PrxQ | Peroxiredoxin, thioredoxin reductase
AS05 093 | Clonality: Polyclonal | Host: Rabbit | Reactivity: A. thaliana, M. esculenta, S. oleracea, Z. mays
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Product Information
His-tagged full length protein (with presequence) of Arabidopsis thaliana was overexpressed in in E.coli. Isolated with HiTrap column (GE Healthcare) Q9LU86, At3g26060
16 kDa
Reactivity
Application examples
Additional information
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.
Background
Peroxiredoxins (EC=1.11.1.15) 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.
Product citations
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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