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NdhB | NAD(P)H-quinone oxidoreductase subunit 2 (chloroplastic)

186 €
Buy 2 items of this product for 140 €/each

AS13 2721 | clonality: polyclonal | host: rabbit | reactivity: Arabidopsis thaliana,

PRODUCT INFORMATION IN PDF

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AS13 2721

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product information
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.

Immunogen

KLH-conjugated synthetic peptide dervied from  Oryza sativa OsChl71 protein, UniProt: Q6Z514

Host Rabbit
Clonality Polyclonal
Clone
Purity Serum
Format Lyophilized
Quantity 50 ĩl
Reconstitution For reconstitution add 50 ĩl of sterile water
Storage The antibody may be stored at -20℃ for one year in its original formulation. Additionally, antibody may be stored at 2℃ to 8℃ for up to 1 month without detectable loss of activity. Avoid repeated freeze-thaw cycles of the diluted antibody.
Tested applications Western Blot (WB)
Related products

AS13 2711 | anti-NAD(P)H dehydrogenase subunit 5, rabbit antibodies

antibodies to proteins involved in electron transfer in chloroplasts

Secondary antibodies

Additional information
application information
Recommended dilution

1:1000 (WB)

Expected | apparent MW

56 | 75 kDa

Confirmed reactivity Arabidopsis thaliana,
Predicted reactivity

Zea mays

Not reactive in Cucumis sativus
Additional information
Selected references Nath et al. (2016). A Nitrogen-Fixing Subunit Essential for Accumulating 4Fe-4S-Containing Photosystem I Core Proteins. Plant Physiol. 2016 Dec;172(4):2459-2470. Epub 2016 Oct 26.

application example



Total protein from Oryza sativa rice (CV. 9311) flag leaf at the tillering stage was ground into a fine powder in liquid nitrogen. An 800 ul aliquot of extraction buffer [62.5 mM TRIS-HCl (pH 7.4), 10% glycerol, 0.1% SDS, 2 mM EDTA, 1 mM phenylmethylsulphonyl fluoride (PMSF), 5% (v/v) b-mercaptoethanol] was added to each 300 mg powder sample. The mixture was vortexed and then chilled on ice for 10 min. Samples were centrifuged at 12,000 rpm for 10min at 4 ℃, and the supernatant was collected and stored at –70 ℃. The protein concentrations of the rice samples were determined using the Bradford method (Bradford, 1976). 20 µg of protein was separated on 12 % SDS-PAGE and blotted 1h to PVDF.
Blots were blocked with for 1h at room temperature (RT) with agitation. Blot was incubated in the primary antibody at a dilution of 1: 1 000 for 1h at RT 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 RT with agitation. Blot was incubated in secondary antibody (anti-rabbit IgG horse radish peroxidase conjugated) diluted to 1:10 000 in for 1h at RT with agitation. The blot was washed as above and developed for 5 min with ECL according to the manufacturer’s instructions. Exposure time was 4 min.

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