Aldolase from rabbit muscle

lyophilized powder, ≥8.0 units/mg protein

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

Quality Level


lyophilized powder

specific activity

≥8.0 units/mg protein


Protein, ≥80% biuret

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.


Looking for similar products? Visit Product Comparison Guide


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 . Product A2714 is essentially sulfate-free and contains citrate buffer salts.


100, 200, 500 units in poly bottle

Biochem/physiol Actions

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

Essentially sulfate-free containing citrate buffer salts

Personal Protective Equipment

dust mask type N95 (US),Eyeshields,Gloves


NONH for all modes of transport

WGK Germany


Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis

Certificate of Origin

Bang Shen et al.
Proceedings of the National Academy of Sciences of the United States of America, 111(9), 3567-3572 (2014-02-20)
Gliding motility and host-cell invasion by apicomplexan parasites depend on cell-surface adhesins that are translocated via an actin-myosin motor beneath the membrane. The current model posits that fructose-1,6-bisphosphate aldolase (ALD) provides a critical link between the cytoplasmic tails of transmembrane...
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...
H Kishi et al.
Proceedings of the National Academy of Sciences of the United States of America, 84(23), 8623-8627 (1987-12-01)
Fructose-1,6-bisphosphate aldolase A (fructose-bisphosphate aldolase; EC deficiency is an autosomal recessive disorder associated with hereditary hemolytic anemia. To clarify the molecular mechanism of the deficiency at the nucleotide level, we have cloned aldolase A cDNA from a patient's poly(A)+...
N C Cross et al.
Lancet (London, England), 335(8685), 306-309 (1990-02-10)
The molecular basis of hereditary fructose intolerance (HFI) was studied in 50 subjects (41 pedigrees, 82 apparently independent mutant alleles of aldolase B) by direct analysis of aldolase B genes amplified by means of the polymerase chain reaction. The mutation...
Lara Babich et al.
ChemSusChem, 5(12), 2348-2353 (2012-11-15)
Herein, we report a new flow process with immobilized enzymes to synthesize complex chiral carbohydrate analogues from achiral inexpensive building blocks in a three-step cascade reaction. The first reactor contained immobilized acid phosphatase, which phosphorylated dihydroxyacetone to dihydroxyacetone phosphate using...
Enzymatic Assay of Fructose-6-Phosphate Kinase Pyrophosphate Dependent
Read More

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service

Social Media

LinkedIn icon
Twitter icon
Facebook Icon
Instagram Icon


Research. Development. Production.

We are a leading supplier to the global Life Science industry with solutions and services for research, biotechnology development and production, and pharmaceutical drug therapy development and production.

© 2021 Merck KGaA, Darmstadt, Germany and/or its affiliates. All Rights Reserved.

Reproduction of any materials from the site is strictly forbidden without permission.