Product nameActive human ATF6 peptide
See all ATF6 proteins and peptides
Amino Acid Sequence
Our Abpromise guarantee covers the use of ab39927 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Preparation and Storage
Stability and Storage
Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
Preservative: 0.02% Sodium Azide
Constituents: 0.1% BSA, PBS, pH 7.2
This product is an active protein and may elicit a biological response in vivo, handle with caution.
- Activating transcription factor 6
- Activating transcription factor 6 alpha
- ATF 6
FunctionTranscription factor that acts during endoplasmic reticulum stress by activating unfolded protein response target genes. 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. Could also be involved in activation of transcription by the serum response factor.
Sequence similaritiesBelongs to the bZIP family. ATF subfamily.
Contains 1 bZIP domain.
DomainThe basic domain functions as a nuclear localization signal.
The basic leucine-zipper domain is sufficient for association with the NF-Y trimer and binding to ERSE.
modificationsDuring unfolded protein response an approximative 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.
N-glycosylated. The glycosylation status may serve as a sensor for ER homeostasis, resulting in ATF6 activation to trigger the unfolded protein response (UPR).
Phosphorylated in vitro by MAPK14/P38MAPK.
Cellular localizationEndoplasmic reticulum membrane and Nucleus. Under ER stress the cleaved N-terminal cytoplasmic domain translocates into the nucleus.
- Information by UniProt
ab39927 has not yet been referenced specifically in any publications.