Thermo Fisher LTQ Orbitrap XL & Orbitrap XL Mass Spectrometry
- Make Thermo Fisher
- Hertz 60Hz US
- Model LTQ LTQ XL & Orbitrap XL
- Serial 01725B-BTD, ETD10355
- Weight 1367.0 Lb
- Voltage 230V
- Warranty 30-Day Warranty, 100% Parts and Labor
- Dimensions 77.0in x 50.0in x 67.0in
- Shipping Type FedEx Ground
- Item Condition Excellent
- Manufacturing Date Does Not Apply
Product Information
Introducing the Thermo Fisher LTQ Orbitrap XL & Orbitrap XL, the ultimate solution for proteomics analyses. This powerful instrument combines CID, HCD, and ETD fragmentation techniques with Orbitrap technology. Delivering exceptional mass accuracy, resolving power, and high sensitivity, this reliable system is the instrument of choice for proteomics and small-molecule research. With outstanding MSn capability and complementary information generation, it's ideal for PTM analyses and de novo sequencing. Manufactured to exacting specifications, it offers resolution, mass range, and dynamic range that's remarkable, making it a vital asset for confident detection, identification, and characterization in the laboratory setting. Please note minor cosmetic damage to the left side of the unit.
Key Features- CID, HCD, and ETD fragmentation techniques
- Outstanding mass accuracy and resolving power
- High sensitivity and MSn capability
- Resolution: 60000 (FWHM) @ m/z 400 with a scan repetition rate of 1 second
- Mass Range: m/z 502000 - m/z 2004000
- Mass Accuracy: <3 ppm RMS for 2 h period with external calibration using defined conditions
- Dynamic Range: >10000 between mass spectra, >4000 between highest and lowest detectable mass in one spectrum
Metric: 1367 kg
Imperial: 3014 lbs
Metric: 77 cm x 50 cm x 67 cm
Imperial: 30.31 in x 19.69 in x 26.38 in
9027200000
Harmonized Code DetailsThe harmonized code 9027200000 is chosen based on the equipment's primary function as a mass spectrometry apparatus used in laboratory and scientific research. This equipment falls under this category due to its highly specialized functions and specifications related to ion separation, accurate mass measurement, and data interpretation in proteomics and small-molecule research.
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