The largest database of trusted experimental protocols

Easy nlc 1200 nano uhplc

Manufactured by Thermo Fisher Scientific

The EASY-nLC 1200 nano-UHPLC is a liquid chromatography system designed for high-performance separation of nanoscale samples. It features a nano-flow pump capable of delivering precise flow rates from 50 nL/min to 2 μL/min. The system is optimized for coupling with mass spectrometry instrumentation for sensitive and high-resolution analysis of complex samples.

Automatically generated - may contain errors

6 protocols using easy nlc 1200 nano uhplc

1

Peptide Analysis by LC-MS/MS

Check if the same lab product or an alternative is used in the 5 most similar protocols
Peptides were resuspended in water with 0.1 % formic acid (FA) and analyzed using EASY-nLC 1200 nano-UHPLC coupled to Q Exactive HF-X Quadrupole-Orbitrap mass spectrometer (Thermo Scientific). The chromatography column consisted of a 40 cm long, 75 μm i.d. microcapillary capped by a 5 μm tip and packed with ReproSil-Pur 120 C18-AQ 2.4 μm beads (Dr. Maisch GmbH). LC solvents were 0.1 % FA in H2O (Buffer A) and 0.1 % FA in 90 % MeCN: 10 % H2O (Buffer B). Peptides were eluted into the mass spectrometer at a flow rate of 300 nL/min. over a 240 min. linear gradient (5–35 % Buffer B) at 65°C. Data were acquired in data-dependent mode (top-20, NCE 28, R = 7’500) after full MS scan (R = 60’000, m/z 400–1’300). Dynamic exclusion was set to 10 s, peptide match to prefer and isotope exclusion was enabled.
+ Open protocol
+ Expand
2

Nano-UHPLC-MS/MS Protocol for Peptide Analysis

Check if the same lab product or an alternative is used in the 5 most similar protocols
Samples were analyzed on an Easy nLC-1200 nano UHPLC (Thermo Fisher Scientific) coupled online via a Nanospray Flex electrospray ion source (Thermo Fisher Scientific) equipped with a column oven (Sonation) to a Q-Exactive HF mass spectrometer (Thermo Fisher Scientific). An amount of 1.3 µg of peptides was separated on self-packed C18 columns (300 mm × 75 µm, ReproSilPur 120 C18-AQ, 1.9 µm; Dr Maisch) using a binary gradient of water (A) and acetonitrile (B) supplemented with 0.1% formic acid (gradient: 0 min, 2.4% B; 2 min, 4.8% B; 92 min, 24% B; 112 min, 35.2% B; 121 min, 60% B). Full mass spectrometry spectra were acquired at a resolution of 120,000 (automatic gain control target, 3 × 106). The 15 most-intense peptide ions were chosen for fragmentation by higher-energy collisional dissociation (resolution, 15,000; isolation width, 1.6 m/z; automatic gain control target, 1 × 105; normalized collision energy, 26%). A dynamic exclusion of 120 s was applied for fragment ion spectra acquisition. For EAE samples, two technical replicates were measured per sample.
+ Open protocol
+ Expand
3

Nano-UHPLC-MS/MS Peptide Analysis

Check if the same lab product or an alternative is used in the 5 most similar protocols
Peptides were resuspended in water with 0.1% formic acid (FA) and analyzed using EASY-nLC 1200 nano-UHPLC coupled to Q Exactive HF-X Quadrupole-Orbitrap mass spectrometer (Thermo Scientific). The chromatography column consisted of a 50 cm long, 75 μm i.d. microcapillary capped by a 5 μm tip and packed with ReproSil-Pur 120 C18-AQ 2.4 μm beads (Dr. Maisch GmbH). LC solvents were 0.1% FA in H2O (Buffer A) and 0.1% FA in 90% MeCN: 10% H2O (Buffer B). Peptides were eluted into the mass spectrometer at a flow rate of 300 nL/min over a 240 min linear gradient (5-35% Buffer B) at 65°C. Data were acquired in data-dependent mode (top-20, NCE 28, R = 7,500) after full MS scan (R = 60,000, m/z 400-1,300). Dynamic exclusion was set to 10 s, peptide match to prefer, and isotope exclusion was enabled.
+ Open protocol
+ Expand
4

Peptide Analysis by Nano-UHPLC-MS

Check if the same lab product or an alternative is used in the 5 most similar protocols
Peptides were resuspended in water with 0.1% formic acid (FA) and analyzed using EASY-nLC 1200 nano-UHPLC coupled to Q Exactive HF-X Quadrupole-Orbitrap mass spectrometer (Thermo Scientific). The chromatography column consisted of a 30 cm long, 75 μm i.d. microcapillary capped by a 5 μm tip and packed with ReproSil-Pur 120 C18-AQ 2.4 μm beads (Dr. Maisch GmbH). LC solvents were 0.1% FA in H2O (Buffer A) and 0.1% FA in 90% MeCN:10% H2O (Buffer B). Peptides were eluted into the mass spectrometer at a flow rate of 300 nL/min over a 240 min linear gradient (5–35% Buffer B) at 65 °C. Data were acquired in data-dependent mode (top-20, NCE 28, R = 7500) after full MS scan (R = 60000, m/z 400–1300). Dynamic exclusion was set to 10 s, peptide match set to prefer, and isotope exclusion was enabled.
+ Open protocol
+ Expand
5

Nano-UHPLC-MS/MS Peptide Analysis

Check if the same lab product or an alternative is used in the 5 most similar protocols
Peptides were resuspended in water with 0.1 % FA and analyzed using an EASY-nLC 1200 nano-UHPLC coupled to a Q Exactive HF-X Quadrupole-Orbitrap mass spectrometer (Thermo Scientific). The chromatography column consisted of a 50 cm long, 75 μm i.d. microcapillary capped by a 5 μm tip and packed with ReproSil-Pur 120 C18-AQ 2.4 μm beads (Dr. Maisch GmbH). LC solvents were 0.1 % FA in H2O (Buffer A) and 0.1 % FA in 90 % MeCN: 10 % H2O (Buffer B). Peptides were eluted into the mass spectrometer at a flow rate of 300 nL/min. over a 90 min linear gradient (5–35 % Buffer B) at 65 °C. Data was acquired in data-dependent mode (top-20, NCE 28, R = 15,000) after full MS scan (R = 60,000, m/z 400 – 1,300). Dynamic exclusion was set to 10 s, peptide match to prefer and isotope exclusion was enabled.
+ Open protocol
+ Expand
6

Targeted Proteomics Analysis of SPTSSB

Check if the same lab product or an alternative is used in the 5 most similar protocols
Peptides were resuspended in water with 0.1 % formic acid (FA) and analyzed using EASY-nLC 1200 nano-UHPLC coupled to Q Exactive HF-X Quadrupole-Orbitrap mass spectrometer (Thermo Scientific). The chromatography column consisted of a 40 cm long, 75 mm i.d. microcapillary capped by a 5 mm tip and packed with ReproSil-Pur 120 C18-AQ 2.4 mm beads (Dr. Maisch GmbH). LC solvents were 0.1 % FA in water (Buffer A) and 0.1 % FA in 90 % MeCN: 10 % water (Buffer B). Peptides were eluted into the mass spectrometer at a flow rate of 300 nL/minute over 240-minute linear gradient (5-35 % Buffer B) at 65 C. Data was acquired in data-dependent mode (top-20, NCE 30, R = 17'500) after full MS scan (R = 60'000, m/z 400-1'300). Dynamic exclusion was set to 10 seconds with peptide match set to prefer and isotope exclusion enabled. For targeted identification of the mouse SPTSSB protein, an inclusion list containing m/z and charge of the expected SPTSSB peptides and deactivated dynamic exclusion were used.
+ Open protocol
+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Sign up for free.
Registration takes 20 seconds.
Available from any computer
No download required

Sign up now

Revolutionizing how scientists
search and build protocols!