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{{/_source.additionalInfo}}Anti-PDC | Pyruvate decarboxylase
(Cat#: AS10 691)
Description
- Immunogen: KLH-conjugated peptide derived from available PDC sequences including Arabidopsis thaliana, PDC1 UniProt: O82647, TAIR: AT4G33070 and PDC2 UniProt: Q9FFT4 TAIR: AT5G54960
- Host: Rabbit
- Clonality: Polyclonal
- Purity: Serum
- 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 : 10 000 (WB)
- Expected | apparent MW: 65 | 65 kDa (Arabidopsis thaliana)
- Confirmed reactivity: Arabidopsis thaliana, Oryza sativa, Zymomonas mobilis
- Not reactive in: No confirmed exceptions from predicted reactivity are currently known
- Pyruvate decarboxylase (PDC) is a homotetrameric enzyme (E.C.4.1.1.1) that catalyses the decarboxylation of pyruvic acid to acetaldehyde carbon dioxide in the cytoplasm. It is also called 2-oxo-acid carboxylase, and pyruvic decarboxylase. In anaerobic conditions, this enzyme is part of the fermentation process that occurs in yeast, especially the Saccharomyces genus, to produce ethanol by fermentation. Pyruvate decarboxylase starts this process by converting pyruvate into acetaldehyde and carbon dioxide. Pyruvate decarboxylase depends on cofactors thiamine pyrophosphate (TPP) and magnesium. This enzyme should not be mistaken for the unrelated enzyme pyruvate dehydrogenase, an oxidoreductase (EC 1.2.4.1), that catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA.
- Ventura et al. (2020). Arabidopsis phenotyping reveals the importance of alcohol dehydrogenase and pyruvate decarboxylase for aerobic plant growth. Sci Rep. 2020 Oct 7;10(1):16669. doi: 10.1038/s41598-020-73704-x. PMID: 33028901; PMCID: PMC7542448.Gil-Monreal et al. (2019). ERF-VII transcription factors induce ethanol fermentation in response to amino acid biosynthesis-inhibiting herbicides. J Exp Bot. 2019 Aug 6. pii: erz355. doi: 10.1093/jxb/erz355. Giuntoli et al. (2014). A trihelix DNA binding protein counterbalances hypoxia-responsive transcriptional activation in Arabidopsis. PLoS Biol. 2014 Sep 16;12(9):e1001950. doi: 10.1371/journal.pbio.1001950. eCollection 2014.
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