The ATF6 endoplasmic reticulum (ER) stress-regulated transcription factor is constitutively expressed and plays a central role in the mammalian unfolded protein response (UPR). This fundamental pathway is responsible for balancing cellular homeostasis under stressful conditions resulting from environmental or physiological perturbations. The ATF6 molecule is anchored in the endoplasmic reticulum (ER) membrane when in its inactive form. Under conditions when a conversion to the ATF6 active form is required, ATF6 translocates to the Golgi and is cleaved by the S1P and S2P proteases. This intramembrane proteolytic event enables the translocation of the activated, N-terminal ATF6 component to the nucleus, where it continues the downstream cascade by binding to ER stress-response elements within ER stress-response genes (ERSRGs).
Western Blot: ATF6 Antibody (70B1413.1) [NBP1-40256] - Analysis of ATF6 in NIH3T3 cell lysate using NBP1-40256 at 3 ug/ml. A band corresponding to full-length ATF6 was detected. We have not characterized the ~36 kDa observed band; it may be an ATF6 breakdown/cleavage product.
Xu's group from the Wolfson Institute published in Nature Cell Biology their data using the ATF6 antibody to examine nitric oxide (NO) signaling within the generalized ER stress response (1). They determined that NO-dependent disruption of mitochondrial respiration affects calcium flux, ATF6 cleavage, and subsequent ATF6 nuclear translocation. Park et al used the ATF6 antibody to probe the role of glucose deprivation role in tumor growth in vivo, and found that the UPR pathway can be targeted and disrupted by a macrocyclic compound versipelostatin in glucose-deprived solid tumors (2). Further studies from the Imperial College with the ATF6 antibody suggest that the tumor-specific downstream UPR-target gene Grp78 could be exploited as a systemic cancer gene therapeutic (3). Their work highlights the use of a dual tumor targeting phage targeting the Grp78 promoter that is versatile for not only gene therapy but also for molecular imaging. The ATF6 antibody was used by Toko's group to monitor pathological and physiological conditions affecting the heart (4). They determined that ATF6 activation triggered by a myocardial infarction (MI) serves to protect injured tissue as well as maintain cardiac function. Immunoblotting with the ATF6 antibody enabled neuropathologists to identify a novel interaction between ER overload and aging dementia, where detrimental polymerization and accumulation of the protein FENIB occurs if the UPR pathway is compromised or suppressed (5).
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