ALD | fructose-1,6 bisphosphate aldolase

345 €

AS08 294 | clonality: polyclonal | host: rabbit | reactivity: A. thaliana, E. tef, G. gracilis, O. sativa, P. falciparum, T. salsuginea


39 st
Item No:
AS08 294

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product information

Fructose-1,6 bisphosphate aldolase (ALD) is an enzyme catalazying a key reaction of glycolysis and energy production, converting D-fructose- 1,6-bisphospate into dihydroxyacetone phosphate and D-glyceraldehyde-3-phosphate. This enzyme is present in plant and animal tissues. Plant enzyme is a class I aldolase which does not require a bivalent metal cofactor. It is located to outer mitochondrial membrane.


overexpressed cytosolic fructose 1,6 bisphosphate aldolase (ALD) based on the sequence from Arabidopsis thaliana Q9LF98, At3g52930

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

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

collection of antibodies to enzymes involved in carbohydrate metabolism

Additional information

to be added when available

application information
Recommended dilution

1: 5000 with standard ECL (WB)

Expected | apparent MW

38 | 38 kDa

Confirmed reactivity

Arabidopsis thaliana, Eragrostis tef, Gracilaria gracilis (red algae), Oryza sativa, Plasmodium chabaudi, Plasmodium falciparum, Thellungiella salsuginea

Predicted reactivity

Glycine max, Oryza sativa, Picea sitchensis, Physcomitrella patens, Pisum sativum, Populus jackii, Spinacia oleracea, Vitis vinifera, Zea mays

Not reactive in

Synechocystis sp.

Additional information

to be added when available

Selected references Yam et al. (2016). Characterization of the Plasmodium Interspersed Repeats (PIR) proteins of Plasmodium chabaudi indicates functional diversity. Sci Rep. 2016 Mar 21;6:23449. doi: 10.1038/srep23449.
Dixit (2015). Sulfur alleviates arsenic toxicity by reducing its accumulation and modulating proteome, amino acids and thiol metabolism in rice leaves. Sci Rep. 2015 Nov 10;5:16205. doi: 10.1038/srep16205.
Vera-Estrella et al. (2014). Comparative 2D-DIGE analysis of salinity responsive microsomal proteins from leaves of salt-sensitive Arabidopsis thaliana and salt-tolerant Thellungiella salsuginea. J Proteomics. 2014 Jun 2. pii: S1874-3919(14)00288-7. doi: 10.1016/j.jprot.2014.05.018.

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