Proteomics & Protien Expression

MALDI-MS Analysis of Proteins

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Selected Protocol from "Proteins and Proteomics: A Laboratory Manual", Richard J. Simpson.

General Method for MALDI-MS Analysis of Proteins and Peptides

David Frecklington
Joint Proteomics Laboratory (JPSL)
Ludwig Institute for Cancer Research
Walter and Eliza Hall Institute of Medical Research
Melbourne, Australia


For MALDI-TOF-MS analysis of proteins and peptides, samples are cocrystallized with an excess of organic matrix that absorbs at a specific wavelength (usually, UV 337nm). Typically, sinapinic acid (SA) is the matrix of choice for large proteins, whereas {alpha}-cyano-4-hydroxy-cinnamic acid (HCCA) is the preferred matrix for peptide mapping. Following a short laser pulse, analytes are protonated and desorbed into the gas phase, and their m/z values are determined in a TOF mass analyzer. Mass accuracy determinations vary from ±0.01% to 0.1% depending on the sample preparation technique and the method used for mass calibration.

Products Available for this Protocol
Protocol Material Description Product #  Product Name Add to Cart
Buffers, Solutions, and Reagents      
Methanol M1775 Methanol, Absolute - Acetone free
TFA T6508 Trifluoroacetic acid, reagent grade
n-octyl glucoside O8001 Octyl β-D-glucopyranoside
Standards Peptide and protein standards for mass spectrometry analysis
MALDI-MS matrices Matrices for MALDI Analysis


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