker (3 mentions) Clinprotool, by Bruker (2 mentions) Proteinscape 3, by Bruker (2 mentions) Microflex lt maldi tof mass spectrometer, by Bruker (2 mentions) Proteinscape, by Bruker (2 mentions) Ultraflextreme 3, by Bruker (2 mentions) Microflex lrf, by Bruker (2 mentions) Mascot server, by Matrix Science (2 mentions) Mbt compass software, by Bruker (2 mentions)

Close spelling variants of this product

FlexAnalysis software package (2 citations) FlexAnalysis (version 3.3) software (2 citations) FlexAnalysis software v.3.3 (7 citations) FlexAnalysis 4.0 (2 citations) FlexAnalysis software (171 citations) FlexAnalysis ver. 3.0 (2 citations) Flexanalysis software (v. 3.0) (2 citations) FlexAnalysis v.3.4 (54 citations) FlexAnalysis 3.4 (233 citations) FlexAnalysis software version 3.4 (19 citations)

114 protocols using flexanalysis

1

MALDI-TOF MS Analysis of Intact Proteins

Check if the same lab product or an alternative is used in the 5 most similar protocols
The MALDI-TOF MS analyses were performed using chemicals at the highest commercially available purity supplied by Fluka Feinchemikalien (a subsidiary of Sigma-Aldrich, NeuUlm, Germany). Ground steel targets (Bruker Daltonik, Bremen, Germany) were used for sample deposition and the sinapinic acid was employed as matrix for MALDI analysis of intact proteins (dried droplet method) [28 (link)]. Protein Calibration Standards I and II (Bruker Daltoniks, Bremen, Germany) were used for external calibration. All the MS spectra were obtained using the MALDI-TOF/TOF mass spectrometer (Bruker Daltonik, Bremen, Germany) equipped with a modified neodymium-doped yttrium aluminum garnet (Nd:YAG) laser operating at the wavelength of 355 nm and frequency of 2 kHz. The system was controlled using the Bruker Daltonik software (flexControl and flexAnalysis). MS spectra of intact proteins were obtained in the linear positive mode in an m/z range of 15,000–30,000, applying an acceleration voltage of 25 kV. All mass spectra were acquired and processed using dedicated software flexControl and flexAnalysis, respectively (both from Bruker Daltonik).
Pryshchepa O., Sagandykova G.N., Pomastowski P., Railean-Plugaru V., Król A., Rogowska A., Rodzik A., Sprynskyy M, & Buszewski B. (2019). A New Approach for Spontaneous Silver Ions Immobilization onto Casein. International Journal of Molecular Sciences, 20(16), 3864.
+ Open protocol
+ Expand
2

Evaluating MALDI-TOF MS Spectra Reproducibility

Check if the same lab product or an alternative is used in the 5 most similar protocols
The reproducibility of MALDI-TOF MS spectra from mosquito specimens engorged on the same vertebrate and collected at different points in time was evaluated by comparing the average spectra obtained from the four spectra of each sample tested using the Flex analysis and ClinProTools 2.2 software (Bruker Daltonics). Specificity of MALDI-TOF MS spectra according to blood host origin was also analysed using the Flex analysis and ClinProTools 2.2 software (Bruker Daltonics). To create an MS database, reference spectra (MSP, Main Spectrum Profile) were created by combining the results of the spectra from at least three specimens per species that were either unfed or fed on the same vertebrate blood, and harvested at the same point in time by the automated function of the MALDI-Biotyper software v3.0. (Bruker Daltonics). MSP were created on the basis of an unbiased algorithm using information on the peak position, intensity and frequency.
Niare S., Berenger J.M., Dieme C., Doumbo O., Raoult D., Parola P, & Almeras L. (2016). Identification of blood meal sources in the main African malaria mosquito vector by MALDI-TOF MS. Malaria Journal, 15, 87.
+ Open protocol
+ Expand
3

MALDI-TOF Mass Spectrometric Analysis

Check if the same lab product or an alternative is used in the 5 most similar protocols
Unless otherwise indicated, each sample destined for mass spectrometric analysis was purified with a C4 ZipTip. Mass spectrometric readings were performed on incubation mixtures (0.6 μL) spotted onto stainless steel sample plates. Analysis of m/z ratios was performed on a Bruker Autoflex MALDI–TOF spectrometer (Bruker Daltonics, Billerica, MA, USA) in linear TOF mode with a 550 ns delay. All spectra represented the sum of 500 single laser shots randomized over ten positions localized on the same spot (500/50). Mass spectrometric data was evaluated with Bruker’s (Billerica, MA, USA) FlexAnalysis and ClinProTools software. For spotting purposes, protein samples were mixed in a 50% aqueous acetonitrile solution (0.6 μL) saturated with sinapinic acid and containing 0.05% TFA.
Liu W., Cohenford M.A., Frost L., Seneviratne C, & Dain J.A. (2014). Inhibitory effect of gold nanoparticles on the D-ribose glycation of bovine serum albumin. International Journal of Nanomedicine, 9, 5461-5469.
+ Open protocol
+ Expand
4

Characterization of Isolate CH-KOV3 by MALDI-TOF MS

Check if the same lab product or an alternative is used in the 5 most similar protocols
Isolate CH-KOV3 was characterized using a Bruker Autoflex II MALDI-TOF MS (Bremen, Germany) equipped with a UV nitrogen laser (337 nm) and a dual microchannel microplate detector. Together with whole (intact) bacteria, crude cell extracts were prepared accordingly [30] and also analyzed as previously described [31] . Spectra were recorded by Flex Control software (Bruker Daltonics, Bremen, Germany), and samples were analyzed in six replicates using Flex Analysis (Bruker Daltonics, Bremen, Germany). For each measurement, at least 3,000 individual spectra (300 shots at laser power from 10 different points of a dried sample spot) were collected and averaged to obtain MALDI-TOF MS spectrum. External calibration was performed with protein standards (Bruker Protein Test Standard, Bruker Daltonics, Bremen, Germany). MALDI BioTyper db 6903 software was used for the protein profile analysis by pattern matching with the libraries.
Djurić A., Gojgić-Cvijović G., Jakovljević D., Kekez B., Kojić J.S., Mattinen M.L., Harju I.E., Vrvić M.M, & Beškoski V.P. (2017). Brachybacterium sp. CH-KOV3 isolated from an oil-polluted environment-a new producer of levan. International journal of biological macromolecules, 104(Pt A).
+ Open protocol
+ Expand
5

MALDI-ToF Imaging Mass Spectrometry Protocol

Check if the same lab product or an alternative is used in the 5 most similar protocols
All MSI experiments were performed using an Ultraflextreme III MALDI-ToF/ToF mass spectrometer (Bruker Daltonik) with a lateral resolution of 100 μm, a laser focus setting of “large” (corresponding to an on-target laser spot size of approximately 80 μm), and 500 accumulated laser shots per pixel (10 laser shots per step of a random walk within each pixel). Negatively charged ions up to m/z 1000 were detected with a digitization rate of 4 GHz in reflectron mode. All pixel mass spectra were processed with a smoothing algorithm (Savitzky-Golay algorithm, width 0.005 m/z, two cycles) and a background subtraction (TopHat algorithm) during data acquisition using FlexAnalysis (ver. 3.4; Bruker Daltonik).
After MSI data acquisition, the slides were washed in 70% ethanol to remove the remaining matrix and then stained with hematoxylin and eosin (H&E). High-resolution digital images of the H&E stained tissues were then recorded using a Pannoramic MIDI slide scanner (3DHISTECH Ld., Budapest, Hungary) and co-registered to the MSI datasets in FlexImaging 3.0 (Bruker Daltonik).
Lou S., Balluff B., Cleven A.H., Bovée J.V, & McDonnell L.A. (2016). Prognostic Metabolite Biomarkers for Soft Tissue Sarcomas Discovered by Mass Spectrometry Imaging. Journal of the American Society for Mass Spectrometry, 28(2), 376-383.
+ Open protocol
+ Expand
6

MALDI-TOF/TOF Imaging Proteomics Protocol

Check if the same lab product or an alternative is used in the 5 most similar protocols
Imaging experiments were conducted using an ultrafleXtreme MALDI TOF/TOF with a 1 kHz Smartbeam laser (Bruker Daltonics, Billerica, MA, USA). Intact proteins were analyzed from 4,000 – 40,000 m/z with the global attenuator offset at 25%, and the lens adjusted to 7 kV. The digitizer was set to 0.08 Gs/s and the pulsed ion extraction was set to 50 ns. MSI was collected at 25 and 50 μm spatial resolution at 30 shots/spot, 1000 Hz, on medium energy distribution set to 75% laser power with hexagon measuring raster. Analysis of MALDI-MSI data was conducted in flexImaging, and flexAnalysis (Bruker Daltonics, Billerica, MA, USA) and SCiLS 2016b (Bremen, Germany). These are described in further detail on page S4 in the Supplementary Information.
Schmitt N.D., Rawlins C.M., Randall E.C., Wang X., Koller A., Auclair J.R., Kowalski J.M., Kowalski P.J., Luther E., Ivanov A.R., Agar N.Y, & Agar J.N. (2019). Genetically Encoded Fluorescent Proteins Enable High-Throughput Assignment of Cell-cohorts Directly from MALDI-MS Images. Analytical chemistry, 91(6), 3810-3817.
+ Open protocol
+ Expand
7

MALDI-TOF MS Profiling of Bacterial Cells

Check if the same lab product or an alternative is used in the 5 most similar protocols
The matrices HCCA (10 mg/mL) was prepared in bacterial solution (EtOH/ACN/H2O, 1:1:1 (v/v/v)). The trifluoroacetic acid (TFA) solution was added to Bacterial Solution with 2.5% v/v of the final concentrations. Then, under sterile conditions, two lapfuls of bacterial cells were suspended in 5 μL of bacterial solution and thoroughly vortexed for 30 s. Two microliters of bacterial suspension was mixed with 2 μL of the matrix, and then 1 μL of the mixture was overlaid on the ground steel MALDI target. After 30 min, when all spots had dried, the target was placed in the ultrafleXtreme MALDI–TOF/TOF mass spectrometer for measurement according to Pomastowski et al. (2015 ). The ultrafleXtreme MALDI–TOF/TOF mass spectrometer is equipped with a modified neodymium-doped yttrium aluminum garnet (Nd:YAG) laser (Smartbeam IITM) operating at the wavelength of 355 nm and the frequency of 2 kHz. IC MALDI–TOF MS spectra were recorded manually in linear positive mode within m/z range of 300–30,000 and applying the acceleration voltage of 25 kV. All the mass spectra were acquired and processed with the dedicated software: flexControl and flexAnalysis, respectively (both from Bruker).
Viorica R.P., Pawel P., Kinga M., Michal Z., Katarzyna R, & Boguslaw B. (2017). Lactococcus lactis as a safe and inexpensive source of bioactive silver composites. Applied Microbiology and Biotechnology, 101(19), 7141-7153.
+ Open protocol
+ Expand
8

MALDI-TOF MS Lipid Analysis Protocol

Check if the same lab product or an alternative is used in the 5 most similar protocols
For MS analysis, lipid spots from primuline stained TLC were scraped off and extracted as described above. The obtained lipid fractions (concentrated to a volume of 10 µl) as well as total extracts (10 µl) were independently pre-mixed 1/1 (v/v) with the different matrix compounds (DHB and 9-AA) prior to deposition onto the MALDI target and investigated by positive and negative ion-mode MALDI-TOF MS, respectively. MALDI-TOF mass spectra were acquired on a Bruker Autoflex mass spectrometer (Bruker Daltonics, Bremen, Germany) which utilizes a pulsed nitrogen laser (337-nm wavelength). The extraction voltage was 20 kV and gated matrix suppression was applied to prevent the saturation of the detector by matrix ions (Petkovic et al. 2001 (link)). For each mass spectrum, 100 single laser shots were averaged. In order to enhance the resolution, all spectra were acquired in the reflector mode using delayed extraction conditions. See Fuchs et al. 2007 (link) and Schiller et al. 2004 (link) for a more detailed methodological description of MALDI-TOF MS with the focus on lipid analysis. All data were processed with the software ‘Flex Analysis’ version 2.2 (Bruker Daltonics). Selected lipids were also analysed subsequent to phosphoplipase A2 (PLA2) digestion in order to determine the fatty acyl composition as previously described (Fuchs et al. 2007 (link)).
Maric S., Thygesen M.B., Schiller J., Marek M., Moulin M., Haertlein M., Forsyth V.T., Bogdanov M., Dowhan W., Arleth L, & Pomorski T.G. (2014). Biosynthetic preparation of selectively deuterated phosphatidylcholine in genetically modified Escherichia coli. Applied microbiology and biotechnology, 99(1), 241-254.
+ Open protocol
+ Expand
9

Mass Spectrometry Data Analysis

Check if the same lab product or an alternative is used in the 5 most similar protocols
Obtained mass spectrometry data were analysed and processed using Data Explorer Software (Version 4.9, Applied Biosystems), flexAnalysis (Version 3.4, Bruker Daltonik) or Data Analyst (Version 1.4.2, Applied Biosystems) according to the equipment used.
Drozd A., Wojewska D., Peris-Díaz M.D., Jakimowicz P, & Krężel A. (2018). Crosstalk of the structural and zinc buffering properties of mammalian metallothionein-2. Metallomics : integrated biometal science, 10(4).
+ Open protocol
+ Expand
10

MALDI-TOF Protein Analysis Protocol

Check if the same lab product or an alternative is used in the 5 most similar protocols
A saturated solution of sinapinic acid (SA) as matrix in 30:70 (v/v) acetonitrile:water, 0.1% trifluoroacetic acid (TFA) and a protein solution in 30:70 (v/v) acetonitrile:water, 0.1% TFA were prepared and mixed in a 1:1 ratio. A total of 1 µL of the previous mixture was deposited into a polished stainless-steel target (Bruker, Bremen, Germany) and allowed to dry. Then, 1 µL of SA matrix solution was deposited into the sample and allowed to dry. The same procedure was followed for the Protein Standard Calibration I solution (Bruker) used for Calibration. The target was introduced in a Autoflex MALDI-TOF (Bruker), spectra were acquired in lineal mode (Flex control, Bruker) and processed by Flex Analysis (Bruker).
Cotrina E.Y., Vilà M., Nieto J., Arsequell G, & Planas A. (2020). Preparative Scale Production of Recombinant Human Transthyretin for Biophysical Studies of Protein-Ligand and Protein-Protein Interactions. International Journal of Molecular Sciences, 21(24), 9640.
+ 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!