FKBP16-4 (FK506-binding protein 16-4) is a chloroplastic peptidyl-prolyl cis-trans isomerase (PPIase) belonging to the immunophilin family. It plays a role in protein folding and stress responses within plant chloroplasts. The FKBP16-4 antibody is a specialized tool designed to detect and study this protein in plant biology research, particularly in species like Arabidopsis thaliana and related homologs .
The FKBP16-4 antibody is primarily used in Western Blot to study:
Stress responses linked to peptidyl-prolyl isomerase activity, which facilitates conformational changes in target proteins .
Evolutionary studies across plant species, leveraging its cross-reactivity with homologs in Panicum and Oryza .
FKBP16-4 localizes to chloroplasts, where it aids in maintaining proteostasis under stress conditions .
Its enzymatic activity is critical for chloroplast function, though substrate specifics remain under investigation .
FKBP16-4 is part of the FKBP family, which broadly regulates:
Stress adaptation in organelles, particularly under oxidative or thermal stress .
Chloroplast development, inferred from its homology to other plant immunophilins .
Structural Role: FKBP16-4’s PPIase domain enables conformational switching in client proteins, essential for chloroplast enzyme activation .
Redundancy: Like other FKBPs, FKBP16-4 may work redundantly with cyclophilins to ensure robust protein folding in plant cells .
Antibody Validation: Optimal dilution ranges (1:1000–1:2000) and blocking conditions (5% skim milk) are critical for reducing background noise .
Limitations: Predicted cross-reactivity requires empirical validation in non-Arabidopsis species .
Substrate Identification: Proteomic studies to map FKBP16-4 interaction networks.
Stress Response Pathways: Elucidating its role in abiotic stress (e.g., drought, salinity) using knockout models.