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Merck

A8811

Aldolase from rabbit muscle

ammonium sulfate suspension, 10-20 units/mg protein

Synonyme(s) :

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

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60,10 €

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94,60 €

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325,00 €

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A propos de cet article

Numéro CAS:
9024-52-6
UNSPSC Code:
12352204
NACRES:
NA.54
Numéro CE :
4.1.2.13 (BRENDA, IUBMB)
MDL number:
MFCD00130453

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Nom du produit

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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Cet article
G6751A2714L2500
Aldolase from rabbit muscle ammonium sulfate suspension, 10-20 units/mg protein

Sigma-Aldrich

A8811

Aldolase from rabbit muscle

α-Glycérophosphate déshydrogénase from rabbit muscle Type I, ammonium sulfate suspension, 100-300 units/mg protein

Sigma-Aldrich

G6751

α-Glycérophosphate déshydrogénase from rabbit muscle

Aldolase from rabbit muscle lyophilized powder, ≥8.0 units/mg protein

Sigma-Aldrich

A2714

Aldolase from rabbit muscle

L-Lactic Dehydrogenase from rabbit muscle Type II, ammonium sulfate suspension, 800-1,200 units/mg protein

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

Classe de stockage

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

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Certificats d'analyse (COA)

Lot/Batch Number
0000512097
0000512099
0000512099
0000512097
0000498772

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Consulter la Bibliothèque de documents

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
Linjun Guo et al.
Acta crystallographica. Section F, Structural biology and crystallization communications, 68(Pt 8), 958-961 (2012-08-08)
4-Hydroxy-3-methyl-2-keto-pentanoate aldolase (asHPAL), an enzyme used in the synthesis of (2S,3R,4S)-4-hydroxyisoleucine, was crystallized in the absence and the presence of 2-ketobutyrate as one of its substrates by the sitting-drop vapour-diffusion method using PEG 400 as a precipitant. Crystals of asHPAL
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