Anti-PsaL | PSI-L subunit of photosystem I

Application example

2 µg of total leaf protein of Arabidopsis thaliana (1) and Hordeum vulgare (2) and total cellular protein of Chlamydomonas reinhardtii (3) and Synechococcus PCC 7942 (4) isolated with PEB (AS08 300) were separated on 4-12% Nupage Bis-Tris gels in in MES running buffer (Invitrogen) at 200V for 35 minutes. Proteins were transferred for 80 minutes at 30V to a PVDF membrane pre-wetted in methanol and equilibrated in 1X transfer buffer. Blots were blocked immediately following transfer in 2% blocking reagent in 20 mM Tris, 137 mM sodium chloride pH 7.6 with 0.1% (v/v) Tween-20 (TBS-T) and probedwith anti-PsaL (AS06 148 1:1000) and secondary HRP-conjugated goat anti-rabbit antibody (1:50 000) for 1 hr in TBS-T containing 2% blocking reagent. Antibody incubations were followed by washings in TBS-T (15, +5, +5, +5 min). All steps were performed at RT with agitation. Signals was detected  using chemiluminescence detection reagent, according to the manufacturers instructions and a CCD imager (FluorSMax, Bio-Rad)

PsaL (PSI-L) is a conserved subunit of type I photosynthetic reaction centers (Photosystem I, PSI). PSI is an integral membrane multi-protein complex that catalyzes the electron transfer from plastocyanin (or cytochrome c6) to ferredoxin (or flavodoxin). Psa-L is binding pigments and has been shown to be involved in trimerization of PSI in cyanobacteria (but not in plants) and bind pigments in plants and cyanobacteria.In plants and algae Psa-L is nuclear encoded and imported post-translationally into the chloroplast where it inserts into the thylakoid membrane.