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AGO set
Tag Antibody Set 

PrxQ | Peroxiredoxin, thioredoxin reductase

AS05 093 | Clonality: Polyclonal | Host: Rabbit | Reactivity: A. thaliana, M. esculenta, S. oleracea, Z. mays

PrxQ | Peroxiredoxin, thioredoxin reductase in the group Antibodies for Plant/Algal  / Environmental Stress / Oxidative stress at Agrisera AB (Antibodies for research) (AS05 093)

PRODUCT INFORMATION IN PDF


Datasheet Product citations Protocols Customer reviews

Product Information

Immunogen

His-tagged full length protein (with presequence) of Arabidopsis thaliana was overexpressed in in E.coli. Isolated with HiTrap column (GE Healthcare) Q9LU86, At3g26060

Host Rabbit
Clonality Polyclonal
Purity Serum
Format Lyophilized
Quantity 200 µl
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 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)
Recommended dilution 1 : 5000 (WB)
Expected | apparent MW

16 kDa

Reactivity

Confirmed reactivity Arabidopsis thaliana, Manihot esculenta, Spinacia oleracea, Zea mays
Predicted reactivity Populus sp. , Triticum aestivum, Oryza sativa
Not reactive in No confirmed exceptions from predicted reactivity are currently known.

Application examples

Additional information

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.

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Background

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

Selected references Yoshida et al. (2018). Thioredoxin-like2/2-Cys peroxiredoxin redox cascade supports oxidative thiol modulation in chloroplasts. Proc Natl Acad Sci U S A. 2018 Aug 13. pii: 201808284. doi: 10.1073/pnas.1808284115.
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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