Pathological a-syn aggregation is mediated by glycosphingolipid chain length and the physiological state of a-synuclein in vivo

Published: 3 December 2021| Version 1 | DOI: 10.17632/nwf89s4y8p.1
Joseph Mazzulli


This data set includes the raw western blot data for main and supplemental figures to accompany Fredriksen et al, PNAS 2021. Please see the main publication for details. Non-specific and/ or irrelevant bands that could not be validated to react with the protein of interest are indicated by an asterisk. Dashed-line boxes indicate the area used for the main figures in the main publication. Cropped out areas of the blot were either blank, or contained validated non-specific bands (identified by SNCA knock-out lysate). We use a multi-channel western blot detection system that permits simultaneous detection of rabbit and mouse secondary antibodies on the same blot. The channels are indicated in the figure as either 700 or 800, corresponding to excitation wavelength in nanometers. Many blots were sequentially probed by multiple antibodies for efficiency purposes, and some images therefore contain residual signals from previous antibody probes. Coomassie images refer to the gel that was used to match with the transferred blots.


Steps to reproduce

please see methods section of main publication.


Western Blot