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PDC | Pyruvate decarboxylase

345 €

AS10 691  |  clonality: polyclonal  |  host: rabbit  |  reactivity: A. thaliana, O. sativa, Z. mobilis

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Item No:
AS10 691

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product information
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.

Immunogen

KLH-conjugated peptide derived from available PDC sequences including Arabidopsis thaliana

Host Rabbit
Clonality Polyclonal
Clone
Purity Serum
Format Lyophilized
Quantity 100 ĩl
Reconstitution For reconstitution add 100 ĩl of sterile water
Storage

store lyophilized/reconstituted at -20°C; once reconstituted 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 lyophilized material adhering to the cap or sides of the tubes.

Tested applications western blot (WB)
Related products

AS10 685 | ADH | alcohol dehydrogenase (hypoxia marker)

Plant and algal protein extraction buffer

Secondary antibodies

Additional information
application information
Recommended dilution

1: 10 000 with standard ECL (WB)

Expected | apparent MW

65 | 65 kDa (Arabidopsis thaliana)

Confirmed reactivity Arabidopsis thaliana, Oryza sativa, Zymomonas mobilis
Predicted reactivity

Brassica napus, Chlamydomonas reinhardtii, Hordeum vulgare, Glycine max, Pisum sativum, Solanum tuberosum, Sorghum bicolor, Ricinus communis, Zea mays, Vitis vinifera

Not reactive in

no confirmed exceptions from predicted reactivity known in the moment

Additional information

to be added when available

Selected references 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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