CPN60B1 antibody recognizes the Chaperonin 60 subunit beta 1 (CPN60B1), a member of the type I chaperonin family involved in protein folding within chloroplasts. Key details include:
Subunit Composition:
Protein Interactions: Binds RuBisCO large and small subunits during oligomer assembly .
The antibody exhibits broad cross-reactivity across plant species, validated by immunoblotting and immunofluorescence:
| Species | Tested Examples |
|---|---|
| Model Plants | Arabidopsis thaliana, Brassica napus, Glycine max, Solanum lycopersicum |
| Crops | Triticum aestivum (wheat), Hordeum vulgare (barley), Vitis vinifera (grape) |
Detects CPN60B1/B2 in chloroplasts under normal conditions .
Identifies heat-inducible nuclear translocation of cpn60-related proteins during stress (e.g., heat shock) in animal cells, suggesting conserved stress-response roles .
In fish cell lines, anti-cpn60 antibodies revealed nuclear accumulation of 57 kDa and 42 kDa proteins post-heat shock, distinct from stress70 family dynamics .
Implicates CPN60B1 in chaperoning nuclear protein assembly during stress .
Heat Shock Adaptation: Nuclear localization of cpn60 homologs during thermal stress suggests a conserved role in stress adaptation across kingdoms .
Antibody Specificity: Reacts with cpn60 isoforms but not TCP1 (cytoplasmic chaperonin), confirming target selectivity .