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{{/_source.additionalInfo}}Anti-DHAR1 | Dehydroascorbate Reductase 1
(Cat#: AS11 1746)
Description
- Immunogen: KLH-conjugated synthetic peptide derived from known DHAR1 sequence of Arabidopsis thaliana Q9FWR4, At1g19570
- Host: Rabbit
- Clonality: Polyclonal
- Purity: Immunogen affinity purified serum in PBS pH 7.4.
- Format: Lyophilized
- Quantity: 200 µg
- Reconstitution: For reconstitution add 200 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 the tubes briefly prior to opening them to avoid any losses that might occur from material adhering to the cap or sides of the tube.
- Tested applications: Western blot (WB)
- Recommended dilutions: 1 : 5000 (WB)
- Expected | apparent MW: 23.6 | 23.4 kDa
- Confirmed reactivity: Arabidopsis thaliana, Kandelia candel, Solanum lycopersicum
- Not reactive in: No confirmed exceptions from predicted reactivity are currently known
- DHAR1 ( Dehydroascorbate Reductase 1) the protein is induced by jasmonic acid and oxidative chemical stresses and is a key component of the ascorbate recycling system. Involved in redox homeostasis under biotic and abiotic inducers. Localized in mitochondria. Synonymes: glutathione-dependent dehydroascorbate reductase 1, chloride intracellular channel homolog 1, CLIC homolog 1, glutathione-dependent dehydroascorbate reductase 1, AtDHAR1, GSH-dependent dehydroascorbate reductase 1, mtDHAR, AT1G19570.
- Szymańska et al. (2019). SNF1-Related Protein Kinases SnRK2.4 and SnRK2.10 Modulate ROS Homeostasis in Plant Response to Salt Stress. Int J Mol Sci. 2019 Jan 2;20(1). pii: E143. doi: 10.3390/ijms20010143.Witzel et al. (2017). Temporal impact of the vascular wilt pathogen Verticillium dahliae on tomato root proteome. J Proteomics. 2017 Oct 3;169:215-224. doi: 10.1016/j.jprot.2017.04.008.Wang et al. (2014). Proteomic analysis of salt-responsive proteins in the leaves of mangrove Kandelia candel during short-term stress. PLoS One. 2014 Jan 8;9(1):e83141. doi: 10.1371/journal.pone.0083141. eCollection 2014.
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