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SRPK2 generally never migrates at its predicted molecular weight (MW) due to post-translational modifications including, but not limited to, phosphorylation. The ~70 kDa band observed by the total antibodies is likely the C-terminal cleavage product. The SRPK2 protein is cleaved at D139 and D403, allowing the N-terminal fragments to travel to the nucleus. Please refer to Figure 3 in this article for more information. Notably, C-terminal phosphorylation of SRPK2 at T492 by Akt seems to prevent this cleavage, so it is uncommon to observe any of the lower MW fragments using a C-terminal phospho-specific SRPK2 antibody.