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You said "a lack of ubiquitination leads to accumulation of Nrf2 in the nucleus, leading to activation of Nrf2 dependent genes". This makes sense to me, but it still does not explain why, in the nuclear compartment, only the 100 kDa bands shows up. Is there an explanation for this, or is this still not clearly known?
Asked on Jul 09 2014
I believe that the Nrf2 that does enter the nucleus is acetylated and phosphorylated, which will make the protein run more slowly through the SDS PAGE gel, making its apparent molecular weight seem larger than based on theoretical amino acid sequence alone.
As is noted in the Q&A from April 24 2013:
"phosphorylation of Ser-40 by PKC in response to oxidative stress dissociates NFE2L2 from its cytoplasmic inhibitor KEAP1, promoting its translocation into the nucleus by similarity. And acetylation at Lys-596 and Lys-599 increases nuclear localization"
Jeremy KasanovAbcam Scientific Support
Answered on Jul 09 2014