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Read our guarantee »Products:Epigenetics and Nuclear Signaling >> Transcription >> Domain Families >> HLH / Leucine Zipper >> Leucine Zipper
Anti-ATF6 antibody
See all ATF6 products (8) ...
Rabbit polyclonal to ATF6
ELISAmore details
Reacts with
Mouse, Rat, Human
Synthetic peptide: EVERTKSRRMTNNQQKTRI, corresponding to amino acids 491-509 of Human ATF6.
EVERTKSRRM TNNQQKTRI
Liquid
Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
Preservative: 0.025% Sodium Azide
Constituents: 50% Glycerol, Whole serum
Whole antiserum
Polyclonal
IgG
Epigenetics and Nuclear Signaling >> Transcription >> Domain Families >> HLH / Leucine Zipper >> Leucine Zipper
Our Abpromise guarantee covers the use of ab22280 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
ELISA: 1/100 - 1/1000.
Transcription 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.
Ubiquitous.
Belongs to the bZIP family. ATF subfamily.
Contains 1 bZIP domain.
The 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.
During 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.
Endoplasmic reticulum membrane and Nucleus. Under ER stress the cleaved N-terminal cytoplasmic domain translocates into the nucleus.
Target information above from: UniProt accessionP18850
The UniProt Consortium
The Universal Protein Resource (UniProt) in 2010
Nucleic Acids Res. 38:D142-D148 (2010).
ab22280 has not yet been referenced specifically in any publications.
Publishing research using ab22280? Please let us know so that we can cite the reference in this datasheet
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