When I look at the SDS-page pattern of alpha synuclein in some studies its band appears higher (around 17 KD) than the real place of its molecular weight (14.4 KD). However, our purified protein appears at around 15 KD. The sequence is OK and N-terminal also was analyzed and it is OK too. Dr.Sidhu in "Abnormal migration of human wild-type -synuclein upon gel electrophoresis" showed that ASN migrated in SDS-PAGE unusually, so why would our protein migrate and appear in its real position?
Thank you for answering the question, but my problem is that our protein (purified alpha synuclein) migratesnormally but in other studies it migrates less and localize in upper position( near 17 KD)
Hi Dina
may they choose another acrylamide percentage ???
do you have the same tag ??? may they have bigger tag ??
also alpha-syn undergo a lot of post-translational modefication which can infleunce its migration on Gel
Thank you Sleman. In all reports it was expressed in E.coli which has not high PTM activity
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