Anti-PsbH | Small subunit H of PSII

Application example

2 µg of total protein from (1) Arabidopsis thaliana leaf extracted with Protein Extration Buffer, PEB (AS08 300), (2) Hordeum vulgare leaf extracted with PEB, (3) Chlamydomonas reinhardtii total cell extracted with PEB, (4) Synechococcus sp. 7942 total cell extracted with PEB, (5) Anabaena sp. total cell extracted with PEB were separated on 4-12% NuPage (Invitrogen) LDS-PAGE and blotted 1h to PVDF. Blots were blocked immediately following transfer in 2% ECL Advance blocking reagent in 20 mM Tris, 137 mM sodium chloride pH 7.6 with 0.1% (v/v) Tween-20 (TBS-T) for 1h at room temperature with agitation. Blots were incubated in the primary antibody at a dilution of 1: 10 000 for 1h at room temperature with agitation. The antibody solution was decanted and the blot was rinsed briefly twice, then washed once for 15 min and 3 times for 5 min in TBS-T at room temperature with agitation. Blots were incubated in secondary antibody (anti-rabbit IgG horse radish peroxidase conjugated) diluted to 1:50 000 in 2% blocking solution for 1h at room temperature with agitation. The blots were washed as above and developed for 5 min with chemiluminescent detection reagent according the manufacturers instructions. Images of the blots were obtained using a CCD imager (FluorSMax, Bio-Rad) and Quantity One software (Bio-Rad). Exposure time was 1 second.

This product can be sold containing ProClin if requested

The PsbH protein was originally named 10- or 9-kDa phosphoprotein in higher plant chloroplasts. It is encoded by the plastome in algae and higher plants. PsbH is also present in cyanobacteria, where it exhibits 56% amino acid identity with the corresponding protein from Arabidopsis. The protein contains 63–90 amino acids, depending on the species, with molecular masses between 7.0 and 9.9 kDa.
PsbH is an intrinsic membrane protein with a single transmembrane helix and its N-terminal region has been suggested to be exposed to the stromal side of the thylakoid membrane. Presence of PsbH already present in etiolated tissue can indicate that the protein may be involved in early stages of PSII assembly.
Obtained biochemical data from PSII complexes isolated from spinach suggest that PsbH, together with other PSII phosphoproteins, may be required for D1 protein turnover by regulating dimeric and monomeric PSII transition through their phosphorylation and dephosphorylation.