Microflex lrf instrument

Manufactured by Bruker

The Microflex LRF is a MALDI-TOF mass spectrometer designed for rapid analysis of large biomolecules. It features a linear reflectron design that enables high-resolution mass determination. The instrument is capable of analyzing a wide range of samples, including proteins, peptides, and small molecules.

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Lab products found in correlation

6530 accurate mass q tof lc ms, by Agilent Technologies (1 mentions) Kta pure system, by GE Healthcare (1 mentions) Hitrap sp sepharose ff, by GE Healthcare (1 mentions) Viia7, by Thermo Fisher Scientific (1 mentions) Hitrap sp hp, by GE Healthcare (1 mentions) Nanovue plus spectrophotometer, by GE Healthcare (1 mentions) Viia 7 real time pcr system, by Thermo Fisher Scientific (1 mentions)

Close spelling variants of this product

Microflex LRF MALDI-TOF MS instrument Microflex LRF MALDI-TOF instrument Microflex LRF Microflex instrument Microflex

3 protocols using microflex lrf instrument

Protein Purification and Characterization

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Chromatography was conducted using an ÄKTA Pure system from GE Healthcare Life Sciences (Piscataway, NJ), and the results were analyzed with the UNICORN Control System. HiTrap SP HP, HiTrap SP Sepharose FF, HiTrap ConA 4B, and HiLoad^® 26/600 Superdex^® 75 pg columns for protein purification were from GE Healthcare Life Sciences.
Protein concentrations were determined with a NanoVue Plus spectrophotometer from GE Healthcare Life Sciences by absorbance at 280 nm using Beer’s law, ε = 0.53 mL·mg^–1·cm^–1, and the molecular mass of the unglycosylated protein.
Differential scanning fluorimetry (DSF),^{39 (link)} which requires the monitoring of fluorescence during thermal denaturation, was performed with a ViiA 7 Real-Time PCR system from Applied Biosystems (Foster City, CA). Denaturation data were obtained with ViiA 7 version 2.0 software and analyzed further with Protein Thermal Shift version 1.4 software, both from Applied Biosystems.
The intact molecular mass of RNase 1 glycoforms was determined by MALDI–TOF mass spectrometry using a microflex LRF instrument from Bruker (Billerica, MA) and by ESI mass spectrometry using a 6530 Accurate-Mass Q-TOF LC/MS from Agilent (Santa Clara, CA).

Ressler V.T, & Raines R.T. (2019). Consequences of the Endogenous N-Glycosylation of Human Ribonuclease 1. Biochemistry, 58(7), 987-996.

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Protein Characterization via MALDI-TOF Mass Spectrometry

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Matrix-assisted laser desorption-ionization–time-of-flight (MALDI–TOF) mass spectra for protein characterization were acquired with a microflex LRF instrument (Bruker).

Cheah K.M., Jun J.V., Wittrup K.D, & Raines R.T. (2022). Host–Guest Complexation by β-Cyclodextrin Enhances the Solubility of an Esterified Protein. Molecular pharmaceutics, 19(11), 3869-3876.

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MALDI-TOF Mass Spectrometry Protocol

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MALDI-TOF mass spectra were recorded on a Bruker Daltonics Microflex LRF instrument (Bruker-Daltonics, Billerica, MA) operating in reflectron mode. The system utilizes a pulsed nitrogen laser, emitting at 337 nm. Typically, 1000–2000 shots were acquired at 60-Hz frequency and 78% laser power, with the laser attenuator offset at 16% for 30% range. The matrix was saturated 2,5-dihydrobenzoic acid in acetonitrile and was premixed with the samples (0.5 mg·ml⁻¹) prior to spotting onto a standard 96-position stainless steel target. Ion source 1 was set to 19.0 kV, and source 2 to 15.9 kV (83.7% of IS 1), with lens and reflector voltages of 9.79 and 19.99 kV, respectively. During the acquisition matrix ion suppression was used up to 200 Da. External calibration used Bruker Peptide Calibration Standard II mono with insulin. The MS data were processed off-line using the Flex Analysis 3.0 software package (Bruker Daltonics).

Gyore J., Parameswar A.R., Hebbard C.F., Oh Y., Bi E., Demchenko A.V., Price N.P, & Orlean P. (2014). 2-Acylamido Analogues of N-Acetylglucosamine Prime Formation of Chitin Oligosaccharides by Yeast Chitin Synthase 2. The Journal of Biological Chemistry, 289(18), 12835-12841.

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