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Chymotrypsin is widely used in shotgun proteomics owing to its orthogonal cleavage specificity relative to trypsin, which enhances sequence coverage of hydrophobic protein regions. However, commercial preparations often display variable cleavage specificity, trypsin contamination, and elevated misse...
ORGANISM(S): Homo sapiens (Human) 
2026-06-08 | PXD072165 | Pride
Quantitative determination of absolute and relative protein amounts is an essential requirement for most current bottom-up proteomics applications, but protein quantitation estimates are affected by several sources of variability such as sample preparation, mass spectrometric acquisition, and data a...
ORGANISM(S): Escherichia coli 
2014-07-30 | PXD001187 | Pride
Data from ProteomeXchange, PXD ID: PXD001187. Enzyme: LysC_Trypsin, file: 121219_S_CCES_01_03_LysC_Try_1to10_Mixt_1_3.mzXML. Published as part of J Proteome Res. 2014 Jul 28 . From the Abstract: {{i}} Here we evaluated both in-solution and filter-aided digestion protocols and assessed their influen...
ORGANISM(S): Enterobacteria_phage_13a_uid30603,enterobacteria_phage_933w_uid14043,enterobacteria_phage_alpha3_uid14570,enterobacteria_phage_ba14_uid30599,enterobacteria_phage_bp_4795_uid14287,enterobacteria_phage_bz13_uid14635,enterobacteria_phage_cdti_uid19737,enterobacteria_phage_ecods1_uid30601,enterobacteria_phage_eps7_uid29287,enterobacteria_phage_epsilon15_uid14285,enterobacteria_phage_es18_uid15174,enterobacteria_phage_felix_01_uid14323,enterobacteria_phage_fels_2_uid32273,enterobacteria_phage_fi_sensu_lato_uid15459,enterobacteria_phage_g4_sensu_lato_uid14318,enterobacteria_phage_hk022_uid14048,enterobacteria_phage_hk620_uid14115,enterobacteria_phage_hk97_uid14592,enterobacteria_phage_i2_2_uid14572,enterobacteria_phage_id18_sensu_lato_uid16628,enterobacteria_phage_id2_moscow_id_2001_uid16591,enterobacteria_phage_if1_uid14039,enterobacteria_phage_ike_uid14627,enterobacteria_phage_ime08_uid50177,enterobacteria_phage_jk06_uid15569,enterobacteria_phage_js10_uid38265,enterobacteria_phage_js98_uid27983,enterobacteria_phage_jse_uid38263,enterobacteria_phage_k1e_uid16228,enterobacteria_phage_k1f_uid15880,enterobacteria_phage_k1_5_uid17059,enterobacteria_phage_lambda_uid14204,enterobacteria_phage_m13_uid14549,enterobacteria_phage_min27_uid29143,enterobacteria_phage_ms2_uid14659,enterobacteria_phage_mu_uid14105,enterobacteria_phage_n15_uid14086,enterobacteria_phage_n4_uid18511,enterobacteria_phage_p1_uid14493,enterobacteria_phage_p22_uid14478,enterobacteria_phage_p2_uid14035,enterobacteria_phage_p4_uid14414,enterobacteria_phage_phi1_uid20789,enterobacteria_phage_phieco32_uid28729,enterobacteria_phage_phiecom_gj1_uid27979,enterobacteria_phage_phip27_uid14599,enterobacteria_phage_phiv10_uid16381,enterobacteria_phage_phix174_sensu_lato_uid14015,enterobacteria_phage_prd1_uid14062,enterobacteria_phage_psp3_uid14345,enterobacteria_phage_rb14_uid37825,enterobacteria_phage_rb16_uid51699,enterobacteria_phage_rb32_uid17997,enterobacteria_phage_rb43_uid15417,enterobacteria_phage_rb49_uid14301,enterobacteria_phage_rb51_uid37819,enterobacteria_phage_rb69_uid15141,enterobacteria_phage_rtp_uid16178,enterobacteria_phage_sf6_uid14498,enterobacteria_phage_sfv_uid14162,enterobacteria_phage_sp6_uid14291,enterobacteria_phage_ssl_2009a_uid34919,enterobacteria_phage_st104_uid14499,enterobacteria_phage_st64t_uid14230,enterobacteria_phage_st_1_uid38669,enterobacteria_phage_t1_uid14496,enterobacteria_phage_t3_uid14336,enterobacteria_phage_t4_uid14044,enterobacteria_phage_t5_uid15143,enterobacteria_phage_t7_uid14460,enterobacteria_phage_tls_uid19775,enterobacteria_phage_vt2_sakai_uid14480,enterobacteria_phage_wa13_sensu_lato_uid16595,enterobacteria_phage_wv8_uid38281,enterobacteria_phage_yyz_2008_uid32231,enterobacteriophage_qbeta_uid15479, Pxd001187, Escherichia_coli_k_12_substr__mg1655 
Plasma proteins were digested with trypsin and the resulting peptides were analyzed by nanoLC–MS/MS on an EASY-nLC 1200 system coupled to an Orbitrap Exploris 480 mass spectrometer. Peptides were loaded onto a self-packed C18 reversed-phase column (25 cm × 100 μm i.d.) and separated at 500 nL/min us...
ORGANISM(S): Homo sapiens (Human) 
2026-06-21 | PXD073684 | Pride
Reliable enzymatic digestion is crucial for successful mass spectrometry-based proteomics. This study compares the arginine-specific protease, GingisREX, with a traditional trypsin/lys-C mixture for identifying E. coli proteins. Using GingisREX resulted in more protein identifications due to fewer p...
ORGANISM(S): Escherichia coli 
2025-05-07 | PXD056345 | Pride
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