V-ATPase, A | Vacuolar H+-ATPase subunit A (ammonium sulfate purified IgG)
AS09 467 | Clonality: Polyclonal | Host: Rabbit | Reactivity: A. thaliana, M. crystallinum, N. tabacum
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68.8 | 70 kDa (Arabidopsis thaliana)
1 µg and 10 µg of crude membrane fraction/lane from Arabidopsis thaliana were separated on 12 % SDS-PAGE and blotted 1h to PVDF membrane (40 min. at 10 V using BioRad semidry transfer). Filters were blocked 1h with 5 % low-fat milk powder in TBS-T (0.05% Triton X.100). Membranes were washed 5 times with TBS-T, each time in a fresh polystyrene box and probed with anti-V-ATPase subunit A antibodies (AS09 467, 1:2000, 1h) and secondary anti-rabbit (1:2000, 1 h). All steps were performed in RT with agitation.
V-ATPase subunit A is a catalytic subunit of V1 complex of vacuolar ATPase. This enzyme (EC=184.108.40.206) is involved in acidification process of various compartements of eucaryotic cell. This protein is coded by VHA-A gene. Alternative names: Vacuolar proton pump subunit alpha, vacuolar H(+)-ATPase subunit A, V-ATPase 69 kDa subunit
Barkla et al. (2016). Single-cell-type quantitative proteomic and ionomic analysis of epidermal bladder cells from the halophyte model plant Mesembryanthemum crystallinum to identify salt-responsive proteins. BMC Plant Biol. 2016 May 10;16(1):110. doi: 10.1186/s12870-016-0797-1.
Yoshihiro et al. (2006) Immunochemical analysis of aquaporin isoforms in Arabidopsis suspension-cultured cells. Cells. Biosci.Biotechnol. Biochem. 70: 980-987.
Related products: V-ATPase, A | Vacuolar H+-ATPase subunit A (ammonium sulfate purified IgG)
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