Dear all,

 

Recently I am secretely expressing an ectodomain of a human membrane protein in 
insect cells. The expression level is moderately high but the target band in 
the SDS-PAGE gel seems smearing and this is cosistent with the western blot 
results. Does it result from the heterogeneous glycosylation of the protein? My 
protein contains quite a lot of N and O linked polysaccharide chains and they 
are important for the function of the protein. Does the heterogeneously 
glycosylated protein affect the crystallization? Does anyone have the 
experience of crystallizing such kind of glycoprotein?

 

Thanks in advance!

 

 

Ru Heng

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