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Luna c18 resin

Manufactured by Phenomenex
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Luna C18 resin is a high-performance liquid chromatography (HPLC) stationary phase material. It is composed of silica particles with a chemically bonded C18 functional group. The C18 resin is designed for the separation and analysis of a wide range of organic compounds, including non-polar and moderately polar molecules.

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Lab products found in correlation

Nanoacquity hplc system, by Thermo Fisher Scientific (13 mentions) Fusion lumos mass spectrometer, by Thermo Fisher Scientific (9 mentions) Fusion lumos, by Thermo Fisher Scientific (9 mentions) M class hplc system, by Thermo Fisher Scientific (9 mentions) Q exactive, by Thermo Fisher Scientific (6 mentions) Trypsin, by Promega (5 mentions) Nanoacquity hplc system, by Waters Corporation (5 mentions) Mascot, by Matrix Science (4 mentions) Sequencing grade trypsin, by Promega (4 mentions) M class hplc system, by Waters Corporation (3 mentions) Q exactive, by Waters Corporation (3 mentions) Q exactive mass spectrometer, by Thermo Fisher Scientific (2 mentions) M class uplc system, by Thermo Fisher Scientific (2 mentions) Thermofisher q exactive, by Thermo Fisher Scientific (2 mentions) C18 sd sorbent, by 3M (2 mentions) Waters nanoacquity hplc system, by Waters Corporation (2 mentions) Bis tris sds page gel, by Thermo Fisher Scientific (2 mentions) Chymotrypsin, by Promega (2 mentions) Orbitrap elite, by Thermo Fisher Scientific (1 mentions) Proteome discoverer v1, by Thermo Fisher Scientific (1 mentions)

39 protocols using luna c18 resin

1

Quantitative Proteomics by nHPLC-MS/MS

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Sample supernatants were analyzed by nHPLC-MS/MS with a NanoAcquity HPLC system (Waters) linked to a Q Exactive mass spectrometer (ThermoFisher). Digested proteins were loaded on a Luna C18 resin (Phenomenex) trapping column and eluted over a Luna C18 resin 75 µm analytical column at a flow rate of 350 nL/min. The mass spectrometer was operated in data-dependent mode, with the Orbitrap operating at 70,000 FWHM for MS and 17,500 FWHM for MS/MS. The fifteen most abundant ions were selected for MS/MS.
Ward E.P., Bartolone S.N., Chancellor M.B., Peters K.M, & Lamb L.E. (2020). Proteomic analysis of bladder biopsies from interstitial cystitis/bladder pain syndrome patients with and without Hunner’s lesions reveals differences in expression of inflammatory and structural proteins. BMC Urology, 20, 180.
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2

In vitro Methylation and Proteomic Analysis

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In vitro methylated His-YY1-DBD by FLAG-CARM1 in presence of SAM was separated on 12% SDS-PAGE. The destained gel bands containing the methylated targeted protein were washed with 25 mM ammonium bicarbonate followed by acetonitrile. Proteins were reduced with 10 mM dithiothreitol at 60° C followed by alkylation with 50 mM iodoacetamide at RT. Proteins were subjected to multi-enzyme digestion as follows: trypsin (Promega) for 4h, chymotrypsin/elastase (Promega) for 12 h at 37° C followed by Quenching with formic acid. Each gel digest was analyzed by nano LC/MS/MS with a Waters NanoAcquity HPLC system interfaced to a ThermoFisher Q Exactive at MS Bioworks, LLC (Ann Arbor, MI). Peptides were eluted through a 75 μm analytical column of Luna C18 resin (Phenomenex) at 350 nL/min. The mass spectrometer was operated in data-dependent mode. MS and MS/MS were performed in the Orbitrap at 70,000 FWHM and 17,500 FWHM resolutions respectively. The fifteen most abundant ions were selected for MS/MS. Byonic mzID files were parsed into Scaffold software to validate and filter and to create a nonredundant list per sample. Data were filtered using a minimum peptide value of 50% (Prophet scores) and a minimum protein value of 95% requiring at least two unique peptides per protein.
Behera A.K., Kumar M., Shanmugam M.K., Bhattacharya A., Rao V.J., Bhat A., Vasudevan M., Gopinath K.S., Mohiyuddin A., Chatterjee A., Sethi G, & Kundu T.K. (2019). Functional interplay between YY1 and CARM1 promotes oral carcinogenesis. Oncotarget, 10(38), 3709-3724.
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3

Nano LC-MS/MS Proteomic Analysis

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Gel digests were sent to MS Bioworks LCC, Ann Arbor MI, for LC-MS/MS. Each gel digest was analyzed by nano LC-MS/MS with a Waters NanoAcquity HPLC system interfaced to a ThermoFisher Q Exactive. Peptides were loaded on a trapping column and eluted over a 75 μm analytical column at 350 nL/min; both columns were packed with Luna C18 resin (Phenomenex). The mass spectrometer was operated in data-dependent mode, with the Orbitrap operating at 60,000 FWHM and 17,500 FWHM for MS and MS/MS, respectively. The 15 most abundant ions were selected for MS/MS.
Batzel G.O., Moreno B.K., Lopez L.S., Nguyen C.K., Livingston B.T., Joester D, & Lyons D.C. (2022). Proteomic and Transcriptomic Analyses in the Slipper Snail Crepidulafornicata Uncover Shell Matrix Genes Expressed During Adult and Larval Biomineralization. Integrative Organismal Biology, 4(1), obac023.
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4

Quantitative Proteomics of CSF Peptides

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Synthetic peptides labeled with Arginine (13C6,15N4) or Lysine (13C6,15N2) at >95% purity were made by New England Peptide MA 01440 USA. The following peptides were used: Myh9 AGVLAHLEEER; IAQLEEQLDNETK. Pon1 IFFYDSENPPGSEVLR; LLIGTVFHR. App TEEISEVK; THTHIVIPYR. A2m AIAYLNTGYQR; LPSDVVEESAR. Apoa1 DYVSQFESSTLGK; WNEEVEAYR. Apob TEVIPPLIENR; GFEPTLEALFGK. C3 GLEVSITAR; SSVAVPYVIVPLK. C9 SIEVFGQFQGK; TTSFNANLALK. Thbs1 FVFGTTPEDILR; IENANLIPPVPDDK. A 3-4 μg aliquot of each CSF tryptic peptide digests was spiked with isotopologe peptides at a concentration of 100 or 133 fmol/μg peptide digest. Peptides mixes were analyzed in analytical duplicate by nano LC/PRM using a Waters NanoAcquity HPLC system interfaced to a Thermo Fisher Fusion Lumos mass spectrometer. 1.5 μg per sample was loaded on a trapping column and eluted over a 75 μm analytical column at 350 nL/min; both columns were packed with Luna C18 resin (Phenomenex). A 1-h gradient was employed. The mass spectrometer was operated in PRM mode without scheduling; instrument settings included 15,000 FWHM resolution, NCE 30, AGC target value 5 × 104, and maximum IT of 22 ms. Data were processed using Skyline v4.2.
Zlatic S.A., Duong D., Gadalla K.K., Murage B., Ping L., Shah R., Fink J.J., Khwaja O., Swanson L.C., Sahin M., Rayaprolu S., Kumar P., Rangaraju S., Bird A., Tarquinio D., Carpenter R., Cobb S, & Faundez V. (2022). Convergent cerebrospinal fluid proteomes and metabolic ontologies in humans and animal models of Rett syndrome. iScience, 25(9), 104966.
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5

Nano-LC-MS/MS Proteomics Analysis

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2 µg of each digested sample was analyzed by nano liquid chromatography - tandem mass spectrometry (LC-MS/MS) with a M-Class HPLC system (Waters, Milfrod, MA) interfaced to a ThermoFisher Fusion Lumos mass spectrometer (Waltham, MA). Peptides were loaded on a trapping column and eluted over a 75 µm analytical column at 350 nL/min; both columns were packed with Luna C18 resin (Phenomenex, Torrance, CA). A 3-hour gradient was employed. The mass spectrometer was operated in data-dependent mode, with the Orbitrap operating at 60,000 full width at half maximum (FWHM) and 15,000 FWHM for MS and MS/MS, respectively. APD was enabled and the instrument was run with a 3 s cycle for MS and MS/MS.
Biesterveld B.E., O’Connell R., Kemp M.T., Wakam G.K., Williams A.M., Pai M.P, & Alam H.B. (2021). Validation of intraosseous delivery of valproic acid in a swine model of polytrauma. Trauma Surgery & Acute Care Open, 6(1), e000683.
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6

Nanoscale Proteomics Workflow

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Half of each digested sample was analyzed by nano LC-MS/MS with a Waters NanoAcquity HPLC system interfaced to a ThermoFisher Q Exactive mass spectrometer. Peptides were loaded on a trapping column and eluted over a 75 μm analytical column at 350 nL/min; both columns were packed with Luna C18 resin (Phenomenex). The mass spectrometer was operated in data-dependent mode, with the Orbitrap operating at 70,000 FWHM and 17,500 FWHM for MS and MS/MS respectively. The fifteen most abundant ions were selected for MS/MS.
Slesarev A., Viswanathan L., Tang Y., Borgschulte T., Achtien K., Razafsky D., Onions D., Chang A, & Cote C. (2019). CRISPR/Cas9 targeted CAPTURE of mammalian genomic regions for characterization by NGS. Scientific Reports, 9, 3587.
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7

Comparative Mass Spectrometry Analyses

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Mass spectrometric analyses were conducted twice with different method. Both methods are described below.

Method 1: The gel digest was analyzed by nano LC/MS/MS with a Waters NanoAcquity HPLC system interfaced to a Thermo Fisher Q Exactive. Peptides were loaded onto a trapping column and eluted over a 75 μm analytical column at 350 nl/min. Both columns were packed with Luna C18 resin (Phenomenex). The mass spectrum was operated in the data‐dependent mode, with MS and MS/MS performed in the Orbitrap at 70,000 FWHM resolution and 17,500 FWHM resolution, respectively. The fifteen most abundant ions were selected for MS/MS.

Method 2: The gel digest was analyzed by nano LC/MS/MS with an AMR Zaplous nanoHPLC system interfaced to a Thermo Fisher Orbitrap ELITE. Peptides were loaded onto a trapping column and eluted over a 200 μm analytical column at 1 μl/min. Both columns were packed with L‐column2 C18 resin (CERI). The mass spectrum was operated in the data‐dependent mode, with MS performed in the Orbitrap at 240,000 FWHM resolution and MS/MS used the linear ion trap mode. The seven most abundant ions were selected for MS/MS.

Nishida K.M., Sakakibara K., Sumiyoshi T., Yamazaki H., Mannen T., Kawamura T., Kodama T, & Siomi M.C. (2020). Siwi levels reversibly regulate secondary piRISC biogenesis by affecting Ago3 body morphology in Bombyx mori. The EMBO Journal, 39(20), e105130.
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8

Rodent Proteome Profiling by Nano LC-MS/MS

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A 2 μg aliquot was analyzed by nano LC/MS/MS with a Waters NanoAcquity HPLC system interfaced to a Thermo Fisher Fusion Lumos. Peptides were loaded on a trapping column and eluted over a 75 μm analytical column at 350 nL/min; both columns were packed with Luna C18 resin (Phenomenex). A 4-h gradient was employed. The mass spectrometer was operated in data-dependent mode, with MS and MS/MS performed in the Orbitrap at 60,000 FWHM resolution and 15,000 FWHM resolution, respectively. APD was turned on. The instrument was run with a 3-s cycle for MS and MS/MS. The acquisition order was randomized. Data Processing Data were processed through the MaxQuant software v1.6.2.3 (www.maxquant.org). Data were searched using Andromeda with the following parameters: Enzyme: Trypsin, Database: Uniprot Rat, Fixed modification: Carbamidomethyl (C), Variable modifications: Oxidation (M), Acetyl (Protein N-term), Fragment Mass Tolerance: 20 ppm Pertinent. MaxQuant settings were: Peptide FDR 0.01 Protein FDR 0.01 Min. peptide Length 7 Min. razor + unique peptides 1 Min. unique peptides 0 Min. ratio count for LFQ 1 Second Peptidesˆ TRUE Match Between Runs∗ TRUE.
Zlatic S.A., Duong D., Gadalla K.K., Murage B., Ping L., Shah R., Fink J.J., Khwaja O., Swanson L.C., Sahin M., Rayaprolu S., Kumar P., Rangaraju S., Bird A., Tarquinio D., Carpenter R., Cobb S, & Faundez V. (2022). Convergent cerebrospinal fluid proteomes and metabolic ontologies in humans and animal models of Rett syndrome. iScience, 25(9), 104966.
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9

Quantitative Proteomics of CORL23 Cells

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DDA analysis of CORL23 cell lines was performed by MS Bioworks (Ann Arbor, MI). DDA experiments were carried out using half of each enriched sample by nano LC-MS/MS using a Waters M-Class system interfaced to a ThermoFisher Fusion Lumos mass spectrometer. Peptides were loaded on a trapping column and eluted over a 75-μm analytical column at 350 nl/min; both columns were packed with Luna C18 resin (Phenomenex). A 2 h reverse phase gradient was employed. The mass spectrometer was operated in a combined data-dependent EThcD/CID mode, with MS and MS/MS performed in the Orbitrap at 60,000 FWHM resolution and 15,000 FWHM resolution, respectively. The instrument was run with a 3-s cycle for MS and MS/MS. DDA data were processed with PEAKS X+ version 10.5 with 10 ppm parent mass tolerance, 0.02 Da fragment mass error tolerance, and no enzyme specificity. Data were searched against the SwissProt Human proteome appended with the custom KRAS peptide sequences. Peptide 8-16V (VVGAVGVGK) and 7-16V (VVVGAVGVGK) identifications were confirmed with analysis of synthetic peptide standards (New England Peptide).
Bear A.S., Blanchard T., Cesare J., Ford M.J., Richman L.P., Xu C., Baroja M.L., McCuaig S., Costeas C., Gabunia K., Scholler J., Posey AD J.r., O’Hara M.H., Smole A., Powell DJ J.r., Garcia B.A., Vonderheide R.H., Linette G.P, & Carreno B.M. (2021). Biochemical and functional characterization of mutant KRAS epitopes validates this oncoprotein for immunological targeting. Nature Communications, 12, 4365.
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10

Nano LC-MS/MS Proteomics Analysis

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2μg of each digested sample was analyzed by nano LC-MS/MS with a M-Class HPLC system (Waters, Milfrod, MA) interfaced to a ThermoFisher Fusion Lumos mass spectrometer (Waltham, MA). Peptides were loaded on a trapping column and eluted over a 75μm analytical column at 350nL/min; both columns were packed with Luna C18 resin (Phenomenex, Torrance, CA). A 3-hour gradient was employed. The mass spectrometer was operated in data-dependent mode, with the Orbitrap operating at 60,000 FWHM and 15,000 FWHM for MS and MS/MS respectively. APD was enabled and the instrument was run with a 3 second cycle for MS and MS/MS.
Biesterveld B.E., Pumiglia L., Iancu A., Shamshad A.A., Remmer H.A., Siddiqui A.Z., O’Connell R.L., Wakam G.K., Kemp M.T., Williams A.M., Pai M.P, & Alam H.B. (2020). Valproic Acid Treatment Rescues Injured Tissues After Traumatic Brain Injury. The journal of trauma and acute care surgery, 89(6), 1156-1165.
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