after purification i added lipid into it i got tetramer the i diluted the protein then also i not get any dimer or monomer but same experiment i did before i get dimer with same concentration
Do you have any expectation about the natural oligomerization state of this protein? Is it normally monomer, dimer, or tetramer in vivo? How are you measuring the oligomerization of the protein?
as others have said - how are you measuring oligomeric state? I'm sure we can then help you :)
From SDS gel it look like 4 time of Monomer
my protein is around 13.5 KDa and i seen band at around 50 KDa
Can you post a picture of your gel and what type of conditions you used for the SDS-PAGE (reducing, non-reducing, boiled, non boiled)?
Some proteins are resistant to denaturation in standard SDS-PAGE sampe buffers. An example is bacterial outer membrane beta-barrel proteins. For these, it is helpful to use SDS-urea gels.
Is it possible that your protein is highly glycosylated, leading to a higher molecular weight? If so, try treating it with PNGase F to deglycosylate N-linked carbohydrate.
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