NdhS | NAD(P)H-quinone oxidoreductase subunit S (chloroplastic)
AS16 4066 | Clonality: Polyclonal | Host: Rabbit | Reactivity: Arabidopsis thaliana, Hordeum vulgare
DATA SHEET IN PDF| Data sheet | Product citations | Add review |
Product Information
Immunogen
KLH-conjugated synthetic peptide dervied from Arabidopsis thaliana NdhS sequence, UniProt: A0A178V0R5, TAIR: AT4G23890
Host
Rabbit
Clonality
Polyclonal
Purity
Affinity purified serum in PBS, pH 7.4
Format
Lyophilized
Quantity
50 µg
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 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
1:10 000 (WB)
Expected | apparent MW
27 kDa
Reactivity
Confirmed reactivity
Arabidopsis thaliana, Hordeum vulgare
Predicted reactivity
Trema orientale, Parasponia andersonii, Populus tomentosa, Prunus avium, Raphanus sativus, Ziziphus jujuba
Species of your interest not listed? Contact us
Species of your interest not listed? Contact us
Not reactive in
no confirmed exceptions from predicted reactivity known in the moment
Application examples
Application examples
Application example
Arabidopsis thaliana leaves from wildtype and ndho mutant were frozen in liquid nitrogen. Leaf tissue was homogenized in ice-cold isolation buffer (330 mm Suc, 25 mm HEPES-KOH, pH 7.4, 10 mm MgCl2, and 10 mm NaF) and filtered through Miracloth. The filtrate was centrifuged at 6,000g for 5 min at 4°C. The thylakoid pellet was resuspended in 25 mm HEPES-KOH, pH 7.4, 10 mm MgCl2, and 10 mm NaF, centrifuged at 6,000g, for 5 min at 4°C, and finally suspended in the isolation buffer and stored at −80°C. The chlorophyll content of isolated thylakoids was determined according to Porra et al. (1989)
Samples were denatured with Laemmli buffer at 65°C for 5 min. and were separated on 12 % SDS-PAGE and blotted 1h to PVDF (0.45um), using semi-dry transfer. Blot was blocked with 5 % milk 1h/RT with agitation. Blot was incubated in the primary antibody at a dilution of 1: 10000 in TBS-T ON/4°C with agitation. The antibody solution was decanted and the blot washed once for 15 min and 3 times for 5 min in TBS-T at RT with agitation. Blot was incubated in Agrisera matching secondary antibody (anti-rabbit IgG horse radish peroxidase conjugated) diluted to 1:25 000 in for 1h/RT with agitation. The blot was washed as above and incubated for 5min min with chemiluminescent detection reagents. Exposure time was 5-10 min.
Courtesy Dr. Lauri Nikkanen, University of Turku, Finland
Arabidopsis thaliana leaves from wildtype and ndho mutant were frozen in liquid nitrogen. Leaf tissue was homogenized in ice-cold isolation buffer (330 mm Suc, 25 mm HEPES-KOH, pH 7.4, 10 mm MgCl2, and 10 mm NaF) and filtered through Miracloth. The filtrate was centrifuged at 6,000g for 5 min at 4°C. The thylakoid pellet was resuspended in 25 mm HEPES-KOH, pH 7.4, 10 mm MgCl2, and 10 mm NaF, centrifuged at 6,000g, for 5 min at 4°C, and finally suspended in the isolation buffer and stored at −80°C. The chlorophyll content of isolated thylakoids was determined according to Porra et al. (1989)
Samples were denatured with Laemmli buffer at 65°C for 5 min. and were separated on 12 % SDS-PAGE and blotted 1h to PVDF (0.45um), using semi-dry transfer. Blot was blocked with 5 % milk 1h/RT with agitation. Blot was incubated in the primary antibody at a dilution of 1: 10000 in TBS-T ON/4°C with agitation. The antibody solution was decanted and the blot washed once for 15 min and 3 times for 5 min in TBS-T at RT with agitation. Blot was incubated in Agrisera matching secondary antibody (anti-rabbit IgG horse radish peroxidase conjugated) diluted to 1:25 000 in for 1h/RT with agitation. The blot was washed as above and incubated for 5min min with chemiluminescent detection reagents. Exposure time was 5-10 min.
Courtesy Dr. Lauri Nikkanen, University of Turku, Finland
Additional information
Background
Background
NAD(P)H-quinone oxidoreductase subunit 2 is involved in the transfer of electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. Alternative names: NAD(P)H dehydrogenase, subunit 2, NADH-plastoquinone oxidoreductase subunit 2.
Product citations
Selected references
Nikkanen et al. (2018). Regulation of cyclic electron flow by chloroplast NADPH‐dependent thioredoxin system. Plant Direct https://doi.org/10.1002/pld3.93
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