Dehydrin (affinity purified)

272 €
Buy 2 items of this product for 202 €/each
Buy 3 items of this product for 185 €/each

AS07 206A | clonality: polyclonal | host: rabbit | reactivity: higher plants


36 st
Item No:
AS07 206A

Info: Product suggestions Add review
product information

Dehydrins are stress proteins involved in formation of plant protective reactions against dehydration. They are normally synthesized in maturating seeds during their dessication, as well as in vegetative tissues of plants treated with abscisic acid or exposed to environmental stress factors that result in cellular dehydration.


KLH-conjugated peptide sequence (K-segment) from dehydrin C terminal conserved in a wide range of plant species including Nicotiana tabacum BAD1349

Host Rabbit
Clonality Polyclonal
Purity Affinity purified serum in PBS, pH 7.4
Format Lyophilized in PBS pH 7.4
Quantity 50 ĩg
Reconstitution For reconstitution add 50 ĩl 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

AS07 206 | anti-dehydrin rabbit antibody

AS10 206S | Dehydrin blocking peptide

collection of antibodies to plant stress proteins

Additional information
application information
Recommended dilution 1 : 1000 (WB)
Expected | apparent MW

9-200 kDa

Confirmed reactivity Brassica oleracea, Pinus sylvestris
Predicted reactivity Glycine max, Hordeum vulgare, Nicotiana tabacum, Oryza sativa, Pisum sativum, Populus sp., Zea mays
Not reactive in No confirmed exceptions from predicted reactivity are currently known.
Additional information
Selected references

to be added when available

application example

western blot using affinity purified anti-dehydrin antibodies

Line C2- 10 µg of Brassica oleracea mitochondrial proteins (C2- plants grown in severe drought conditions) isolated as described by Rurek et al., 2015 (doi: 10.1016/j.bbabio.2015.01.005) were separated by 12% SDS-PAGE and electroblotted in semi-dry conditions (Towbin buffer) to Immobilon-P membrane (Millipore). Blots were CBB R 250 briefly stained, destained, wet-scanned and after completed destaining, they were blocked in 5% skimmed milk (dissolved in PBS-T containing 0.1% Tween 20) in 1h, RT. Primary antisera (at 1: 1000, diluted in 2% skimmed milk in PBS-T) were bound by overnight incubation of blots at 4°C. After blot washing (2 times quick, 2 times of 5 min, and 10 min at the end), secondary goat anti-rabbit IgGs, HRP- conjugated (Agrisera product AS09 602; at 1: 50000, diluted in 2% milk/ PBS-T) were bound in 1 h, RT. Blots were washed (as above) with copious amounts of PBS-T and chemiluminescence signals acquired by using standard ECL reagents on RTG film between 3 s and 2 min (periods of the given image acquisition were indicated).

western blot using anti-dehydrin antibodies on nuclear fraction

In the nuclear fraction of Arabidopsis thaliana, few HMW proteins immunoreactive with anti-dehydrin anstiserum were also detected. The differences between their abundance in WT and 9-11 lines could be, however, ascribed to the actual protein loading on the blot. Experimental procedure was conducted as above.

Lines WT and 9-11- ca. 20 µg of proteins enriched in nuclear fraction from Arabidopsis thaliana leaf rosettes (WT- wild type; 9-11- T-DNA insertion mutants for h2a.z gene encoding particular histon H2A.Z isoform) were resolved by SDS-PAGE and HMW (high-molecular weight) proteins immunoreactive with dehydrin antisera were analysed. After separation, proteins were electroblotted and immunodetected essentially in the same manner as it was indicated above.

Application of WT/9-11 blot was possible due to the courtesy of  the Department of Biotechnology (Institute of Molecular Biology and Biotechnology, Faculty of Biology, Adam Mickiewicz University in Poznań). All remaining blots as well as all immunodetection assays were prepared by Dr Michał Rurek (Department of Molecular and Cellular Biology of the same Institute). 

||| For other applications, usage on species other than stated above or any other questions, please use the LiveChat option or contact us at