{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070201/checksum.txt"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070201/LL2092_HKHP_p1p12.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070201/LL2092_250pg_wet.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070201/LL2092_RAW_p3p4.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070201/LL2092_250pg_dry.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070201/Search_Result.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070201/LL2092_HYEAB.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["ryan.kelly@byu.edu"],"submitter":["Ryan Kelly"],"technology_type":["Mass Spectrometry","Bottom-up proteomics","Data-independent acquisition"],"software":[""],"submitter_keywords":["Nanolc-ms/ms","288 spd","High-throughput scp","5-min cycle time"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD070201"],"sample_protocol":["Single-Cell Isolation: The single-cell sample preparation followed the protocol published previously. In brief, single-cell dispensing was performed into DDM-treated 384-well PCR plates using the Tecan UNO dispenser (Männedorf, Switzerland). During dispensing, size-based gating was applied with a diameter range of 15–17 µm for HeLa cells and 12–14 µm for both K562 and RAW264.7 cells. Plates were centrifuged at 380 ×g immediately following dispensing to ensure cells were driven to the bottom of each well. HeLa and K562 cells were dispensed to the same plate. Each plate contained 100 HeLa cells and 100 K562 cells, and a total of two plates were analyzed by LC/MS. As for RAW 264.7 cells, 100 cells for each control and lipopolysaccharide treated group were sorted to the same plate.   Digestion: Immediately after isolation of all cell types, wells containing single cells were subjected to in-well proteolytic digestion69. A 200 nL volume of digestion solution was dispensed into each well using the Tecan UNO dispenser. The digestion mix consisted of 10 µL of 0.2 ng/nL Rapid Trypsin/Lys-C (Promega, Cat# V507C) in Resuspension Buffer (Promega, Cat# V181A), 10 µL of 1% DDM in Rapid Digest Buffer (Promega, Cat# VA106A), and 180 µL of Rapid Digest Buffer, resulting in final concentrations of 10 ng/µL Trypsin/Lys-C and 0.05% DDM. This corresponds to an enzyme-to-substrate (E:S) ratio of 10:1, assuming ~200 pg of total protein per cell. The digest mix solution was also dispensed into empty wells for the purpose of reagent blanks. Plates were centrifuged, sealed with a silicone mat, wrapped in aluminum foil, and incubated in a humidified oven at 70°C for 1 hour. After digestion, plates were cooled to 4 °C for 15 min., sealed with aluminum sealing foil, and stored at −20°C until LC-MS/MS analysis.  HeLa Digest standard was prepared using Pierce™ HeLa Protein Digest Standard (ThermoFisher, Ref# 88329). Dilutions were prepared at 10 ng/µL and 5 ng/µL for library creation, and at 250 pg/µL with 0.1% formic acid for system evaluation.  The HeLa Digest standard was also prepared at 1.25 ng/µL and dispensed with the D100 HP dispenser at 200 nL per well to DDM-treated 384-well plates for the evaluation of sample recovery following reconstitution.   K562 Digest Standard was prepared from Promega MS-Compatible Human Digest (Promega, V6951) and diluted to 10 ng/uL with 0.1% Formic Acid to 10n/uL for library creation.   HYE Digest Standard: The HYE mixture (Human, Yeast, and E. coli peptides) was prepared using Pierce™ HeLa Protein Digest Standard (ThermoFisher, Ref# 88329), Yeast protein extract (Promega, Cat# V7461), and MassPREP™ E. coli Digest Standard (Waters, Part#186003196). Two mixtures were prepared: HYE A and HYE B. For HYE A, 100 µL each of the three components—HeLa, Yeast, and E. coli digests were combined, yielding final concentrations of 20 ng/µL, 9.23 ng/µL, and 1.54 ng/µL, respectively. HYE B was prepared similarly, with final concentrations of 20 ng/µL, 4.62 ng/µL, and 6.15 ng/µL, respectively. The solution was diluted to achieve a final HeLa component concentration of 10 ng/µL for library creation and 250 pg/µL for system evaluation.  Multicolumn nanoLC setup: The multicolumn LC system was constructed as described previously. The trap columns (100 μm i.d. × 35 mm long and packed with 3.5 µm diameter media having 100 Å pores), analytical columns (30 μm i.d. × 50 mm long; 1.7 µm diameter, 100 Å C18 particles) and emitters (10 μm i.d.) were purchased from MicrOmics Technologies, LLC (Spanish Fork, UT). Mobile phase A and B were LC-MS-grade water with 0.1% formic acid and acetonitrile with 0.1 % formic acid (Honeywell, Charlotte, NC).  Mass Spectrometry  The evaluation of carryover was performed using Orbitrap Exploris 480 mass spectrometer (Thermo Fisher Scientific). The ion transfer tube temperature was set as 250 ℃ and the spray voltage was set as 2.1 kV. Full scan was applied in positive ionization mode with m/z ranging from 375-975 at 120K resolution. Injection time was set to 22 ms and AGC target was set to 300%. The RF lens was set as 50%. MS/MS scan mode was DIA with isolation window set to 16 Th for m/z range of 400-800 to generate 25 scan events. HCD collision energy was 30% with AGC set at 2000% and injection time set to auto.  The analysis of 250 pg HeLa digests, HYE and all single-cell samples were performed on the Orbitrap Astral mass spectrometer (Thermo Fisher Scientific, San Jose, CA). FAIMS was applied with the carrier gas flow set at 3.5 L/min and CV set at -45 V. The ion transfer tube temperature was set as 250 ℃. Full scan was applied with m/z ranging from 400-800 at 240K resolution. Injection time was 100 ms and AGC target was 500%. RF lens was 45%. MS/MS scan range was set as 150–2000 with DIA isolation window set to 8 Th, generate 49 scan events. Normalized HCD collision energy was 25% with AGC set to800% and maximum injection time set to 12 ms."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["All MS raw files were identified and quantified using DIA-NN 1.9 with Human, Mouse, Yeast, and Ecoli UniProt protein database downloaded in December 2024 through MSConnect73 at near-real-time to monitor system stability.  The data reported in this study were processed using Spectronaut (v19.8) directDIA+ workflow, using the same UniProt protein database that was used for MSConnect. Trypsin/Lys-C was specified as the digestion enzyme, with a peptide length range of 7–52 amino acids and up to two missed cleavages. A maximum of five modifications were allowed per peptide, including fixed carbamidomethylation and variable modifications such as protein N-terminal acetylation and methionine oxidation. The false discovery rate for PSMs, peptides, and protein groups was controlled at 1%. Quantification was performed at the MS1 level, and cross-run normalization was disabled.    Five Spectronaut projects were created to organize and analyze the datasets. The HeLa digest standard project included 250 pg, 5 ng, and 10 ng inputs injected directly, while a second project analyzed 250 pg HeLa digests prepared by the reconstituted injection mode. The third project contained HYE Mix A and B at 250 pg, 5 ng, and 10 ng input levels to benchmark quantification accuracy across known organismal ratios. The fourth project included single-cell HeLa and K562 analyses, reagent blanks, and 10 ng digests from each cell type for reference. The final project analyzed RAW 264.7 macrophages under control and LPS-treated conditions, supplemented with 10 ng bulk digests to generate a spectral library. In all projects, the larger-input runs (5–10 ng) were used to improve protein identification for the low-input (pg-level and single-cell) datasets.   Downstream data analysis and visualization were performed using in-house Python scripts. Protein-level data were filtered to exclude entries with more than 33% missing values, and intensity values were median-normalized within each group."],"omics_type":["Proteomics"],"labhead":["Ryan T. Kelly"],"instrument_platform":[""],"labhead_affiliation":["Department of Chemistry and Biochemistry, Brigham Young University, Provo, Utah 84602, United States"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)","Mus Musculus (mouse)"],"publication":["Not available"],"submitter_mail":["ryan.kelly@byu.edu"],"submitter_affiliation":["Brigham Young University"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"High-Throughput Label-free Single-Cell Proteomics Enabled by Multicolumn NanoLC with a 5-min Cycle Time","description":"Mass spectrometry (MS)-based single-cell proteomics (SCP) enables proteome-wide analysis at single-cell resolution, offering insights into cellular heterogeneity, biological processes, and disease mechanisms. However, conventional nanoLC-MS workflows are constrained by long gradients and low throughput, limiting their application to large cohorts. Here, we present a multicolumn nanoLC–MS platform that achieves 5-minute separation windows with 100% duty cycles at ~100 nL/min, enabling the analysis of up to 288 single cells per day with minimal additional hardware. The system provides stable peptide separation, negligible carryover, and robust retention-time reproducibility across 2,000 consecutive injections. Over the course of this study, we successfully analyzed more than 4,000 samples with ~288 samples per day (SPD) throughput. The platform identified ~4,400 proteins per 250 pg digest injection and an average of ~3,200 proteins per single HeLa cell with maxima exceeding 4,300, which is comparable to state-of-the-art longer-gradient workflows. Quantitative benchmarking with mixed-species standards confirmed accurate measurements across ~6,000 proteins. The workflow distinguished proteomic profiles across hundreds of single cells and, importantly, profiling of RAW264.7 macrophages revealed LPS-induced markers and macrophage activation pathways. Together, these results establish a robust and scalable platform for high-throughput SCP, demonstrating the feasibility of thousands of single-cell analyses within a single study while maintaining deep proteome coverage and biological interpretability.","dates":{"publication":"2026-05-21","submission":"2025-11-03"},"accession":"PXD070201","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:1131","NEWT:35795","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NEWT:1334565","NEWT:625351","NEWT:258594","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:247480","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:475174","NEWT:1599","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:12215","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:1596","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NEWT:1748418","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:3767","NEWT:1589","NEWT:135622","NEWT:4615","NEWT:672127","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:3760","NEWT:1584","NEWT:36630","NEWT:1585","NEWT:383379","NEWT:381198","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:7719","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:224308","NEWT:3347","NEWT:49928","NEWT:3349","NEWT:160621","NEWT:2502409","NEWT:212790","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:370038","NEWT:498211","NEWT:345076","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:1310173","NEWT:200795","NEWT:2579791","NEWT:44685","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:260499","NEWT:410661","NEWT:329854","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:2649329","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NCBITaxon:37162","NEWT:270643","NEWT:3715","NEWT:2065263","NEWT:177437","NEWT:717966","NEWT:10891","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:28174","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:244366","NEWT:1246791","NEWT:176597","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:926571","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2499525","NEWT:2853422","NEWT:1122984","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:45972","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:1502","NEWT:128017","NEWT:2836","NEWT:376686","NEWT:237610","NEWT:95486","EFO:0001352","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:987059","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:1509","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1579","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:1922344","NEWT:108458","NEWT:5936","NEWT:85692","NEWT:321967","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:279010","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:415978","NEWT:1255228","NEWT:410289","NEWT:191701","NEWT:373153","NEWT:1640278","NEWT:9054","NEWT:472","NEWT:940825","NEWT:29459","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:41122","NEWT:5911","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:11723","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166314","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:3726","NEWT:906914","NEWT:81231006","NEWT:30455","NEWT:28141","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:548","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:2126348","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:542","NEWT:2903","NEWT:185579","NEWT:872227","NEWT:13076","NEWT:2587410","NEWT:207340","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:2126337","NEWT:550","NEWT:10804","NEWT:33941","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:9995","NEWT:575412","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:6493","NEWT:10832","NEWT:6494","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