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PsbA | D1 protein of PSII, C-terminal (rabbit antibody) (thylakoid membrane marker)

AS05 084 | Clonality: Polyclonal | Host: Rabbit | Reactivity: [global antibody] for higher plants, algae, liverwort, cyanobacteria, diatoms | cellular [compartment marker] of thylakoid membrane

Benefits of using this antibody

PsbA | D1 protein of PSII, C-terminal (rabbit antibody) (thylakoid membrane marker) in the group Antibodies Plant/Algal  / Compartment Markers / Chloroplast marker / Thylakoid membrane marker at Agrisera AB (Antibodies for research) (AS05 084)
PsbA | D1 protein of PSII, C-terminal (rabbit antibody) (thylakoid membrane marker)



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Product Information

Immunogen

KLH-conjugated synthetic peptide derived from available plant, algal and cyanobacterial PsbA sequences, including Arabidopsis thaliana UniProt: A4QJR4, TAIR: AtCg00020 , Oryza sativa P0C434, Populus alba Q14FH6, Physcomitrella patens Q6YXN7, Chlamydomonas reinhardtii P07753, Synechocystis sp. P14660 and many others

Host Rabbit
Clonality Polyclonal
Purity Serum
Format Lyophilized
Quantity 50 ĩl
Reconstitution For reconstitution add 50 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 Immunofluorescence (IF), ImmunoGold (IG), Western blot (WB)
Recommended dilution 1: 500 (IF),  1: 200 (IG),  1 : 10 000 (WB)
Expected | apparent MW

38 | 28-30 kDa

Reactivity

Confirmed reactivity Alniaria alnifolia, Anabaena 7120, Arabidopsis thaliana, Artemisia annua, Arundo sp., Begonia sp. , Cannabis sativa L., Chlamydomonas reinhardtii, Chlorella ohadii, Chromera velia, Chlorella vulgaris, Colobanthus quitensis Kunt Bartl, Coscinodiscus wailesii, Craterostigma sp., Cyanidioschyzon merolae, Cytisus cantabricus (Wilk.) Rchb. F, Desmodesmus sp., Dianthus caryophyllus, Ditylum brightwellii, Eucalyptus globulus, Fraxinus rhynchophylla, Glycine max, Halomicronema hongdechloris, Hieracium pilosella L., Hordeum vulgare, Lasallia hispanica, Lindernia sp., Manihot esculenta, Marchantia polymorpha (liverwort), Medicago truncatula, Miscanthus x giganteus, Microcystis aeruginosa, Mirkania micrantha, Nicotiana benthamiana, Nicotiana tabcum, Panicum miliaceum, Panax ginseng, Panicum maximum, Paulinella chromatophora (amoeba), Pheodactylum tricornutum CCAP 1055/1, Physcomitrium patens, Picea glauca, Pinus strobus, Pisum sativum, Prochlorococcus sp. (surface and deep water ecotype), Pisum sativum, Skeletonema costatum (diatom), Solanum lycopersicum, Spartina alterniflora, Spinacia oleracea, Spirodela polyrhiza, Symbiodinium sp, Synechococcus sp. PCC 7942, Synechococcus elongatus UTEX 2973, Synechocystis sp. 6803, Syntrichia muralis, Thalassiosira weissflogii, Tetradesmus obliquus, Triticum aestivum, Triticale, Zea may, Quercus ilex
Predicted reactivity

Algae (brown and red), Brassica napus, Conifers, Cyanobacteria, Dictos, Cannabis sativa, Galdieria sulphuraria, Lactuca sativa, Lycopersicum esculentum, Medicago sativa, Nannochloropsis sp., Oryza sativa, Ostreococcus sp. Pisum sativum, Sesamum indicum, Thalassiosira pseudonana, Zosteria marina, Vitis vinifera cellular [compartment marker] of thylakoid membrane


Species of your interest not listed? Contact us
Not reactive in No confirmed exceptions from predicted reactivity are currently known

Application examples

Application examples

Application example

Western blot anti-PsbA rabbit antibody

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, (5) Anabaena sp. 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% ECL Advance blocking reagent (GE Healthcare) 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, recommended secondary antibody AS09 602) diluted to 1:50 000 in 2% blocking solution for 1h at room temperature with agitation. The blots were washed as above and developed for 5 min with chemiluminescent 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).



western blot using anti-PsbA antibodies on Med4

Varying amounts of PsbA protein standard (AS01 016S) 250 fmol (1), 125 fmol (2), 62.5 fmol (3), 31.25 fmol (4), 15.625 fmol (5) and 2 µg of total protein from Med4 (6,7) extracted with Protein Extration Buffer, PEB (AS08 300). Samples were diluted with 1X sample buffer (NuPAGE LDS sample buffer (Invitrogen) supplemented with 50 mM DTT and heat at 70°C for 5 min and keept on ice before loading. Protein samples were separated on 4-12% Bolt Plus gels,  LDS-PAGE and blotted for 70 minutes to PVDF using tank transfer. Blots were blocked immediately following transfer in 2% blocking reagent or 5% non-fat milk dissolved 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: 10 000 (in blocking reagent) for 1h at room temperature with agitation. The antibody solution was decanted and the blot was rinsed briefly twice, and then washed 1x15 min and 3x5 min with TBS-T at room temperature with agitation. Blots were incubated in secondary antibody (goat anti-rabbit IgG horse radish peroxidase conjugated, recommended secondary antibody AS09 602, Agrisera) diluted to 1:25 000 in blocking reagent for 1h at room temperature with agitation. The blots were washed as above. The blot was developed with chemiluminescent detection reagent according the manufacturers instructions. Images of the blots were obtained using a CCD imager (VersaDoc MP 4000) and Quantity One software (Bio-Rad). Exposure time was 30 seconds.

Reactant: Arabidopsis thaliana (Thale cress)

Application: Western Blotting

Pudmed ID: 21689410

Journal: BMC Plant Biol

Figure Number: 8B

Published Date: 2011-06-20

First Author: Balsemão-Pires, E., Jaillais, Y., et al.

Impact Factor: 4.142

Open Publication

AtTSPO accumulation and chloroplast localization upon salt stress. (A) Immunoblot analysis of OxAtTSPO:eGFP (OxM1TSPO:eGFP, OxM21TSPO:eGFP and OxM42TSPO:eGFP) fusion proteins detected in plants with an antibody to GFP. Plants were untreated, or treated with 150 mM NaCl. As a control wild-type plants and plants over-expressing GFP (OxeGFP) seedlings were used. (B) Anti-GFP immunoblot of trypsinized chloroplasts from Arabidopsis plants either untreated or treated with 150 mM NaCl. Control immunoblots were probed with antibodies chloroplast proteins RuBisCo and D1; and to cytosolic UGPase. Each lane represents equal amounts of chloroplasts.


Reactant: Nicotiana tabacum (Common tobacco)

Application: Western Blotting

Pudmed ID: 23227265

Journal: PLoS One

Figure Number: 4B

Published Date: 2012-12-12

First Author: Almoguera, C., Prieto-Dapena, P., et al.

Impact Factor: 2.942

Open Publication

Membrane protein complexes of PSII and PSI survive in the 35S:A9 seedlings.(A) Western detection of complexes after the H2O2 treatments. The PSII complexes (top) separated by BN-PAGE were detected using anti-D1 (DE-loop) antibodies at 1/5,000 dilution. The PSI complexes (bottom) were detected using anti-PsaB antibodies at 1/4,000 dilution. PSII symbols: •, and the bracket on top respectively mark the dimeric PSII complex, and the PSII-LHCII super-complexes. The asterisk marks the CVII (CP43-less PSII monomer) complex. PSI symbols: • marks the PSI-LHCI super-complex that co-migrates in our gel system with the dimeric PSII complex; the asterisk marks the PSI monomer. (B) The PSII complexes also withstand drastic dehydration. The thylakoid samples were analyzed immediately (0 h) after the dehydration treatment (DT), and following rehydration for 16 h, DT (16 h). In this case the complexes were detected using anti-D1 (C-terminal) antibodies at 1/15,000 dilution. An additional PSII complex mentioned in the text is indicated: CV (**, PSII monomer).


Reactant: Phaeodactylum tricornutum

Application: Western Blotting

Pudmed ID: 28631733

Journal: Nat Commun

Figure Number: 2G

Published Date: 2017-06-20

First Author: Flori, S., Jouneau, P. H., et al.

Impact Factor: 13.783

Open Publication

Immunolocalization of photosystems and of cyt b6f in the thylakoid membranes of P. tricornutum.(a–c) TEM images of P. tricornutum labelled with antibodies directed against the PsaA subunit of PSI (a), the PsbA subunit of PSII (b) and the PetA subunit of cyt b6f (c). (d) TEM micrograph of P. tricornutum thylakoid membranes showing four distinct areas: the internal membranes (‘core’: violet); the external, peripheral membranes (‘per.’: green); the pyrenoid (‘pyr.’: orange) and the envelope (‘env.’: magenta). Bars: 200?nm. (e) Principal component analysis of PSI, cyt b6f and PSII immunolocalization with the PsbA (solid squares), PsbC (open squares), PetA (cyan circle), PsaC (solid triangles) and PsaA (open triangles) antibodies. See also Supplementary Fig. 4. A total of 258 images from four independent cultures were analysed. The first two components represent more than 91% of the variance (see Supplementary Table 1, and Methods for a more detailed explanation). Green arrow: peripheral variable; violet arrow: core variable; orange arrow: pyrenoid variable; Magenta arrow: envelope variable. (f) 2D representation of the barycentre for the PSI (? PsaA+? PsaC antibodies, black square), cyt b6f (PetA, cyan circle) and PSII (? PsbA+? PsbC antibodies, red triangle) distributions. The point size along an axis is proportional to the s.d. along the corresponding component. (g) Solubilization of P. tricornutum thylakoid membranes with increasing concentrations of digitonin (0.1%, 0.2%, 0.5%, 1%). Pellet (P) and supernatant (S) were analysed by western blotting with the same anti PSI, PSII and cyt b6f antibodies as in a–c. Representative data set of an experiment replicated on three different biological samples.


Reactant: Arabidopsis thaliana (Thale cress)

Application: Western Blotting

Pudmed ID: 31240258

Journal: Commun Biol

Figure Number: 2A

Published Date: 2019-06-27

First Author: Pralon, T., Shanmugabalaji, V., et al.

Impact Factor: None

Open Publication

Thylakoid protein phosphorylation and state transitions are disturbed after high light treatment in pgr6 background. a Total protein extracts of 4-week-old wild type (WT), pgr6-1, pgr6?2, sps2 and stn7/stn8 analysed by immunoblotting with anti-phosphothreonine antibody; the principal thylakoid phospho proteins are indicated on the right according to their size. Core photosystem II proteins D1 (PsbA) and D2 (PsbD) are indicated as a single band due to their poor resolution. Actin was used as a loading control. b Lhcb1 and Lhcb2 phosphorylation levels were visualised after separation on Phostag™-pendant acrylamide gels. The upper band corresponds to the phosphorylated form (p-), stn7/stn8 double mutant is a non-phosphorylated control. c Average transient of the variable room temperature chlorophyll fluorescence measured during the transition from red (660nm) supplemented with far-red light (720nm) state 1 to pure red light state 2 (n?=?4 independent pots containing 2–3 plants). The fluorescence curves from pgr6 and sps2 are shifted on the x-axis to allow visualising the FMST1 and FMST2 values. The x-axis time scale refers to the wild-type curve. d Calculated quenching related to state transition (qT?=?(FMST1?–?FMST2)/FM), expressed as the percentage of FM that is dissipated by the state 1 to state 2 transition, of wild type (WT), pgr6?1 and sps2 under moderate light (120?mol?m?2?s?1) (ML) and after 3?h of high light (500?mol?m?2?s?1) (HL). Whiskers and box plot shows the minimum, first quartile, median, average, third quartile and maximum of each dataset (n?=?4 biologically independent samples); p-values are calculated via a two-tailed Student’s t test. e STN7 phosphorylation level visualised after separation on Phostag™-pendant acrylamide gels. The upper band corresponds to the phosphorylated form (p-), a protein sample from stn7/stn8 double mutant was loaded as a control for the antibody specificity. Uncropped images of the membranes displayed in a, b and e are available as Supplementary Fig. 11. Data points for items c, d are available as Supplementary data 2


Reactant: Arabidopsis thaliana (Thale cress)

Application: Western Blotting

Pudmed ID: 31819921

Journal: Plant Direct

Figure Number: 4A

Published Date: 2019-11-01

First Author: Bethmann, S., Melzer, M., et al.

Impact Factor: None

Open Publication

High light?induced changes of the D1 and ZEP protein content. Detached leaves of Arabidopsis (a), pea (b), spinach (c) and tobacco (d) plants were vacuum?infiltrated with H2O or 3 mM SM, as indicated in each panel. Leaves were exposed to HL for 8 hr at 2,000 ĩmol photons m?2 s?1 and 4°C and then transferred to LL (10–20 ĩmol photons m?2 s?1) for 16 hr. Total leaf protein extracts equivalent to 5 ĩg protein were separated by SDS?PAGE. The abundance of ZEP and D1 protein, as well as of the large subunit of RubisCO (RbcL) was assessed by immunoblotting with specific antibodies. Representative blots from at least 3 biological replicates are shown


Reactant: Pisum sativum (Pea)

Application: Western Blotting

Pudmed ID: 31819921

Journal: Plant Direct

Figure Number: 4B

Published Date: 2019-11-01

First Author: Bethmann, S., Melzer, M., et al.

Impact Factor: None

Open Publication

High light?induced changes of the D1 and ZEP protein content. Detached leaves of Arabidopsis (a), pea (b), spinach (c) and tobacco (d) plants were vacuum?infiltrated with H2O or 3 mM SM, as indicated in each panel. Leaves were exposed to HL for 8 hr at 2,000 ĩmol photons m?2 s?1 and 4°C and then transferred to LL (10–20 ĩmol photons m?2 s?1) for 16 hr. Total leaf protein extracts equivalent to 5 ĩg protein were separated by SDS?PAGE. The abundance of ZEP and D1 protein, as well as of the large subunit of RubisCO (RbcL) was assessed by immunoblotting with specific antibodies. Representative blots from at least 3 biological replicates are shown


Reactant: Nicotiana tabacum (Common tobacco)

Application: Western Blotting

Pudmed ID: 31819921

Journal: Plant Direct

Figure Number: 4C

Published Date: 2019-11-01

First Author: Bethmann, S., Melzer, M., et al.

Impact Factor: None

Open Publication

High light?induced changes of the D1 and ZEP protein content. Detached leaves of Arabidopsis (a), pea (b), spinach (c) and tobacco (d) plants were vacuum?infiltrated with H2O or 3 mM SM, as indicated in each panel. Leaves were exposed to HL for 8 hr at 2,000 ĩmol photons m?2 s?1 and 4°C and then transferred to LL (10–20 ĩmol photons m?2 s?1) for 16 hr. Total leaf protein extracts equivalent to 5 ĩg protein were separated by SDS?PAGE. The abundance of ZEP and D1 protein, as well as of the large subunit of RubisCO (RbcL) was assessed by immunoblotting with specific antibodies. Representative blots from at least 3 biological replicates are shown


Reactant: Spinacia oleracea (Spinach)

Application: Western Blotting

Pudmed ID: 31819921

Journal: Plant Direct

Figure Number: 4D

Published Date: 2019-11-01

First Author: Bethmann, S., Melzer, M., et al.

Impact Factor: None

Open Publication

High light?induced changes of the D1 and ZEP protein content. Detached leaves of Arabidopsis (a), pea (b), spinach (c) and tobacco (d) plants were vacuum?infiltrated with H2O or 3 mM SM, as indicated in each panel. Leaves were exposed to HL for 8 hr at 2,000 ĩmol photons m?2 s?1 and 4°C and then transferred to LL (10–20 ĩmol photons m?2 s?1) for 16 hr. Total leaf protein extracts equivalent to 5 ĩg protein were separated by SDS?PAGE. The abundance of ZEP and D1 protein, as well as of the large subunit of RubisCO (RbcL) was assessed by immunoblotting with specific antibodies. Representative blots from at least 3 biological replicates are shown


Reactant: Arabidopsis thaliana (Thale cress)

Application: Western Blotting

Pudmed ID: 32269582

Journal: Front Plant Sci

Figure Number: 7B

Published Date: 2020-04-10

First Author: Pralon, T., Collombat, J., et al.

Impact Factor: 5.435

Open Publication

Double mutant maintains thylakoid protein phosphorylation and state transitions after high light. (A) Total protein extracts of wild type (WT), abc1k1.1, -2, abc1k3.1, -2, and abc1k1/abc1k3.1, -2 light-exposed leaves were separated by SDS PAGE, transferred on nitrocellulose membrane and decorated with anti-phosphothreonine antibody. The main thylakoid phospho-proteins are indicated on the right according to their size. Core photosystem II proteins D1 (PsbA) and D2 (PsbD) are indicated together due their poor resolution. (B) The accumulation of the principal photosynthetic complexes was assessed using antibodies against specific subunits of each complex: anti-Lhcb2 for the major LHCII, anti-D1 (PsbA) for PSII, anti-PetC for cytochrome b6f, anti-PsaD and anti-PsaC for PSI, and anti-AtpC for ATP synthase. Actin signal is shown as a loading control. (C) Fluorescence quenching related to the state transitions (qT) of wild type (WT), abc1k1.1, -2, abc1k3.1, -2, and abc1k1/abc1k3.1, -2 under moderate light (120 ?mol of photons m–2 s–1) (ML) and after 3 h of high light (500 ?mol of photons m–2 s–1) (HL). qT was calculated from the maximal chlorophyll fluorescence measured after 10 min exposure to red light (660 nm) supplemented with far-red illumination (720 nm) “State 1” (FMST1) or to pure red light “State 2” (FMST2). Quenching related to state transition was calculated as qT = (FMST1 – FMST2)/FM. Each value represents the average of a pot containing 2–3 plants. Superscript letters are used to indicate statistically different groups (p < 0.05) by paired Student’s t-test.

Additional information

Additional information

Due to biology of PsbA (D1) protein a number of degradation products can apprear in a sample and may be observed when using anti-PsbA antibodies, including products having apparent molecular weights of 24kDa and 16kDa. D1 degradation is a complex set of events and the products observed can be influenced by both the extraction procedure and the physiology of the cells prior to harvest. Third, cross-linking may occur between D1 and cytochrome b559, shifting the protein higher in the gel. In cyanobacteria (PCC7942), three different bands were competed out by preincubating the antibody with the PsbA free peptide, indicating that all bands are indeed PsbA and its precursors or breakdown products. Competition assays were also performed with spinach and Chlamydomonas, confirming the identity of PsbA bands.

Anti-PsbA antibodies will not detect D2 protein, as the peptide used to generate PsbA antibodies has no homology to the D2 sequence.

This product can be sold containing ProClin if requested.

The antibody is appropriate for detecting both, 24 kDa or the 10 kDa C-terminal fragments, whichever is generated under given treatment conditions. In our analysis we have seen both, ca. 24 kDa and ca. 10 kDa fragments from different samples, depending on treatments and isolation procedures.

Rabbit anti-PsbA antibody can detect more than one band of PsbA protein, e.g. precursor and mature protein as compare to the hen anti-PsbA antibodies AS01 016.

This antibody will detect the phosphorylated form of D1 as an alternate band to the main band on a high resolution gel.

The antibody will bind to cross-linked proteins: D1/D2, D1/cyt b559, D1/CP43.

Related products

Related products

AS01 016S | PsbA protein standard for a quantitative western blot
AS05 084PRE | PsbA | D1 protein of PSII, C-terminal , pre-immune serum
AS11 1786  | Anti-PsbA N-terminal, rabbit antibodies
AS10 704 | Anti-PsbA | D1 protein of PSII, DE-loop, rabbit antibodies
AS13 2669 | Anti-PsbA | D1 protein of PSII, phosphorylated, rabbit antibodies

Plant and algal protein extraction buffer

Secondary antibodies

Background

Background

The psbA gene has been cloned from many species of plants, green algae, and cyanobacteria. The psbA gene is located in the chloroplast genome and encodes for the D1 protein, a core component of Photosystem II. PsbA/D1 is rapidly cycled under illumination in all oxygenic photobionts. Tracking PsbA pools using the Global PsbA antibody can show the functional content of Photosystem II in a wide range of samples. Alternative names: 32 kDa thylakoid membrane protein, photosystem II protein D1

Product citations

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Byeon et al. (2022) Canopy height affects the allocation of photosynthetic carbon and nitrogen in two deciduous tree species under elevated CO2. J Plant Physiol. 2022 Jan;268:153584. doi: 10.1016/j.jplph.2021.153584. Epub 2021 Dec 2. PMID: 34890847.
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Mursalimov et al. (2021) Chlorophyll deficiency delays but does not prevent melanogenesis in barley seed melanoplasts. Protoplasma. https://doi.org/10.1007/s00709-021-01669-3 (Cryosections)
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Ananyev et al. (2017). Photosystem II-Cyclic Electron Flow Powers Exceptional Photoprotection and Record Growth in the Microalga Chlorella ohadii.Biochim Biophys Acta. 2017 Jul 19. pii: S0005-2728(17)30105-6. doi: 10.1016/j.bbabio.2017.07.001.
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