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PeptideAtlas provides a multi-organism, publicly accessible compendium of peptides identified in a large set of tandem mass spectrometry proteomics experiments collected for human, mouse, yeast, and several other organisms.

(last updated: Nov 28, 2017)

Data or Model Molecule

46 Results - per page

AccessionSample TitleSummaryOrganismCharacteristicsInstrumentTreatmentGrowthDigestionExtractSeparationReference
PAe001361Kc-Wnt-a-dsh836_exp_082Kc-Wnt-a-dsh836_exp_082 Kc cellsLTQPMID:17450130
PAe001357Dm_S2_membrane_exp_024Dm_S2_membrane_exp_024 Hypotonic lysis of S2 cells. -Amount used for experiment: 2mg -Labeling buffer used: 1% RapiGestheavy ICAT only used for labeling -Enzyme: Trypsin-Separation: SCX (60 fractions)LTQPMID:17450130
PAe001374Dm_Lar_HL_exp_043Dm_Lar_HL_exp_043 Larvae from yw flies were pricked using a tungsten needle and and centrifuged into a eppendorf containing siliconized glass wool and frozen immediately. Total proteins were precipitated using ice-cold acetone and dissolved in labelling buffer (6M Urea, 50mM Tris/HCl pH 8.3, 0.05% SDS, 5mM EDTA). No ICAT labelling was done and these samples were purified using seppak clean up.LTQPMID:17450130
PAe001375Dm_S2_Nuclear_FFE_exp_053Dm_S2_Nuclear_FFE_exp_053 Hypotonic lysis of S2 cells, Nuclear fraction prepared by high salt extraction -Labeling buffer used: 6M Urea, 50mM Tris/HCl pH 8.3, 0.05% SDS, 5mM EDTA -Enzyme: Trypsin - Peptide FFE - No modification of cysteinesLTQPMID:17450130
PAe001376Dm_Kc_Gel_exp_066Dm_Kc_Gel_exp_066 Gelfiltration was done on a Superose 6 column (HR 10/30, Amersham-Pharmacia, Switzerland) controlled by an automatic fast protein liquid chromatography (FPLC) station (Amersham-Pharmacia) at room temperature. The column was equilibrated with a native buffer containing 150 mM NaCl, 1 mM DTT, 0.2 mM sodium-vanadate, 5mM EDTA, 1 g/ml Aprotinin (Sigma-Aldrich, Germany), and 50 mM Tris pH 7.2. The column was calibrated with Catalase (232 kDa), Albumine (67 kDa), Ovalbumin (43 kDa), Chymotrypsinogen (25 kDa), Ribonuclease A (15.6 kDa; all Amersham-Pharmacia), and Cytidin (Merk, Switzerland). Before loading onto the column cytosolic fractions were cleared of nucleic acids by precipitation with polyethyleneimine (Sigma-Aldrich, 0.1% w/v). 200 l of the cleared cytosolic fraction (1 mg/ml protein) was loaded onto the column and eluted at a flow rate of 0.3 ml/minute. Fractions of 0.6 ml calculated to be < 25 kDa were collected. The eluate was precipitated by trichloroacetic acid (50%), the pelleLTQPMID:17450130
PAe001378Dm_Lar_membrane_exp_038Dm_Lar_membrane_exp_038 Total larval extract prepared in RIPA buffer. 2-3g of the acetone precipitated extract was resuspended in 5mM TrisHCl, pH8.0 Overlayed with 48% sucrose, 28.5% Sucrose, 10% Sucrose and spun in an ultracentrifuge @21'000rpm in aTHSA64 rotor for 3h30min @ 4erlayed with 48% sucrose, 28.5% Sucrose, 10% Sucremoved diluted 1:1 with dH2O and pelleted by ultracentrifugation @21'000rpm in aTHSA64 rotor for 2h @ 4 28.5% Sucrose, 10% Sucrd 1x with dH2O (no resuspension).The pellet was resuspended in 1% RapiGest, 50mM Tris-HCl pH8.3, EDTA 5mM.The membranes (5-10 mg total) were labeled 1:1 using cleavable ICAT.LTQPMID:17450130
PAe001379Dm_Adult_Heads_Cytoplasm_exp_044Dm_Adult_Heads_Cytoplasm_exp_044 Adult: heads, cytoplasmic fractions (soluble proteins) -Enzyme: Trypsin1:1 labeling using cleavable ICAT -Separation: SCX (60 fractions) -Avidin colums was used. -Sample validation: The head fraction was inspected for contaminants through the microscope and contaminating parts were removed manually.-SepPack cleanup was doneLTQPMID:17450130
PAe001380Dm_Lar_IPG_exp_057Dm_Lar_IPG_exp_057 2 mg Proteins from yw larvae extracted by RIPA bufferTryptic digestRan on peptide IPG strips 3.4-4.8 (non liner gradient , 22cm, Amersham Pharmacia)LTQPMID:17450130
PAe001382Dm_Adult_Heads_Membrane_exp_025Dm_Adult_Heads_Membrane_exp_025 -Flies were frozen in liquid nitrogen and the heads were isolated by sieving. -Sample validation: The head fraction was inspected for contaminants through the microscope and contaminating parts were removed manually. Then hypotonic lysis as for the S2LTQPMID:17450130
PAe001383Dm_Lar_FB_suc_exp_027Dm_Lar_FB_suc_exp_027 Fatbodies were extracted by ultracentrifugation from 3rd Instar larvae -20% Sucrose treated ICAT-labeled using (heavy) normal (untreated) ICAT-labeled (light) -Amount used for experiment: 2mg per sample -Labeling buffer used: 8M Urea, 50mM Tris/HCl pH 8.3, 0.25% SDS, 5mM EDTA -Enzyme: Trypsin -Separation: SCX (60 fractions)Avidin column usedSepPack purification usedLTQPMID:17450130
PAe001384Dm_Emb_2hAEL_exp_030Dm_Emb_2hAEL_exp_030 embryos were collected for 20 minutes and aged for 1hour 30 minutes.Total extract from these embryos -Amount used for experiment: 2mg -Labeling buffer used: 6M Urea, 50mM Tris/HCl pH 8.3, 0.05% SDS, 5mM EDTA -Enzyme: Trypsin -Separation: SCX (60 fractions) -Avidin colums was used.-SepPack cleanup was doneLTQPMID:17450130
PAe001385Dm_Kc_N-Glyc_exp_041Dm_Kc_N-Glyc_exp_041 DrosophilaLTQPMID:17450130
PAe001386Dm_Lar_FB_rap_exp_028Dm_Lar_FB_rap_exp_028 Fatbodies were extracted by ultracentrifugation from 3rd Instar larvae -Rapamycin-treated ICAT-labeled using (light) -normal (untreated) ICAT-labeled (heavy) -Amount used for experiment: 2mg per sample -Labeling buffer used: 8M Urea, 50mM Tris/HCl pH 8.3, 0.25% SDS, 5mM EDTA -Enzyme: Trypsin -Separation: SCX (60 fractions)Avidin column usedSepPack purification usedLTQPMID:17450130
PAe001388Dm_Emb_0-24hAEL_exp_055Dm_Emb_0-24hAEL_exp_055 embryos were collected 0-24h AEL.Total extractCarbamido-methylation of cysLTQPMID:17450130
PAe001343Kc-Wnt-a-wg2026_exp_079Kc-Wnt-a-wg2026_exp_079 Kc cellsLTQPMID:17450130
PAe001340Dm_S2_cytoplasmic_exp_032Dm_S2_cytoplasmic_exp_032 Hypotonic lysis of S2 cells. -Amount used for experiment: 2mg -Labeling buffer used: 6M Urea, 50mM Tris/HCl pH 8.3, 0.05% SDS, 5mM EDTA -Enzyme: Trypsin -Separation: SCX (60 fractions)-Avidin columns was used.LTQPMID:17450130
PAe001341Dm_Adult_HL_exp_029Dm_Adult_HL_exp_029 Flies were punched with a needle and centrifuged on a glasswool cushion.The haemolymph (clear liquid) was collected at the bottom of the tube.60 SCX fractions; ICAT labelingAvidin usedSepPack cleanupLTQPMID:17450130
PAe001342Dm_Kc_exp_068Dm_Kc_exp_068 Kc cellsLTQPMID:17450130
PAe001344Dm_Adult_Heads_Cytoplasm_exp_015Dm_Adult_Heads_Cytoplasm_exp_015 -Strain: yw -Enzyme: Trypsin1:1 labeling using cleavable ICAT -Separation: SCX (60 fractions) -Avidin colums was used. -Sample validation: The head fraction was inspected for contaminants through the microscope and contaminating parts were removed manuaLTQPMID:17450130
PAe001347Dm_Lar_FFE_Protein_exp_061Dm_Lar_FFE_Protein_exp_061 Whole proetin extracts were prepared using RIPA buffer from 3rd Instar larvae -Amount used for experiment: 25mg per sample -Labeling buffer used: 1% Rapigest -No trypsin used -ICAT labelled-FFE - pH 4-7LTQPMID:17450130
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