Microflex lrf 20

Manufactured by Bruker

Sourced in United States, Germany

The Microflex LRF 20 is a compact and versatile MALDI-TOF mass spectrometer designed for rapid and accurate identification of microorganisms. It features a robust and reliable design, providing high-performance analysis in a small footprint.

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Lab products found in correlation

Trypsin, by Promega (26 mentions) Flexanalysis 3, by Bruker (9 mentions) Mascot, by Matrix Science (7 mentions) α cyano 4 hydroxycinnamic acid, by Merck Group (4 mentions) α cyano 4 hydroxycinnamic acid chca, by Merck Group (2 mentions) Avance 400 spectrometer, by Bruker (2 mentions) Sodium bicarbonate, by Merck Group (2 mentions) Ammonium bicarbonate, by Merck Group (2 mentions) Dynabead antibody coupling kit, by Thermo Fisher Scientific (1 mentions) Lambda 365 spectrophotometer, by PerkinElmer (1 mentions) Co ip kit, by Thermo Fisher Scientific (1 mentions) Anti cav1 antibody, by Cell Signaling Technology (1 mentions) Acetonitrile, by Merck Group (1 mentions) Trifluoroacetic acid tfa, by Merck Group (1 mentions) Mascot software, by Matrix Science (1 mentions) Mascot server 2, by Matrix Science (1 mentions) Flexcontrol 3, by Bruker (1 mentions) Protein calibration standard 1, by Bruker (1 mentions) Precision plus protein standard, by Bio-Rad (1 mentions) Mini protean tgxtm stain free gel, by Bio-Rad (1 mentions)

Close spelling variants of this product

Microflex (153 citations) Microflex LRF (34 citations)

44 protocols using microflex lrf 20

MALDI-TOF Mass Spectrometry Protein Identification

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The procedure was performed as previously described.
²³ (link) Briefly, the purified G1D7 antibody was bound to M‐270 epoxy magnetic beads (Dynabead Antibody Coupling Kit; Life Technologies) according to the manufacturer's protocol. The G1D7‐bound protein band from MDM‐MB‐231 cell lysates was digested with trypsin and subjected to matrix‐assisted laser desorption ionization time‐of‐flight analysis (Microflex LRF 20; Bruker Daltonics). Spectra were acquired at 300 shots per spectrum over an m/z range of 700–4000 and calibrated through two‐point internal calibration using trypsin auto‐digestion peaks (m/z 842.5099, 2211.1046). The peak list was generated using the Flex Analysis 3.0 software. The threshold used for peak‐picking was as follows: a minimum resolution of monoisotopic mass was set at 500, and the signal‐to‐noise ratio (S/N) was established at 6. The search program MASCOT, developed by Matrixscience (http://www.matrixscience.com/), was used for protein identification via peptide mass fingerprinting. The following parameters were used for the database search: trypsin as the cleaving enzyme, a maximum of one missed cleavage, iodoacetamide (Cys) as complete modification, oxidation (Met) as partial modification, monoisotopic masses, and a mass tolerance of ±0.2 Da.

Higashi T., Saigo C., Chikaishi W., Hayashi H., Hanamatsu Y., Futamura M., Matsuhashi N, & Takeuchi T. (2024). Implication of IZUMO2 in the cell‐in‐cell phenomenon: A potential therapeutic target for triple‐negative breast cancer. Thoracic Cancer, 15(7), 513-518.

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Protein Identification by Peptide Mass Fingerprinting

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For identification of components of the 62-kDa band on SDS-PAGE (Fig. 1F) by peptide mass fingerprinting (PMF) with MALDI-TOF MS, the in-gel-digested protein sample was mixed with α-cyano-4-hydroxycinnamic acid in 50% acetonitrile and 0.1% TFA and subjected to MALDI-TOF MS (Microflex LRF 20, Bruker Daltonics) as described (42 (link)). Spectra were collected from 300 shots per spectrum over m/z range 600 to 3000 and calibrated by two-point internal calibration using trypsin auto-digestion peaks (m/z 842.5099, 2211.1046). Peak list was generated using Flex Analysis 3.0. Threshold used for peak-picking was as follows: 500 for minimum resolution of monoisotopic mass, 5 for S/N. The search program Mascot (43 (link)) developed by Matrixscience (http://www.matrixscience.com/) was used for protein identification by PMF. The following parameters were used for the database search: trypsin as the cleaving enzyme, a maximum of one missed cleavage, iodoacetamide (Cys) as a complete modification, oxidation (Met) as a partial modification, monoisotopic masses, and a mass tolerance of ±0.2 Da. PMF acceptance criteria are probability scoring. Detailed Mascot search parameters are summarized in Table S1.

Koga J., Yazawa M., Miyamoto K., Yumoto E., Kubota T., Sakazawa T., Hashimoto S., Sato M, & Yamane H. (2021). Sphingadienine-1-phosphate levels are regulated by a novel glycoside hydrolase family 1 glucocerebrosidase widely distributed in seed plants. The Journal of Biological Chemistry, 297(5), 101236.

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Proteomic Analysis of HSF-1 Interactome

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HSF-1 immunoprecipitation assay was performed using Dynabeads^® Co-Immunoprecipitation Kit (Novex, USA). Total cell lystaes were incubated with 5 mg of antibody-coupled magnetic Dynabeads^® M-270 Epoxy beads and the HSF-1-pull down products were subjected to 10% denaturing polyacrylamide gel electrophoresis followed by immunoblotting. To identify proteins by peptide mass fingerprinting, protein bands were excised, digested with trypsin (Promega, Madison, WI), mixed with a-cyano-4-hydroxycinnamic acid in 50% acetonitrile/0.1% trifluoroacetic acid, and subjected to MALDI-TOF analysis (Microflex LRF 20, Bruker Daltonics, Billerica, MA, USA). Peak list was generated using Flex Analysis 3.0 followed by protein identification using MASCOT, Matixscience (http://www.matrixscience.com).

Bhardwaj M., Paul S., Jakhar R., Khan I., Kang J.I., Kim H.M., Yun J.W., Lee S.J., Cho H.J., Lee H.G, & Kang S.C. (2017). Vitexin confers HSF-1 mediated autophagic cell death by activating JNK and ApoL1 in colorectal carcinoma cells. Oncotarget, 8(68), 112426-112441.

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Protein Identification by Mass Spectrometry

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For protein identification by PMF, protein spots were excised, digested with trypsin (Promega, Madison, WI, USA), mixed with a-cyano-4-hydroxycinnamic acid in 50% acetonitrile/0.1% TFA, and subjected to MALDI-TOF analysis (Microflex LRF 20, Bruker Daltonics). Spectra were collected from 300 shots per spectrum over the m/z range of 600–3000 and calibrated by two-point internal calibration using trypsin auto-digestion peaks (m/z 842.5099, 2211.1046). The peak list was generated using Flex Analysis 3.0. The threshold used for peak-picking was as follows: 500 for a minimum resolution of monoisotopic mass, 5 for S/N. The search program MASCOT, developed by Matrixscience, was used for protein identification by PMF. The following parameters were used for the database search: trypsin as the cleaving enzyme, a maximum of one missed cleavage, iodoacetamide (Cys) as a complete modification, oxidation (Met) as a partial modification, monoisotopic masses, and a mass tolerance of ±0.1 Da. The PMF acceptance criteria involve probability scoring.

Shin E., Kang H., Lee H., Lee S., Jeon J., Seong K., Youn H, & Youn B. (2022). Exosomal Plasminogen Activator Inhibitor-1 Induces Ionizing Radiation-Adaptive Glioblastoma Cachexia. Cells, 11(19), 3102.

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MALDI-TOF MS Protein Identification

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The protein band of interest was excised from the gel and analyzed by matrix-assisted laser desorption ionization-time-of-flight mass spectrometry (MALDI-TOF MS) (Microflex LRF 20, Bruker Daltonik GmbH, Bremen, Germany). The peptide masses were entered into Mascot (http://www.matrixscience.com/), and the NCBI database was searched to identify the protein.

Yu Y., Hayashi S., Cai X., Fang C., Shi W., Tsutsui H, & Sheng J. (2014). Pu-Erh Tea Extract Induces the Degradation of FET Family Proteins Involved in the Pathogenesis of Amyotrophic Lateral Sclerosis. BioMed Research International, 2014, 254680.

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MALDI-TOF Mass Spectrometry for Protein Identification

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Protein spots were excised, digested with trypsin (Promega, Madison, WI), mixed with α-cyano-4-hydroxycinnamic acid (CHCA; Sigma-Aldrich) in 50% acetonitrile/0.1% trifluoroacetic acid, and used for MALDI-TOF analysis (Microflex LRF 20, Bruker Daltonics) as described by Fernandez et al. [29] . Spectra were collected from 300 shots per spectrum over an m/z range of 600-3000 and calibrated using a two-point internal calibration of trypsin autodigested peaks (m/z 842.5099, 2211.1046). The peak list was generated using Flex Analysis 3.0. The threshold used for peak-picking was 500 for the minimum resolution of monoisotopic mass and 5 for S/N. The search program MASCOT, developed by Matrixscience (http://www.matrixscience.com), was used, and the MASCOT probabilitybased MOWSE (molecular weight search) score was calculated for PMF. For the database search, the following parameters were used: trypsin included as the cleaving enzyme, a maximum of one missed cleavage, iodoacetamide (Cys) as a complete modification, oxidation (Met) as a partial modification, monoisotopic masses, and a mass tolerance of ± 0.1 Da. The PMF acceptance criteria were based on probability scoring as follows: -10*Log (P), where P is the probability that the observed match is a random event, and a score greater than 62 is significant (p<0.05).

Choi J.W., Kim K.E., Lee C.Y., Lee J., Seo H.H., Lim K.H., Choi E., Lim S., Lee S., Kim S.W, & Hwang K.C. (2016). Alterations in Cardiomyocyte Differentiation-Related Proteins in Rat Mesenchymal Stem Cells Exposed to Hypoxia. Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology, 39(4).

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Spectroscopic Characterization of Labeled DNA

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All solvents and reagents were purchased from commercial sources and used as received. ¹H /¹³C NMR spectra were recorded with a Bruker Avance 400 spectrometer, using tetra-methyl-silane as a reference. The solvent for spectroscopic studies was of spectroscopic grade and used as received. UV–Vis spectra were measured with Helios Gamma and Cary 100 UV–Vis spectrophotometers. Fluorescence spectra were recorded with HORIBA scientific SAS and PTI spectrophotometers. High-resolution mass spectra were obtained from a Bruker Microflex LRF20 matrix-assisted laser desorption/ionisation time-of-flight (MALDI-TOF). IR spectra were measured with Nicolet Impact 400D spectrophotometer. The unlabelled and labelled DNA oligonucleotides (see Table S1) were purchased from IDT DNA purified in HPLC grade, and the labelling dyes were 5’-FAM (FAM: 6-carboxyfluorescein) and 3’-TAMRA (TAMRA: 6-carboxytetramethylrhodamine). All concentrations of oligonucleotides were estimated by UV absorption using the extinction coefficients and expressed in strand molarity. Ligands were dissolved in DMSO to give 5 mM stock solutions. All solutions were stored at − 20 °C and defrosted and diluted immediately before use in the suitable buffer to the appropriate concentrations.

Gil-Martínez A., Hernández A., Galiana-Roselló C., López-Molina S., Ortiz J., Sastre-Santos Á., García-España E, & González-García J. (2023). Development and application of metallo-phthalocyanines as potent G-quadruplex DNA binders and photosensitizers. Journal of Biological Inorganic Chemistry, 28(5), 495-507.

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Protein Identification by Peptide Mass Fingerprinting

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For protein identification by peptide mass fingerprinting (PMF), protein spots were excised, digested with trypsin (Promega, Madison, WI, USA), mixed with α cyano-4-hydroxycinnamic acid in 50% acetonitrile/0.1% trifluoroacetic acid, and subjected to matrix-assisted laser desorption/ionization-time of flight (MALDI-TOF) analysis (Microflex LRF 20; Bruker Daltonics, Billerica, MA, USA). Spectra were collected from 300 shots per spectrum over an m/z range of 600–3,000 and calibrated by two-point internal calibration using trypsin autodigestion peaks (m/z 842.5099, 2,211.1046). A peak list was generated using Flex Analysis 3.0 (Bruker Daltonik, Bremen, Germany). The threshold used for peak-picking was as follows: 500 for minimum resolution of monoisotopic mass, 5 for S/N. The MASCOT search program (http://www.matrixscience.com/) was used for protein identification by PMF. The following parameters were used for the database search: trypsin as the cleaving enzyme, a maximum of one missed cleavage, iodoacetamide (Cys) as a complete modification, oxidation (Met) as a partial modification, monoisotopic masses, and a mass tolerance of ±0.1 Da. PMF acceptance criteria was based on probability scoring.

Kim D., Kwon S., Jeon H., Ryu S., Ha K.T, & Kim S. (2017). Proteomic change by Korean Red Ginseng in the substantia nigra of a Parkinson's disease mouse model. Journal of Ginseng Research, 42(4), 429-435.

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Identifying Protein Interactors of DJ1

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To identify partner proteins of DJ1, scrutinized gels were scanned on a UMAX Power Look 1120 (Maxium Technologies, Akron, OH, USA). Separated interacting partners were identified by protein mass fingerprinting (PMF). For this, excised protein bands were digested with trypsin (Promega, Madison, WI, USA) and mixed with α-cyano-4-hydroxycinnamic acid in 50% acetonitrile/0.1% TFA, followed by MALDI-TOF analysis (Microflex LRF 20, Bruker Daltonics, Billerica, MA, USA) as described by Fernandez et al. 23 (link) using MASCOT (Mascot Sever 2.3) developed by Matrix science (http://www.matrixscience.com) as the search programme. trypsin as the cleaving enzyme, a maximum of one missed cleavage, iodoacetamide (Cys) as a complete modification, oxidation (Met) as a partial modification, monoisotopic masses and a mass tolerance of ±0.1 D were used as parameters for the database search.

Chaudhari H.N., Kim S.W, & Yun J.W. (2015). Gender-dimorphic regulation of DJ1 and its interactions with metabolic proteins in streptozotocin-induced diabetic rats. Journal of Cellular and Molecular Medicine, 19(5), 996-1009.

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Peptide Mass Fingerprinting for Protein Identification

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Proteins were identified by peptide mass fingerprinting (PMF). Protein spots were excised, digested with trypsin (Promega, Madison, WI, USA), and mixed with α cyano-4-hydroxycinnamic acid in 50% acetonitrile/0.1% TFA for MALDI-TOF analysis (Microflex LRF 20, BrukerDaltonics, Billerica, MA, USA) as described by Fernandez et al [14 (link)]. Spectra were collected from 300 shots per spectrum over the 600~3000 m/z range and calibrated by a two-point internal calibration using trypsin auto-digestion peaks (m/z 842.5099, 2211.1046). The peak list was generated by Flex Analysis 3.0 software, with a peak selection threshold of 500 for the minimum resolution of monoisotopic mass and 5 for S/N. Protein identification by PMF was performed using the search program MASCOT, developed by Matrix Science (http://www.matrixscience.com/). The following parameters were used for the database search: trypsin as the cleaving enzyme, a maximum value of one missed cleavage, iodoacetamide (Cys) as a complete modification, oxidation (Met) as a partial modification, monoisotopic mass, and a mass tolerance for peptide ion (m/z) of ±0.1 Da. PMF acceptance criteria were based on probability scoring.

Hwang M., Han M.H., Park H.H., Choi H., Lee K.Y., Lee Y.J., Kim J.M., Cheong J.H., Ryu J.I., Min K.W., Oh Y.H., Ko Y, & Koh S.H. (2019). LGR5 and Downstream Intracellular Signaling Proteins Play Critical Roles in the Cell Proliferation of Neuroblastoma, Meningioma and Pituitary Adenoma. Experimental Neurobiology, 28(5), 628-641.

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