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{{/_source.additionalInfo}}Anti-GLDH | Galactono-1,4 lactone dehydrogenase
(Cat#: AS06 182)
Description
- Immunogen: Recombinant C-terminal of Zea mays GLDH, UniProt: C0HFL3
- Host: Rabbit
- Clonality: Polyclonal
- Purity: Total IgG. Protein G purified in PBS pH 7.4.
- Format: Lyophilized
- Quantity: 100 µl
- Reconstitution: For reconstitution add 100 µl of sterile water
- Storage: Store lyophilized/reconstituted 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: Western blot (WB)
- Recommended dilutions: 1 : 5000 (WB)
- Expected | apparent MW: 68 kDa
- Confirmed reactivity: Avena sativa, Glycine max, Hordeum vulgare, Helianthus annuus, Oryza sativa, Zea mays
- Not reactive in: No confirmed exceptions from predicted reactivity are currently known
- Galactono-1,4-lactone dehydrogenase (GLDH) is the enzyme which catalyses last step of ascorbic acid (AA) synthesis in the mitochondria of plant cells. Alternative name: GaLDH
- Chen et al. (2019). Composition of Mitochondrial Complex I during the Critical Node of Seed Aging in Oryza sativa. Journal of Plant Physiology Volume 236, May 2019, Pages 7-14.Schimmeyer et al. (2016). L-Galactono-1,4-lactone dehydrogenase is an assembly factor of the membrane arm of mitochondrial complex I in Arabidopsis. Plant Mol Biol. 2016 Jan;90(1-2):117-26. doi: 10.1007/s11103-015-0400-4. Epub 2015 Oct 31.Ostaszewska-Bugajska et al. (2016). Changes in the OXPHOS system in leaf and root mitochondria of Arabidopsis thaliana subjected to long-term sulphur deficiency. Acta Physiologiae Plantarum 38:141.Bartoli et al. (2005). Ascorbate content in wheat leaves is not determined by maximal L-galactono-1, 4-lactone dehydrogenase (GalLDH) activity under drought stress. Plant Cell Environ 28:1073-1081.
- Mitochondrial, membrane or meristematic fractions were shown to be richer in GLDH expression