Anti-ATF6 antibody (ab22280)
- Storage instructionsShipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
- Storage bufferPreservative: 0.025% Sodium Azide
Constituents: 50% Glycerol, Whole serum
- PurityWhole antiserum
- Clonality Polyclonal
- Research Areas
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||ELISA: 1/100 - 1/1000.|
- 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.
- Tissue specificityUbiquitous.
- 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.
- Activating transcription factor 6 alpha antibodyActivating transcription factor 6 antibodyATF 6 antibody
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References for Anti-ATF6 antibody (ab22280)
ab22280 has not yet been referenced specifically in any publications.