A8811

Aldolase from rabbit muscle

Name: Aldolase from rabbit muscle
Brand: SIGMA
Price: 356 ILS

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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100 UNITS

₪356.00

200 UNITS

₪404.00

1000 UNITS

₪1,634.00

5000 UNITS

₪5,353.00

₪356.00

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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

Key Documents

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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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This Item	G6751	A2714	L2500
Sigma-Aldrich A8811 Aldolase from rabbit muscle	Sigma-Aldrich G6751 α-Glycerophosphate Dehydrogenase from rabbit muscle	Sigma-Aldrich A2714 Aldolase from rabbit muscle	Sigma-Aldrich L2500 L-Lactic Dehydrogenase from rabbit muscle
biological source rabbit muscle	biological source rabbit muscle	biological source rabbit muscle	biological source -
specific activity 10-20 units/mg protein	specific activity 100-300 units/mg protein	specific activity ≥8.0 units/mg protein	specific activity 800-1,200 units/mg protein
form ammonium sulfate suspension	form ammonium sulfate suspension	form lyophilized powder	form ammonium sulfate suspension
storage temp. 2-8°C	storage temp. 2-8°C	storage temp. −20°C	storage temp. 2-8°C
foreign activity glyceraldehyde-3-phosphate dehydrogenase ≤0.03%, phosphoglucose isomerase ≤0.6%, triosephosphate isomerase ≤0.05%, lactic dehydrogenase ≤0.03%, pyruvate kinase ≤0.1%	foreign activity Lactic dehydrogenase, pyruvate kinase, aldolase, and glyceraldehyde-3-phosphate dehydrogenase ≤0.01%, Triosephosphate isomerase ≤0.02%	foreign activity glyceraldehyde-3-phosphate dehydrogenase ≤0.03%, lactic dehydrogenase ≤0.03%, phosphoglucose isomerase ≤0.6%, pyruvate kinase ≤0.1%, triosephosphate isomerase ≤0.05%	foreign activity pyruvate kinase, myokinase, malic dehydrogenase, glutamic-pyruvic transaminase, glutamic-oxalacetic transaminase and α-glycerophosphate dehydrogenase ≤0.01%
Quality Level 200	Quality Level 200	Quality Level 300	Quality Level 200

Analysis Note

Protein determined by biuret.

Application

Aldolase from rabbit muscle has been used:

in standard 1-phosphofructokinase from rabbit muscle (RPFK-1) assay[1]
as a standard in the characterization of metabolic enzymes from glaucomatous tissues[2]
in fructose 2,6-bisphosphate assay of human cell lines[3]

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 [4].

Biochem/physiol Actions

Aldolase interaction with Wiskott-Aldrich syndrome protein (WASP) may modulate actin dynamics.[5] It reverses the inhibition elicited by ascorbate on Muscle-type LDH (LDH-m4).[6]

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 [4].

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.[7]

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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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)

Effects of long-term exposure to elevated temperature on Zea mays endosperm development during grain fill.

Susan K Boehlein et al.

The Plant journal : for cell and molecular biology, 99(1), 23-40 (2019-02-13)

Cereal yields decrease when grain fill proceeds under conditions of prolonged, moderately elevated temperatures. Endosperm-endogenous processes alter both rate and duration of dry weight gain, but underlying mechanisms remain unclear. Heat effects could be mediated by either abnormal, premature cessation

Using catalytic atom maps to predict the catalytic functions present in enzyme active sites.

Geoffrey R Nosrati et al.

Biochemistry, 51(37), 7321-7329 (2012-08-23)

Catalytic atom maps (CAMs) are minimal models of enzyme active sites. The structures in the Protein Data Bank (PDB) were examined to determine if proteins with CAM-like geometries in their active sites all share the same catalytic function. We combined

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Aldolase from rabbit muscle