A number of degradation products may be observed when using anti-PsbA antibodies, including products having apparent molecular weights of 24kDa and 16kDa. D1 degradation is a complex set of events and the products observed can be influenced by both the extraction procedure and the physiology of the cells prior to harvest. Third, cross-linking may occur between D1 and cytochrome b559, shifting the protein higher in the gel. In cyanobacteria (PCC7942), three different bands are competed out by preincubating the antibody with the PsbA free peptide, indicating that all bands are indeed PsbA and its precursors or breakdown products. Competition assays are also performed with spinach and Chlamydomonas, confirming the identity of PsbA bands. Anti-PsbA antibodies will not detect D2 protein, as the peptide used to generate PsbA antibodies has no homology to the D2 sequence.Example of a simulataneous western blot detection with RbcL, PsbA and PsaC antibodies.,The antibody is appropriate for detecting both, 24 kDa or the 10 kDa C-terminal fragments, whichever is generated under given treatment conditions.In our analysis we have seen both, ca. 24 kDa and ca. 10 kDa fragments from different samples, depending on treatments and isolation procedures. This antibody will also detect the phosphorylated form of D1as an alternate band to the main band on a high resolution gel.
The PsbA (D1) protein of photosystem II cycles rapidly under light in all oxygen-containing photoorganisms. Disruption of the PsbA cycle, or loss of the PsbA pool, is at the heart of photosynthetic photoinhibition in cyanobacteria, algae, and plants under a variety of conditions, including excessive light, low temperature, and UV exposure. Tracking PsbA pools with Global PsbA antibodies can reveal the functional content of photosystem II in a wide range of samples.
For research use only, not for clinical use.