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MDFI was significantly hypermethylated in colorectal cancer tissues when compared with adjacent normal colorectal tissues.
I-mfa domain proteins may be involved in their oncogenic functions by negatively regulating their transcriptional activities.
I-mfa functions as a molecular switch to suppress the store dependence of TRPC1 (zeige TRPC1 ELISA Kits)
These results suggest that the physical and functional interaction between Zic (zeige ZIC1 ELISA Kits) and I-mfa proteins can play a role in the vertebrate development.
This protein is a transcription factor that negatively regulates other myogenic family proteins. Studies of the mouse homolog, I-mf, show that it interferes with myogenic factor function by masking nuclear localization signals and preventing DNA binding. Knockout mouse studies show defects in the formation of vertebrae and ribs that also involve cartilage formation in these structures.
myoD family inhibitor
, MyoD family inhibitor
, inhibitor of MyoD family a
, myogenic repressor I-mf