Name:
Phone:
E-mail:
Address:


 


Fd-GOGAT | Ferredoxin-dependent Glutamate synthase

AS20 4428 | Clonality: Polyclonal  |  Host: Rabbit |  Reactivity: Arabidopsis thaliana, Spinacia oleracea, Synechocystis sp. PCC6803, Zea mays
Fd-GOGAT | Ferredoxin-dependent Glutamate synthase  in the group Antibodies for Plant/Algal  / Spinacia oleracea at Agrisera AB (Antibodies for research) (AS20 4428)

DATA SHEET IN PDF

Qty: 
305
How to cite this product:
Product name, number (Agrisera, Sweden)

Data sheet Product citations Protocols Add review

Product Information

Immunogen Purified full length, tag cleaved, recombinant Zea mays GOGAT, UniProt: P23225
Host Rabbit
Clonality Polyclonal
Purity Total IgG, purified on Protein A
Format Liquid at 2 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: 2000 - 1: 5000 (WB)
Expected | apparent MW 175 kDa (Zea mays), 168 kDa (Arabidopsis thaliana)

Reactivity

Confirmed reactivity Arabidopsis thaliana, Spinacia oleracea, Synechocystis sp. PCC6803, Zea mays
Predicted reactivity Species of your interest not listed? Contact us
Not reactive in No confirmed exceptions from predicted reactivity are currently known.

Application examples

Application examples Western blot using anti-FdGOGAT antibodies

Recombinant FdGOGAT from Zea mays (1), 10 µg of Arabidopsis thaliana total leaf extract (2), 10 µg of Zea mays total leaf extract (3),were freshly extracted 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: 2500 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.

Western blot using anti-FdGOGAT antibodies on cyanobacterial extract
Total cell extract from Synechocystis PCC6803 freshly extracted 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: 2000 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

Related products

Background

Background Glutamine oxoglutarate aminotransferase (GOGAT) is an enzyme involved in synthesis of glutamate from glutamine and alpha-ketoglutarate. GOGAT has two forms in plants: ferredoxin-dependent GOGAT (Fd-GOGAT) and NADH-dependent GOGAT (NADH-GOGAT). 95% of GOGAT found in plants is the Fd-GOGAT type. Fd-GOGAT is encoded by two genes, glu1 and glu2 in Arabidopsis. Fd-GOGAT (both forms) is highly conserved among plants, red algae, and cyanobacteria. Ferredoxin-dependent glutamate synthase, chloroplastic (Fd-GOGAT) is involved in glutamate biosynthesis in leaf. This protein required for the reassimilation of ammonium ions generated during photorespiration. Gene name is GlsF.

Product citations

Selected references Ariga and Hase (2014). Multiple complexes of nitrogen assimilatory enzymes in spinach chloroplasts: possible mechanisms for the regulation of enzyme function. PLoS One. Oct 1;9(10):e108965. doi: 10.1371/journal.pone.0108965.
Sakaibara et al. (1991). Molecular cloning and characterization of complementary DNA encoding for ferredoxin-dependent glutamate synthase in maize leaf. J Biol Chem. Feb 5;266(4):2028-35.

Related products: Fd-GOGAT | Ferredoxin-dependent Glutamate synthase

AS16 ECL-S-N | low pico to mid femtogram and extreme low femtogram detection
From 15 €
AS09 602 |  Clonality: Polyclonal | Host: Goat | Reactivity: Rabbit IgG (H&L)
190 €
AS07 242  |  Clonality: Polyclonal  |  Host: Rabbit  |  Reactivity: ...
286 €
Buy 2 items of this product for 214.00 €/items
Buy 3 items of this product for 195.00 €/items
AS08 310  |  Clonality: Polyclonal  |  Host: Rabbit   |  Reactivity:...
286 €
Buy 2 items of this product for 214.00 €/items
Buy 3 items of this product for 195.00 €/items