HSP101 | ClpB heat shock protein, C-terminal
AS08 287 | Clonality: Polyclonal | Host: Rabbit | Reactivity: A. thaliana, A. tequilana, Citrus sp., C. sativus
|Datasheet||Product citations||Protocols||Customer reviews|
prepare a leaf extract from a leaf without stress and one that has been heat stressed as follows: Take a whole leaf (in the case of plants with small leaves, like Arabidopsis thaliana), or part of a leaf and place on wet filter paper in a petri dish. Heat stress in the dark at 38°C/90 minutes to 2 hours and then allow to recover for 2 hours at room temperature in low light (leave it on the lab bench). You should be able to load 10 ug for western blotting and compare the non-heat stressed to the heat stressed sample.
Use Arabidopsis thaliana leaf as a positive control. Following such treatment 1 ug of a total protein from Arabidopsis thaliana allows detection of HSP101.
Hsp101/ClpB is a member of HSP100 protein family. These proteins help protein aggregates formed during heat stress to fall apart to allow them to be refolded by other chaperones. In spite of expression during heat stress members of HSP100 protein family are also expressed during seed development.
McLoughlin et al. (2016) Class I and II Small Heat Shock Proteins Together with HSP101 Protect Protein Translation Factors during Heat Stress. Plant Physiol. 2016 Oct;172(2):1221-1236.
Janicka-Russak et al. (2013). Modification of plasma membrane proton pumps in cucumber roots as an adaptation mechanism to salt stress. J Pant Physiol. March 14.
Janicka-Russak et al. (2012). Different effect of cadmium and copper on H+-ATPase activity in plasma membrane vesicles from Cucumis sativus roots. J. Exp. Botany, March 2012, ahead of print.