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Thermo fusion lumos

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The Thermo Fusion Lumos is a laboratory instrument designed for mass spectrometry analysis. It provides high-resolution detection and identification of complex molecular samples.

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Lab products found in correlation

Easy nlc 1200 uhplc system, by Thermo Fisher Scientific (4 mentions) Reprosil pur c18 aq beads, by Dr. Maisch (4 mentions) Irt peptide, by Biognosys (2 mentions) Picofrit 10 μm, by New Objective (2 mentions) Picofrit 10 mm opening, by New Objective (2 mentions) Easy nlc 1200, by Thermo Fisher Scientific (1 mentions) Easy spray, by Thermo Fisher Scientific (1 mentions)

Spelling variants of this product

Fusion Lumos (74 citations) Thermo Orbitrap Fusion Lumos (8 citations) Thermo Fusion Lumos mass spectrometer (6 citations) Thermo Orbitrap Fusion Lumos Tribrid Mass Spectrometer (4 citations) Thermo Orbitrap Fusion Lumos Tribrid (3 citations) Thermo Orbitrap Fusion Lumos mass spectrometer (3 citations)

5 protocols using thermo fusion lumos

1

DIA-based Quantitative Proteomics of ccRCC Samples

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Unlabeled, digested peptide material from individual tissue samples (ccRCC and NAT) was spiked with index Retention Time (iRT) peptides (Biognosys) and subjected to data-independent acquisition (DIA) analysis. Peptides (~0.8 μg) were separated on an Easy nLC 1200 UHPLC system (Thermo Scientific) on an in-house packed 20 cm x 75 μm diameter C18 column (1.9 μm Reprosil-Pur C18-AQ beads (Dr. Maisch GmbH); Picofrit 10 μm opening (New Objective)). The column was heated to 50°C using a column heater (Phoenix-ST). The flow rate was 0.200 μl/min with 0.1% formic acid and 3% acetonitrile in water (A) and 0.1% formic acid, 90% acetonitrile (B). The peptides were separated with a 7%–30% B gradient in 84 mins and analyzed using the Thermo Fusion Lumos mass spectrometer (Thermo Scientific). The DIA segment consisted of one MS1 scan (350-1650 m/z range, 120K resolution) followed by 30 MS2 scans (variable m/z range, 30K resolution). Additional parameters were as follows: MS1: RF Lens – 30%, AGC Target 4.0e5, Max IT – 50 ms, charge state include - 2-6; MS2: isolation width (m/z) – 0.7, AGC Target - 2.0e5, Max IT – 120 ms.
Clark D.J., Dhanasekaran S.M., Petralia F., Pan J., Song X., Hu Y., da Veiga Leprevost F., Reva B., Lih T.S., Chang H.Y., Ma W., Huang C., Ricketts C.J., Chen L., Krek A., Li Y., Rykunov D., Li Q.K., Chen L.S., Ozbek U., Vasaikar S., Wu Y., Yoo S., Chowdhury S., Wyczalkowski M.A., Ji J., Schnaubelt M., Kong A., Sethuraman S., Avtonomov D.M., Ao M., Colaprico A., Cao S., Cho K.C., Kalayci S., Ma S., Liu W., Ruggles K., Calinawan A., Gümüş Z.H., Geiszler D., Kawaler E., Teo G.C., Wen B., Zhang Y., Keegan S., Li K., Chen F., Edwards N., Pierorazio P.M., Chen X.S., Pavlovich C.P., Hakimi A.A., Brominski G., Hsieh J.J., Antczak A., Omelchenko T., Lubinski J., Wiznerowicz M., Linehan W.M., Kinsinger C.R., Thiagarajan M., Boja E.S., Mesri M., Hiltke T., Robles A.I., Rodriguez H., Qian J., Fenyö D., Zhang B., Ding L., Schadt E., Chinnaiyan A.M., Zhang Z., Omenn G.S., Cieslik M., Chan D.W., Nesvizhskii A.I., Wang P, & Zhang H. (2019). Integrated Proteogenomic Characterization of Clear Cell Renal Cell Carcinoma. Cell, 179(4), 964-983.e31.
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2

Comprehensive Proteomic Profiling Workflow

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Global proteome and phosphoproteome fractions were analyzed using the same instrumentation and methodology. Peptides (~0.8 μg) were separated on an Easy nLC 1200 UHPLC system (Thermo Scientific) on an in-house packed 20 cm x 75 mm diameter C18 column (1.9 mm Reprosil-Pur C18-AQ beads (Dr. Maisch GmbH); Picofrit 10 mm opening (New Objective)). The column was heated to 50°C using a column heater (Phoenix-ST). The flow rate was 0.200 μl/min with 0.1% formic acid and 2% acetonitrile in water (A) and 0.1% formic acid, 90% acetonitrile (B). The peptides were separated with a 6%–30% B gradient in 84 min and analyzed using the Thermo Fusion Lumos mass spectrometer (Thermo Scientific). Parameters were as follows: MS1: resolution – 60,000, mass range – 350 to 1800 m/z, RF Lens – 30%, AGC Target 4.0e5, Max IT – 50 ms, charge state include - 2-6, dynamic exclusion – 45 s, top 20 ions selected for MS2; MS2: resolution-50,000, high-energy collision dissociation activation energy (HCD)-37, isolation width (m/z) – 0.7, AGC Target – 2.0e5, Max IT – 105 ms.
Clark D.J., Dhanasekaran S.M., Petralia F., Pan J., Song X., Hu Y., da Veiga Leprevost F., Reva B., Lih T.S., Chang H.Y., Ma W., Huang C., Ricketts C.J., Chen L., Krek A., Li Y., Rykunov D., Li Q.K., Chen L.S., Ozbek U., Vasaikar S., Wu Y., Yoo S., Chowdhury S., Wyczalkowski M.A., Ji J., Schnaubelt M., Kong A., Sethuraman S., Avtonomov D.M., Ao M., Colaprico A., Cao S., Cho K.C., Kalayci S., Ma S., Liu W., Ruggles K., Calinawan A., Gümüş Z.H., Geiszler D., Kawaler E., Teo G.C., Wen B., Zhang Y., Keegan S., Li K., Chen F., Edwards N., Pierorazio P.M., Chen X.S., Pavlovich C.P., Hakimi A.A., Brominski G., Hsieh J.J., Antczak A., Omelchenko T., Lubinski J., Wiznerowicz M., Linehan W.M., Kinsinger C.R., Thiagarajan M., Boja E.S., Mesri M., Hiltke T., Robles A.I., Rodriguez H., Qian J., Fenyö D., Zhang B., Ding L., Schadt E., Chinnaiyan A.M., Zhang Z., Omenn G.S., Cieslik M., Chan D.W., Nesvizhskii A.I., Wang P, & Zhang H. (2019). Integrated Proteogenomic Characterization of Clear Cell Renal Cell Carcinoma. Cell, 179(4), 964-983.e31.
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3

Peptide Identification by Liquid Chromatography-Mass Spectrometry

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The eluted peptides were lyophilized using a SpeedVac (Thermo Savant) and resuspended in 10 μL of 1% formic acid/5% acetonitrile. All mass spectrometric experiments were performed on a Thermo Fusion Lumos mass spectrometer connected to an Easy-nLC 1200 via an Easy Spray (Thermo Fisher Scientific). The peptides mixture was loaded onto a 15 cm column with 0.075 mm inner diameter column packed with C18 2-μm reversed phase resins (PepMap RSLC), and separated within a 60 min linear gradient from 95% solvent A (0.1% formic acid/2% acetonitrile/98% water) to 28% solvent B (0.1% formic acid/80% acetonitrile) at a flow rate of 300 nL/min. The spray voltage was set to 2.1 KV and the temperature of ion transfer capillary was 275 °C, and RF lens was 60%. The mass spectrometer was operated in positive ion mode and employed in the data-dependent mode to automatically switch between MS and MS/MS using the Tune and Xcalibur 4.0.27.19 software package. One full MS scan from 350 to 1500 m/z was acquired at high resolution R = 60,000 (defined at m/z = 400), followed by fragmentation of the twenty most abundant multiply charged ions (singly charged ions and ions with unassigned charge states were excluded), for ions with charge states 2–7 and collision energy of 30%. Dynamic exclusion was used automatically.
Meng S., Xia W., Xia L., Zhou L., Xu J., Pan X, & Meng L. (2021). A Pilot Study of Rare Renal Amyloidosis Based on FFPE Proteomics. Molecules, 26(23), 7234.
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4

Comprehensive Proteomic Profiling Workflow

Check if the same lab product or an alternative is used in the 5 most similar protocols
Global proteome and phosphoproteome fractions were analyzed using the same instrumentation and methodology. Peptides (~0.8 μg) were separated on an Easy nLC 1200 UHPLC system (Thermo Scientific) on an in-house packed 20 cm x 75 mm diameter C18 column (1.9 mm Reprosil-Pur C18-AQ beads (Dr. Maisch GmbH); Picofrit 10 mm opening (New Objective)). The column was heated to 50°C using a column heater (Phoenix-ST). The flow rate was 0.200 μl/min with 0.1% formic acid and 2% acetonitrile in water (A) and 0.1% formic acid, 90% acetonitrile (B). The peptides were separated with a 6%–30% B gradient in 84 min and analyzed using the Thermo Fusion Lumos mass spectrometer (Thermo Scientific). Parameters were as follows: MS1: resolution – 60,000, mass range – 350 to 1800 m/z, RF Lens – 30%, AGC Target 4.0e5, Max IT – 50 ms, charge state include - 2-6, dynamic exclusion – 45 s, top 20 ions selected for MS2; MS2: resolution-50,000, high-energy collision dissociation activation energy (HCD)-37, isolation width (m/z) – 0.7, AGC Target – 2.0e5, Max IT – 105 ms.
Clark D.J., Dhanasekaran S.M., Petralia F., Pan J., Song X., Hu Y., da Veiga Leprevost F., Reva B., Lih T.S., Chang H.Y., Ma W., Huang C., Ricketts C.J., Chen L., Krek A., Li Y., Rykunov D., Li Q.K., Chen L.S., Ozbek U., Vasaikar S., Wu Y., Yoo S., Chowdhury S., Wyczalkowski M.A., Ji J., Schnaubelt M., Kong A., Sethuraman S., Avtonomov D.M., Ao M., Colaprico A., Cao S., Cho K.C., Kalayci S., Ma S., Liu W., Ruggles K., Calinawan A., Gümüş Z.H., Geiszler D., Kawaler E., Teo G.C., Wen B., Zhang Y., Keegan S., Li K., Chen F., Edwards N., Pierorazio P.M., Chen X.S., Pavlovich C.P., Hakimi A.A., Brominski G., Hsieh J.J., Antczak A., Omelchenko T., Lubinski J., Wiznerowicz M., Linehan W.M., Kinsinger C.R., Thiagarajan M., Boja E.S., Mesri M., Hiltke T., Robles A.I., Rodriguez H., Qian J., Fenyö D., Zhang B., Ding L., Schadt E., Chinnaiyan A.M., Zhang Z., Omenn G.S., Cieslik M., Chan D.W., Nesvizhskii A.I., Wang P, & Zhang H. (2019). Integrated Proteogenomic Characterization of Clear Cell Renal Cell Carcinoma. Cell, 179(4), 964-983.e31.
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5

DIA-based Quantitative Proteomics of ccRCC Samples

Check if the same lab product or an alternative is used in the 5 most similar protocols
Unlabeled, digested peptide material from individual tissue samples (ccRCC and NAT) was spiked with index Retention Time (iRT) peptides (Biognosys) and subjected to data-independent acquisition (DIA) analysis. Peptides (~0.8 μg) were separated on an Easy nLC 1200 UHPLC system (Thermo Scientific) on an in-house packed 20 cm x 75 μm diameter C18 column (1.9 μm Reprosil-Pur C18-AQ beads (Dr. Maisch GmbH); Picofrit 10 μm opening (New Objective)). The column was heated to 50°C using a column heater (Phoenix-ST). The flow rate was 0.200 μl/min with 0.1% formic acid and 3% acetonitrile in water (A) and 0.1% formic acid, 90% acetonitrile (B). The peptides were separated with a 7%–30% B gradient in 84 mins and analyzed using the Thermo Fusion Lumos mass spectrometer (Thermo Scientific). The DIA segment consisted of one MS1 scan (350-1650 m/z range, 120K resolution) followed by 30 MS2 scans (variable m/z range, 30K resolution). Additional parameters were as follows: MS1: RF Lens – 30%, AGC Target 4.0e5, Max IT – 50 ms, charge state include - 2-6; MS2: isolation width (m/z) – 0.7, AGC Target - 2.0e5, Max IT – 120 ms.
Clark D.J., Dhanasekaran S.M., Petralia F., Pan J., Song X., Hu Y., da Veiga Leprevost F., Reva B., Lih T.S., Chang H.Y., Ma W., Huang C., Ricketts C.J., Chen L., Krek A., Li Y., Rykunov D., Li Q.K., Chen L.S., Ozbek U., Vasaikar S., Wu Y., Yoo S., Chowdhury S., Wyczalkowski M.A., Ji J., Schnaubelt M., Kong A., Sethuraman S., Avtonomov D.M., Ao M., Colaprico A., Cao S., Cho K.C., Kalayci S., Ma S., Liu W., Ruggles K., Calinawan A., Gümüş Z.H., Geiszler D., Kawaler E., Teo G.C., Wen B., Zhang Y., Keegan S., Li K., Chen F., Edwards N., Pierorazio P.M., Chen X.S., Pavlovich C.P., Hakimi A.A., Brominski G., Hsieh J.J., Antczak A., Omelchenko T., Lubinski J., Wiznerowicz M., Linehan W.M., Kinsinger C.R., Thiagarajan M., Boja E.S., Mesri M., Hiltke T., Robles A.I., Rodriguez H., Qian J., Fenyö D., Zhang B., Ding L., Schadt E., Chinnaiyan A.M., Zhang Z., Omenn G.S., Cieslik M., Chan D.W., Nesvizhskii A.I., Wang P, & Zhang H. (2019). Integrated Proteogenomic Characterization of Clear Cell Renal Cell Carcinoma. Cell, 179(4), 964-983.e31.
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