AtpH | ATP synthase subunit c, chloroplastic (100 ĩl)

355 €

AS09 591  |  Clonality: Polyclonal  |  Host: Rabbit  |  Reactivity: A. thaliana, C. reinhardtii


8 st
Item No:
AS09 591

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product information

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.


KLH-conjugated peptides derived from AtpH subunit c of Arabidopsis thaliana P56760, AtCg00140 and Chlamydomonas reinhardtii Q37304

Host Rabbit
Clonality Polyclonal
Purity Serum
Format Lyophilized
Quantity 100 µl
Reconstitution For reconstitution add 100 µl of sterile water.
Storage Store lyophilized/reconstituted at -20°C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please, remember to spin tubes briefly prior to opening them to avoid any losses that might occur from lyophilized material adhering to the cap or sides of the tubes.
Tested applications Western blot (WB)
Related products

AS08 370 | anti-ATP synthase whole enzyme

AS08 304 | anti-ATP synthase subunit alpha

AS05 085 | anti-ATP synthase subunit beta

AS08 312 | anti-ATP synthase subunit gamma antibody

Plant protein extraction buffer

Secondary antibodies

Additional information
application information
Recommended dilution 1 : 10 000 (WB)
Expected | apparent MW

8 kDa (for Arabidopsis thaliana)

Confirmed reactivity Arabidopsis thaliana, Chlamydomonas reinhardtii
Predicted reactivity

Algae, Cannabis sativa, Glycine max,  Hordeum vulgare, Oryza sativa, Ostreococcus tauri, Physcomitrella patens, Pinus thunbergii, Pisum sativum, Populus alba,  Zea mays, Vitis vinifera

Not reactive in No confirmed exceptions from predicted reactivity are currently known.
Additional information Please 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 Schulz et al. (2017). Molecular architecture of the N-type ATPase rotor ring from Burkholderia pseudomallei. EMBO Rep. 2017 Apr;18(4):526-535. doi: 10.15252/embr.201643374.

application example

10 ug of chlorophyll/well of Chlamydomonas reinhardtii total cell extract (1), Chlamydomonas reinhardtii subunit gamma deletion mutant thylakoid membrane fraction (2), Arabidospsis thaliana thylakoid membrane fraction (3), Chlamydomonas reinhardtii thylakoid membrane preparation (4) were separated on 12-18% acrylamide-8M urea gel and blotted to nitrocellulose membrane. Filters were blocked 1 h with 5% dry milk in 1 x PBS and probed with anti-ATP synthase subunit c antibody (AS09 591, 1: 10 000, 1h) and secondary HRP-conjugated anti-rabbit antibody (1: 10 000, 1 h) in 1 x PBS containing 5% dry milk. All steps were performed at RT with agitation. Signal was detected with standard ECL (GE Healthcare), exposure time 30’’.

Arabidopsis membrane preparation has been done according to Lezhneva et al. (2008) A novel pathway of cytochrome c biogenesis is involved in the assembly of the cytochrome b6f complex in arabidopsis chloroplasts. J Biol. Chem., 283:24608-24616 and Chlamydomonas membranes were prepared according to Chua & Bennoun (1975) Thylakoid membrane polypeptides of Chlamydomonas reinhardtii: wild-type and mutant strains deficient in photosystem II reaction center. PNAS 72:2175-2179

Courtesy Dr. Yves Choquet


western blot using anti-AtpH antibodies

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