PrxQ | Peroxiredoxin, thioredoxin reductase
AS05 093 | Clonality: Polyclonal | Host: Rabbit | Reactivity: A. thaliana, M. esculenta, S. oleracea, Z. mays
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This product can be sold containing proclin if requested.
In stroma fractions a weak background reaction at 28 kDa is visible. No crossreactivity in any thylakoid fractions.
Peroxiredoxins (EC=22.214.171.124) belong to the enzyme family which is ubiquitous in all kingdoms of life. Prx Q enzyme acting by reducing hydroperoxides. Peroxiredoxins have no heme group, unlike the other peroxidases, but perform their enzymatic activity using cysteine residues with redox-active thiol groups. The ability of peroxiredoxins to hydrolyze hydroperoxides suggests that this protein family has a general function in oxidant defence.
Yoshida et al. (2016). Hisabori T1.Two distinct redox cascades cooperatively regulate chloroplast functions and sustain plant viability. Proc Natl Acad Sci U S A. 2016 Jul 5;113(27):E3967-76. doi: 10.1073/pnas.1604101113. Epub 2016 Jun 22.
Yoshida et al. (2015). Thioredoxin Selectivity for Thiol-Based Redox Regulation of Target Proteins in Chloroplasts. J Biol Chem. 2015 Apr 15. pii: jbc.M115.647545.
Feifei et al. (2014). Comparison of Leaf Proteomes of Cassava (Manihot esculenta Crantz) Cultivar NZ199 Diploid and Autotetraploid Genotypes. PLoS One. 2014 Apr 11;9(4):e85991. doi: 10.1371/journal.pone.0085991. eCollection 2014.
Wu et al. (2013). Proteomic and Phytohormone Analysis of the Response of Maize (Zea mays L.) Seedlings to Sugarcane Mosaic Virus. PLoS One. July 23;8(7).
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