A8811

Aldolase from rabbit muscle

Name: Aldolase from rabbit muscle
Brand: SIGMA

ammonium sulfate suspension, 10-20 units/mg protein

Synonym(s):

D-Fructose-1,6-bisphosphate-D-glyceraldehyde-3-phosphate-lyase, Fructose-diphosphate Aldolase

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About This Item

CAS Number:

9024-52-6

UNSPSC Code:

12352204

NACRES:

NA.54

EC Number:

4.1.2.13 (BRENDA, IUBMB)

MDL number:

MFCD00130453

Product Name

Aldolase from rabbit muscle, ammonium sulfate suspension, 10-20 units/mg protein

biological source

rabbit muscle

form

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.

2-8°C

Quality Level

200

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Analysis Note

Protein determined by biuret.

Application

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 .

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 .

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.

Other Notes

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

Storage Class

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

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Structure of rabbit muscle aldolase at low resolution.

Sygusch J, et al.

The Journal of Biological Chemistry, 260(28), 15286-15290 (1985)

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)

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)

Aldolase and actin protect rabbit muscle lactate dehydrogenase from ascorbate inhibition

Russell PJ, et al.

Journal of Enzyme Inhibition and Medicinal Chemistry, 19(1), 91-98 (2004)

Native and denatured forms of proteins can be discriminated at edge plane carbon electrodes.

Veronika Ostatná et al.

Analytica chimica acta, 735, 31-36 (2012-06-21)

In an attempt to develop a label-free electrochemical method for detection of changes in protein structures based on oxidizability of tyrosine and tryptophan residues we tested different types of carbon electrodes. We found that using edge plane pyrolytic graphite electrode

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