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{{/_source.additionalInfo}}Anti-Fd-GOGAT | Ferredoxin-dependent Glutamate synthase
(Cat#: AS20 4428)
Description
- Immunogen: Purified full-length, tag cleaved, recombinant Zea mays GOGAT, UniProt: P23225
- Host: Rabbit
- Clonality: Polyclonal
- Purity: Total IgG. Protein A purified in PBS, 50% glycerol. Filter sterilized.
- Format: Liquid at 2 mg/ml.
- Quantity: 100 µg
- 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), Western blot (WB)
- Recommended dilutions: 1: 2000 - 1: 5000 (WB)
- Expected | apparent MW: 175 kDa (Zea mays), 168 kDa (Arabidopsis thaliana)
- Confirmed reactivity: Arabidopsis thaliana, Spinacia oleracea, Synechocystis sp. PCC6803, Zea mays
- Not reactive in: No confirmed exceptions from predicted reactivity are currently known
- 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.
- 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.
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