PsbP | 23 kDa protein of the oxygen evolving complex (OEC) of PSII (anti-peptide)
AS06 167 | Clonality: Polyclonal | Host: Rabbit | Reactivity: A. thaliana, H. vulgare, N. tabacum, P.abies, P. sativum, P. patens
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KLH-conjugated synthetic peptide derived from PsbP protein of Arabidopsis thaliana Q42029, At1g06680
28 | 23 kDa (Arabidopsis thaliana)
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Chlamydomonas reinhardtii, Synechococcus sp. PCC 7942, Zostera marina
2 µg of total protein from (1) Arabidopsis thaliana leaf extracted with Protein Extration Buffer, PEB (AS08 300), (2) Hordeum vulgare leaf extracted with PEB, (3) Chlamydomonas reinhardtii total cell extracted with PEB, (4) Synechococcus sp. 7942 total cell extracted with PEB, were separated on 4-12% NuPage (Invitrogen) LDS-PAGE and blotted 1h to PVDF. Blots were blocked immediately following transfer in 2% blocking reagent in 20 mM Tris, 137 mM sodium chloride pH 7.6 with 0.1% (v/v) Tween-20 (TBS-T) for 1h at room temperature with agitation. Blots were incubated in the primary antibody at a dilution of 1: 50 000 for 1h at room temperature with agitation. The antibody solution was decanted and the blot was rinsed briefly twice, then washed once for 15 min and 3 times for 5 min in TBS-T at room temperature with agitation. Blots were incubated in secondary antibody (anti-rabbit IgG horse radish peroxidase conjugated) diluted to 1:10 000 in 2% blocking solution for 1h at room temperature with agitation. The blots were washed as above and developed for 5 min withchemiluminescent detection reagent according the manufacturers instructions. Images of the blots were obtained using a CCD imager (FluorSMax, Bio-Rad) and Quantity One software (Bio-Rad).
Reactant: Arabidopsis thaliana (Thale cress)
Application: Western Blotting
Pudmed ID: 28791032
Journal: Front Plant Sci
Figure Number: 2A
Published Date: 2017-08-10
First Author: Kohzuma, K., Froehlich, J. E., et al.
Impact Factor: 5.435Open Publication
Changes in the protein levels of photosynthetic components under extended dark exposure in wild-type and gamera-1. Immunoblot detection of photosynthetic proteins from leaves of Ws and gamera-1 plants incubated after dark adaptation for 0, 2, and 4 days was examined. Specifically, essentially thylakoid fractions were assayed to determine the content of the following proteins: ?-subunit of ATP synthase; the D1 protein, OEC17, OEC23, and OEC33 of PSII; Cyt f and Rieske protein of the cytochrome b6f complex; and the F and D subunits of PSI, after extended dark treatment. Proteins were resolved via SDS-PAGE gel based on equal microgram chlorophyll per lane loading and processed as described in Section “Materials and Methods”. The Large subunit of RuBisco and LHCII stained with either CBB or Ponceau red, respectively, are presented here as loading controls. DAD indicates days after dark adaptation.
PsbP - 23 kDa extrinsic protein of photosystem II (PSII). Processing of the protein results in a protein with molecular mass of around 20 kDa. PsbP is required to optimize water splitting process in PSII, by probaböy by optimisation of calcium and Cl- levels. The protein is found in higher plants and algae but is not conserved in cyanobacteria. Synonymes:Oxygen-evolving enhancer protein 2-1, chloroplastic, OEE2, 23 kDa subunit of oxygen evolving system of photosystem II, OEC 23 kDa subunit, OEC23, 23 kDa thylakoid membrane protein
Tamburino et al. (2017). Chloroplast proteome response to drought stress and recovery in tomato (Solanum lycopersicum L.). BMC Plant Biol. 2017 Feb 10;17(1):40. doi: 10.1186/s12870-017-0971-0.
Pavlovi? et al. (2016). Light-induced gradual activation of photosystem II in dark-grown Norway spruce seedlings. Biochim Biophys Acta. 2016 Feb 18. pii: S0005-2728(16)30028-7. doi: 10.1016/j.bbabio.2016.02.009.
Albanese et al. (2016). Isolation of novel PSII-LHCII megacomplexes from pea plants characterized by a combination of proteomics and electron microscopy. Photosynth Res. 2016 Jan 9.
Grassl et al. (2012). Early events in plastid protein degradation in stay-green Arabidopsis reveal differential regulation beyond the retention of LHCII and chlorophyll. J. Proteome Res. October 2.
Lang et al. (2011).Simultaneous isolation of pure and intact chloroplasts and mitochondria from moss as the basis for sub-cellular proteomics. Plant Cell Rep. Feb;30(2):205-15. (reactivity confirmed for Physcomitrella patens).
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