Glycoprotein
Is it possible that glycosylation of proteins may not be accurately measured by Refeyn? The actual protein size is approximately 490 kDa, but with glycosylation, the molecular weight significantly increases to around 750 kDa. However, when we measure it, the values are consistently in the range of 530-580 kDa. This seems to differ quite a bit from the expected value, making it hard to consider it within the margin of error. I would appreciate your insight on this matter.
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Hi KIM,
If you are confident that the protein is heterogenous and heavily glycosylated then another option could be that the trimer may not be present in large quantities under the conditions used. Depending on the dissociation constant it may be that the trimer may not be forming at the protein concentration used for mass photometry with the dimer being primarily observed at around 500kDa.
Hope that helps.
Kind regards,
Team Refeyn