BZIP17 is a membrane-associated basic leucine zipper (bZIP) transcription factor activated through proteolytic cleavage during stress responses . Antibodies targeting BZIP17 are critical for:
Detecting proteolytic processing: Western blot analyses reveal cleavage events under salt or ER stress, with full-length (~70 kDa) and processed (~50 kDa) forms observed .
Subcellular localization tracking: Immunofluorescence and GFP-tagged studies show ER-to-nucleus translocation post-activation .
Chromatin immunoprecipitation (ChIP): Used to identify genome-wide targets, as demonstrated in heat-stressed MYC-bZIP17 transgenic plants .
Co-regulation with bZIP28/bZIP60: Shares 132/133 targets with bZIP28 but shows distinct activation kinetics .
Antagonism with NPR1: BZIP17-mediated UPR suppresses salicylic acid pathways during pathogen responses .
Processing assays: Antibodies distinguish between full-length (ER-localized) and cleaved (nuclear) forms .
Mutant controls: No signal detected in bzip17 knockout lines .
Tag-based validation: Epitope tags (MYC/GFP) enable antibody cross-verification in transgenic lines .
Functional redundancy: Partial overlap with bZIP28 complicates phenotype interpretation in single mutants .
Post-translational focus: Transcript levels remain stable under stress, necessitating protein-level antibody assays .
Species cross-reactivity: Limited data exist for non-Arabidopsis systems, though homologs are implicated in Catharanthus roseus and Boea hygrometrica .