AS10 651 | Clonality:Polyclonal | Host:Rabbit | Reactivity: Arabidopsis thaliana, Helianthus annuus
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47.7 kDa (Arabidopsis thaliana)
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Coomassie staining of three recombinant sunflower ENO proteins after purification on IMAC column and SDS PAGE separation (A) Immunodetection carried out with the anti-Enolase antibody (B) (AS10 651 at 1:2000 dilution). The detection was done with the Goat Anti-Rabbit IgG (H+L) Alkaline phosphatase conjugated (AS09 607 at 1:5000 dilution). In (A) and (B), the lanes were loaded as follows: M indicates the molecular weight markers Lane 1- Recombinant (6xHis)HaENO2 (cytosolic and active isoform) Lane 2- Recombinant (6xHis)ΔHaENO1 (plastidial isoform with the N-terminal transit peptide removed) Lane 3- Recombinant (6xHis)HaENO3 (cytosolic and inactive isoform) In panel (A), 0.7 µg protein was loaded per lane. In panel (B) 50 ng protein was loaded per lane. The faint band seen below the main band in lane 1 in (B) is likely a degradation product of the recombinant protein. No band was detected in lanes 2 and 3.
Recombinant sunflower enolases are described Troncoso-Ponce et al. Plant Science (2018) 272:117-130).
Courtesy of Dr. Jean Rivoal, IRBV, Université de Montréal, Canada
Enolase (2-phospho-D-glycerate hydrolase or phosphopyruvate dehydratase) is an essential glycolytic metalloenzyme. It is catalyzing the interconversion of 2-phosphoglycerate and phosphoenolpyruvate.
Alternative name: Bifunctional enolase 2/transcriptional activator
Zhang et al. (2018). Nitric oxide induces monosaccharide accumulation through enzyme S-nitrosylation. Plant Cell Environ. 2017 Sep;40(9):1834-1848. doi: 10.1111/pce.12989.
Chen et al.(2009) System analysis of an Arabidopsis mutant altered in de novo fatty acid synthesis reveals diverse changes in seed composition and metabolic regulation. Plant Physiol.
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