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Ferredoxin, apicoplast (Plasmodium falciparum)

AS20 4429 | Clonality: Polyclonal  |  Host: Rabbit |  Reactivity: Plasmodium falciparum
Ferredoxin, apicoplast (Plasmodium falciparum) in the group Antibodies Other Species / Bacteria at Agrisera AB (Antibodies for research) (AS20 4429)



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Product Information

Immunogen Ferredoxin purified from Malaria parasite, Plasmodium falciparum,  UniProt:Q8IED5

Host Rabbit
Clonality Polyclonal
Purity Total IgG. Protein A purified in PBS, 50% glycerol. Filter sterilized.
Format Liquid at 4 mg/ml.
Quantity 200 ĩg
Storage Store 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 ELISA (ELISA), Immunofluorescence (IF), Western blot (WB)
Recommended dilution 1: 500 - 1: 2000 (WB)
Expected | apparent MW 18 kDa

Reactivity

Confirmed reactivity Plasmodium falciparum

Application examples

Application examples Western blot
Western blot using anti-Plasmodium falciparum ferredoxin

10 ng of purified, recombinant pf FNR from Plasmodium falciparum (1), partially purified ferredoxin from culture ofPlasmodium falciparum (2), 1.4 ng of purified, recombinant ferredoxin fromPlasmodium falciparum (3) with 2x SDS-sample buffer (+ 2ME) for SDS-PAGE 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.

Immunofluorescence


Immunofluorescence using anti-Plasmodium falciparum ferredoxin antibodies

Trophozoit and shizont stages of Plasmodium falciparum were stained with the anti-ferredoxin antibodies (right panels, red color). Nuclear DNA was stained with DAPI (middle panels, blue color). Dark spots in bright field microscopy (left panels) are hemozoin pigment.
Plasmodium falciparum parasitic cells were fixed with 4 % paraformaldehyde in PBS on ice for 30 minutes, spread onto slides and air dried. Permabilization was done with: PBS with 1 % Triton X-100. Blocking: 3 % BSA in PBS for 3 h.
Secondary antibody: Cy3 conjugated, 1: 1000
Primary antibody: 1: 100

Additional information

Related products

Background

Background Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.

Product citations

Selected references Kimata and Ariga et al. (2007). Cloning and Characterization of Ferredoxin and ferredoxin-NADP+ Reductase From Human Malaria Parasite. J Biochem. 141(3):421-8. doi: 10.1093/jb/mvm046.
Kabayashi et al. (2007). Mitochondria and Apicoplast of Plasmodium Falciparum: Behaviour on Subcellular Fractionation and the Implication. Mitochondrion 7(1-2):125-32. doi: 10.1016/j.mito.2006.11.021.
immunogen: Ferredoxin purified from Malaria parasite, Plasmodium falciparum,  UniProt:Q8IED5

Host: Rabbit
Clonality: Polyclonal
Purity: Total IgG. Protein A purified in PBS, 50% glycerol. Filter sterilized.
Format: Liquid at 4 mg/ml.
Quantity: 200 ĩg
storage: Store 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: ELISA (ELISA), Immunofluorescence (IF), Western blot (WB)
recommended dilution: 1: 500 - 1: 2000 (WB)
calculated | apparent molecular mass [kDa]: 18 kDa
Confirmed reactivity: Plasmodium falciparum
Picture (footer): Western blot
Western blot using anti-Plasmodium falciparum ferredoxin

10 ng of purified, recombinant pf FNR from Plasmodium falciparum (1), partially purified ferredoxin from culture ofPlasmodium falciparum (2), 1.4 ng of purified, recombinant ferredoxin fromPlasmodium falciparum (3) with 2x SDS-sample buffer (+ 2ME) for SDS-PAGE 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.

Immunofluorescence


Immunofluorescence using anti-Plasmodium falciparum ferredoxin antibodies

Trophozoit and shizont stages of Plasmodium falciparum were stained with the anti-ferredoxin antibodies (right panels, red color). Nuclear DNA was stained with DAPI (middle panels, blue color). Dark spots in bright field microscopy (left panels) are hemozoin pigment.
Plasmodium falciparum parasitic cells were fixed with 4 % paraformaldehyde in PBS on ice for 30 minutes, spread onto slides and air dried. Permabilization was done with: PBS with 1 % Triton X-100. Blocking: 3 % BSA in PBS for 3 h.
Secondary antibody: Cy3 conjugated, 1: 1000
Primary antibody: 1: 100
background: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
All references: Kimata and Ariga et al. (2007). Cloning and Characterization of Ferredoxin and ferredoxin-NADP+ Reductase From Human Malaria Parasite. J Biochem. 141(3):421-8. doi: 10.1093/jb/mvm046.
Kabayashi et al. (2007). Mitochondria and Apicoplast of Plasmodium Falciparum: Behaviour on Subcellular Fractionation and the Implication. Mitochondrion 7(1-2):125-32. doi: 10.1016/j.mito.2006.11.021.

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