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PDC | Pyruvate decarboxylase

AS10 691  |  Clonality: Polyclonal  |  Host: Rabbit  |  Reactivity: A. thaliana, O. sativa, Z. mobilis

PDC | Pyruvate decarboxylase  in the group Antibodies Plant/Algal  / Environmental Stress / Hypoxia at Agrisera AB (Antibodies for research) (AS10 691)
PDC | Pyruvate decarboxylase



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Product Information

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 dilution 1 : 10 000 (WB)
Expected | apparent MW

65 | 65 kDa (Arabidopsis thaliana)

Reactivity

Confirmed reactivity Arabidopsis thaliana, Oryza sativa, Zymomonas mobilis
Predicted reactivity Aegilops tauschii , Brassica napus, Chlamydomonas reinhardtii, Cocos nucifera, Dichanthelium oligosanthes, Fragaria ananassa, Hordeum vulgare, Glycine max, Nannochloropsis gaditana, Nicotiana tabacum, Panicum miliaceum, Phoenix dactylifera, Pisum sativum, Potamogeton distinctus, Saccharum officinarum, Solanum tuberosum, Sorghum bicolor, Ricinus communis, Rosa chinensis, Trifolium pratense, Zea mays, Vitis vinifera
Species of your interest not listed? Contact us
Not reactive in No confirmed exceptions from predicted reactivity are currently known

Application examples

Reactant: Arabidopsis thaliana (Thale cress)

Application: Western Blotting

Pudmed ID: 25226037

Journal: PLoS Biol

Figure Number: 3D

Published Date: 2014-09-01

First Author: Giuntoli, B., Lee, S. C., et al.

Impact Factor: 7.279

Open Publication

HRA1 contributes to plant submergence survival.(A) Effect of HRA1 misexpression on rosette growth in air, or after recovery from 72 h submergence in darkness. Scale bar, 2 cm. (B) Percentage of plants surviving flooding-induced hypoxia (n?=?5), dry weight of rosette plants kept under control growth conditions (n?=?6), and dry weight of rosettes after postsubmergence recovery (n?=?6). Data are mean ± s.d.; *p<0.05, significant differences from the wild type after one-way ANOVA. (C) HRA1 regulates target gene transcripts in an age-dependent manner in leaves of plants treated with complete submergence. Transcripts were measured before submergence (“control conditions”), after 4 h submergence in darkness (“submergence”), and after 1 h de-submergence in the light (“reoxygenation”). Relative transcript values were calculated using old leaves of the wild type under control conditions as the reference sample. Data are mean ± s.d. (n?=?3); letters indicate statistically significant differences between genotypes after one-way ANOVA (p<0.05) performed independently on each leaf type. (D) Western blot analysis of ADH and PDC protein accumulation in leaves at different developmental stages from control and submerged (4 h) plants. The full-size images of the hybridized membranes can be found in Figure S10. (E) Stability of the translational fusion RAP2.12:RrLuc protein (RrLuc, Renilla reniformis luciferase) in Arabidopsis mesophyll protoplasts upon transfection with increasing amounts of 35S:HRA1. RAP2.12:RrLuc abundance was evaluated from the RrLuc relative activity, measured through a dual luciferase assay. Data are mean ± s.d. (n?=?4), and the asterisks indicate statistically significant differences (p<0.05) from protoplasts expressing RAP2.12:RrLuc alone, after one-way ANOVA.

Additional information

Related products

Background

Background

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.

Product citations

Selected references 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.
More images:

Reactant: Arabidopsis thaliana (Thale cress)

Application: Western Blotting

Pudmed ID: 25226037

Journal: PLoS Biol

Figure Number: 3D

Published Date: 2014-09-01

First Author: Giuntoli, B., Lee, S. C., et al.

Impact Factor: 7.279

Open Publication

HRA1 contributes to plant submergence survival.(A) Effect of HRA1 misexpression on rosette growth in air, or after recovery from 72 h submergence in darkness. Scale bar, 2 cm. (B) Percentage of plants surviving flooding-induced hypoxia (n?=?5), dry weight of rosette plants kept under control growth conditions (n?=?6), and dry weight of rosettes after postsubmergence recovery (n?=?6). Data are mean ± s.d.; *p<0.05, significant differences from the wild type after one-way ANOVA. (C) HRA1 regulates target gene transcripts in an age-dependent manner in leaves of plants treated with complete submergence. Transcripts were measured before submergence (“control conditions”), after 4 h submergence in darkness (“submergence”), and after 1 h de-submergence in the light (“reoxygenation”). Relative transcript values were calculated using old leaves of the wild type under control conditions as the reference sample. Data are mean ± s.d. (n?=?3); letters indicate statistically significant differences between genotypes after one-way ANOVA (p<0.05) performed independently on each leaf type. (D) Western blot analysis of ADH and PDC protein accumulation in leaves at different developmental stages from control and submerged (4 h) plants. The full-size images of the hybridized membranes can be found in Figure S10. (E) Stability of the translational fusion RAP2.12:RrLuc protein (RrLuc, Renilla reniformis luciferase) in Arabidopsis mesophyll protoplasts upon transfection with increasing amounts of 35S:HRA1. RAP2.12:RrLuc abundance was evaluated from the RrLuc relative activity, measured through a dual luciferase assay. Data are mean ± s.d. (n?=?4), and the asterisks indicate statistically significant differences (p<0.05) from protoplasts expressing RAP2.12:RrLuc alone, after one-way ANOVA.

All references: 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.
Confirmed reactivity: Arabidopsis thaliana, Oryza sativa, Zymomonas mobilis
predicted reactivity: Aegilops tauschii , Brassica napus, Chlamydomonas reinhardtii, Cocos nucifera, Dichanthelium oligosanthes, Fragaria ananassa, Hordeum vulgare, Glycine max, Nannochloropsis gaditana, Nicotiana tabacum, Panicum miliaceum, Phoenix dactylifera, Pisum sativum, Potamogeton distinctus, Saccharum officinarum, Solanum tuberosum, Sorghum bicolor, Ricinus communis, Rosa chinensis, Trifolium pratense, Zea mays, Vitis vinifera
Species of your interest not listed? Contact us
not reactive in: No confirmed exceptions from predicted reactivity are currently known
calculated | apparent molecular mass [kDa]:

65 | 65 kDa (Arabidopsis thaliana)

Clonality: Polyclonal
Format: Lyophilized
Host: Rabbit
immunogen:

KLH-conjugated peptide derived from available PDC sequences including Arabidopsis thaliana, PDC1 UniProt: O82647, TAIR: AT4G33070 and PDC2 UniProt: Q9FFT4 TAIR: AT5G54960

Purity: Serum
Quantity: 100 µl
recommended dilution: 1 : 10 000 (WB)
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)
background:

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.

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