ATF6 Rabbit pAb
ATF6 Rabbit pAb
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- 文献引用 : 1
- 实验流程
- 背景知识
Application
| WB, IHC-P, IHC-F, IF |
|---|---|
| Primary Accession | P18850 |
| Reactivity | Rat, Human, Mouse |
| Predicted | Pig, Rabbit, Horse |
| Host | Rabbit |
| Clonality | Polyclonal |
| Calculated MW | 74585 Da |
| Physical State | Liquid |
| Immunogen | KLH conjugated synthetic peptide derived from human ATF6 |
| Epitope Specificity | 301-400/670 |
| Isotype | IgG |
| Purity | affinity purified by Protein A |
| Buffer | 0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol. |
| SUBCELLULAR LOCATION | Endoplasmic reticulum membrane; Single-pass type II membrane protein. Processed cyclic AMP-dependent transcription factor ATF-6 alpha: Nucleus. Note=Under ER stress the cleaved N-terminal cytoplasmic domain translocates into the nucleus. |
| Important Note | This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications. |
| Background Descriptions | 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 also interacts 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. |
| Gene ID | 22926 |
|---|---|
| Other Names | Cyclic AMP-dependent transcription factor ATF-6 alpha, cAMP-dependent transcription factor ATF-6 alpha, Activating transcription factor 6 alpha, ATF6-alpha, Processed cyclic AMP-dependent transcription factor ATF-6 alpha, ATF6 |
| Dilution | WB=1:500-2000,IHC-P=1:100-500,IHC-F=1:100-500,ICC/IF=1:100-500,IF=1:100-500,Flow-Cyt=1 µg /test |
| Storage | Store at -20 °C for one year. Avoid repeated freeze/thaw cycles. When reconstituted in sterile pH 7.4 0.01M PBS or diluent of antibody the antibody is stable for at least two weeks at 2-4 °C. |
For Research Use Only. Not For Use In Diagnostic Procedures.
| Name | ATF6 |
|---|---|
| Function | [Cyclic AMP-dependent transcription factor ATF-6 alpha]: Precursor of the transcription factor form (Processed cyclic AMP- dependent transcription factor ATF-6 alpha), which is embedded in the endoplasmic reticulum membrane (PubMed:10564271, PubMed:11158310, PubMed:11779464). Endoplasmic reticulum stress promotes processing of this form, releasing the transcription factor form that translocates into the nucleus, where it activates transcription of genes involved in the unfolded protein response (UPR) (PubMed:10564271, PubMed:11158310, PubMed:11779464). |
| Cellular Location | Endoplasmic reticulum membrane; Single-pass type II membrane protein. Golgi apparatus membrane; Single-pass type II membrane protein. Note=Translocates from the endoplasmic reticulum to the Golgi, where it is processed. |
| Tissue Location | Ubiquitous.. |
Research Areas

Application Protocols
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
REFERENCES
Zhu C.,et al.Mol. Cell. Biol. 17:4957-4966(1997).
Yoshida H.,et al.J. Biol. Chem. 273:33741-33749(1998).
Gregory S.G.,et al.Nature 441:315-321(2006).
Hai T.,et al.Genes Dev. 3:2083-2090(1989).
Hai T.,et al.Genes Dev. 4:682-682(1990).
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