Characterization
Description(s):ER stress (UPR) response is governed by three transmembrane sensors: PERK, IRE1 and ATF6. These stress sensors control a complex ER-to-nucleus signaling pathway that transmits information across the ER membrane to an extensive gene-expression program. Two major transcription factors for UPR are ATF4 and ATF6. Both ATF4 and ATF6 belong to a basic leucine zipper ATF/CREB family, but have distinct functions UPR. ATF6 is a type II transmembrane ER protein that is activated by proteolytic cleavage. Active ATF6 translocates to the nucleus where it forms active homodimers or dimerizes with NF-Y and XBP1s and binds to promoter regions containing ATF/cAMP response elements (CREs) and/or ER Stress Elements (ERSE). ATF4 belongs to PERK-eIF2-ATF4 axis and regulates the expression of genes involved in amino acid biosynthesis and transport functions, antioxidant stress responses, and apoptosis. ATF4 induces both pro-survival (early) and pro-apoptotic (late) transcriptional programs. Prolonged or extreme ER stress uses ATF4 to upregulate proapoptotic protein C/EBP homologous protein (CHOP). To distinguish the function of ATF4 and ATF6 in ER stress, Signosis has developed ATF4 /ATF6 ELISA kit for detecting and comparing ATF4 and ATF6 DNA binding activities for human, mouse and rat samples.
Applicable Grid:
ATF4 and ATF6 ELISA Kits Available:
Principle
TF ELISA kit is high sensitive and specific assay with a simple and optimized procedure. The 96-well (8X12 strip) clear plate is pre-immobilized with the TF consensus sequencing oligo. The activated TF in nuclear extract or the whole cell lysate is added in the well and binds to the oligo. The activated TF is detected with a specific antibody against the subunit and a HRP conjugated secondary antibody. The assay utilizes colorimetric detection method, which can be easily measured by spectrophotometry.
Literature
View user manual| 1. The Lipophilic 4‐Phenylbutyric Acid Derivative Prevents Aggregation and Retention of Misfolded Proteins. Azoulay-Ginsburg, Salome, et al. Chemistry – A European Journal, 2019, doi:10.1002/chem.201904292. |
