Ultraflex extreme

Manufactured by Bruker

Sourced in Germany

The Ultraflex Extreme is a high-performance mass spectrometer designed for advanced analytical applications. It features a robust and reliable design, delivering accurate and reproducible results. The core function of the Ultraflex Extreme is to perform sensitive and precise mass analysis of a wide range of samples.

Automatically generated - may contain errors

Lab products found in correlation

Flexanalysis version 3, by Bruker (1 mentions)

Spelling variants of this product

Ultraflex extreme MALDI-TOF-TOF-MS (2 citations) Ultraflex Extreme MALDI-TOF/TOF mass spectrometer (2 citations)

4 protocols using ultraflex extreme

MALDI-TOF Protein Identification Protocol

Check if the same lab product or an alternative is used in the 5 most similar protocols

MALDI-TOF (MALDI-Time of Flight) was performed using Bruker ultra flex extreme. The instrument parameters were set as follows: detector, reflector mode; accelerating voltage, 25 kV; delay time, 1 μs; laser intensity, 2500. Acquisition was made in the range m/z 700–3500 Da. A total of 500 shots were performed per spectrum, and 20–25 spectra were accumulated per sample to increase the signal to noise ratio. Spectra were acquired in the positive ion mode. A volume of 2 μL of digested sample was mixed with 2 μL of saturated hydroxylcinnamic acid solution and from this mixture 1 μL was deposited onto a stainless steel MALDI sample target and air-dried. Searches were performed against the SWISS PROT protein sequence database allowing for up to 100 ppm error tolerance and up to one missed trypsin cleavage site. The carbamido-methylation of cysteines and methionine oxidation were selected as variable modifications during the search. MS/MS process was done by using LIFT method. The MS & MS/MS spectra were combined & searched using MASCOT against SWISS PROT protein sequence database allowing for up to 0.1 ppm error tolerance.

Ghosh S., Mukherjee S., Sengupta N., Roy A., Dey D., Chakraborty S., Chattopadhyay D., Banerjee A, & Basu A. (2016). Network analysis reveals common host protein/s modulating pathogenesis of neurotropic viruses. Scientific Reports, 6, 32593.

+ Open protocol

+ Expand

MALDI-TOF/TOF MS Lipid, Protein, and Peptide Analysis

Check if the same lab product or an alternative is used in the 5 most similar protocols

MS data were collected in positive mode (detection range: m/z 400–900 for lipids, m/z 2,000–20,000 for proteins, and m/z 1,000–3,000 for peptides) and negative mode (detection range: m/z 400–900 for lipids), raster width 50 μm, 500 shots per raster, on a Bruker Daltonics Ultraflex Extreme Matrix-Assisted Laser Desorption Ionization Time-of-Flight/Time-of-Flight Mass Spectrometer (MALDI-TOF/TOF MS) using flexControl software (version 3.4.105). Subsequently, data were analyzed using the software packages flexImaging (version 3.4.54) and flexAnalysis (version 3.4.57). All MALDI-MSI specific materials, equipment, instruments, and software were obtained from Bruker Daltonics (Billerica, MA).

Scott A.J., Jones J.W., Orschell C.M., MacVittie T.J., Kane M.A, & Ernst R.K. (2014). Mass Spectrometry Imaging Enriches Biomarker Discovery Approaches with Candidate Mapping. Health physics, 106(1), 120-128.

+ Open protocol

+ Expand

MALDI-TOF/TOF-MS Analysis of Glycopeptides

Check if the same lab product or an alternative is used in the 5 most similar protocols

One microliter of enriched glycopeptides was spotted onto a 600-μm Anchor Chip Target (Bruker Daltonics, Bremen, Germany) followed by a 1-μL matrix solution prepared by dissolving 20 mg/mL of dihydroxy benzoic acid (DHB) in TA-30 solution (30% ACN in 0.1% TFA). Peptide Calibrant II Mono was also spotted for external calibration. MALDI-TOF/TOF–MS analysis was carried out on an Ultraflex Extreme mass spectrometer (Bruker Daltonics, Bremen, Germany). Spectra were acquired in positive reflection mode with 1000 laser shots per spectrum. The resolution was kept at 15,000–20,000. Spectra in the mass range 1000–5500 Da were processed using Flex Analysis Version 3.4 supplied by Bruker Daltonics.

Sajid M.S., Saleem S., Jabeen F., Najam-ul-Haq M, & Ressom H.W. (2022). Terpolymeric platform with enhanced hydrophilicity via cysteic acid for serum intact glycopeptide analysis. Mikrochimica acta, 189(8), 277.

+ Open protocol

+ Expand

MALDI-TOF/TOF Analysis of Enriched Glycopeptides

Check if the same lab product or an alternative is used in the 5 most similar protocols

For the analysis of enriched glycopeptides, 1 μL of eluate was deposited on a MALDI plate, and then 1 μL of DHB matrix (12.5 mg/mL in ACN/H₂O/TFA, 50:49.9:0.1 by volume) was spotted onto 600 μm anchorchips (Bruker Daltonics, Bremen, Germany). The Bruker peptide calibration mixture was spotted for external calibration. MALDI-TOF/TOF MS was carried out on a time-of-flight Ultraflex Extreme mass spectrometer (Bruker Daltonics, Bremen, Germany). Peptide mass maps were acquired in positive reflection mode, averaging 800 laser shots per spectrum. Resolution was 15000–20000. The Bruker calibration mixtures were used to calibrate the spectrum to a mass tolerance within 0.1 Da. Each acquired mass spectrum (m/z range 1000–5000) was processed using the software FlexAnalysis v.2.4 supplied by Bruker Daltonics. The peak detection algorithm was SNAP (Sort Neaten Assign and Place), signal-to-noise (S/N) threshold was 3, and the quality factor threshold was 50.

Shi Z., Pu L., Guo Y., Fu Z., Zhao W., Zhu Y., Wu J, & Wang F. (2017). Boronic Acid-Modified Magnetic Fe3O4@mTiO2 Microspheres for Highly Sensitive and Selective Enrichment of N-Glycopeptides in Amniotic Fluid. Scientific Reports, 7, 4603.

+ 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?

Revolutionizing how scientists
search and build protocols!