Fd1 | Ferredoxin 1 (chloroplastic)
AS20 4434 | Clonality: Polyclonal | Host: Rabbit | Reactivity: Arabidopsis thaliana, Zea mays
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Product Information
Immunogen
Purified full length, tag cleaved, recombinant maize Fd1, UniProt: P27787
Host
Rabbit
Clonality
Polyclonal
Purity
Total IgG, purified on Protein A
Format
Liquid at 1 mg/ml in PBS, 50% glycerol, Filter sterilized, No preservative or carrier added,
Quantity
100 µg
Storage
Store at -20°C; once 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 material adhering to the cap or sides of the tubes
Tested applications
ELISA (ELISA), Western blot (WB)
Recommended dilution
1: 1000 - 1: 5000 (WB)
Expected | apparent MW
12 | 15 kDa
Reactivity
Confirmed reactivity
Arabidopsis thaliana, Zea mays
Predicted reactivity
Brassica napus, Brassica oleracea, Eutrema salsugineum, Raphanus sativus
Species of your interest not listed? Contact us
Species of your interest not listed? Contact us
Not reactive in
Nicotiana benthamiana
Application examples
Application examples
Recombinant Fd1 from Zea mays (1), 10 μg/well of leaf total protein of Arabidopsis thaliana wild type leaf (2), Zea mays leaf (3) were freshly extracted with 2x SDS-sample buffer (+ 2ME) for SDS-PAGE. For IP, 150mM NaCL, 1% Triton X-100, 50 mM Tris-HCl (pH 8.0) and denatured with 4X SDS buffer at 95°C for 5 min. Samples were separated on 10% SDS-PAGE and blotted 1h to PVDF membrane. Blot was blocked with 3 % skim milk/TBS-T, 1h/RT with agitation. Blot was incubated in the primary antibody at a dilution of 1: 1000 in TBS-T for 1h/RT. The antibody solution was decanted and the blot was washed 4 times for 10 min in TBS-T at RT with agitation. Blot was incubated in matching secondary antibody (anti-rabbit IgG horse radish peroxidase conjugated) diluted to 1:10 000 in for 1h/RT with agitation. The blot was washed as above and developed with a chemiluminescent detection reagent, following manufacture's recommendation.
Molecular weight of mature Fd1 is around 12 kDa but it migrates at 15 kDa in applied gel system.
200 nmol of recombinant Ferredoxin-1 (Fd1) from Arabidopsis thaliana (1),
200 nmol of recombinant Ferredoxin-2 (Fd2) from Arabidopsis thaliana (2),
200 nmol of recombinant Ferredoxin-3 (Fd3) from Arabidopsis thaliana (3),
20 nmol of recombinant Ferredoxin-4 (Fd4) from Arabidopsis thaliana (4),
Leaf extract of Arabidopsis thaliana, soluble fraction precipitated with 70 % ammonium sulfate (5),
Leaf extract of Arabidopsis thaliana, insoluble fraction precipitated with 70 % ammonium sulfate (6),
Root extract of Arabidopsis thaliana (7). Samples were separated on 10% SDS-PAGE and blotted 1h to PVDF membrane. Blot was blocked with 3 % skim milk/TBS-T, 1h/RT with agitation. Blot was incubated in the primary antibody at a dilution of 1: 200 in TBS-T for 1h/RT. The antibody solution was decanted and the blot was washed 4 times for 10 min in TBS-T at RT with agitation. Blot was incubated in matching secondary antibody (anti-rabbit IgG horse radish peroxidase conjugated) diluted to 1:10 000 in for 1h/RT with agitation. The blot was washed as above and developed with a chemiluminescent detection reagent, following manufacture's recommendation.
Recombinant Fd1 from Zea mays (1), 10 μg/well of leaf total protein of Arabidopsis thaliana wild type leaf (2), Zea mays leaf (3) were freshly extracted with 2x SDS-sample buffer (+ 2ME) for SDS-PAGE. For IP, 150mM NaCL, 1% Triton X-100, 50 mM Tris-HCl (pH 8.0) and denatured with 4X SDS buffer at 95°C for 5 min. Samples were separated on 10% SDS-PAGE and blotted 1h to PVDF membrane. Blot was blocked with 3 % skim milk/TBS-T, 1h/RT with agitation. Blot was incubated in the primary antibody at a dilution of 1: 1000 in TBS-T for 1h/RT. The antibody solution was decanted and the blot was washed 4 times for 10 min in TBS-T at RT with agitation. Blot was incubated in matching secondary antibody (anti-rabbit IgG horse radish peroxidase conjugated) diluted to 1:10 000 in for 1h/RT with agitation. The blot was washed as above and developed with a chemiluminescent detection reagent, following manufacture's recommendation.
Molecular weight of mature Fd1 is around 12 kDa but it migrates at 15 kDa in applied gel system.
200 nmol of recombinant Ferredoxin-1 (Fd1) from Arabidopsis thaliana (1),
200 nmol of recombinant Ferredoxin-2 (Fd2) from Arabidopsis thaliana (2),
200 nmol of recombinant Ferredoxin-3 (Fd3) from Arabidopsis thaliana (3),
20 nmol of recombinant Ferredoxin-4 (Fd4) from Arabidopsis thaliana (4),
Leaf extract of Arabidopsis thaliana, soluble fraction precipitated with 70 % ammonium sulfate (5),
Leaf extract of Arabidopsis thaliana, insoluble fraction precipitated with 70 % ammonium sulfate (6),
Root extract of Arabidopsis thaliana (7). Samples were separated on 10% SDS-PAGE and blotted 1h to PVDF membrane. Blot was blocked with 3 % skim milk/TBS-T, 1h/RT with agitation. Blot was incubated in the primary antibody at a dilution of 1: 200 in TBS-T for 1h/RT. The antibody solution was decanted and the blot was washed 4 times for 10 min in TBS-T at RT with agitation. Blot was incubated in matching secondary antibody (anti-rabbit IgG horse radish peroxidase conjugated) diluted to 1:10 000 in for 1h/RT with agitation. The blot was washed as above and developed with a chemiluminescent detection reagent, following manufacture's recommendation.
Additional information
Background
Background
Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. It occupies a key position both for transferring the photoreducing power to Fd-NADP+ oxidoreductase (FNR), hence the formation of NADPH, and for mediating the cyclic electron flow around photosystem I (PSI).
Product citations
Selected references
Hanke and Hase (2008). Variable Photosynthetic Roles of Two Leaf-Type Ferredoxins in Arabidopsis, as Revealed by RNA Interference. Photochem Photobiol. 84(6):1302-9. doi: 10.1111/j.1751-1097.2008.00411.x.
Kimata and Hase (1989). Localization of Ferredoxin Isoproteins in Mesophyll and Bundle Sheath Cells in Maize Leaf. Plant Physiol. 89(4):1193-7. doi: 10.1104/pp.89.4.1193.
Kimata and Hase (1989). Localization of Ferredoxin Isoproteins in Mesophyll and Bundle Sheath Cells in Maize Leaf. Plant Physiol. 89(4):1193-7. doi: 10.1104/pp.89.4.1193.
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