ATF6 Mouse anti-Human, Mouse, Rat, Clone: 3B7E4, Proteintech

Description

• The fully glycosylated form of ATF6, a 670 amino acid protein, exhibits an electrophoretic mobility of ∽90 kDa in denaturing SDS-gels, in part because of the glycosylated modifications
• ATF6 has 3 consensus sites for N-linked glycosylation and exists ATF6 is a transcription factor that acts during endoplasmic reticulum stress by activating unfolded protein response target genes
• It binds DNA on the 5′-CCAC[GA]-3′half of the ER stress response element (ERSE) (5′-CCAAT-N(9)-CCAC[GA]-3′) and of ERSE II (5′-ATTGG-N-CCACG-3′)
• Binding to ERSE requires binding of NF-Y to ERSE
• ATF6 could also be involved in activation of transcription by the serum response factor
• ATF6 exists as a homodimer and heterodimer with ATF6 beta
• The dimer interacts with the nuclear transcription factor Y (NF-Y) trimer through direct binding to NF-Y subunit C (NF-YC)
• It Interacts also with the transcription factors GTF2I, YY1 and SRF
• Under ER stress the cleaved N-terminal cytoplasmic domain translocates into the nucleus
• The basic domain of ATF6 functions as a nuclear localization signal and the basic leucine-zipper domain is sufficient for association with the NF-Y trimer and binding to ERSE
• During the unfolded protein response an approximately 50 kDa fragment containing the cytoplasmic transcription factor domain is released by proteolysis
• The cleavage seems to be performed sequentially by site-1 and site-2 proteases
• ATF6 is N-glycosylated, phosphorylated in vitro by MAPK14/P38MAPK and belongs to the bZIP family.