Omix c18 10μl tips

Manufactured by Agilent Technologies

Sourced in United States

The OMIX C18 10μL tips are a type of laboratory equipment designed for precision pipetting tasks. They are made with a C18 coating and have a volume capacity of 10 microliters. These tips are intended for use in a variety of laboratory applications that require accurate and consistent liquid handling.

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Lab products found in correlation

Trypsin, by Promega (1 mentions) Rapigest sf, by Waters Corporation (1 mentions) Pierce bca protein assay kit, by Thermo Fisher Scientific (1 mentions) Edta free protease inhibitor cocktail, by Roche (1 mentions) Solu trypsin, by Merck Group (1 mentions) Hplc grade acetonitrile, by Thermo Fisher Scientific (1 mentions) Proteomics grade trypsin, by Merck Group (1 mentions) Bovine serum albumin (bsa), by Merck Group (1 mentions) Iodoacetamide, by Merck Group (1 mentions) Ammonium bicarbonate, by Thermo Fisher Scientific (1 mentions) Amicon ultra 3 kda centrifugal filters, by Merck Group (1 mentions) Dithiotreitol, by Merck Group (1 mentions) Formic acid, by Merck Group (1 mentions) Trypsin, by Thermo Fisher Scientific (1 mentions)

Spelling variants of this product

C18 OMIX tips (32 citations) OMIX C18 tips (25 citations) OMIX tips (6 citations)

4 protocols using omix c18 10μl tips

Trypsin Digestion and Peptide Cleanup

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Eluates (10μL) were incubated with 20μL reduction-alkylation buffer [50mM Tris-HCl, pH8.0, 2M Urea, 1mM Dithiothreitol (DTT), 3mM iodoacetamide (IAA)] in the dark at room temperature for 45 minutes. After quenching IAA with 3mM DTT, trypsin (Promega) was added to samples at a 1:100 enzyme:substrate ratio and incubated overnight at 37°C. Peptides were acidified with formic acid (1% final concentration) and desalted using OMIX C18 10μL tips (Agilent) following the manufacturer’s protocol. Briefly, tips were conditioned with 50% acetonitrile, 0.1% formic acid and sequentially equilibrated in two volumes of 0.1% formic acid before binding peptides. Bound peptides were sequentially rinsed in two volumes of 0.1% formic acid and eluted twice, first in 50% acetonitrile, 0.1% formic acid, and then in 90% acetonitrile, 0.1% formic acid. Elutions were combined, dried under vacuum centrifugation, and suspended in 12μL of 3.0% acetonitrile, 0.1% formic acid prior to mass spectrometry.

Batra J., Hultquist J.F., Liu D., Shtanko O., Dollen J.V., Satkamp L., Jang G.M., Luthra P., Schwarz T.M., Small G.I., Arnett E., Anantpadma M., Reyes A., Leung D.W., Kaake R., Haas P., Schmidt C.B., Schlesinger L.S., LaCount D.J., Davey R.A., Amarasinghe G.K., Basler C.F, & Krogan N.J. (2018). Protein interaction mapping identifies RBBP6 as a negative regulator of Ebola virus replication. Cell, 175(7), 1917-1930.e13.

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Protein Extraction and Digestion Protocol

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Cell pellets were lysed in 50 μl of 0.1% RapiGest SF (Waters) with repeated pipetting, vortexing, and probe sonication at 20 kHz. EDTA-free protease inhibitor cocktail (Roche) combined with Benzonase Nuclease (Fisher Scientific) was added prior to cell lysis to reduce proteolysis and digest nucleic acids. To remove cell debris, lysates were centrifuged at 16,000g and 4 °C for 10 min. Total protein of lysates was measured with Pierce BCA protein assay kit (Fisher Scientific). Proteins were denaturated, and disulfide bonds were reduced by 10 mM dithiothreitol at 70 °C for 15 min and alkylated with 20 mM iodoacetamide at room temperature (RT) in the dark for 45 min. Digestion was completed overnight at 37 °C using recombinant dimethylated SOLu-trypsin (Sigma-Aldrich) with a trypsin:protein ratio 1:20. Trifluoroacetic acid (1%) was added to cleave and precipitate RapiGest SF, and 1 μl of 0.4 M L-methionine was added to limit methionine oxidation during storage. OMIX C18 10 μl tips (Agilent Technologies) were used for desalting and microextraction of tryptic peptides. Finally, samples were diluted in 5% acetonitrile with 0.1% formic acid.

Fu Z., Rais Y., Bismar T.A., Hyndman M.E., Le X.C, & Drabovich A.P. (2021). Mapping Isoform Abundance and Interactome of the Endogenous TMPRSS2-ERG Fusion Protein by Orthogonal Immunoprecipitation–Mass Spectrometry Assays. Molecular & Cellular Proteomics : MCP, 20, 100075.

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Quantitative Proteomics Sample Preparation

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The reagents used in this study were as follows. Acetonitrile (HPLC grade) and ammonium bicarbonate were from Fisher Scientific (NJ, USA). Amicon^® Ultra 3KDa centrifugal filters and formic acid were from EMD Millipore (Merck KGaA, Darmstadt, Germany). Proteomics-grade trypsin, dithiotreitol, iodoacetamide, and bovine serum albumin (>98 % pure) were from Sigma-Aldrich (Oakville, ON, Canada). Proteomics-grade trypsin/lys-C mix was from Promega (Madison, WI, USA). Ultrapure grade urea was from Amresco (Solon, OH, USA). Ultrapure water was from Milli-Q (Millipore, Molsheim, France). Crude unlabeled, crude isotopically labeled (lysine: 6 × 13C, 2 × 15N, arginine: 8 × 13C, 2 × 15N) and purified isotopically labeled peptides were from JPT Peptide Technologies (Berlin, Germany). OMIX C18 10 μl tips were from Agilent Technologies (Lake Forest, CA, USA).

Konvalinka A., Batruch I., Tokar T., Dimitromanolakis A., Reid S., Song X., Pei Y., Drabovich A.P., Diamandis E.P., Jurisica I, & Scholey J.W. (2016). Quantification of angiotensin II-regulated proteins in urine of patients with polycystic and other chronic kidney diseases by selected reaction monitoring. Clinical Proteomics, 13, 16.

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Streptactin Protein Purification and Digestion

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Streptactin purified proteins were reduced and alkylated on beads with 20 uL reduction-alkylation buffer [50mM Tris-HCl, pH8.0, 2M Urea, 1mM Dithiothreitol (DTT), 3mM iodoacetamide] and incubated in the dark for 45 minutes with gentle shaking. An additional 3mM DTT was added to quench the reaction, and proteins were digested with 0.75μg trypsin (Invitrogen). Digests were allowed to proceed overnight at 37C.
The next day, the beads were pelleted by centrifugation at 300×g for 3 minutes. The peptide containing supernatant was removed using a gel-loading tip and transferred to a new tube. Formic acid was added to a final concentration of 1% to acidify the peptides. Peptides were desalted using Agilent OMIX C18 10μL tips according to the manufacturer’s protocol with the following modifications. Briefly, tips were conditioned with 50% acetonitrile, 0.1% formic acid and then equilibrated by two rinses with 0.1% formic acid. Peptides were bound by repeated pipetting, rinsed twice in 0.1% formic acid, and eluted in 50% acetonitrile. A second elution in 90% acetonitrile was used to ensure complete recovery. Peptides were dried under vacuum centrifugation and suspended in 12μL of 3.0% acetonitrile, 0.1% formic acid.

Rialdi A., Hultquist J., Morales D.J., Peralta Z., Campisi L., Fenouil R., Moshkina N., Wang Z.Z., Laffleur B., Michael R., Haas K., Pefanis E., Albrecht R.A., Pache L., Chanda S., Jen J., Ochando J., Byun M., Basu U., Garcia-Sastre A., Krogan N., van Bakel H, & Marazzi I. (2017). The RNA exosome syncs IAV-RNAPII transcription to promote viral ribogenesis and infectivity.. Cell, 169(4), 679-692.e14.

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