HSP70 | Heat shock protein 70 (mitochondrial)
AS08 347 | Clonality: Polyclonal | Host: Rabbit | Reactivity: Arabidopsis thalian, Brassica oleracea, Hordeum vulagre
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73 | 70 kDa
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25 μg of Arabidopsis thaliana leaf extract and 15 μg)Arabidopsis thaliana mitochondrial fraction were separated on 10% gel and blotted on nitrocellulose membrane using wet transfer (0.22% CAPS, pH 11). Filters where blocked (1.5h) in 5% milk in TBST (1X TBS, 0,1% Tween 20), incubated with 1: 1000 anti-HSP70 mitochondrial antibodies (2h in TBST) followed by incubation with 1: 10 000 secondary anti-rabbit (1h) HRP-coupled antibodies and visualized with standard ECL on Kodak autoradiography film for 15-60 s. Mitochondria were isolated as described by Urantowka et al. (Plant Mol Biol, 2005, 59:239-52). Mitochondrial pellets were suspended in 1X Laemmli buffer (5% beta-mercaptoetanol, 3.7% glycerol, 1.1% SDS, 23 mM Tris- HCl pH 6.8, 0.01% bromophenol blue), heated (95°C, 5 min.) and centrifuged (13 000rpm, 1 min.). Leaf extracts were prepared as described by Martinez-Garcia et al. (Plant J., 1999, 20:251-7).
Heat-shock protein 70 (Hsp70) is the major stress-inducible protein in vertebrates and is highly conserved throughout evolution. It plays a role as a molecular chaperone and is important for allowing cells to cope with acute stressor insult, especially those affecting the protein machinery. Heat shock cognate protein 70 (HSC70), is a highly conserved protein and a member of the family of molecular chaperones.
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