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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Purified c subunit from Spinacia oleracea UniProt: P69447.
8 kDa (for Arabidopsis thaliana)
Algae, Cannabis sativa, Glycine max, Oryza sativa, Physcomitrella patens, Pisum sativum, Populus alba, Pinus thunbergii, Zea mays, Vitis vinifera
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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 chemiluminescence detection reagent.
This product can be sold containing proclin if requested.
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.
F-type ATPase (ATP synthase) is the universal enzyme that synthesizes ATP from ADP and phosphate using the energy stored in a transmembrane ion gradient. Multiple copies of the c subunit build up the ring structure (in spinach a 14-mer of ~112 kDa) of the membrane bound Fo-part of the enzyme.
Lawrence et al. (2010). Recombinant production and purification of the subunit c of chloroplast ATP synthase. Protein Expression and Purification 76: 15-24.
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