Aldolase from rabbit muscle

ammonium sulfate suspension, 10-20 units/mg protein

D-Fructose-1,6-bisphosphate-D-glyceraldehyde-3-phosphate-lyase, Fructose-diphosphate Aldolase
CAS Number:
Enzyme Commission number:
MDL number:

Quality Level


ammonium sulfate suspension

specific activity

10-20 units/mg protein

foreign activity

glyceraldehyde-3-phosphate dehydrogenase ≤0.03%
lactic dehydrogenase ≤0.03%
phosphoglucose isomerase ≤0.6%
pyruvate kinase ≤0.1%
triosephosphate isomerase ≤0.05%

storage temp.


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General description

Aldolase exists as three isoforms in rabbit, which includes type A from muscle, type B from liver and brain associated type C. Aldolases correspond to a molecular weight of 158 kDa and exists as tetramer.


Aldolase from rabbit muscle has been used:
  • in standard 1-phosphofructokinase from rabbit muscle (RPFK-1) assay
  • as a standard in the characterization of metabolic enzymes from glaucomatous tissues
  • in fructose 2,6-bisphosphate assay of human cell lines

Aldolase is used to convert fructose 1,6-diphosphate to dihydroxyacetone phosphate and glyceraldehyde 3-phosphate. Aldolase, from rabbit muscle has been used for stereospecific deprotonation at DHAP C3 .


5000 units in glass bottle
100, 200, 1000 units in poly bottle

Biochem/physiol Actions

Aldolase interaction with Wiskott-Aldrich syndrome protein (WASP) may modulate actin dynamics. It reverses the inhibition elicited by ascorbate on Muscle-type LDH (LDH-m4).
Aldolase is involved in gluconeogenesis, the Calvin cycle and glycolysis. Aldolase, from rabbit muscle, is a class I aldolase which forms covalent Schiff base intermediates. The active site of aldolase is in the center of the α/β 8 barrel fold .

Unit Definition

One unit will convert 1.0 μmole of fructose 1,6-diphosphate to dihydroxyacetone phosphate and glyceraldehyde 3-phosphate per min at pH 7.4 at 25 °C.

Physical form

Crystalline suspension in 2.5 M (NH4)2SO4, 0.01 M Tris, pH 7.5, 0.001 M EDTA

Analysis Note

Protein determined by biuret.


NONH for all modes of transport

WGK Germany


Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis

Certificate of Origin

Effect of lithium salts on lactate dehydrogenase, adenylate kinase, and 1-phosphofructokinase activities
Russell P, et al.
Journal of Enzyme Inhibition and Medicinal Chemistry, 25(4), 551-556 (2010)
Structure of rabbit muscle aldolase at low resolution.
Sygusch J, et al.
The Journal of Biological Chemistry, 260(28), 15286-15290 (1985)
A hydrophobic pocket in the active site of glycolytic aldolase mediates interactions with Wiskott-Aldrich syndrome protein
St-Jean M, et al.
The Journal of biological chemistry, 282(19), 14309-14315 (2007)
Clotilde LowKam et al.
The Journal of biological chemistry, 285(27), 21143-21152 (2010-04-30)
Tagatose-1,6-bisphosphate aldolase from Streptococcus pyogenes is a class I aldolase that exhibits a remarkable lack of chiral discrimination with respect to the configuration of hydroxyl groups at both C3 and C4 positions. The enzyme catalyzes the reversible cleavage of four...
Masahiko Hayakawa et al.
Chembiochem : a European journal of chemical biology, 13(15), 2191-2195 (2012-09-12)
Programming an anti-flu strategy: A new and potent neuraminidase inhibitor that maintains long-term systemic exposure of an antibody and the therapeutic activity of the neuraminadase inhibitor zanamivir has been created. This strategy could provide a promising new class of influenza...
Instructions for working with enzymes supplied as ammonium sulfate suspensions
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