AtpH | ATP synthase subunit c, chloroplastic
AS05 071 | Clonality: Polyclonal | Host: Rabbit | Reactivity: A. thaliana, S. oleracea, N. benthamina, T. elongatus
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1: 1000 - 1: 10 000 (WB)
|Expected | apparent MW||
8 kDa (for Arabidopsis thaliana)
Arabidopsis thaliana, Nicotiana benthamina, Spinacia oleracea, Thermosynechococcus elongatus
dicots including Glycine max, Pisum sativum, Vitis vinifera, monocolts indlucing Oryza sativa, Zea mays, trees: Populus alba, Pinus thunbergii, moss: Physcomitrella patens, green algae
|Not reactive in||
no confirmed exceptions from predicted reactivity known in the moment
Note that increased incubation at 95ºC (20-30 min) prior to loading is recommended to break the multimeric c-mer structure, detection of partial ring structures (e.g. 5 or 6 subunits) may occur.
|Selected references||Nath et al. (2016). A Nitrogen-Fixing Subunit Essential for Accumulating 4Fe-4S-Containing Photosystem I Core Proteins. Plant Physiol. 2016 Dec;172(4):2459-2470. Epub 2016 Oct 26.
Lawrence et al. (2010). Recombinant production and purification of the subunit c of chloroplast ATP synthase. Protein Expression and Purification 76: 15-24.
0.7 μg of purified ATP-synthase complex from Spinacia oleracea (CF0F1) (1), 15.3 µg of purified ATP-synthase complex (CF0F1) from Nicotiana benthamiana (2) and 48.6 µg of Thermosynechococcus elongatus thylakoid preparation (3) were separated on 12% polyacrylamide gel and blotted on PVDF membrane. Filters where blocked (0.5h), incubated with 1: 1000 anti-AtpH antibodies (1h), followed by incubation with 1: 5 000 secondary anti-rabbit antibody (1.25h), coupled to HRP and visualized with standard ECL.
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